Updated on 2025/08/15

写真a

 
FUTAMI Junichiro
 
Organization
Faculty of Interdisciplinary Science and Engineering in Health Systems Professor
Position
Professor
Homepage
http://www.okayama-u.ac.jp/user/proteng/
Profile
Medical protein engineering Lab is working to realize medical application of protein engineering. Our on-going efforts focus on innovative application of denatured protein solubilization techniques for immune-oncology.
External link

Degree

  • 修士(工学)

  • Ph.D. ( Okayama University )

Research Interests

  • Biochemistry

  • Immuno-Oncology

  • Biotechnology

  • Protein Engineering

Research Areas

  • Nanotechnology/Materials / Chemistry and chemical methodology of biomolecules

  • Life Science / Tumor diagnostics and therapeutics

  • Manufacturing Technology (Mechanical Engineering, Electrical and Electronic Engineering, Chemical Engineering) / Biofunction and bioprocess engineering

  • Life Science / Molecular biology

Education

  • Okayama University   自然科学研究科   生物資源科学専攻

    1996.4 - 1999.3

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    Country： Japan

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  • Okayama University   工学研究科   生体機能応用工学専攻

    1994.4 - 1996.3

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  • Okayama University   工学部   生体機能応用工学科

    1990.4 - 1994.3

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    Country： Japan

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Research History

  • 学術研究院ヘルスシステム統合科学学域 教授

    2022.4

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  • 岡山大学大学院ヘルスシステム統合科学研究科 研究教授

    2019.12 - 2022.3

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  • Okayama University   Department of Interdisciplinary Science and Engineering in Health Systems   PI Associate Professor

    2018.4 - 2019.12

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  • Okayama University   Graduate School of Natural Science and Technology   PI Associate Professor

    2008.10 - 2018.3

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  • Okayama University   Graduate School of Natural Science and Technology   Senior Assistant Professor

    2005.10 - 2008.9

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  • NEDO-P/J PD fellow

    2003.2 - 2005.9

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  • Smimitomo Pharm. Genomics Research Group

    2002.4 - 2003.1

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  • NCI-Frederick, Guest PD Fellow

    2000.1 - 2000.12

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  • JSPS PD-Fellow

    1999.4 - 2002.3

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  • JSPS DC2 Fellow

    1997.4 - 1999.3

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Professional Memberships

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Committee Memberships

  • 日本生化学会   評議員  

    2016.9   

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    Committee type：Academic society

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  • 日本生物工学会   和文誌編集委員  

    2016.6 - 2022.6   

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    Committee type：Academic society

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  • 日本生物工学会   代議員  

    2013   

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    Committee type：Academic society

    日本生物工学会

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Papers

  • Autoantibody spark response predicts treatment outcome in patients receiving chemoradiation followed by durvalumab therapy. Reviewed International journal

    Takeru Mori, Mio Kitagawa, Tomokazu Hasegawa, Masanori Someya, Takaaki Tsuchiya, Toshio Gocho, Tomoko Honjo, Mirei Date, Mariko Morii, Ai Miyamoto, Junichiro Futami

    Scientific reports   15 ( 1 )   27502 - 27502   2025.7

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    Authorship：Last author,　Corresponding author   Language：English   Publishing type：Research paper (scientific journal)  

    The PACIFIC regimen, comprising chemoradiotherapy (CRT) followed by maintenance with the immune checkpoint inhibitor (ICI) durvalumab, has become the standard of care for patients with unresectable non-small cell lung cancer (NSCLC). Although ICI is used to prevent recurrence by targeting residual microtumors, biomarkers capable of monitoring immune activity during this phase remain lacking. Here, we evaluated whether temporal changes in serum autoantibody levels can predict treatment efficacy. This retrospective study included 20 patients with unresectable stage II or III NSCLC who received the PACIFIC regimen. Serum autoantibodies against 130 antigens were quantified before CRT, after CRT, and two weeks after the first ICI dose. The primary outcome was progression-free survival (PFS), and its association with autoantibody dynamics was examined. We observed an immediate and strong autoantibody response (spark response [SR]) after ICI initiation in patients with favorable treatment outcomes. Patients with SR and programmed death ligand 1 (PD-L1) expression ≥ 50% showed better PFS (two-year PFS; 72.9% vs. 18.2%, p = 0.0021). These findings suggest that serial monitoring of serum autoantibodies can provide a noninvasive approach to assess immune activity and predict treatment outcomes in patients receiving CRT or ICI therapy.

    DOI： 10.1038/s41598-025-12069-5

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  • Pre-folding purification procedures for inclusion body-derived non-tagged cationic recombinant proteins with multiple disulfide bonds for efficient refolding. Reviewed International journal

    Shuichiro Kimura, Wataru Yamamoto, Ai Miyamoto, Koreyoshi Imamura, Junichiro Futami

    Biotechnology progress   e3532   2025.1

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    Authorship：Last author,　Corresponding author   Language：English   Publishing type：Research paper (scientific journal)  

    The production of disulfide-containing recombinant proteins often requires refolding of inclusion bodies before purification. A pre-refolding purification step is crucial for effective refolding because impurities in the inclusion bodies interfere with refolding and subsequent purification. This study presents a new pre-refolding procedure using a reversible S-cationization technique for protein solubilization and purification by reversed-phase high performance liquid chromatography. This pre-folding purification step improves refolding yield by effectively removing the refolding inhibitors from contaminates from bacterial inclusion bodies, and reducing proteolytically degraded products. Because this procedure does not require a peptide tag for affinity purification, it is a superior technique to subsequently perform a simplified downstream process wherein the affinity tag needs to be removed. This study reports improved refolding and purification procedure to obtain the highly cationic (pI = 9.25) mouse vascular endothelial cell growth factor (188 amino acids form) that is used as a model protein in our study; this protein shows a homodimeric conformation and possesses multiple disulfides.

    DOI： 10.1002/btpr.3532

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  • An S100A8/A9 Neutralizing Antibody Potently Ameliorates Contact Hypersensitivity and Atopic Dermatitis Symptoms. Reviewed International journal

    Yuma Gohara, Rie Kinoshita, Nahoko Tomonobu, Fan Jiang, Yukiko Matsunaga, Yuki Hashimoto, Tomoko Honjo, Ken-Ichi Yamamoto, Hitoshi Murata, Toshiki Ochi, Ni Luh Gede Yoni Komalasari, Akira Yamauchi, Futoshi Kuribayashi, Yoshihiko Sakaguchi, Junichiro Futami, Yusuke Inoue, Eisaku Kondo, Shinichi Toyooka, Shin Morizane, Akira Ishiko, Shigeru Morita, Kazumi Sagayama, Kenichiro Nakao, Masakiyo Sakaguchi

    The Journal of investigative dermatology   2025.1

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    Language：English   Publishing type：Research paper (scientific journal)  

    Contact hypersensitivity and atopic dermatitis are pervasive inflammatory skin diseases with similar symptoms, and their global prevalence is steadily increasing. Many compounds and biotics have been developed to target molecules critical to the etiology or pathogenesis of contact hypersensitivity and atopic dermatitis. However, these molecules are sometimes ineffective or lose their potency during the therapeutic course. Therefore, innovative medicines are still needed for the treatment of intractable cases. We focused on S100A8/A9, a heterodimer complex of S100A8 and S100A9 that is abundant in the extracellular milieu of inflammatory skin lesions. Although S100A8/A9 is primarily recognized as a diagnostic marker protein, we have previously shown that it also plays a crucial role in contact hypersensitivity and atopic dermatitis progression. This insight inspired us to develop its inhibitory antibody, leading to the ground-breaking Ab45. In this study, we demonstrated that Ab45 effectively prevented disease symptoms in various models and that its disease-ameliorating activity likely involved the downregulation of several disease-relevant molecules, including Il-23a, Il-36g, S100a8, and S100a9. We also created a humanized version of Ab45, HuAb45, which exhibited similar effectiveness. These antibodies show great promise for the treatment of contact hypersensitivity and atopic dermatitis and possibly for other inflammatory skin diseases.

    DOI： 10.1016/j.jid.2025.01.007

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  • Enhanced design of pCMViR-TSC plasmid vector for sustainably high cargo gene expression in mammalian cells. Reviewed International journal

    Masakiyo Sakaguchi, Rie Kinoshita, Nahoko Tomonobu, Yoshihiko Sakaguchi, Junichiro Futami, Akira Yamauchi, Hitoshi Murata, Ken-Ichi Yamamoto, Tetta Takahashi, Yuma Gohara, Toshiki Ochi, Fan Jiang, Ni Luh Gede Yoni Komalasari, Youyi Chen, I Made Winarsa Ruma, I Wayan Sumardika, Jin Zhou, Tomoko Honjo, Futoshi Kuribayashi, Kazumi Sagayama, Shinichi Toyooka, Eisaku Kondo, Yusuke Inoue

    In vitro cellular & developmental biology. Animal   2024.11

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    Language：English   Publishing type：Research paper (scientific journal)  

    The first-generation pCMViR-TSC, implemented through the promoter sandwich rule, yields 10- to 100-fold higher gene expression than the standard plasmid used with the CMV (cytomegalovirus) or CAG promoter. However, the vector's shortcomings limit its utility to transient expression only, as it is not suitable for establishing stable transformants in mammalian cells. To overcome this weakness, we here introduce the improved plasmid vector pSAKA-4B, derived from pCMViR-TSC as a second-generation chromosome-insertable vector. This vector facilitates the linear entry of the expression unit into the TTAA site of DNA universally with transposase assistance. The vector is helpful for the indefinite expression of our target gene. The new vector system is proven here to be efficient in establishing stable transformants with a high likelihood of positive clones that exhibit significantly elevated expression levels of the delivered foreign gene. This system, alongside the first-generation vector, is therefore instrumental for diverse basic research endeavors concerning genes, proteins, cells, and animals, and potentially for clinical applications such as gene therapy.

    DOI： 10.1007/s11626-024-00992-2

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  • Dissection of the signal transduction machinery responsible for the lysyl oxidase-like 4-mediated increase in invasive motility in triple-negative breast cancer cells: mechanistic insight into the integrin-β1-NF-κB-MMP9 axis. Reviewed

    Jiang F, Chen Y, Tomonobu N, Kinoshita R, Komalasari NLGY, Kasano-Camones CI, Ninomiya K, Murata H, Yamamoto KI, Gohara Y, Ochi T, Ruma IMW, Sumardika IW, Zhou J, Honjo T, Sakaguchi Y, Yamauchi A, Kuribayashi F, Futami J, Kondo E, Inoue Y, Toyooka S, Sakaguchi M

    Frontiers in oncology   14 ( 1371307 )   2024.5

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    Language：English   Publishing type：Research paper (scientific journal)  

    <h4>Background</h4>Triple-negative breast cancer (TNBC) cells are a highly formidable cancer to treat. Nonetheless, by continued investigation into the molecular biology underlying the complex regulation of TNBC cell activity, vulnerabilities can be exposed as potential therapeutic targets at the molecular level. We previously revealed that lysyl oxidase-like 4 (LOXL4) promotes the invasiveness of TNBC cells via cell surface annexin A2 as a novel binding substrate of LOXL4, which promotes the abundant localization of integrin-β1 at the cancer plasma membrane. However, it has yet to be uncovered how the LOXL4-mediated abundance of integrin-β1 hastens the invasive outgrowth of TNBC cells at the molecular level.<h4>Methods</h4>LOXL4-overexpressing stable clones were established from MDA-MB-231 cells and subjected to molecular analyses, real-time qPCR and zymography to clarify their invasiveness, signal transduction, and matrix metalloprotease (MMP) activity, respectively.<h4>Results</h4>Our results show that LOXL4 potently promotes the induction of matrix metalloprotease 9 (MMP9) via activation of nuclear factor-κB (NF-κB). Our molecular analysis revealed that TNF receptor-associated factor 4 (TRAF4) and TGF-β activated kinase 1 (TAK1) were required for the activation of NF-κB through Iκβ kinase kinase (IKKα/β) phosphorylation.<h4>Conclusion</h4>Our results demonstrate that the newly identified LOXL4-mediated axis, integrin-β1-TRAF4-TAK1-IKKα/β-Iκβα-NF-κB-MMP9, is crucial for TNBC cell invasiveness.

    DOI： 10.3389/fonc.2024.1371307

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  • Lysyl oxidase-like 4 promotes the invasiveness of triple-negative breast cancer cells by orchestrating the invasive machinery formed by annexin A2 and S100A11 on the cell surface. Reviewed International journal

    Tetta Takahashi, Nahoko Tomonobu, Rie Kinoshita, Ken-Ichi Yamamoto, Hitoshi Murata, Ni Luh Gede Yoni Komalasari, Youyi Chen, Fan Jiang, Yuma Gohara, Toshiki Ochi, I Made Winarsa Ruma, I Wayan Sumardika, Jin Zhou, Tomoko Honjo, Yoshihiko Sakaguchi, Akira Yamauchi, Futoshi Kuribayashi, Eisaku Kondo, Yusuke Inoue, Junichiro Futami, Shinichi Toyooka, Yoshito Zamami, Masakiyo Sakaguchi

    Frontiers in oncology   14   1371342 - 1371342   2024

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    Language：English   Publishing type：Research paper (scientific journal)  

    BACKGROUND: Our earlier research revealed that the secreted lysyl oxidase-like 4 (LOXL4) that is highly elevated in triple-negative breast cancer (TNBC) acts as a catalyst to lock annexin A2 on the cell membrane surface, which accelerates invasive outgrowth of the cancer through the binding of integrin-β1 on the cell surface. However, whether this machinery is subject to the LOXL4-mediated intrusive regulation remains uncertain. METHODS: Cell invasion was assessed using a transwell-based assay, protein-protein interactions by an immunoprecipitation-Western blotting technique and immunocytochemistry, and plasmin activity in the cell membrane by gelatin zymography. RESULTS: We revealed that cell surface annexin A2 acts as a receptor of plasminogen via interaction with S100A10, a key cell surface annexin A2-binding factor, and S100A11. We found that the cell surface annexin A2/S100A11 complex leads to mature active plasmin from bound plasminogen, which actively stimulates gelatin digestion, followed by increased invasion. CONCLUSION: We have refined our understanding of the role of LOXL4 in TNBC cell invasion: namely, LOXL4 mediates the upregulation of annexin A2 at the cell surface, the upregulated annexin 2 binds S100A11 and S100A10, and the resulting annexin A2/S100A11 complex acts as a receptor of plasminogen, readily converting it into active-form plasmin and thereby enhancing invasion.

    DOI： 10.3389/fonc.2024.1371342

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  • Hydrophobicity and molecular mass‐based separation method for autoantibody discovery from mammalian total cellular proteins Reviewed

    Mirei Date, Ai Miyamoto, Tomoko Honjo, Tsugumi Shiokawa, Hiroko Tada, Nobuhiro Okada, Junichiro Futami

    Protein Science   32 ( 10 )   2023.9

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    Authorship：Last author,　Corresponding author   Publishing type：Research paper (scientific journal)   Publisher：Wiley  

    Abstract

    Serum autoantibody profiles are unique to individuals and reflect the level and history of autoimmunity and tumor immunity. The identification of autoantibody biomarkers is critical for the development of immune monitoring systems for immune‐related disorders. Here, we present a practical method for large‐scale autoantibody discovery using total cellular proteins from cultured mammalian cells. We found that nucleic acid‐free and fully denatured water‐soluble total cellular proteins from mammalian cells were superior, allowing precise separation by reversed‐phase HPLC after preparing a large set of homogeneous total cellular proteins. After separating the proteins based on hydrophobicity, the fractionated samples were subjected to molecular mass analysis using conventional SDS‐PAGE. The resulting two‐dimensional gel electrophoresis was successfully employed for immune blotting and LC–MS/MS analysis. All procedures, including TRIzol‐based total cellular protein extraction, solubilization of denatured proteins, reversed‐phase HPLC separation, and SDS‐PAGE, were highly reproducible and easily scalable. We propose this novel two‐dimensional gel electrophoresis system as an alternative proteomics‐based methodology suitable for large‐scale autoantibody discovery.

    DOI： 10.1002/pro.4771

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  • Novel extracellular role of REIC/Dkk-3 protein in PD-L1 regulation in cancer cells. Reviewed International journal

    Yuma Gohara, Nahoko Tomonobu, Rie Kinoshita, Junichiro Futami, Léna Audebert, Youyi Chen, Ni Luh Gede Yoni Komalasari, Fan Jiang, Chikako Yoshizawa, Hitoshi Murata, Ken-Ichi Yamamoto, Masami Watanabe, Hiromi Kumon, Masakiyo Sakaguchi

    Journal of molecular medicine (Berlin, Germany)   101 ( 4 )   431 - 447   2023.3

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    Language：English   Publishing type：Research paper (scientific journal)  

    The adenovirus-REIC/Dkk-3 expression vector (Ad-REIC) has been the focus of numerous clinical studies due to its potential for the quenching of cancers. The cancer-suppressing mechanisms of the REIC/DKK-3 gene depend on multiple pathways that exert both direct and indirect effects on cancers. The direct effect is triggered by REIC/Dkk-3-mediated ER stress that causes cancer-selective apoptosis, and the indirect effect can be classified in two ways: (i) induction, by Ad-REIC-mis-infected cancer-associated fibroblasts, of the production of IL-7, an important activator of T cells and NK cells, and (ii) promotion, by the secretory REIC/Dkk-3 protein, of dendritic cell polarization from monocytes. These unique features allow Ad-REIC to exert effective and selective cancer-preventative effects in the manner of an anticancer vaccine. However, the question of how the REIC/Dkk-3 protein leverages anticancer immunity has remained to be answered. We herein report a novel function of the extracellular REIC/Dkk-3-namely, regulation of an immune checkpoint via modulation of PD-L1 on the cancer-cell surface. First, we identified novel interactions of REIC/Dkk-3 with the membrane proteins C5aR, CXCR2, CXCR6, and CMTM6. These proteins all functioned to stabilize PD-L1 on the cell surface. Due to the dominant expression of CMTM6 among the proteins in cancer cells, we next focused on CMTM6 and observed that REIC/Dkk-3 competed with CMTM6 for PD-L1, thereby liberating PD-L1 from its complexation with CMTM6. The released PD-L1 immediately underwent endocytosis-mediated degradation. These results will enhance our understanding of not only the physiological nature of the extracellular REIC/Dkk-3 protein but also the Ad-REIC-mediated anticancer effects. KEY MESSAGES: • REIC/Dkk-3 protein effectively suppresses breast cancer progression through an acceleration of PD-L1 degradation. • PD-L1 stability on the cancer cell membrane is kept high by binding with mainly CMTM6. • Competitive binding of REIC/Dkk-3 protein with CMTM6 liberates PD-L1, leading to PD-L1 degradation.

    DOI： 10.1007/s00109-023-02292-w

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  • Toll-like receptor 4 promotes bladder cancer progression upon S100A8/A9 binding, which requires TIRAP-mediated TPL2 activation. Reviewed International journal

    Acosta Gonzalez Herik Rodrigo, Nahoko Tomonobu, Haruka Yoneda, Rie Kinoshita, Yosuke Mitsui, Takuya Sadahira, Shin-Ichi Terawaki, Yuma Gohara, Ni Luh Gede Yoni Komalasari, Fan Jiang, Hitoshi Murata, Ken-Ichi Yamamoto, Junichiro Futami, Akira Yamauchi, Futoshi Kuribayashi, Yusuke Inoue, Eisaku Kondo, Shinichi Toyooka, Masahiro Nishibori, Masami Watanabe, Yasutomo Nasu, Masakiyo Sakaguchi

    Biochemical and biophysical research communications   634   83 - 91   2022.12

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    Bladder cancer is an often widely disseminated and deadly cancer. To block the malignant outgrowth of bladder cancer, we must elucidate the molecular-level characteristics of not only bladder cancer cells but also their surrounding milieu. As part of this effort, we have long been studying extracellular S100A8/A9, which is elevated by the inflammation associated with certain cancers. Extracellularly enriched S100A8/A9 can hasten a shift to metastatic transition in multiple types of cancer cells. Intriguingly, high-level S100A8/A9 has been detected in the urine of bladder-cancer patients, and the level increases with the stage of malignancy. Nonetheless, S100A8/A9 has been investigated mainly as a potential biomarker of bladder cancers, and there have been no investigations of its role in bladder-cancer growth and metastasis. We herein report that extracellular S100A8/A9 induces upregulation of growth, migration and invasion in bladder cancer cells through its binding with cell-surface Toll-like receptor 4 (TLR4). Our molecular analysis revealed the TLR4 downstream signal that accelerates such cancer cell events. Tumor progression locus 2 (TPL2) was a key factor facilitating the aggressiveness of cancer cells. Upon binding of S100A8/A9 with TLR4, TPL2 activation was enhanced by an action with a TLR4 adaptor molecule, TIR domain-containing adaptor protein (TIRAP), which in turn led to activation of the mitogen-activated protein kinase (MAPK) cascade of TPL2. Finally, we showed that sustained inhibition of TLR4 in cancer cells effectively dampened cancer survival in vivo. Collectively, our results indicate that the S100A8/A9-TLR4-TPL2 axis influences the growth, survival, and invasive motility of bladder cancer cells.

    DOI： 10.1016/j.bbrc.2022.09.116

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  • Immune State Conversion of the Mesenteric Lymph Node in a Mouse Breast Cancer Model. Reviewed International journal

    Tsukasa Shigehiro, Maho Ueno, Mayumi Kijihira, Ryotaro Takahashi, Chiho Umemura, Eman A Taha, Chisaki Kurosaka, Megumi Asayama, Hiroshi Murakami, Ayano Satoh, Yoshimasa Nakamura, Junichiro Futami, Junko Masuda

    International journal of molecular sciences   23 ( 19 )   2022.9

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    Language：English   Publishing type：Research paper (scientific journal)  

    Secondary lymphoid tissues, such as the spleen and lymph nodes (LNs), contribute to breast cancer development and metastasis in both anti- and pro-tumoral directions. Although secondary lymphoid tissues have been extensively studied, very little is known about the immune conversion in mesenteric LNs (mLNs) during breast cancer development. Here, we demonstrate inflammatory immune conversion of mLNs in a metastatic 4T1 breast cancer model. Splenic T cells were significantly decreased and continuously suppressed IFN-γ production during tumor development, while myeloid-derived suppressor cells (MDSCs) were dramatically enriched. However, T cell numbers in the mLN did not decrease, and the MDSCs only moderately increased. T cells in the mLN exhibited conversion from a pro-inflammatory state with high IFN-γ expression to an anti-inflammatory state with high expression of IL-4 and IL-10 in early- to late-stages of breast cancer development. Interestingly, increased migration of CD103+CD11b+ dendritic cells (DCs) into the mLN, along with increased (1→3)-β-D-glucan levels in serum, was observed even in late-stage breast cancer. This suggests that CD103+CD11b+ DCs could prime cancer-reactive T cells. Together, the data indicate that the mLN is an important lymphoid tissue contributing to breast cancer development.

    DOI： 10.3390/ijms231911035

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  • Histidine-Rich Glycoprotein Suppresses the S100A8/A9-Mediated Organotropic Metastasis of Melanoma Cells Reviewed

    Nahoko Tomonobu, Rie Kinoshita, Hidenori Wake, Yusuke Inoue, I Made Winarsa Ruma, Ken Suzawa, Yuma Gohara, Ni Luh Gede Yoni Komalasari, Fan Jiang, Hitoshi Murata, Ken-ichi Yamamoto, I Wayan Sumardika, Youyi Chen, Junichiro Futami, Akira Yamauchi, Futoshi Kuribayashi, Eisaku Kondo, Shinichi Toyooka, Masahiro Nishibori, Masakiyo Sakaguchi

    International Journal of Molecular Sciences   23 ( 18 )   10300 - 10300   2022.9

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    Publishing type：Research paper (scientific journal)   Publisher：MDPI AG  

    The dissection of the complex multistep process of metastasis exposes vulnerabilities that could be exploited to prevent metastasis. To search for possible factors that favor metastatic outgrowth, we have been focusing on secretory S100A8/A9. A heterodimer complex of the S100A8 and S100A9 proteins, S100A8/A9 functions as a strong chemoattractant, growth factor, and immune suppressor, both promoting the cancer milieu at the cancer-onset site and cultivating remote, premetastatic cancer sites. We previously reported that melanoma cells show lung-tropic metastasis owing to the abundant expression of S100A8/A9 in the lung. In the present study, we addressed the question of why melanoma cells are not metastasized into the brain at significant levels in mice despite the marked induction of S100A8/A9 in the brain. We discovered the presence of plasma histidine-rich glycoprotein (HRG), a brain-metastasis suppression factor against S100A8/A9. Using S100A8/A9 as an affinity ligand, we searched for and purified the binding plasma proteins of S100A8/A9 and identified HRG as the major protein on mass spectrometric analysis. HRG prevents the binding of S100A8/A9 to the B16-BL6 melanoma cell surface via the formation of the S100A8/A9 complex. HRG also inhibited the S100A8/A9-induced migration and invasion of A375 melanoma cells. When we knocked down HRG in mice bearing skin melanoma, metastasis to both the brain and lungs was significantly enhanced. The clinical examination of plasma S100A8/A9 and HRG levels showed that lung cancer patients with brain metastasis had higher S100A8/A9 and lower HRG levels than nonmetastatic patients. These results suggest that the plasma protein HRG strongly protects the brain and lungs from the threat of melanoma metastasis.

    DOI： 10.3390/ijms231810300

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  • The immunoreceptor SLAMF8 promotes the differentiation of follicular dendritic cell-dependent monocytic cells with B cell-activating ability. Reviewed International journal

    Masaki Magari, Miku Nishioka, Tomomi Hari, Sayaka Ogawa, Kaho Takahashi, Naoya Hatano, Naoki Kanayama, Junichiro Futami, Hiroshi Tokumitsu

    FEBS letters   2022.8

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    Language：English   Publishing type：Research paper (scientific journal)  

    Follicular dendritic cells (FDCs) play a crucial role in generating high-affinity antibody-producing B cells during the germinal center (GC) reaction. Herein, we analysed the altered gene expression profile of a mouse FDC line, FL-Y, following lymphotoxin β receptor stimulation, and observed increased Slam-family member 8 (Slamf8) mRNA expression. Forced Slamf8 expression and SLAMF8-Fc addition enhanced the ability of FL-Y cells to induce FDC-induced monocytic cell (FDMC) differentiation. FDMCs accelerated GC-phenotype proliferation in cultured B cells, suggesting that they are capable of promoting GC responses. Furthermore, a pulldown assay showed that SLAMF8-Fc could bind to SLAMF8-His. Overall, the homophilic interaction of SLAMF8 promotes FDMC differentiation and SLAMF8 might act as a novel regulator of GC responses by regulating FDMC differentiation.

    DOI： 10.1002/1873-3468.14468

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  • Dkk3/REIC Deficiency Impairs Spermiation, Sperm Fibrous Sheath Integrity and the Sperm Motility of Mice. Reviewed International journal

    Ruizhi Xue, Wenfeng Lin, Hirofumi Fujita, Jingkai Sun, Rie Kinoshita, Kazuhiko Ochiai, Junichiro Futami, Masami Watanabe, Hideyo Ohuchi, Masakiyo Sakaguchi, Zhengyan Tang, Peng Huang, Yasutomo Nasu, Hiromi Kumon

    Genes   13 ( 2 )   2022.1

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    Language：English   Publishing type：Research paper (scientific journal)  

    The role of Dickkopf-3 (Dkk3)/REIC (The Reduced Expression in Immortalized Cells), a Wnt-signaling inhibitor, in male reproductive physiology remains unknown thus far. To explore the functional details of Dkk3/REIC in the male reproductive process, we studied the Dkk3/REIC knock-out (KO) mouse model. By examining testicular sections and investigating the sperm characteristics (count, vitality and motility) and ultrastructure, we compared the reproductive features between Dkk3/REIC-KO and wild-type (WT) male mice. To further explore the underlying molecular mechanism, we performed RNA sequencing (RNA-seq) analysis of testicular tissues. Our results showed that spermiation failure existed in seminiferous tubules of Dkk3/REIC-KO mice, and sperm from Dkk3/REIC-KO mice exhibited inferior motility (44.09 ± 8.12% vs. 23.26 ± 10.02%, p < 0.01). The Ultrastructure examination revealed defects in the sperm fibrous sheath of KO mice. Although the average count of Dkk3/REIC-KO epididymal sperm was less than that of the wild-types (9.30 ± 0.69 vs. 8.27 ± 0.87, ×106), neither the gap (p > 0.05) nor the difference in the sperm vitality rate (72.83 ± 1.55% vs. 72.50 ± 0.71%, p > 0.05) were statistically significant. The RNA-seq and GO (Gene Oncology) enrichment results indicated that the differential genes were significantly enriched in the GO terms of cytoskeleton function, cAMP signaling and calcium ion binding. Collectively, our research demonstrates that Dkk3/REIC is involved in the process of spermiation, fibrous sheath integrity maintenance and sperm motility of mice.

    DOI： 10.3390/genes13020285

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  • Engineering Cancer/Testis Antigens With Reversible S-Cationization to Evaluate Antigen Spreading. Reviewed International journal

    Ai Miyamoto, Tomoko Honjo, Mirei Masui, Rie Kinoshita, Hiromi Kumon, Kazuhiro Kakimi, Junichiro Futami

    Frontiers in oncology   12   869393 - 869393   2022

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    Serum autoantibody to cancer/testis antigens (CTAs) is a critical biomarker that reflects the antitumor immune response. Quantitative and multiplexed anti-CTA detection arrays can assess the immune status in tumors and monitor therapy-induced antitumor immune reactions. Most full-length recombinant CTA proteins tend to aggregate. Cysteine residue-specific S-cationization techniques facilitate the preparation of water-soluble and full-length CTAs. Combined with Luminex technology, we designed a multiple S-cationized antigen-immobilized bead array (MUSCAT) assay system to evaluate multiple serum antibodies to CTAs. Reducible S-alkyl-disulfide-cationized antigens in cytosolic conditions were employed to develop rabbit polyclonal antibodies as positive controls. These control antibodies sensitively detected immobilized antigens on beads and endogenous antigens in human lung cancer-derived cell lines. Rabbit polyclonal antibodies successfully confirmed the dynamic ranges and quantitative MUSCAT assay results. An immune monitoring study was conducted using the serum samples on an adenovirus-mediated REIC/Dkk-3 gene therapy clinical trial that showed a successful clinical response in metastatic castration-resistant prostate cancer. Autoantibody responses were closely related to clinical outcomes. Notably, upregulation of anti-CTA responses was monitored before tumor regression. Thus, quantitative monitoring of anti-CTA antibody biomarkers can be used to evaluate the cancer-immunity cycle. A quality-certified serum autoantibody monitoring system is a powerful tool for developing and evaluating cancer immunotherapy.

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  • Identification of Neoantigens in Two Murine Gastric Cancer Cell Lines Leading to the Neoantigen-Based Immunotherapy. Reviewed International journal

    Koji Nagaoka, Changbo Sun, Yukari Kobayashi, Takayuki Kanaseki, Serina Tokita, Toshihiro Komatsu, Kazuhiro Maejima, Junichiro Futami, Sachiyo Nomura, Keiko Udaka, Hidewaki Nakagawa, Toshihiko Torigoe, Kazuhiro Kakimi

    Cancers   14 ( 1 )   2021.12

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    To develop combination immunotherapies for gastric cancers, immunologically well-characterized preclinical models are crucial. Here, we leveraged two transplantable murine gastric cancer cell lines, YTN2 and YTN16, derived from the same parental line but differing in their susceptibility to immune rejection. We established their differential sensitivity to immune checkpoint inhibitors (ICI) and identified neoantigens. Although anti-CTLA-4 mAbs eradicated YTN16 tumors in 4 of 5 mice, anti-PD-1 and anti-PD-L1 mAbs failed to eradicate YTN16 tumors. Using whole-exome and RNA sequencing, we identified two and three neoantigens in YTN2 and YTN16, respectively. MHC class I ligandome analysis detected the expression of only one of these neoantigens, mutated Cdt1, but the exact length of MHC binding peptide was determined. Dendritic cell vaccine loaded with neoepitope peptides and adoptive transfer of neoantigen-specific CD8+ T cells successfully inhibited the YTN16 tumor growth. Targeting mutated Cdt1 had better efficacy for controlling the tumor. Therefore, mutated Cdt1 was the dominant neoantigen in these tumor cells. More mCdt1 peptides were bound to MHC class I and presented on YTN2 surface than YTN16. This might be one of the reasons why YTN2 was rejected while YTN16 grew in immune-competent mice.

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  • Unusual aggregation property of recombinantly expressed cancer-testis antigens in mammalian cells. Reviewed International journal

    Hannaneh Ahmadi, Kohei Shogen, Kana Fujita, Tomoko Honjo, Kazuhiro Kakimi, Junichiro Futami

    Journal of biochemistry   170 ( 3 )   435 - 443   2021.10

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    Transient expression of human intracellular proteins in human embryonic kidney (HEK) 293 cells is a reliable system for obtaining soluble proteins with biologically active conformations. Contrary to conventional concepts, we found that recombinantly expressed intracellular cancer-testis antigens (CTAs) showed frequent aggregation in HEK293 cells. Although experimental subcellular localization of recombinant CTAs displayed proper cytosolic or nuclear localization, some proteins showed aggregated particles in the cell. This aggregative property was not observed in recombinant housekeeping proteins. No significant correlation was found between the aggregative and biophysical properties, such as hydrophobicity, contents of intrinsically disordered regions and expression levels, of CTAs. These results can be explained in terms of structural instability of CTAs, which are specifically expressed in the testis and aberrantly expressed in cancer cells and function as a hub in the protein-protein network using intrinsically disordered regions. Hence, we speculate that recombinantly expressed CTAs failed to form this protein complex. Thus, unfolded CTAs formed aggregated particles in the cell.

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  • 創意化学的な生体高分子の生物工学 特集によせて

    二見 淳一郎, 山口 哲志

    生物工学会誌   99 ( 4 )   162   2021

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  • 創意化学的な生体高分子の生物工学 変性タンパク質工学と免疫プロファイリング技術開発

    二見淳一郎

    生物工学会誌   99 ( 4 )   2021

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  • A suitable and effective stepwise oxidative refolding procedure for highly‐cationic tetrameric avidin in nucleic acid free conditions Reviewed International journal

    Shuichiro Kimura, Koreyoshi Imamura, Junichiro Futami

    Biotechnology Progress   36 ( 5 )   e3031   2020.9

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    Optimized conditions are needed to refold recombinant proteins from bacterial inclusion bodies into their biologically active conformations. In this study, we found two crucial requirements for efficient refolding of cationic tetrameric chicken avidin. The first step is to eliminate nucleic acid contaminants from the bacterial inclusion body. The electrostatic interactions between the remaining nucleic acids and proteins strongly enhanced protein aggregation during the refolding process. The cysteine specific reversible S-cationization procedure was successfully employed for large-scale preparation of nucleic acid free denatured protein without purification tag system. The second step is the intramolecular disulfide formation prior to refolding in dialysis removing denaturant. Disulfide intact monomeric avidin showed efficient formation of biologically active tetrameric conformation during the refolding process. Using this optimized refolding procedure, highly cationic avidin derivative designed as an intracellular delivery carrier of biotinylated protein was successfully prepared.

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    Other Link： https://onlinelibrary.wiley.com/doi/full-xml/10.1002/btpr.3031

  • Serum Antibody Against NY-ESO-1 and XAGE1 Antigens Potentially Predicts Clinical Responses to Anti-Programmed Cell Death-1 Therapy in NSCLC. Reviewed International journal

    Yoshihiro Ohue, Koji Kurose, Takahiro Karasaki, Midori Isobe, Takaaki Yamaoka, Junichiro Futami, Isao Irei, Takeshi Masuda, Masaaki Fukuda, Akitoshi Kinoshita, Hirokazu Matsushita, Katsuhiko Shimizu, Masao Nakata, Noboru Hattori, Hiroyuki Yamaguchi, Minoru Fukuda, Ryohei Nozawa, Kazuhiro Kakimi, Mikio Oka

    Journal of thoracic oncology : official publication of the International Association for the Study of Lung Cancer   14 ( 12 )   2071 - 2083   2019.12

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    INTRODUCTION: Programmed cell death-1 (PD-1) inhibitors effectively treat NSCLC and prolong survival. Robust biomarkers for predicting clinical benefits of good response and long survival with anti-PD-1 therapy have yet to be identified; therefore, predictive biomarkers are needed to select patients with benefits. METHODS: We conducted a prospective study to explore whether serum antibody against NY-ESO-1 and/or XAGE1 cancer-testis antigens predicted primarily good clinical response and secondarily long survival with anti-PD-1 therapy for NSCLC. The serum antibody was detected by enzyme-linked immunosorbent assay, and tumor immune microenvironment and mutation burden were analyzed by immunohistochemistry and next-generation sequencing. RESULTS: In the discovery cohort (n = 13), six antibody-positive NSCLC cases responded to anti-PD-1 therapy (two complete and four partial responses), whereas seven antibody-negative NSCLC cases did not. Antibody positivity was associated with good response and survival, regardless of tumor programmed death ligand 1 (PD-L1) expression, mutation burden, and CD8+ T-cell infiltration. In the validation cohort (n = 75), 17 antibody-positive NSCLC cases responded well to anti-PD-1 therapy as compared with 58 negative NSCLC cases (objective response rate 65% versus 19%, p = 0.0006) and showed significantly prolonged progression-free survival and overall survival. Antibody titers highly correlated with tumor reduction rates. In the multivariate analysis, response biomarkers were tumor programmed death ligand 1 expression and antibody positivity, and only antibody positivity was a significantly better predictive biomarker of progression-free survival (hazard ratio = 0.4, p = 0.01) and overall survival (hazard ratio = 0.2, p = 0.004). CONCLUSIONS: Our results suggest that NY-ESO-1 and/or XAGE1 serum antibodies are useful biomarkers for predicting clinical benefits in anti-PD-1 therapy for NSCLC and probably for other cancers.

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  • 研究室主宰者の自戒 Invited

    二見 淳一郎

    生物工学会誌   97 ( 11 )   671 - 674   2019.11

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  • Upregulation of Mobility in Pancreatic Cancer Cells by Secreted S100A11 Through Activation of Surrounding Fibroblasts. Reviewed International journal

    Yosuke Mitsui, Nahoko Tomonobu, Masami Watanabe, Rie Kinoshita, I Wayan Sumardika, Chen Youyi, Hitoshi Murata, Ken-Ichi Yamamoto, Takuya Sadahira, Acosta Gonzalez Herik Rodrigo, Hitoshi Takamatsu, Kota Araki, Akira Yamauchi, Masahiro Yamamura, Hideyo Fujiwara, Yusuke Inoue, Junichiro Futami, Ken Saito, Hidekazu Iioka, Eisaku Kondo, Masahiro Nishibori, Shinichi Toyooka, Yasuhiko Yamamoto, Yasutomo Nasu, Masakiyo Sakaguchi

    Oncology research   27 ( 8 )   945 - 956   2019.8

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    S100A11, a member of the S100 family of proteins, is actively secreted from pancreatic ductal adenocarcinoma (PDAC) cells. However, the role of the extracellular S100A11 in PDAC progression remains unclear. In the present study, we investigated the extracellular role of S100A11 in crosstalking between PDAC cells and surrounding fibroblasts in PDAC progression. An abundant S100A11 secreted from pancreatic cancer cells stimulated neighboring fibroblasts through receptor for advanced glycation end products (RAGE) upon S100A11 binding and was followed by not only an enhanced cancer cell motility in vitro but also an increased number of the PDAC-derived circulating tumor cells (CTCs) in vivo. Mechanistic investigation of RAGE downstream in fibroblasts revealed a novel contribution of a mitogen-activated protein kinase kinase kinase (MAPKKK), tumor progression locus 2 (TPL2), which is required for positive regulation of PDAC cell motility through induction of cyclooxygenase 2 (COX2) and its catalyzed production of prostaglandin E2 (PGE2), a strong chemoattractive fatty acid. The extracellularly released PGE2 from fibroblasts was required for the rise in cellular migration as well as infiltration of their adjacent PDAC cells in a coculture setting. Taken together, our data reveal a novel role of the secretory S100A11 in PDAC disseminative progression through activation of surrounding fibroblasts triggered by the S100A11-RAGE-TPL2-COX2 pathway. The findings of this study will contribute to the establishment of a novel therapeutic antidote to PDACs that are difficult to treat by regulating cancer-associated fibroblasts (CAFs) through targeting the identified pathway.

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  • Newly developed anti-S100A8/A9 monoclonal antibody efficiently prevents lung tropic cancer metastasis. Reviewed International journal

    Rie Kinoshita, Hiroki Sato, Akira Yamauchi, Yuta Takahashi, Yusuke Inoue, I Wayan Sumardika, Youyi Chen, Nahoko Tomonobu, Kota Araki, Kazuhiko Shien, Shuta Tomida, Hidejiro Torigoe, Kei Namba, Eisuke Kurihara, Yusuke Ogoshi, Hitoshi Murata, Ken-Ichi Yamamoto, Junichiro Futami, Endy Widya Putranto, I Made Winarsa Ruma, Hiromasa Yamamoto, Junichi Soh, Toshihiko Hibino, Masahiro Nishibori, Eisaku Kondo, Shinichi Toyooka, Masakiyo Sakaguchi

    International journal of cancer   145 ( 2 )   569 - 575   2019.7

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    The metastatic dissemination of cancer cells to remote areas of the body is the most problematic aspect in cancer patients. Among cancers, melanomas are notoriously difficult to treat due to their significantly high metastatic potential even during early stages. Hence, the establishment of advanced therapeutic approaches to regulate metastasis is required to overcome the melanoma disease. An accumulating mass of evidence has indicated a critical role of extracellular S100A8/A9 in melanoma distant metastasis. Lung S100A8/A9 is induced by melanoma cells from distant organs and it attracts these cells to its enriched lung environment since melanoma cells possess several receptors that sense the S100A8/A9 ligand. We hence aimed to develop a neutralizing antibody against S100A8/A9 that would efficiently block melanoma lung metastasis. Our protocol provided us with one prominent antibody, Ab45 that efficiently suppressed not only S100A8/A9-mediated melanoma mobility but also lung tropic melanoma metastasis in a mouse model. This prompted us to make chimeric Ab45, a chimera antibody consisting of mouse Ab45-Fab and human IgG2-Fc. Chimeric Ab45 also showed significant inhibition of the lung metastasis of melanoma. From these results, we have high hopes that the newly produced antibody will become a potential biological tool to block melanoma metastasis in future clinical settings.

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  • Critical role of the MCAM-ETV4 axis triggered by extracellular S100A8/A9 in breast cancer aggressiveness. Reviewed International journal

    Youyi Chen, I Wayan Sumardika, Nahoko Tomonobu, Rie Kinoshita, Yusuke Inoue, Hidekazu Iioka, Yosuke Mitsui, Ken Saito, I Made Winarsa Ruma, Hiroki Sato, Akira Yamauchi, Hitoshi Murata, Ken-Ichi Yamamoto, Shuta Tomida, Kazuhiko Shien, Hiromasa Yamamoto, Junichi Soh, Junichiro Futami, Miyoko Kubo, Endy Widya Putranto, Takashi Murakami, Ming Liu, Toshihiko Hibino, Masahiro Nishibori, Eisaku Kondo, Shinichi Toyooka, Masakiyo Sakaguchi

    Neoplasia (New York, N.Y.)   21 ( 7 )   627 - 640   2019.7

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    Metastatic breast cancer is the leading cause of cancer-associated death in women. The progression of this fatal disease is associated with inflammatory responses that promote cancer cell growth and dissemination, eventually leading to a reduction of overall survival. However, the mechanism(s) of the inflammation-boosted cancer progression remains unclear. In this study, we found for the first time that an extracellular cytokine, S100A8/A9, accelerates breast cancer growth and metastasis upon binding to a cell surface receptor, melanoma cell adhesion molecule (MCAM). Our molecular analyses revealed an important role of ETS translocation variant 4 (ETV4), which is significantly activated in the region downstream of MCAM upon S100A8/A9 stimulation, in breast cancer progression in vitro as well as in vivo. The MCAM-mediated activation of ETV4 induced a mobile phenotype called epithelial-mesenchymal transition (EMT) in cells, since we found that ETV4 transcriptionally upregulates ZEB1, a strong EMT inducer, at a very high level. In contrast, downregulation of either MCAM or ETV4 repressed EMT, resulting in greatly weakened tumor growth and lung metastasis. Overall, our results revealed that ETV4 is a novel transcription factor regulated by the S100A8/A9-MCAM axis, which leads to EMT through ZEB1 and thereby to metastasis in breast cancer cells. Thus, therapeutic strategies based on our findings might improve patient outcomes.

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  • Melanoma cell adhesion molecule is the driving force behind the dissemination of melanoma upon S100A8/A9 binding in the original skin lesion. Reviewed International journal

    Youyi Chen, I Wayan Sumardika, Nahoko Tomonobu, I Made Winarsa Ruma, Rie Kinoshita, Eisaku Kondo, Yusuke Inoue, Hiroki Sato, Akira Yamauchi, Hitoshi Murata, Ken-Ichi Yamamoto, Shuta Tomida, Kazuhiko Shien, Hiromasa Yamamoto, Junichi Soh, Ming Liu, Junichiro Futami, Kaori Sasai, Hiroshi Katayama, Miyoko Kubo, Endy Widya Putranto, Toshihiko Hibino, Bei Sun, Masahiro Nishibori, Shinichi Toyooka, Masakiyo Sakaguchi

    Cancer letters   452   178 - 190   2019.6

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    Since metastasis accounts for the majority of cancer-associated deaths, studies on the mechanisms of metastasis are needed to establish innovative strategies for cancer treatment. We previously reported that melanoma cell adhesion molecule (MCAM) functions as a critical receptor for S100A8/A9, and binding of S100A8/A9 to MCAM results in the migration of melanoma cells to lung tissue. However, the critical role of MCAM in the original melanoma skin lesion is still not clear. In this study, we aimed to determine the importance of the S100A8/A9-MCAM axis in melanoma dissemination in a skin lesion as a critical early step for metastasis. Mechanistic studies revealed the downstream signaling of MCAM that signaled the induction of metastasis. S100A8/A9-MCAM binding activates mitogen-activated protein kinase kinase kinase 8 (MAP3K8), also termed TPL2, leading to strong activation of the transcription factor ETV4 and subsequent induction of matrix metalloproteinase-25 (MMP25), and finally to induction of melanoma lung tropic metastasis. Collectively, our results demonstrate a crucial role of the S100A8/A9-MCAM signaling axis in metastatic onset of melanoma cells and indicate that strategies targeting the identified pathway may be useful for the establishment of innovative anti-cancer therapies.

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  • Extracellular S100A11 Plays a Critical Role in Spread of the Fibroblast Population in Pancreatic Cancers. Reviewed International journal

    Hitoshi Takamatsu, Ken-Ichi Yamamoto, Nahoko Tomonobu, Hitoshi Murata, Yusuke Inoue, Akira Yamauchi, I Wayan Sumardika, Youyi Chen, Rie Kinoshita, Masahiro Yamamura, Hideyo Fujiwara, Yosuke Mitsui, Kota Araki, Junichiro Futami, Ken Saito, Hidekazu Iioka, I Made Winarsa Ruma, Endy Widya Putranto, Masahiro Nishibori, Eisaku Kondo, Yasuhiko Yamamoto, Shinichi Toyooka, Masakiyo Sakaguchi

    Oncology research   27 ( 6 )   713 - 727   2019.6

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    The fertile stroma in pancreatic ductal adenocarcinomas (PDACs) has been suspected to greatly contribute to PDAC progression. Since the main cell constituents of the stroma are fibroblasts, there is crosstalking(s) between PDAC cells and surrounding fibroblasts in the stroma, which induces a fibroblast proliferation burst. We have reported that several malignant cancer cells including PDAC cells secrete a pronounced level of S100A11, which in turn stimulates proliferation of cancer cells via the receptor for advanced glycation end products (RAGE) in an autocrine manner. Owing to the RAGE+ expression in fibroblasts, the extracellular abundant S100A11 will affect adjacent fibroblasts. In this study, we investigated the significance of the paracrine axis of S100A11-RAGE in fibroblasts for their proliferation activity. In in vitro settings, extracellular S100A11 induced upregulation of fibroblast proliferation. Our mechanistic studies revealed that the induction is through RAGE-MyD88-mTOR-p70 S6 kinase upon S100A11 stimulation. The paracrine effect on fibroblasts is linked mainly to triggering growth but not cellular motility. Thus, the identified pathway might become a potential therapeutic target to suppress PDAC progression through preventing PDAC-associated fibroblast proliferation.

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  • exSSSRs (extracellular S100 soil sensor receptors)-Fc fusion proteins work as prominent decoys to S100A8/A9-induced lung tropic cancer metastasis. Reviewed International journal

    Rie Kinoshita, Hiroki Sato, Akira Yamauchi, Yuta Takahashi, Yusuke Inoue, I Wayan Sumardika, Youyi Chen, Nahoko Tomonobu, Kota Araki, Kazuhiko Shien, Shuta Tomida, Hidejiro Torigoe, Kei Namba, Eisuke Kurihara, Yusuke Ogoshi, Hitoshi Murata, Ken-Ichi Yamamoto, Junichiro Futami, Endy Widya Putranto, I Made Winarsa Ruma, Hiromasa Yamamoto, Junichi Soh, Toshihiko Hibino, Masahiro Nishibori, Eisaku Kondo, Shinichi Toyooka, Masakiyo Sakaguchi

    International journal of cancer   144 ( 12 )   3138 - 3145   2019.6

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    Within the "seed and soil" theory of organ tropic cancer metastasis is a growing compilation of evidence that S100A8/A9 functions as a soil signal that attracts cancer cells to certain organs, which prove beneficial to their growth. S100A8/A9-sensing receptors including Toll-like receptor 4 (TLR4), advanced glycation end products (RAGE), and also important receptors we recently succeeded in identifying (EMMPRIN, NPTNβ, MCAM, and ALCAM) have the potential to become promising therapeutic targets. In our study, we prepared extracellular regions of these novel molecules and fused them to human IgG2-Fc to extend half-life expectancy, and we evaluated the anti-metastatic effects of the purified decoy proteins on metastatic cancer cells. The purified proteins markedly suppressed S100A8/A9-mediated lung tropic cancer metastasis. We hence expect that our novel biologics may become a prominent medicine to prevent cancer metastasis in clinical settings through cutting the linkage between "seed and soil".

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  • Neuroplastin-β mediates S100A8/A9-induced lung cancer disseminative progression. Reviewed International journal

    I Wayan Sumardika, Youyi Chen, Nahoko Tomonobu, Rie Kinoshita, I Made Winarsa Ruma, Hiroki Sato, Eisaku Kondo, Yusuke Inoue, Akira Yamauchi, Hitoshi Murata, Ken-Ichi Yamamoto, Shuta Tomida, Kazuhiko Shien, Hiromasa Yamamoto, Junichi Soh, Junichiro Futami, Endy Widya Putranto, Toshihiko Hibino, Masahiro Nishibori, Shinichi Toyooka, Masakiyo Sakaguchi

    Molecular carcinogenesis   58 ( 6 )   980 - 995   2019.6

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    Compiling evidence indicates an unusual role of extracellular S100A8/A9 in cancer metastasis. S100A8/A9 secreted from either cancer cells or normal cells including epithelial and inflammatory cells stimulates cancer cells through S100A8/A9 sensor receptors in an autocrine or paracrine manner, leading to cancer cell metastatic progression. We previously reported a novel S100A8/A9 receptor, neuroplastin-β (NPTNβ), which plays a critical role in atopic dermatitis when it is highly activated in keratinocytes by an excess amount of extracellular S100A8/A9 in the inflammatory skin lesion. Interestingly, our expression profiling of NPTNβ showed significantly high expression levels in lung cancer cell lines in a consistent manner. We hence aimed to determine the significance of NPTNβ as an S100A8/A9 receptor in lung cancer. Our results showed that NPTNβ has strong ability to induce cancer-related cellular events, including anchorage-independent growth, motility and invasiveness, in lung cancer cells in response to extracellular S100A8/A9, eventually leading to the expression of a cancer disseminative phenotype in lung tissue in vivo. Mechanistic investigation revealed that binding of S100A8/A9 to NPTNβ mediates activation of NFIA and NFIB and following SPDEF transcription factors through orchestrated upstream signals from TRAF2 and RAS, which is linked to anchorage-independent growth, motility and invasiveness. Overall, our results indicate the importance of the S100A8/A9-NPTNβ axis in lung cancer disseminative progression and reveal a pivotal role of its newly identified downstream signaling, TRAF2/RAS-NFIA/NFIB-SPDEF, in linking to the aggressive development of lung cancers.

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  • β-1,3-Galactosyl-O-Glycosyl-Glycoprotein β-1,6-N-Acetylglucosaminyltransferase 3 Increases MCAM Stability, Which Enhances S100A8/A9-Mediated Cancer Motility. Reviewed International journal

    I Wayan Sumardika, Chen Youyi, Eisaku Kondo, Yusuke Inoue, I Made Winarsa Ruma, Hitoshi Murata, Rie Kinoshita, Ken-Ichi Yamamoto, Shuta Tomida, Kazuhiko Shien, Hiroki Sato, Akira Yamauchi, Junichiro Futami, Endy Widya Putranto, Toshihiko Hibino, Shinichi Toyooka, Masahiro Nishibori, Masakiyo Sakaguchi

    Oncology research   26 ( 3 )   431 - 444   2018.4

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    We previously identified novel S100A8/A9 receptors, extracellular matrix metalloproteinase inducer (EMMPRIN), melanoma cell adhesion molecule (MCAM), activated leukocyte cell adhesion molecule (ALCAM), and neuroplastin (NPTN) β, that are critically involved in S100A8/A9-mediated cancer metastasis and inflammation when expressed at high levels. However, little is known about the presence of any cancer-specific mechanism(s) that modifies these receptors, further inducing upregulation at protein levels without any transcriptional regulation. Expression levels of glycosyltransferase-encoding genes were examined by a PCR-based profiling array followed by confirmation with quantitative real-time PCR. Cell migration and invasion were assessed using a Boyden chamber. Western blotting was used to examine the protein level, and the RNA level was examined by Northern blotting. Immunohistochemistry was used to examine the expression pattern of β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase 3 (GCNT3) and MCAM in melanoma tissue. We found that GCNT3 is overexpressed in highly metastatic melanomas. Silencing and functional inhibition of GCNT3 greatly suppressed migration and invasion of melanoma cells, resulting in the loss of S100A8/A9 responsiveness. Among the novel S100A8/A9 receptors, GCNT3 favorably glycosylates the MCAM receptor, extending its half-life and leading to further elevation of S100A8/A9-mediated cellular motility in melanoma cells. GCNT3 expression is positively correlated to MCAM expression in patients with high-grade melanomas. Collectively, our results showed that GCNT3 is an upstream regulator of MCAM protein and indicate the possibility of a potential molecular target in melanoma therapeutics through abrogation of the S100A8/A9-MCAM axis.

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  • β-1,3-Galactosyl-

    Sumardika, I. W., Youyi, C., Kondo, E., Inoue, Y., Ruma, I. M. W., Murata, H., Kinoshita, R., Yamamoto, K. I., Tomida, S., Shien, K., Sato, H., Yamauchi, A., Futami, J., Putranto, E. W., Hibino, T., Toyooka, S., Nishibori, M., Sakaguchi, M.

    Oncol Res   26 ( 3 )   2018

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  • Mitochondrial determinants of mammalian longevity Reviewed

    Yasuhiro Kitazoe, Masami Hasegawa, Masashi Tanaka, Midori Futami, Junichiro Futami

    OPEN BIOLOGY   7 ( 10 )   2017.10

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    DOI： 10.1098/rsob.170083

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  • Evaluation of irreversible protein thermal inactivation caused by breakage of disulphide bonds using methanethiosulphonate Reviewed

    Junichiro Futami, Ai Miyamoto, Atsushi Hagimoto, Shigeyuki Suzuki, Midori Futami, Hiroko Tada

    SCIENTIFIC REPORTS   7 ( 1 )   12471 - 3275   2017.9

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  • Robust cancer-specific gene expression by a novel cassette with hTERT and CMV promoter elements Reviewed

    Masakiyo Sakaguchi, Takuya Sadahira, Hideo Ueki, Rie Kinoshita, Hitoshi Murata, Ken-Ichi Yamamoto, Junichiro Futami, Yasutomo Nasu, Kazuhiko Ochiai, Hiromi Kumon, Nam-Ho Huh, Masami Watanabe

    ONCOLOGY REPORTS   38 ( 2 )   1108 - 1114   2017.8

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  • Expression of tumor suppressor REIC/Dkk-3 by a newly improved adenovirus vector with insertion of a hTERT promoter at the 3'-side of the transgene Reviewed

    Endy Widya Putranto, Rie Kinoshita, Masami Watanabe, Takuya Sadahira, Hitoshi Murata, Ken-Ichi Yamamoto, Junichiro Futami, Ken Kataoka, Yusuke Inoue, I. Made Winarsa Ruma, I. Wayan Sumardika, Chen Youyi, Miyoko Kubo, Yoshihiko Sakaguchi, Kenji Saito, Yasutomo Nasu, Hiromi Kumon, Nam-Ho Huh, Masakiyo Sakaguchi

    ONCOLOGY LETTERS   14 ( 1 )   1041 - 1048   2017.7

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    DOI： 10.3892/ol.2017.6201

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  • Enhanced in-cell folding of reversibly cationized transcription factor using amphipathic peptide Reviewed

    Midori Futami, Tomoki Nakano, Mayu Yasunaga, Masahiro Makihara, Takashi Asama, Yoshihisa Hagihara, Yoshihiro Nakajima, Junichiro Futami

    JOURNAL OF BIOSCIENCE AND BIOENGINEERING   123 ( 4 )   419 - 424   2017.4

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  • タンパク質を巻き戻すコツと原理

    二見淳一郎

    生物工学会誌   95 ( 6 )   328 - 332   2017

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  • ß-1,3-galactosyl-O-glycosyl-glycoprotein ß-1,6-N-acetylglucosaminyltransferase 3 Increases MCAM Stability, Which Enhances S100A8/A9-Mediated Cancer Motility. Reviewed

    Sumardika IW, Youyi C, Kondo E, Inoue Y, Ruma IMW, Murata H, Kinoshita R, Yamamoto KI, Tomida S, Shien K, Satoh H, Yamauchi A, Futami J, Putranto EW, Hibino T, Toyooka S, Nishibori M, Sakaguchi M

    Oncol Res   2017

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  • Active Secretion of Dimerized S100A11 Induced by the Peroxisome in Mesothelioma Cells. Reviewed International journal

    Satomi Saho, Hiroki Satoh, Eisaku Kondo, Yusuke Inoue, Akira Yamauchi, Hitoshi Murata, Rie Kinoshita, Ken-Ichi Yamamoto, Junichiro Futami, Endy Widya Putranto, I Made Winarsa Ruma, I Wayan Sumardika, Chen Youyi, Ken Suzawa, Hiromasa Yamamoto, Junichi Soh, Shuta Tomida, Yoshihiko Sakaguchi, Ken Saito, Hidekazu Iioka, Nam-Ho Huh, Shinichi Toyooka, Masakiyo Sakaguchi

    Cancer microenvironment : official journal of the International Cancer Microenvironment Society   9 ( 2-3 )   93 - 105   2016.12

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    S100A11, a small Ca2+ binding protein, acts extracellularly as a mediator of cancer progression. That raises the question of how a protein that lacks the classical secretory signal is able to be secreted outside cells without being damaged. Some insights into this question have been obtained, and there has been accumulating evidence indicating a pivotal role of a non-classical vesicle-mediated pathway using lysosomes or peroxisomes for the protein secretion. To obtain a more precise insight into the secretory mechanism of S100A11, we first screened representative cancer cells exhibiting significantly active secretion of S100A11. From the results of profiling, we turned our attention to aggressive cancer mesothelioma cells. In mesothelioma cells, we found that abundant dimeric S100A11 was produced selectively in the peroxisome after transportation of monomeric S100A11 through an interaction with PEX14, a peroxisome membrane protein, resulting in peroxisomal secretion of dimerized S100A11. In an extracellular environment in vitro, dimerized S100A11 promoted mesothelial cell invasion indirectly with the help of fibroblast cells. Overall, the results indicate that the peroxisome functions as an essential vesicle for the production of dimerized S100A11 and the subsequent secretion of the protein from mesothelioma cells and that peroxisome-mediated secretion of dimerized S100A11 might play a critical role in mesothelioma progression in a tumor microenvironment.

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  • MCAM, as a novel receptor for S100A8/A9, mediates progression of malignant melanoma through prominent activation of NF-kappa B and ROS formation upon ligand binding Reviewed

    I. Made Winarsa Ruma, Endy Widya Putranto, Eisaku Kondo, Hitoshi Murata, Masami Watanabe, Peng Huang, Rie Kinoshita, Junichiro Futami, Yusuke Inoue, Akira Yamauchi, I. Wayan Sumardika, Chen Youyi, Ken-Ichi Yamamoto, Yasutomo Nasu, Masahiro Nishibori, Toshihiko Hibino, Masakiyo Sakaguchi

    CLINICAL & EXPERIMENTAL METASTASIS   33 ( 6 )   609 - 627   2016.8

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    DOI： 10.1007/s10585-016-9801-2

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  • An efficient method for the preparation of preferentially heterodimerized recombinant S100A8/A9 coexpressed in Escherichia coli Reviewed

    Junichiro Futami, Yuki Atago, Akari Azuma, Endy Widya Putranto, Rie Kinoshita, Hitoshi Murata, Masakiyo Sakaguchi

    Biochemistry and Biophysics Reports   6   94 - 100   2016.7

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    DOI： 10.1016/j.bbrep.2016.03.009

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  • Development of Antibody Detection System to Evaluate Activation of Anti-Tumor Immune Response Invited

    FUTAMI Junichiro

    33 ( 5 )   19 - 24   2016.5

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  • Identification of novel extracellular protein for PCB/biphenyl metabolism in Rhodococcus jostii RHA1 Reviewed

    Yuki Atago, Jun Shimodaira, Naoto Araki, Nor'azizi Bin Othman, Zuriati Zakaria, Masao Fukuda, Junichiro Futami, Hirofumi Hara

    BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY   80 ( 5 )   1012 - 1019   2016.5

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    DOI： 10.1080/09168451.2015.1127134

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  • 硬い肉をやわらかくする

    二見淳一郎

    Fuji Sankei Business i. よくわかるバイオ（第26回）   2016

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  • Sensitive Multiplexed Quantitative Analysis of Autoantibodies to Cancer Antigens with Chemically S-Cationized Full-Length and Water-Soluble Denatured Proteins Reviewed

    Junichiro Futami, Hidenori Nonomura, Momoko Kido, Naomi Niidoi, Nao Fujieda, Akihiro Hosoi, Kana Fujita, Komako Mandai, Yuki Atago, Rie Kinoshita, Tomoko Honjo, Hirokazu Matsushita, Akiko Uenaka, Eiichi Nakayama, Kazuhiro Kakimi

    BIOCONJUGATE CHEMISTRY   26 ( 10 )   2076 - 2084   2015.10

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    DOI： 10.1021/acs.bioconjchem.5b00328

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  • The cysteine-rich core domain of REIC/Dkk-3 is critical for its effect on monocyte differentiation and tumor regression Reviewed

    Rie Kinoshita, Masami Watanabe, Peng Huang, Shun-Ai Li, Masakiyo Sakaguchi, Hiromi Kumon, Junichiro Futami

    ONCOLOGY REPORTS   33 ( 6 )   2908 - 2914   2015.6

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    DOI： 10.3892/or.2015.3885

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  • Advanced Utilization of Denatured Protein by Cationization Techniques Invited Reviewed

    FUTAMI Junichiro

    KAGAKU TO SEIBUTSU   53 ( 4 )   245 - 251   2015.4

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    Language：Japanese   Publishing type：Research paper (scientific journal)   Publisher：Japan Society for Bioscience, Biotechnology, and Agrochemistry  

    DOI： 10.1271/kagakutoseibutsu.53.245

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    Other Link： https://jlc.jst.go.jp/DN/JLC/20009210033?from=CiNii

  • A vaccine strategy with multiple prostatic acid phosphatase-fused cytokines for prostate cancer treatment Reviewed

    Kei Fujio, Masami Watanabe, Hideo Ueki, Shun-Ai Li, Rie Kinoshita, Kazuhiko Ochiai, Junichiro Futami, Toyohiko Watanabe, Yasutomo Nasu, Hiromi Kumon

    ONCOLOGY REPORTS   33 ( 4 )   1585 - 1592   2015.4

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    DOI： 10.3892/or.2015.3770

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  • Denatured Mammalian Protein Mixtures Exhibit Unusually High Solubility in Nucleic Acid-Free Pure Water Reviewed

    Junichiro Futami, Haruna Fujiyama, Rie Kinoshita, Hidenori Nonomura, Tomoko Honjo, Hiroko Tada, Hirokazu Matsushita, Yoshito Abe, Kazuhiro Kakimi

    PLOS ONE   9 ( 11 )   e113295   2014.11

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    DOI： 10.1371/journal.pone.0113295

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  • DNAX-activating Protein 10 (DAP10) Membrane Adaptor Associates with Receptor for Advanced Glycation End Products (RAGE) and Modulates the RAGE-triggered Signaling Pathway in Human Keratinocytes Reviewed

    Masakiyo Sakaguchi, Hitoshi Murata, Yumi Aoyama, Toshihiko Hibino, Endy Widya Putranto, I. Made Winarsa Ruma, Yusuke Inoue, Yoshihiko Sakaguchi, Ken-ichi Yamamoto, Rie Kinoshita, Junichiro Futami, Ken Kataoka, Keiji Iwatsuki, Nam-ho Huh

    JOURNAL OF BIOLOGICAL CHEMISTRY   289 ( 34 )   23389 - 23402   2014.8

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    DOI： 10.1074/jbc.M114.573071

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  • Dramatic Increase in Expression of a Transgene by Insertion of Promoters Downstream of the Cargo Gene Reviewed

    Masakiyo Sakaguchi, Masami Watanabe, Rie Kinoshita, Haruki Kaku, Hideo Ueki, Junichiro Futami, Hitoshi Murata, Yusuke Inoue, Shun-Ai Li, Peng Huang, Endy Widya Putranto, I. Made Winarsa Ruma, Yasutomo Nasu, Hiromi Kumon, Nam-ho Huh

    MOLECULAR BIOTECHNOLOGY   56 ( 7 )   621 - 630   2014.7

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    DOI： 10.1007/s12033-014-9738-0

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  • A novel gene expression system strongly enhances the anticancer effects of a REIC/Dkk-3-encoding adenoviral vector Reviewed

    Masami Watanabe, Masakiyo Sakaguchi, Rie Kinoshita, Haruki Kaku, Yuichi Ariyoshi, Hideo Ueki, Ryuta Tanimoto, Shin Ebara, Kazuhiko Ochiai, Junichiro Futami, Shun-Ai Li, Peng Huang, Yasutomo Nasu, Nam-Ho Huh, Hiromi Kumon

    ONCOLOGY REPORTS   31 ( 3 )   1089 - 1095   2014.3

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    DOI： 10.3892/or.2013.2958

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  • Inhibition of RAGE signaling through the intracellular delivery of inhibitor peptides by PEI cationization Reviewed

    Endy Widya Putranto, Hitoshi Murata, Ken-Ichi Yamamoto, Ken Kataoka, Hidenori Yamada, Jun-Ichiro Futami, Masakiyo Sakaguchi, Nam-Ho Huh

    INTERNATIONAL JOURNAL OF MOLECULAR MEDICINE   32 ( 4 )   938 - 944   2013.10

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    DOI： 10.3892/ijmm.2013.1467

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  • 【特集】タンパク質生産と溶解性制御：タンパク質の溶解性を操るタンパク質カチオン化技術 Invited

    二見 淳一郎

    バイオインダストリー   15 - 21   2013.7

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  • Protein cationization techniques for artificial control of physical property of protein and their medical applications Reviewed

    Junichiro Futami

    Seikagaku   85 ( 1 )   21 - 25   2013

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  • Uniformly Cationized Protein Efficiently Reaches the Cytosol of Mammalian Cells Reviewed

    Midori Futami, Yasuyoshi Watanabe, Takashi Asama, Hitoshi Murata, Hiroko Tada, Megumi Kosaka, Hidenori Yamada, Junichiro Futami

    BIOCONJUGATE CHEMISTRY   23 ( 10 )   2025 - 2031   2012.10

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  • A New Cytosolic Pathway from a Parkinson Disease-associated Kinase, BRPK/PINK1 ACTIVATION OF AKT VIA MTORC2 Reviewed

    Hitoshi Murata, Masakiyo Sakaguchi, Yu Jin, Yoshihiko Sakaguchi, Jun-ichiro Futami, Hidenori Yamada, Ken Kataoka, Nam-ho Huh

    JOURNAL OF BIOLOGICAL CHEMISTRY   286 ( 9 )   7182 - 7189   2011.3

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  • Polyethylenimine-cationized beta-catenin protein transduction activates the Wnt canonical signaling pathway more effectively than cationic lipid-based transduction Reviewed

    Midori Kitazoe, Junichiro Futami, Mitsuo Nishikawa, Hidenori Yamada, Yoshitake Maeda

    BIOTECHNOLOGY JOURNAL   5 ( 4 )   385 - 392   2010.4

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    DOI： 10.1002/biot.200900132

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  • タンパク質カチオン化技術の工学的応用 Invited

    二見 淳一郎

    ケミカルエンジニアリング   55 ( 3 )   2010.3

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  • Efficient cross-presentation of soluble exogenous antigens introduced into dendritic cells using a weak-based amphiphilic peptide Reviewed

    Nobuhito Ikeuchi, Junichiro Futami, Akihiro Hosoi, Shuichi Noji, Makoto Kurachi, Satoshi Ueha, Shin-ichiro Fujii, Hidenori Yamada, Koji Matsushima, Fuminori Moriyasu, Kazuhiro Kakimi

    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS   392 ( 2 )   217 - 222   2010.2

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    DOI： 10.1016/j.bbrc.2010.01.019

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  • Immunological aspects of REIC/Dkk-3 in monocyte differentiation and tumor regression Reviewed

    Masami Watanabe, Yuji Kashiwakura, Peng Huang, Kazuhiko Ochiai, Junichiro Futami, Shun-Ai Li, Munenori Takaoka, Yasutomo Nasu, Masakiyo Sakaguchi, Nam-Ho Huh, Hiromi Kumon

    INTERNATIONAL JOURNAL OF ONCOLOGY   34 ( 3 )   657 - 663   2009.3

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  • Intracellular delivery of glutathione S-transferase-fused proteins into mammalian cells by polyethylenimine-glutathione conjugates Reviewed

    Hitoshi Murata, Junichiro Futami, Midori Kitazoe, Takayuki Yonehara, Hidetaka Nakanishi, Megumi Kosaka, Hiroko Tada, Masakiyo Sakaguchi, Yasuyuki Yagi, Masaharu Seno, Nam-ho Huh, Hidenori Yamada

    JOURNAL OF BIOCHEMISTRY   144 ( 4 )   447 - 455   2008.10

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    DOI： 10.1093/jb/mvn087

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  • Design of cytotoxic ribonucleases by cationization to enhance intracellular protein delivery Reviewed

    Junichiro Futami, Hidenori Yamada

    CURRENT PHARMACEUTICAL BIOTECHNOLOGY   9 ( 3 )   180 - 184   2008.6

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    DOI： 10.2174/138920108784567326

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  • Transient cell proliferation with polyethylenimine-cationized N-terminal domain of simian virus 40 large T-antigen Reviewed

    Hitoshi Murata, Junichiro Futami, Midori Kitazoe, Megumi Kosaka, Hiroko Tada, Masaharu Seno, Hidenori Yamada

    JOURNAL OF BIOSCIENCE AND BIOENGINEERING   105 ( 1 )   34 - 38   2008.1

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  • S100A11, an dual mediator for growth regulation of human keratinocytes Reviewed

    Masakiyo Sakaguchi, Hiroyuki Sonegawa, Hitoshi Murata, Midori Kitazoe, Jun-ichiro Futami, Ken Kataoka, Hidenori Yamada, Nam-ho Huh

    MOLECULAR BIOLOGY OF THE CELL   19 ( 1 )   78 - 85   2008.1

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    DOI： 10.1091/mbc.E07-07-0682

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  • Truncation of annexin A1 is a regulatory lever for linking epidermal growth factor signaling with cytosolic phospholipase A2 in normal and malignant squamous epithelial cells Reviewed

    Masakiyo Sakaguchi, Hitoshi Murata, Hiroyuki Sonegawa, Yoshihiko Sakaguchi, Jun-ichiro Futami, Midori Kitazoe, Hidenori Yamada, Nam-ho Huh

    JOURNAL OF BIOLOGICAL CHEMISTRY   282 ( 49 )   35679 - 35686   2007.12

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  • 'Crystal lattice engineering,' an approach to engineer protein crystal contacts by creating intermolecular symmetry: Crystallization and structure determination of a mutant human RNase 1 with a hydrophobic interface of leucines Reviewed

    Hidenori Yamada, Taro Tamada, Megumi Kosaka, Kohei Miyata, Shinya Fujiki, Masaru Tano, Masayuki Moriya, Mamoru Yamanishi, Eijiro Honjo, Hiroko Tada, Takeshi Ino, Hiroshi Yamaguchi, Junichiro Futami, Masaharu Seno, Takashi Nomoto, Tomoko Hirata, Motonobu Yoshimura, Ryota Kuroki

    PROTEIN SCIENCE   16 ( 7 )   1389 - 1397   2007.7

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    DOI： 10.1110/ps.072851407

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  • Exploiting protein cationization techniques in future drug development Reviewed

    Junichiro Futami, Midori Kitazoe, Hiroshi Murata, Hidenori Yamada

    EXPERT OPINION ON DRUG DISCOVERY   2 ( 2 )   261 - 269   2007.2

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    DOI： 10.1517/17460441.2.2.261

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  • Leucyl/phenylalanyl-tRNA-protein transferase-mediated chemoenzymatic coupling of N-terminal arg/lys units in posttranslationally processed proteins with non-natural amino acids Reviewed

    Masumi Taki, Atsushi Kuno, Shinsuke Matoba, Yuki Kobayashi, Junichiro Futami, Hiroshi Murakami, Hiroaki Suga, Kazunari Taira, Tsunemi Hasegawa, Masahiko Sisido

    CHEMBIOCHEM   7 ( 11 )   1676 - +   2006.11

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    DOI： 10.1002/cbic.200600181

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  • Denatured and reversibly cationized p53 readily enters cells and simultaneously folds to the functional protein in the cells Reviewed

    H Murata, M Sakaguchi, J Futami, M Kitazoe, T Maeda, H Doura, M Kosaka, H Tada, M Seno, N Huh, H Yamada

    BIOCHEMISTRY   45 ( 19 )   6124 - 6132   2006.5

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  • Mechanisms of the growth-inhibitory effect of the RNase-EGF fused protein against EGFR-overexpressing cells Reviewed

    S Hoshimoto, M Ueda, H Jinno, M Kitajima, J Futami, M Seno

    ANTICANCER RESEARCH   26 ( 2A )   857 - 863   2006.3

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  • In vivo protein transduction to the CNS Reviewed

    LT Loftus, HF Li, AJ Gray, C Hirata-Fukae, BA Stoica, J Futami, H Yamada, PS Aisen, Y Matsuoka

    NEUROSCIENCE   139 ( 3 )   1061 - 1067   2006

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    DOI： 10.1016/j.neuroscience.2006.01.041

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  • 1P136 Crystal Lattice Engineering : Crystallization and Structure Determination of Human RNase 1 Mutants with a Hydrophobic Interface of Leucines(4. Protein engineering,Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)

    Yamada Hidenori, Miyata Kohei, Fujiki Shinya, Tano Masaru, Moriya Masayuki, Ino Takeshi, Kosaka Megumi, Tada Hiroko, Futami Junichiro, Yamanishi Mamoru, Yamaguchi Hiroshi, Seno Masaharu, Nomoto Takashi, Hirata Tomoko, Yoshimura Motonobu, Honjo Eijiro, Tamada Taro, Kuroki Ryota

    Seibutsu Butsuri   46 ( 2 )   S180   2006

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    DOI： 10.2142/biophys.46.S180_4

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  • Visceral adipose tissue-derived serine protease inhibitor: A unique insulin-sensitizing adipocytokine in obesity Reviewed

    K Hida, J Wada, J Eguchi, H Zhang, M Baba, A Seida, L Hashimoto, T Okada, A Yasuhara, A Nakatsuka, K Shikata, S Hourai, J Futami, E Watanabe, Y Matsuki, R Hiramatsu, S Akagi, H Makino, YS Kanwar

    PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA   102 ( 30 )   10610 - 10615   2005.7

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    DOI： 10.1073/pnas.0504703102

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  • Protein transduction assisted by polyethylenimine-cationized carrier proteins Reviewed

    M Kitazoe, H Murata, J Futami, T Maeda, M Sakaguchi, M Miyazaki, M Kosaka, H Tada, M Seno, N Huh, M Namba, M Nishikawa, Y Maeda, H Yamada

    JOURNAL OF BIOCHEMISTRY   137 ( 6 )   693 - 701   2005.6

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    DOI： 10.1093/jb/mvi081

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  • Intracellular delivery of proteins into mammalian living cells by polyethylenimine-cationization Reviewed

    J Futami, M Kitazoe, T Maeda, E Nukui, M Sakaguchi, J Kosaka, M Miyazaki, M Kosaka, H Tada, M Seno, Y Sasaki, NH Huh, M Namba, H Yamada

    JOURNAL OF BIOSCIENCE AND BIOENGINEERING   99 ( 2 )   95 - 103   2005.2

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  • Targeted disruption of transcriptional regulatory function of p53 by a novel efficient method for introducing a decoy oligonucleotide into nuclei Reviewed

    M Sakaguchi, T Nukui, H Sonegawa, H Murata, J Futami, H Yamada, N Huh

    NUCLEIC ACIDS RESEARCH   33 ( 9 )   e88   2005

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    DOI： 10.1093/nar/gni088

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  • Protein Transduction using Cationic Polymers Invited

    FUTAMI Junichiro, YAMADA Hdenori

    21 ( 6 )   20 - 27   2004.6

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  • Insertional-fusion of basic fibroblast growth factor endowed ribonuclease 1 with enhanced cytotoxicity by steric blockade of inhibitor interaction Reviewed

    H Tada, M Onizuka, K Muraki, W Masuzawa, J Futami, M Kosaka, M Seno, H Yamada

    FEBS LETTERS   568 ( 1-3 )   39 - 43   2004.6

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    DOI： 10.1016/j.febslet.2004.05.007

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  • Construction and characterization of RNase-based targeted therapeutics Reviewed

    Newton, D. L., Futami, J., Ruby, D., Rybak, S. M.

    Methods Mol Biol   207   283 - 304   2003

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  • RNase 3 (ECP) is an extraordinarily stable protein among human pancreatic-type RNases Reviewed

    T Maeda, K Mahara, M Kitazoe, J Futami, A Takidani, M Kosaka, H Tada, M Seno, H Yamada

    JOURNAL OF BIOCHEMISTRY   132 ( 5 )   737 - 742   2002.11

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  • Optimum modification for the highest cytotoxicity of cationized ribonuclease Reviewed

    J Futami, E Nukui, T Maeda, M Kosaka, H Tada, M Seno, H Yamada

    JOURNAL OF BIOCHEMISTRY   132 ( 2 )   223 - 228   2002.8

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  • EGFRを分子標的としたRNase-EGF recombinantタンパクの殺細胞効果

    星本 相淳, 上田 政和, 神野 浩光, 相浦 浩一, 渡辺 靖夫, 北島 政樹, 二見 淳一郎, 妹尾 昌治

    日本外科学会雑誌   103 ( 臨増 )   532 - 532   2002.3

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  • Preparation of potent cytotoxic ribonucleases by cationization: Enhanced cellular uptake and decreased interaction with ribonuclease inhibitor by chemical modification of carboxyl groups Reviewed

    J Futami, T Maeda, M Kitazoe, E Nukui, H Tada, M Seno, M Kosaka, H Yamada

    BIOCHEMISTRY   40 ( 25 )   7518 - 7524   2001.6

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    DOI： 10.1021/bi010248g

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  • Three-dimensional structure of human RNase 1 Delta N7 at 1.9 angstrom resolution Reviewed

    J Pous, G Mallorqui-Fernandez, R Peracaula, SS Terzyan, J Futami, H Tada, H Yamada, M Seno, R de Llorens, FX Gomis-Ruth, M Coll

    ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY   57   498 - 505   2001.4

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    DOI： 10.1107/S0907444901001147

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  • Stabilization of human RNase 1 by introduction of a disulfide bond between residues 4 and 118 Reviewed

    J Futami, H Tada, M Seno, S Ishikami, H Yamada

    JOURNAL OF BIOCHEMISTRY   128 ( 2 )   245 - 250   2000.8

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  • Convenient and efficient in vitro folding of disulfide-containing globular protein from crude bacterial inclusion bodies Reviewed

    J Futami, Y Tsushima, H Tada, M Seno, H Yamada

    JOURNAL OF BIOCHEMISTRY   127 ( 3 )   435 - 441   2000.3

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  • Inhibition of cell growth by a fused protein of human ribonuclease 1 and human basic fibroblast growth factor Reviewed

    J Futami, M Seno, M Ueda, H Tada, H Yamada

    PROTEIN ENGINEERING   12 ( 11 )   1013 - 1019   1999.11

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    Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)  

    DOI： 10.1093/protein/12.11.1013

    Web of Science

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  • Molecular targeting for epidermal growth factor receptor expressed on breast cancer cells by human fusion protein Reviewed

    Masakazu Ueda, Kyriakos Psarras, Hiromitsu Jinno, Tadashi Ikeda, Kohji Enomoto, Masaki Kitajima, Junichiro Futami, Hidenori Yamada, Masaharu Seno

    Breast Cancer   4 ( 4 )   253 - 255   1997.12

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    DOI： 10.1007/BF02966516

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  • Tissue-specific expression of pancreatic-type RNases and RNase inhibitor in humans Reviewed

    J Futami, Y Tsushima, Y Murato, H Tada, J Sasaki, M Seno, H Yamada

    DNA AND CELL BIOLOGY   16 ( 4 )   413 - 419   1997.4

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    DOI： 10.1089/dna.1997.16.413

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  • RECOMBINANT HUMAN PANCREATIC RIBONUCLEASE PRODUCED IN ESCHERICHIA-COLI - IMPORTANCE OF THE AMINO-TERMINAL SEQUENCE Reviewed

    J FUTAMI, M SENO, M KOSAKA, H TADA, S SENO, H YAMADA

    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS   216 ( 1 )   406 - 413   1995.11

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    DOI： 10.1006/bbrc.1995.2638

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  • MOLECULAR-CLONING AND EXPRESSION OF HUMAN RIBONUCLEASE-4 CDNA

    M SENO, J FUTAMI, Y TSUSHIMA, K AKUTAGAWA, M KOSAKA, H TADA, H YAMADA

    BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION   1261 ( 3 )   424 - 426   1995.4

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  • NUCLEOTIDE-SEQUENCE ENCODING HUMAN PANCREATIC RIBONUCLEASE Reviewed

    M SENO, J FUTAMI, M KOSAKA, S SENO, H YAMADA

    BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION   1218 ( 3 )   466 - 468   1994.8

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Books

  • 酵素利用技術体系 3-1表面修飾による酵素機能の向上

    NTS  2010 

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  • ゲノミクス・プロテオミクスの新展開:生物情報の解析と応用

    2004 

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MISC

  • Linear epitope-specific autoantibody discovery method and improved autoantibody assaying system

    伊達実鈴, 塩川つぐみ, 多田宏子, 森壮流, 本莊知子, 宮本愛, 二見淳一郎

    日本生物工学会大会講演要旨集   76th   2024

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  • S100A8/A9 promotes bladder cancer progression by the TIRAP-TPL2 signaling upon the binding with TLR4

    友信奈保子, 木下理恵, 合原勇馬, KOMALASARI Yoni, 二見淳一郎, 山内明, 近藤英作, 豊岡伸一, 阪口政清

    日本癌学会学術総会抄録集(Web)   82nd   2023

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  • 代替2次元分離法の開発による自己抗体バイオマーカー探索の効率化

    益井実鈴, 塩川つぐみ, 多田宏子, 本莊知子, 宮本愛, 二見淳一郎

    日本蛋白質科学会年会プログラム・要旨集   23rd (CD-ROM)   2023

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  • がん免疫サイクルを評価する自己抗体バイオマーカー群の精密測定法の開発

    宮本 愛, 本莊 知子, 益井 実鈴, 木下 理恵, 公文 裕巳, 垣見 和宏, 二見 淳一郎

    日本がん免疫学会総会プログラム・抄録集   26回   102 - 102   2022.6

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  • Binding of REIC/Dkk-3 to its receptor suppresses PD-L1 expression in triple negative breast cancer

    吉澤智香子, 合原勇馬, 友信奈保子, 木下理恵, 二見淳一郎, 村田等, 山本健一, 阪口政清

    日本分子生物学会年会プログラム・要旨集(Web)   45th   2022

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  • Optimization of autoantibody biomarker search by developing an alternative two-dimensional separation method

    益井実鈴, 塩川つぐみ, 多田宏子, 宮本愛, 二見淳一郎

    日本生物工学会大会講演要旨集   74th   2022

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  • A novel two-dimensional electrophoresis technique for the screening of autoantibody

    益井実鈴, 塩川つぐみ, 多田宏子, 二見淳一郎

    日本生物工学会大会講演要旨集   73rd   2021

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  • 部位特異ビオチン化とrefolding assayを組み合わせたneo-antigenスクリーニング法の開発

    峯苫 智晴, 垣見 和宏, 二見 淳一郎

    日本生物工学会大会講演要旨集   2019年   230 - 230   2019.8

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  • Melanoma cell adhesion molecule (MCAM) induces dissemination of melanoma upon S100A8/A9 binding

    友信奈保子, 木下理恵, 近藤英作, 山内明, 二見淳一郎, 豊岡伸一, 阪口政清

    日本癌学会学術総会抄録集(Web)   78th   2019

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  • パッキング相互作用に着目したタンパク質結晶化法

    小坂恵, 山田秀徳, 二見淳一郎, 多田宏子, 今村維克, 玉田太郎

    日本結晶学会年会講演要旨集   2019   2019

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  • パッキングのコントロールにより,難結晶性蛋白質の結晶化を促進する結晶化法

    小坂恵, 山田秀徳, 二見淳一郎, 多田宏子, 今村維克, 玉田太郎

    日本細胞生物学会大会(Web)   71st   2019

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  • Novel therapeutic approach based on S100A8/A9-mediated organ tropic cancer metastasis

    木下理恵, 友信奈保子, 山内明, 枝園和彦, 冨田秀太, 村田等, 二見淳一郎, 近藤英作, 豊岡伸一, 阪口政清

    日本癌学会学術総会抄録集(Web)   78th   2019

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  • 変性タンパク質への部位特異的biotin化条件の最適化とneoantigenスクリーニングへの応用

    峯苫 智晴, 垣見 和宏, 二見 淳一郎

    日本生物工学会大会講演要旨集   平成30年度   105 - 105   2018.8

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  • 抗がん抗原抗体で腫瘍免疫応答をモニタリングするMUSCAT-Assay

    二見 淳一郎, 本莊 知子, 吉岡 実咲, 勝河 祐希, Hannaneh Ahmadi, 木下 理恵, 藤枝 奈緒, 垣見 和宏

    日本がん免疫学会総会プログラム・抄録集   22回   122 - 122   2018.7

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  • がん免疫細胞治療(γδT細胞治療)におけるバイオマーカーの検索

    藤枝 奈緒, 大平 公亮, 小林 由香利, 神原 佳織, 泉 謙道, 高橋 卓也, 木村 真之介, 小林 史弥, 松下 博和, 二見 淳一郎, 垣見 和宏

    日本成人病(生活習慣病)学会会誌   44   77 - 77   2018.1

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  • 難結晶性蛋白質のパッキングをコントロールする結晶化法の開発と評価

    小坂恵, 山田秀徳, 二見淳一郎, 多田宏子, 今村維克, 玉田太郎

    日本結晶学会年会講演要旨集   2018   2018

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  • 疎水性残基導入が難結晶性タンパク質の結晶化に与える影響

    小坂恵, 山田秀徳, 二見淳一郎, 多田宏子, 今村維克, 玉田太郎

    日本生化学会大会(Web)   90th   2017

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  • タンパク質のパッキングをコントロールする疎水性残基導入

    小坂恵, 山田秀徳, 二見淳一郎, 多田宏子, 今村維克, 玉田太郎

    日本結晶学会年会講演要旨集   2017   2017

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  • 全長・水溶性がん抗原タンパク質を用いたAntigen-Spreadingの定量評価技術の開発

    二見 淳一郎, 細井 亮宏, 松下 博和, 垣見 和宏

    日本癌学会総会記事   75回   P - 2336   2016.10

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  • 疎水相互作用がカギを握る難結晶性タンパク質の結晶化法

    小坂恵, 山田秀徳, 二見淳一郎, 多田宏子, 玉田太郎

    日本結晶学会年会講演要旨集   2016   2016

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  • 疎水性残基の導入が蛋白質の結晶化に及ぼす影響

    小坂恵, 山田秀徳, 二見淳一郎, 多田宏子, 玉田太郎

    日本分子生物学会年会プログラム・要旨集(Web)   39th   2016

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  • 疎水性残基を変異導入する蛋白質結晶化促進法

    小坂恵, 山田秀徳, 二見淳一郎, 多田宏子, 玉田太郎

    日本蛋白質科学会年会プログラム・要旨集   16th   2016

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  • 2P-067 Sensitive analysis of anti-cancer immune responses by chemically Scationized full-length and water-soluble cancer antigens

    Futami Junichiro, Nonomura Hidenori, Kido Momoko, Niidoi Naomi, Fujieda Nao, Hosoi Akihiro, Fujita Kana, Mandai Komako, Atago Yuki, Kinoshita Rie, Honjo Tomoko, Matsushita Hirokazu, Uenaka Akiko, Nakayama Eiichi, Kakimi Kazuhiro

    67   191 - 191   2015

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  • 難結晶性蛋白質の結晶化を促進する疎水性残基導入

    小坂恵, 山田秀徳, 二見淳一郎, 多田宏子, 安達基泰, 玉田太郎, 黒木良太

    日本結晶学会年会講演要旨集   2015   2015

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  • 疎水性残基導入が難結晶性蛋白質の結晶化に及ぼす影響

    小坂恵, 山田秀徳, 二見淳一郎, 多田宏子, 安達基泰, 玉田太郎, 黒木良太

    日本蛋白質科学会年会プログラム・要旨集   15th   2015

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  • 蛋白質のパッキングをコントロールする結晶化タグの開発と評価

    小坂恵, 山田秀徳, 二見淳一郎, 多田宏子, 安達基泰, 玉田太郎, 黒木良太

    日本結晶学会年会講演要旨集   2014   2014

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  • 疎水性結晶化タグの導入による蛋白質結晶化促進法の開発

    小坂恵, 松田京子, 山田秀徳, 二見淳一郎, 多田宏子, 岡崎伸生, 玉田太郎, 黒木良太

    日本蛋白質科学会年会プログラム・要旨集   12th   2012

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  • 難結晶性蛋白質の結晶化に向けた結晶化タグの開発と評価

    田路太地, 小坂恵, 山田秀徳, 二見淳一郎, 多田宏子, 岡崎伸生, 玉田太郎, 黒木良太

    日本蛋白質科学会年会プログラム・要旨集   12th   2012

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  • タンパク質のパッキングをコントロールする結晶化法の開発

    小坂恵, 直井里美, 山田秀徳, 二見淳一郎, 多田宏子, 岡崎伸生, 玉田太郎, 黒木良太

    日本結晶学会年会講演要旨集   2011   2011

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  • 結晶格子工学によるウシRNase Aの結晶空間群の変更

    土井慎一, 小坂恵, 二見淳一郎, 多田宏子, 玉田太郎, 岡崎伸生, 黒木良太, 山田秀徳

    生化学   2008

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  • 内臓脂肪組織に由来するセリンプロテアーゼ阻害剤 : Vaspin の同定肥満状態でインスリン感受性を高める新規アディポサイトカイン

    肥田 和之, 和田 淳, 江口 潤, HONG Zhang, 馬場 雅子, 清田 綾, 橋本 泉, 岡田 達夫, 安原 章浩, 中司 敦子, 赤木 滋, 四方 賢一, 宝来 真志, 二見 淳一郎, 渡辺 英二郎, 松木 泰, 平松 隆司, 槇野 博史, KANWAR Yashpal S.

    岡山醫學會雜誌   118 ( 3 )   215 - 220   2007.1

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    Language：Japanese   Publisher：岡山医学会  

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    Other Link： http://ousar.lib.okayama-u.ac.jp/13354

  • 2B11-4 Intracellular delivery of GST-fused proteins by polyethlenimineglutathione conjugates

    MURATA Hitoshi, FUTAMI Junichiro, KITAZOE Midori, KOSAKA Megumi, TADA Hiroko, KAI Takashi, SENO Masaharu, YAMADA Hidenori

    19   63 - 63   2007

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  • 1C16-5 Development of protein transduction technology by cationization and analysis of their mechanisms

    FUTAMI Junichiro, KITAZOE Midori, MURATA Hitoshi, WATANABE Yasuyoshi, YAGI Yasuyuki, TADA Hiroko, SENO Masaharu, Kai Hiroshi, YAMADA Hidenori

    17   103 - 103   2005

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  • 523 Design of fusion proteins by domain insertion

    Tada Hiroko, Onizuka Masayuki, Masuzawa Wataru, Futami Junichiro, Kosaka Megumi, Seno Masaharu, Yamada Hidenori

    14   78 - 78   2002

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  • Cytotoxic proteins generated by insertion of a carrier protein into ribonuclease.

    Tada Hiroko, Onizuka Masayuki, Futami Junichiro, Maeda takashi, Seno Masaharu, Yamada Hidenori

    13   266 - 266   2001

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  • PP-815 上皮増殖因子受容体(EGFR)過剰発現癌に対する生理活性物質を用いた低免疫原性ターゲッテイング療法の開発

    神野 浩光, 上田 政和, 菊地 潔, 池田 正, 北島 政樹, 二見 淳一郎, 妹尾 昌治

    日本外科学会雑誌   101   411 - 411   2000.3

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    Language：Japanese   Publisher：一般社団法人日本外科学会  

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  • Effects of Eosinophil Cationic Protein (ECP) on Mammalian Cell Lines.

    Maeda Takashi, Kitazoe Midori, Futami Junichiro, Tada Hiroko, Seno Masaharu, Yamada Hidenori

    12   198 - 198   2000

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  • Effect of Eosinophil Cationic Protein (ECP) on Carcinoma Cells.

    Maeda Takashi, Kitazoe Midori, Futami Junichiro, Tada Hiroko, Seno Masaharu, Yamada Hidenori

    11   152 - 152   1999

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  • 5種類のヒト膵臓由来型リボヌクレアーゼの比較

    村藤 裕, 二見 淳一郎, 津島 義明, 松本 佳世子, 堀井 史子, 多田 宏子, 妹尾 昌治, 山田 秀徳

    日本分子生物学会年会プログラム・講演要旨集   19   247 - 247   1996.8

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  • ヒトリボヌクレアーゼを用いた細胞増殖阻害剤の開発

    二見 淳一郎, 多田 慎太郎, 妹尾 昌治, 山田 秀徳

    日本分子生物学会年会プログラム・講演要旨集   19   722 - 722   1996.8

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  • SH基の保護試験alkyl methanethiosulfonateの蛋白質工学への応用

    竹内 倫太郎, 山口 博之, 谷川 真三郎, 津島 義明, 眞砂 明典, 二見 淳一郎, 小坂 恵, 多田 宏子, 妹尾 昌治, 山田 秀徳

    日本分子生物学会年会プログラム・講演要旨集   19   381 - 381   1996.8

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Presentations

  • 自己抗体バイオマーカーの網羅的定量評価系のバリデーション

    宮本 愛, 本莊 知子, 伊達 実鈴, 森 壮流, 大橋 圭明, 木浦 勝行, 垣見 和宏, 二見 淳一郎

    日本がん免疫学会総会プログラム・抄録集  2023.6  日本がん免疫学会

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    Event date： 2023.6

    Language：Japanese  

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  • 自己抗体バイオマーカーを用いたがん免疫サイクルを評価する精密測定法の開発

    宮本愛, 本莊知子, 益井実鈴, 木下理恵, 公文裕巳, 垣見和宏, 二見淳一郎

    第44回蛋白質の構造と機能に関する九州シンポジウム  2022.8.20 

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    Event date： 2022.8.21

    Presentation type：Oral presentation (general)  

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  • 代替2次元分離法を用いた自己抗体バイオマーカータンパク質の効率的な探索

    益井実鈴, 塩川つぐみ, 多田宏子, 二見淳一郎

    第44回蛋白質の構造と機能に関する九州シンポジウム  2022.8.20 

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    Event date： 2022.8.20 - 2022.8.21

    Presentation type：Poster presentation  

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  • がん免疫サイクルを評価する自己抗体バイオマーカー群の精密測定法の開発

    宮本愛, 本莊知子, 益井実鈴, 木下理恵, 公文裕巳, 垣見和宏, 二見淳一郎

    第26回日本がん免疫学会総会  2022.7.20 

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    Event date： 2022.7.22

    Presentation type：Oral presentation (general)  

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  • がん免疫サイクルを評価する自己抗体バイオマーカー群の精密測定法の開発

    宮本 愛, 本莊 知子, 益井 実鈴, 木下 理恵, 公文 裕巳, 垣見 和宏, 二見 淳一郎

    日本がん免疫学会総会プログラム・抄録集  2022.6  日本がん免疫学会

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  • デキストラン－低親和リガンド conjugate による結合親和性の増強

    福田華梨, 宮本 愛, 本莊知子, 二見淳一郎

    日本生物工学会西日本支部大会2024（第７回講演会）  2024.11.16 

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  • 網羅的自己抗体データの機械学習による肺がん識別パネルの構築と最適化検討

    森 壮流, 宮本 愛, 本莊知子, 伊達実鈴, 渡邉洋美, 大橋圭明, 木浦勝行, 垣見和宏, 二見淳一郎

    日本生物工学会西日本支部大会2024（第７回講演会）  2024.11.16 

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  • Immune Monitoring & Profiling Technology for Precision Medicine Invited

    Junichiro FUTAMI

    2024 USTP x SixERS Joint Symposium  2024.10.24 

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  • 配列エピトープを認識する自己抗体バイオマーカーの効率的な探索法と評価系の改良

    伊達 実鈴, 塩川 つぐみ, 多田 宏子, 森 壮流, 本莊 知子, 宮本 愛, 二見 淳一郎

    第76回日本生物工学会大会  2024.9.9 

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  • 自己抗体バイオマーカーの網羅的定量評価システム開発と機械学習を用いたがん識別能の向上

    宮本 愛, 森 壮流, 伊達 実鈴, 本莊 知子, 大橋 圭明, 木浦 勝之, 垣見 和宏, 二見 淳一郎

    第76回日本生物工学会大会  2024.9.9 

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  • 自己抗体プロファイルの機械学習によるがん識別性能の評価

    森 壮流, 宮本 愛, 本莊 知子, 伊達 実鈴, 渡邉 洋美, 大橋 圭明, 木浦 勝之, 垣見 和宏, 二見 淳一郎

    第28回日本がん免疫学会総会・第37回日本バイオセラピィ学会学術集会総会 合同大会  2024.7.11 

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  • 変性状態の細胞内総タンパク質が示す溶解性を利用した新規プロテオミクス

    伊達実鈴, 塩川つぐみ, 多田宏子, 本莊知子, 宮本愛, 岡田宣宏, 二見 淳一郎

    第 75 回日本生物工学会大会  2023.9.5 

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  • 代替 2 次元分離法の開発による自己抗体バイオマーカー探索の効率化

    益井実鈴、塩川つぐみ、多田宏子、本莊知子、宮本愛、二見淳一郎

    第 23 回日本蛋白質科学会年会  2023.7.6 

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  • 自己抗体バイオマーカーの網羅的定量評価系による 免疫プロファイリング・モニタリング技術 Invited

    二見淳一郎

    第15回 日本血液疾患免疫療法学会学術集会シンポジウム：抗体マーカー  2023.6.23 

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  • 自己抗体免疫プロファイリング/モニタリング技術 と個別化医療サポートへの可能性 Invited

    二見淳一郎

    第96回日本内分泌学会学術総会：中堅若手の会 YECセミナー 『自己免疫とがん免疫研究のフロンティア』  2023.6.1 

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  • 自己抗体バイオマーカーの網羅的定量評価データの 統計解析による免疫プロファイリング

    森壮流, 宮本愛, 本莊知子, 益井実鈴, 二見淳一郎

    第64回日本生化学会中四国支部例会  2023.5.26 

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  • 自己抗体バイオマーカーのプロファイリング・ モニタリング技術による個別化医療のサポート Invited

    二見淳一郎

    第129回 岡山県医用工学研究会 オンラインセミナー 蛋白質機能の解明・創発に基づく医用工学・創薬への展開  2023.2.28 

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    Presentation type：Oral presentation (invited, special)  

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  • ヒト自己抗体が認識する構造/配列エピトープ解析

    山本莉加, 本莊知子, 宮本愛, 二見淳一郎

    日本生物工学会 西日本支部 第6回講演会  2022.11.26 

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  • がん免疫応答を末梢血で評価する自己抗体バイオマーカー群の 網羅的精密測定法開発

    宮本愛, 本莊知子, 益井実鈴, 木下理恵, 公文裕巳, 二見淳一郎

    第１回日本抗体学会設立記念学術大会  2022.11.26 

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  • タグなしタンパク質の高効率なrefoldingと精製法の開発

    山本航, 木村修一郎, 二見淳一郎

    日本生物工学会 西日本支部 第6回講演会  2022.11.26 

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  • 新規2次元分離法を用いた自己抗体バイオマーカータンパク質の効率的な探索法の開発 Invited

    益井実鈴

    日本生物工学会西日本支部大会2022（第６回講演会）第11回生物工学学生優秀賞（飛翔賞） 受賞講演  2022.11.26 

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  • 一人ひとりにあった医療をどう実現するか？－工学研究者と病院の現場の連携ー「個人に最適化された医療を生物工学で切り拓く」

    二見淳一郎

    岡山大学大学院ヘルスシステム統合科学研究科サイエンス・カフェ2022  2022.11.19 

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    Presentation type：Public lecture, seminar, tutorial, course, or other speech  

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  • 代替 2 次元分離法の開発による自己抗体バイオマーカー探索の効率化

    益井実鈴, 塩川つぐみ, 多田宏子, 二見淳一郎

    第74回日本生物工学会大会  2022.10.20 

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  • がん免疫サイクルのレベルを末梢血で評価する自己抗体バイオマーカー群網羅的測定法の確立

    宮本愛, 本莊知子, 益井実鈴, 木下理恵, 公文裕巳, 垣見和宏, 二見淳一郎

    第74回日本生物工学会大会  2022.10.20 

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  • 変性タンパク質工学から見えてきた天然変性タンパク質の姿

    二見淳一郎

    第74回日本生物工学会大会 シンポジウム「生体分子の相互作用 における曖昧さの意義」  2022.10.18 

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  • 自己抗体免疫プロファイリング/モニタリング技術による個別化医療のサポート Invited

    二見淳一郎

    Basic Biology Seminar in Okayama  2022.10.14 

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  • 免疫プロファイリングプラットフォームの完成にはバイオバンクの検体がぜひとも必要である Invited

    二見淳一郎

    第7回クリニカルバイオバンク学会  2022.7.8 

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  • 新規2次元分離プロテオミクスによる自己抗体バイオマーカー探索法の開発

    益井 実鈴, 塩川 つぐみ, 多田 宏子, 二見 淳一郎

    第73回日本生物工学会大会  2021.10.29 

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  • 自己抗体バイオマーカーの網羅的迅定量評価による腫瘍免疫応答モニタリング

    宮本愛, 田中健介, 本莊知子, 二見 淳一郎

    第62回 日本生化学会 中国・四国支部例会  2021.9.10 

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  • Expi293での安価な分泌タンパク質生産

    森彩良, 宮本愛, 本荘知子, 二見淳一郎

    第62回 日本生化学会 中国・四国支部例会  2021.9.10 

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  • 新規2次元分離法を用いた自己抗体バイオマーカータンパク質の効率的な探索法の開発

    益井 実鈴, 塩川 つぐみ, 多田 宏子, 二見 淳一郎

    第62回 日本生化学会 中国・四国支部例会  2021.9.10 

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  • 自己抗体バイオマーカーの迅速定量評価技術によるがん免疫サイクルのモニタリング

    田中健介, 宮本愛, 本莊知子, 二見淳一郎

    日本生物工学会西日本支部大会2020（第５回講演会)  2020.11.14 

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  • 自己免疫疾患関連の自己抗原リソース強化から考察された抗原性との物性相関

    橋口万澄, 宮本愛, 本莊知子, 二見淳一郎

    日本生物工学会西日本支部大会2020（第５回講演会)  2020.11.14 

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  • 細胞内総タンパク質可溶化技術を活用した新規プロテオミクス解析技術の開発

    益井実鈴, 馬場龍之介, 塩川つぐみ, 多田宏子, 二見淳一郎

    日本生物工学会西日本支部大会2020（第５回講演会)  2020.11.14 

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  • Unusual aggregation properties of forced expressed cancer/testis antigens in mammalian cell

    Hannaneh Ahmadi, Kouhei Shogeni, Yuki Katsukawa, Kana Fujita, Junichiro Futami

    2019.9.19 

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  • 可逆的カチオン化転写因子タンパク質の生細胞内導入における効率と経路の検討

    中野智貴, 周伯揚, 二見翠, 二見淳一郎

    2019.9.17 

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  • エピゲノム薬を用いた複合免疫療法における診断薬開発の基礎検討

    勝河祐希, Hannaneh Ahmadi, 本莊 知子, 二見淳一郎

    第71回日本生物工学会大会  2019.9.17 

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  • 部位特異的ビオチン化とrefolding assayを組み合せたneo-antigenスクリーニング法の開発

    峯苫智晴, 垣見和宏, 二見淳一郎

    第71回日本生物工学会大会  2019.9.17 

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  • 抗がん抗原抗体が認識するエピトープ解析とがん免疫サイクル活性化の評価

    吉岡実咲, 本莊知子, 木下理恵, 二見淳一郎

    2019.9.17 

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  • MUSCAT-Assay法での自己抗体モニタリングによる腫瘍免疫応答評価

    二見淳一郎, 本莊知子, 吉岡実咲, 勝河祐希, Hannaneh Ahmadi, 尾崎龍之介, 木下理恵, 鵜殿平一郎, 垣見和宏

    第23回日本がん免疫学会  2019.8.23 

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  • 腫瘍免疫応答を迅速にモニタリングする MUSCAT-Assay

    二見淳一郎

    第1回ファーマラボEXPO  2019.7.5 

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  • 腫瘍免疫応答の活性化をモニタリングするマウス自己抗体のプロテオーム解析

    尾﨑龍之介, 勝河祐希, 二見淳一郎

    日本生物工学会 西日本支部 第4回講演会  2018.12.1 

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  • 分子内SS結合保護試薬による タンパク質の耐熱性向上

    萩本 惇史, 宮本 愛, 二見 淳一郎

    日本生物工学会 西日本支部 第4回講演会  2018.12.1 

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  • ペプチド転移酵素を利用した細胞質内送達リガンドの調製法の開発

    田中綾乃, 宮田尚也, 宮本愛, 二見淳一郎

    日本生物工学会 西日本支部 第4回講演会  2018.12.1 

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  • 複合免疫療法に向けたがんの抗原性向上に関する基礎検討

    第70回日本生物工学会大会  2018.9.5 

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  • REIC/Dkk-3タンパク質の相互作用分子解析と抗がん免疫活性化の分子機構解明

    第70回日本生物工学会大会  2018.9.5 

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  • 変性タンパク質への部位特異的biotin化条件の最適化とneoantigenスクリーニングへの応用

    第70回日本生物工学会大会  2018.9.5 

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  • 抗腫瘍関連抗原抗体をバイオマーカーとした高感度測定系の開発

    第70回日本生物工学会大会  2018.9.5 

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  • 抗がん抗原抗体で腫瘍免疫応答をモニタリングするMUSCAT-Assay

    二見 淳一郎

    第22回日本がん免疫学会総会  2018.8.3 

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  • 変性タンパク質への部位特異的biotin化技術を活用したNeo-antigenスクリーニング法の開発

    第59回 日本生化学会 中国・四国支部例会  2018.5.26 

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  • 腫瘍関連抗原の生産系の構築とAntigen-Spreading測定系の開発

    第59回 日本生化学会 中国・四国支部例会  2018.5.26 

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  • エピゲノム薬を用いたがんの抗原性向上に関する基礎検討

    第59回 日本生化学会 中国・四国支部例会  2018.5.26 

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  • 不溶化する組換えタンパク質の巻き戻しと高度利用

    ライフサイエンス技術部会/反応分科会 技術セミナー  2018 

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  • がん免疫細胞治療（γδT 細胞治療）におけるバイオマーカーの検索

    第52回日本成人病学会学術集会  2018 

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  • SH保護試薬を用いたジスルフィド結合含有タンパク質の加熱不可逆失活機構の評価

    2017年度生命科学系学会合同年次大会  2017 

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  • 腫瘍免疫応答の活性化をモニタリングするMUSCAT-assay

    第１１２回 岡山県医用工学研究会 平成２９年度 第２回セミナー・交流会  2017 

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  • 腫瘍免疫応答の活性化をモニタリングする抗体検査診断薬の標準化

    第69回日本生物工学会大会  2017 

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  • REIC/Dkk-3タンパク質の相互作用分子解析による抗がん免疫活性機構の解明

    2017年度生命科学系学会合同年次大会  2017 

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  • Analysis of structural propensity of epitopes for antibody against cancer specific antigen observed in cancer patients

    2017年度生命科学系学会合同年次大会  2017 

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  • 複合がん免疫療法でのコンパニオン診断薬開発に向けた自家製陽性コントロールの評価

    生物工学若手研究者の集い（若手会）夏のセミナー2017  2017 

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  • 自己抗原・がん抗原タンパク質の固定化法の開発

    生物工学若手研究者の集い（若手会）夏のセミナー2017  2017 

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  • 腫瘍関連抗原に対するAntigen-Spreading測定系の開発

    生物工学若手研究者の集い（若手会）夏のセミナー2017  2017 

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  • SH保護試薬によるジスルフィド結合含有タンパク質の加熱不可逆失活の抑制

    第69回日本生物工学会大会  2017 

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  • 変性タンパク質の可溶化技術を利用した腫瘍免疫応答の活性化をモニタリングするコンパニオン診断薬の開発

    第41回蛋白質と酵素の構造と機能に関する九州シンポジウム  2017 

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  • 腫瘍免疫を活性化するREIC/Dkk-3タンパク質の相互作用分子の解析

    第69回日本生物工学会大会  2017 

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  • Hek293細胞を用いた全長がん抗原タンパク質の網羅的調製条件の最適化

    第68回日本生物工学会大会  2016 

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  • Optimization of preparation methodology for multiple full-length cancer antigens using Hek293 cells

    2016 

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  • Quantitative analysis of antigen-spreading using water-soluble and full-length cancer antigens

    第75回日本癌学会学術総会  2016 

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  • 動物細胞内で強制発現させたがん抗原タンパク質の細胞内凝集

    第68回日本生物工学会大会  2016 

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  • 受容体を介したヒト細胞内タンパク質の標的細胞質内への送達技術の開発

    第39回日本分子生物学会年会  2016 

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  • Quantitative analysis of activation of anti-tumor immunoresponce

    BioJAPAN2016  2016 

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  • 疎水性残基の導入が蛋白質の結晶化に及ぼす影響

    第39回日本分子生物学会年会  2016 

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  • 受容体を介したタンパク質細胞内導入技術の開発

    第3回 日本生物工学会 西日本支部 講演会  2016 

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  • ジスルフィド結合含有タンパク質の加熱不可逆失活抑制法の開発

    第3回 日本生物工学会 西日本支部 講演会  2016 

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  • HEK293細胞内で不溶性として発現する全長がん抗原タンパク質の可溶化法

    第39回日本分子生物学会年会  2016 

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  • 腫瘍免疫応答の活性化測定の標準化

    第3回 日本生物工学会 西日本支部 講演会  2016 

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  • REIC/DKK3タンパク質の免疫賦活化機構の解明

    第3回 日本生物工学会 西日本支部 講演会  2016 

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  • ハイマンノース型遊離糖鎖のタンパク質リフォールディング促進機能

    日本農芸化学会中四国支部第41回講演会  2015 

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  • 動物細胞由来の変性状態の総タンパク質混合物が核酸除去により示す高い水溶性

    第15回日本蛋白質科学会年会  2015 

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  • 放線菌RHA1株のビフェニル代謝に関与するタンパク質の新規同定と解析

    日本農芸化学会2015年度岡山大会  2015 

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  • カチオン化全長・水溶性がん抗原タンパク質の調製条件の最適化

    第15回日本蛋白質科学会年会  2015 

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  • 受容体を介したタンパク質細胞内導入技術の開発

    第15回日本蛋白質科学会年会  2015 

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  • 難結晶性蛋白質の結晶化を促進する疎水性残基導入

    日本結晶学会年会  2015 

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  • 疎水性基導入が難結晶性蛋白質の結晶化に及ぼす影響

    第15回日本蛋白質科学会年会  2015 

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  • S-カチオン化全長・水溶性抗原を用いた高感度抗体検出技術による腫瘍免疫応答の定量評価

    第67回日本生物工学会大会  2015 

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  • カチオン化全長・水溶性がん抗原タンパク質を用いた高感度抗体検出試薬の調製条件の最適化

    日本分子生物学会・日本生化学会合同年会BMB2015  2015 

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  • フレキシブルな構造のヒト細胞内タンパク質を標的細胞内へ送達する技術開発

    日本分子生物学会・日本生化学会合同年会BMB2015  2015 

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  • Yoshito Abe, Takatoshi Ohkuri, 木村吉伸, 前田 恵, 二見淳一郎, Tadashi Ueda

    日本薬学会  2014 

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  • ヒト抗体 L 鎖変異体の安定性に対する添加剤の影響

    第14回日本蛋白質科学会年会  2014 

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  • ヒト全長Cancer/Testis抗原の効率的な生産系の開発

    第14回日本蛋白質科学会年会  2014 

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  • 遊離N-グリカンのタンパク質リフォールディング促進機能

    日本生化学会  2014 

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  • タンパク質カチオン化技術を用いた高感度抗体検出技術の開発

    第66回日本生物工学会  2014 

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  • 放線菌RHA1 株のビフェニル代謝に関与する新規同定タンパク質の機能解析

    第66回日本生物工学会  2014 

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  • 高純度・水溶性ヒト全長Cancer/Testis 抗原リソースの整備

    第66回日本生物工学会  2014 

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  • 遊離N―グリ力ンはタンパク質リフォールディングを促進する

    第 33 回日本糖質学会年会  2014 

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  • Physiological Function of Free N-glycan involved in Protein Folding

    Annual meeting of glycobiology 2013  2013 

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  • 放線菌RHA1株のビフェニル代謝に関する新規遺伝子の同定と解析

    日本生物工学会  2013 

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  • 変性状態のタンパク質の高度利用と診断薬への応用

    化学工学会 第45回秋季大会  2013 

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  • 全長・水溶性がん抗原タンパク質を用いた抗体検査法の開発

    日本生物工学会  2013 

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  • 多種類ヒトCT抗原の効率的な生産系システムの開発

    日本生物工学会  2013 

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  • ヒト全長CT 抗原の効率的生産システムの開発

    日本蛋白質科学会  2013 

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  • 用途に応じたタンパク質の効率的生産

    中性子利用研究セミナー  2013 

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  • Protein Cationization Techniques for Biomedical Engineering

    Young Asian Biochemical Engineers' Community (YABEC)  2012 

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  • 細胞内導入型転写因子と両親媒性ペプチドの併用による機能発現の向上

    日本生物工学会西日本支部・日本農芸化学会中四国支部合同講演会  2012 

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  • 難結晶性蛋白質の結晶化に向けた結晶化タグの開発と評価

    第12回日本蛋白質科学会年会  2012 

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  • タンパク質カチオン化技術を用いた高純度・可溶性がん抗原タンパク質の調製技術の開発

    第34回東大病院22世紀医療センター：産学連携メディカルフロンティアセミナー  2012 

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  • 細胞内導入型RAGE阻害ペプチドの開発

    日本生物工学会西日本支部第2回講演会  2012 

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  • 疎水性結晶化タグの導入による蛋白質結晶化促進法の開発

    第12回日本蛋白質科学会年会  2012 

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  • 転写因子タンパク質のin cell folding法 による機能発現技術の開発

    第64回日本生物工学会大会  2012 

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  • 変性状態の細胞内総タンパク質が示す溶解性に関する研究

    第64回日本生物工学会大会  2012 

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  • カチオン化アビジンを介したビオチン化タンパク質細胞導入法における導入効率の最適化

    第64回日本生物工学会大会  2012 

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  • 大腸菌を用いた膜貫通蛋白質の高発現

    第64回日本生物工学会大会  2012 

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  • 両親媒性ペプチドの併用による可逆的変性カチオン化タンパク質のin cell folding技術の改善

    日本生物工学会西日本支部第2回講演会  2012 

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  • 可逆的変性カチオン化法を活用した高純度・水溶性がん抗原タンパク質の調製

    第64回日本生物工学会大会  2012 

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  • TAPS-sulfonateを用いた高純度・水溶性がん抗原タンパク質の調製方法

    日本生物工学会西日本支部第2回講演会  2012 

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  • タンパク質カチオン化技術を活用した細胞機能制御

    日本高分子学会・バイオ・高分子研究会  2011 

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  • 可逆的変性カチオン化法を用いた変性タンパク質の高度精製とin cell foldin

    第63回日本生物工学会大会  2011 

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  • 凍結乾燥保存が可能な細胞内導入型転写因子

    第11回日本蛋白質科学会年会  2011 

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  • タンパク質カチオン化技術によるタンパク質の物性操作と医用応用

    第8回産総研健康工学研究部門講演会  2010 

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  • 変性タンパク質の可溶化技術：原理と応用

    第163回農芸化学特別セミナー  2010 

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  • 変性タンパク質の可溶化技術と工学的応用

    日本蛋白質科学会年会  2010 

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  • タンパク質カチオン化技術を活用した細胞機能制御

    日本組織培養学会  2010 

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  • タンパク質可逆的修飾試薬を活用したがん免疫への応用

    第33回日本分子生物学会年会会  2010 

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  • 可逆的タンパク質マンノース化試薬の合成と評価

    第32回日本分子生物学会年会  2009 

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  • タンパク質カチオン化技術を駆使した医用工学への応用研究

    第2回高度医療都市を創出する未来技術国際シンポジウム  2009 

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  • 可逆的変性カチオン化法を用いた細胞内導入型転写因子の開発

    日本蛋白科学会  2009 

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  • Exploiting protein cationization techniques in future cell therapy

    Joint Conference of 10th CTS and 36th JSOPMB  2009 

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  • 細胞内総タンパク質の可逆的変性カチオン化と溶解性に関する研究

    第32回日本分子生物学会年会  2009 

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  • ナノ構造体内部への高密度タンパク質封入に向けたタンパク質カチオン化技術の検討

    日本生化学・分子生物学会合同年会BMB2008  2008 

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  • Differential delivery of antigen to dendoritic cells potentiates the MHC class I and/or II-restricted T cell responses

    67回 日本癌学会総会  2008 

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  • タンパク質カチオン化技術の医用工学への応用

    大阪大学蛋白質研究所セミナー：蛋白質を創る、知る、使う 〜蛋白質科学と産業応用〜  2008 

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  • タンパク質カチオン化技術を利用したがん治療技術の開発戦略

    第1回高度医療都市を創出する未来技術国際シンポジウム  2008 

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  • 人工転写因子蛋白質を用いた細胞内導入条件の最適化

    日本生化学・分子生物学会合同年会BMB2008  2008 

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  • タンパク質の化学修飾（カチオン化）を駆使した創薬支援研究

    第3回 新薬創生研究会  2007 

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  • 人工転写因子を用いたタンパク質細胞内導入効率の定量化

    第30回日本分子生物学会年会・第80回日本生化学会大会 合同大会(BMB2007)  2007 

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  • ポリエチレンイミン(PEI)-グルタチオンキャリアーを用いたGST-融合タンパク質の細胞導入

    第５９回日本生物工学会大会  2007 

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  • 細胞内導入型転写因子の開発に向けた基礎検討

    第３１回蛋白質と酵素の構造と機能に関する九州シンポジウム  2007 

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  • Design and characterization of hybrid proteins constructed by domain insertion fusion.

    20th IUBMB international congress of biochemistry and molecular biology and 11th FAOBMB congress  2006 

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  • Artificial regulation of cell proliferation by protein transduction of N-terminal domain of simian virus 40 large T antigen using PEI-cationization method.

    20th IUBMB international congress of biochemistry and molecular biology and 11th FAOBMB congress  2006 

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  • タンパク質カチオン化技術 －タンパク質の細胞内導入と生産技術への応用－

    蛋白質と酵素の構造と機能に関する九州シンポジウム  2006 

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  • Crystal Lattice Engineering: Crystallization and Structure Determination of Human RNase 1 Mutants with a Hydrophobic Interface of Leucines.

    5th East Asian Biophysics Symposium & 44th Annual Meeting of the Biophysical Society of Japan  2006 

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  • Applications of intracellular delivery of a protein by cationiczation. From in vitro folding to in cell folding of denatured proteins.

    A satellite Meeting of International Conference of 43rd Japanese Symposium and 4th Peptide Engeneering Meeting. Membrane-permeable peptides: Chemistry, biology and therapeutic applications  2006 

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  • β-cateninタンパク質導入による人為的Wntシグナル制御

    2006年分子生物学フォーラム  2006 

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  • 分子間疎水相互作用の導入によるヒト RNase1 の結晶化と構造解析

    第５回日本蛋白質科学会年会  2005 

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  • ポリエチレンイミン（PEI）カチオン化法によるタンパク質細胞内導入技術の開発

    第23回 バイオテクノロジーシンポジウム  2005 

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  • カチオン性ポリマーを用いた変性蛋白質の可溶化技術と細胞内導入技術の開発

    産学連携を指向した九州バイオサイエンスシンポジウム・疾患プロテオミクス最前線  2005 

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  • Quantitative analysis of intracellular delivery of cationized proteins

    日本生化学会大会  2005 

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  • 蛋白質カチオン化による細胞内導入技術開発と機構解明

    日本生物工学会大会  2005 

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  • Artificial Control of Cell Proliferation Using an N-terminal Domain of Simian Virus 40 Large T Antigen by Means of PEI-cationization.

    The American Society for Cell Biology 45th Annual Meeting  2005 

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  • 蛋白質カチオン化法とHIV-TATペプチドを介した蛋白質細胞内導入の比較

    日本分子生物学会年会  2005 

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  • ｶﾁｵﾝ性ｷｬﾘｱｰによるﾀﾝﾊﾟｸ質導入技術の開発

    第22回ﾊﾞｲｵｼﾝﾎﾟｼﾞｳﾑ  2004 

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  • 蛍光共鳴ｴﾈﾙｷﾞｰ移動原理に基づく免疫学的測定法を利用した細胞内ｼｸﾞﾅﾙ伝達経路の解析技術とPEIを用いたﾀﾝﾊﾟｸ質の細胞内導入技術の開発

    第22回ﾊﾞｲｵｼﾝﾎﾟｼﾞｳﾑ  2004 

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  • カチオン化SV40T抗原N末端ドメインによる細胞増殖の人工制御

    第27回日本分子生物学会年会  2004 

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  • ﾀﾝﾊﾟｸ質生細胞内導入法によるliving cell imagingにおけるﾊﾞｯｸｸﾞﾗｳﾝﾄﾞ低減化技術

    第27回日本分子生物学会年会  2004 

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  • T7 RNA Polymeraseの細胞内導入による外部制御可能な一過性遺伝子発現

    日本生化学大会  2004 

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  • 大腸菌インクルージョンボディからのニワトリアビジン四量体の酸化的リフォールディング

    日本生化学大会  2004 

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  • がん免疫サイクルのレベルを末梢血で評価する自己抗体バイオマーカー群網羅的測定法の確立

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Industrial property rights

  • 抗S100A8/A9抗体とその用途

    阪口 政清, 豊岡 伸一, 冨田 秀太, 枝園 和彦, 佐藤 博紀, 木下 理恵, 二見 淳一郎, 荒木 恒太, 岡▲崎▼ 幹生, 近藤 英作, 井上 裕介, 山内 明

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    Applicant：国立大学法人 岡山大学

    Application no：JP2019016100  Date applied：2019.4.15

    Publication no：WO2019-208290  Date published：20191031

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  • REIC/Dkk-3タンパク質を有効成分として含むTGFβ阻害剤

    二見淳一郎, 木下理恵, 公文裕巳

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    Applicant：桃太郎源株式会社

    Application no：特願2017-119919  Date applied：2017.6.19

    Announcement no：特開PCT/JP2017/022588  Date announced：2017.12.28

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  • 活性構造のREIC/Dkk-3タンパク質を特異的に認識して結合する抗体、及び該抗REIC/Dkk-3抗体を用いた癌治療のモニタリング

    公文 裕巳, 木下 理恵, 二見 淳一郎

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    Applicant：国立大学法人 岡山大学

    Application no：特願2017-543279  Date applied：2016.9.27

    Publication no：WO2017-057308  Date published：201746

    Patent/Registration no：特許第6975424号  Date registered：2021.11.10 

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  • 抗体検出用試薬の製造方法、及びその用途

    二見 淳一郎, 垣見 和宏, 前川 隆司, 白木 正人

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    Applicant：国立大学法人 岡山大学

    Application no：特願2013-531595  Date applied：2013.3.29

    Publication no：WO2013-147233  Date published：2013103

    Patent/Registration no：特許6168497  Date registered：2017.7.7  Date issued：2017.7.7

    6168497

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  • ＲＥＩＣ／Ｄｋｋ－３タンパク質の部分領域ポリペプチド

    公文 裕巳, 渡部 昌実, 二見 淳一郎, 藤井 康之, 植木 英雄, 落合 和彦

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    Applicant：国立大学法人 岡山大学

    Application no：特願2012-522733  Date applied：2011.7.1

    Publication no：WO2012-002582  Date published：201215

    Patent/Registration no：特許5936129  Date registered：2016.5.20  Date issued：2016.5.20

    5936129

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  • チオスルホナート化合物、タンパク質及び／又はペプチドの可逆的カチオン化剤並びに可溶化方法

    二見 淳一郎, 山田 秀徳, 久良木 豪, 矢木 恵一郎

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    Applicant：国立大学法人 岡山大学

    Application no：特願2012-507073  Date applied：2011.3.24

    Publication no：WO2011-118731  Date published：2011929

    Patent/Registration no：特許5713006  Date registered：2015.3.20 

    特許第5713006号

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  • タンパク質の細胞内導入剤

    山田 秀徳, 村田 等, 二見 淳一郎, 阪口 政清, 許 南浩, 八木 康行, 甲斐 敬

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    Applicant：株式会社日本触媒

    Application no：特願2007-046025  Date applied：2007.2.26

    Announcement no：特開2008-115150  Date announced：2008.5.22

    Patent/Registration no：特許第5097412号  Date registered：2012.9.28 

    特許第５０９７４１２号

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  • 細胞増殖剤及び細胞の増殖方法

    山田 秀徳, 二見 淳一郎, 村田 等, 阪口 政清, 許 南浩, 八木 康行, 甲斐 敬

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    Applicant：株式会社日本触媒

    Application no：特願2005-356631  Date applied：2005.12.9

    Announcement no：特開2007-159429  Date announced：2007.6.28

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  • タンパク質及び／又はペプチドの細胞内導入方法

    二見 淳一郎, 中西 秀高, 山田 秀徳, 甲斐 敬

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    Applicant：株式会社日本触媒

    Application no：特願2005-147250  Date applied：2005.5.19

    Announcement no：特開2006-006316  Date announced：2006.1.12

    Patent/Registration no：特許4885476  Date registered：2011.12.16  Date issued：2011.12.16

    特許第４８８５４７６号

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  • 可逆的カチオン化による変性タンパク質の細胞内導入と活性化の方法

    山田 秀徳, 二見 淳一郎, 村田 等, 前田 貴志, 阪口 政清

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    Applicant：株式会社日本触媒

    Application no：特願2003-356571  Date applied：2003.10.16

    Announcement no：特開2005-120017  Date announced：2005.5.12

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  • タンパク質及び/又はペプチドの細胞内導入用試験キット

    山田 秀徳, 二見 淳一郎, 中西 秀高

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    Applicant：株式会社日本触媒

    Application no：特願2003-149359  Date applied：2003.5.27

    Announcement no：特開2004-350526  Date announced：2004.12.16

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  • 蛋白質またはペプチドの細胞内導入方法

    山田 秀徳, 二見 淳一郎, 中西 秀高

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    Applicant：株式会社日本触媒

    Application no：特願2002-342486  Date applied：2002.11.26

    Announcement no：特開2004-049214  Date announced：2004.2.19

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  • 蛋白質又はペプチドの細胞内導入方法

    山田 秀徳, 二見 淳一郎, 前田 貴志, 北添 翠

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    Applicant：株式会社日本触媒

    Application no：特願2002-287280  Date applied：2002.9.30

    Announcement no：特開2004-121041  Date announced：2004.4.22

    Patent/Registration no：特許第3996028号  Date registered：2007.8.10 

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Awards

  • ベストティーチャー賞（物理化学1）

    2023.3   岡山大学工学部  

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  • ベストティーチャー賞（工学基礎実験実習）

    2022.3   岡山大学工学部  

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  • 研究功績賞

    2021.3   岡山大学工学部  

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  • 新産業創出研究奨励大賞

    2019.10   公益財団法人両備檉園記念財団  

    二見 淳一郎

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  • BBB Awards for Excellence to Authors (2016) Vol. 80

    2017  

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    Country：Japan

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  • 内山勇三科学技術賞

    2015  

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    Country：Japan

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Research Projects

  • Development of a Predictive Method for Immune-Related Liver Injury Using Autoantibody Biomarkers

    Grant number：25K10536  2025.04 - 2030.03

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research  Grant-in-Aid for Scientific Research (C)

    竹内 康人, 二見 淳一郎, 宮本 愛, 高木 章乃夫

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    Grant amount：\4680000 （ Direct expense: \3600000 、 Indirect expense：\1080000 ）

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  • Immunological analysis and POC establishment of comprehensive neoantigen-specific immunotherapy for cold tumor

    Grant number：23H03780  2023.04 - 2026.03

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research  Grant-in-Aid for Scientific Research (B)

    神垣 隆, 二見 淳一郎, 瀧本 理修, 近藤 聡英

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    Grant amount：\18850000 （ Direct expense: \14500000 、 Indirect expense：\4350000 ）

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  • Study on immunogenicity, physicochemical property, and immune monitoring of cancer/testis antigens

    Grant number：22H01881  2022.04 - 2025.03

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research  Grant-in-Aid for Scientific Research (B)

    二見 淳一郎

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    Grant amount：\17420000 （ Direct expense: \13400000 、 Indirect expense：\4020000 ）

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  • 免疫モニタリング情報を個別化医療に活用するための自己抗体reference database整備

    2022.04 - 2024.09

    バイオバンク・ネットワークの試料・情報を利用する第1回研究課題公募  https://biobank-search.megabank.tohoku.ac.jp/v2/news?id=6ftSYV0jy8bJEODBMUJMTD

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    Authorship：Principal investigator 

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  • 簡易モニタリングのための好酸球を用いた頭頸部がん免疫治療バイオマーカーの開発

    Grant number：21K09666  2021.04 - 2025.03

    日本学術振興会  科学研究費助成事業 基盤研究(C)  基盤研究(C)

    西川 大輔, 花井 信広, 松下 博和, 二見 淳一郎, 澤部 倫

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    Grant amount：\2470000 （ Direct expense: \1900000 、 Indirect expense：\570000 ）

    我々の研究グループでは、頭頸部がんで初めて、免疫チェックポイント阻害薬（ICI）治療前の末梢血の好酸球や、治療後の変化が、再発転移頭頸部がんに対するNivolumabの治療バイオマーカーとなることを報告してきた。本研究では、これらの研究成果を発展させ、頭頸部がんにおいて末梢血の好酸球と、抗腫瘍免疫を担うTリンパ球や、抗原提示の要因となる腫瘍抗原、それに関連するサイトカインの関係が、治療によってどう変化するかを評価する。本研究の目的は、どのような施設においても簡易に利用可能なバイオマーカーを開発することである。
    本研究の対象は、愛知県がんセンター頭頸部外科、薬物療法科（腫瘍内科）にて、再発・転移頭頸部がんでICI治療を行った患者である。研究開始以前にICI治療を受けた頭頸部扁平上皮がん患者（すでに保管されている凍結検体を使用）、研究開始後にICI治療を受ける頭頸部扁平上皮がん患者を対象とする。
    本研究では、研究協力者との連携体制の整備が重要であり、現在整備をすすめている状況である。末梢血をICI治療前後、増悪時に採取し、研究所の腫瘍免疫制御トランスレーショナルリサーチ分野（TR分野）にて、抹消単核細胞（PBMC）と血清に分離、凍結保存する具体的な連携手順書を作成中である。また、抗原パネルアッセイについて岡山大学工学部化学生命系学科と協議を行っている。また、実際の診療において、ICI投与の前後の前後の採血が必要となるため、患者の不利益が生じないような、計画を準備中である。
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  • 免疫プロファイリングプラットフォームによる疾患の早期診断・迅速モニタリングシステムの開発

    2019.11 - 2021.09

    JST  JST-STARTプログラム 

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    Authorship：Principal investigator 

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  • がん免疫サイクルの観点からみたAd-REICと分泌REICタンパク質の分子機構の解明と新規創薬

    2019.06 - 2022.02

    特別電源所在県科学技術振興事業 

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    Authorship：Coinvestigator(s) 

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  • REICタンパク質の機能解析による新たな創薬基盤プラットフォームの構築

    2016.06 - 2018.02

    特別電源所在県科学技術振興事業 

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  • Development of companion diagnostics for personalized cancer immunotherapy using denatured protein solubilization technology

    Grant number：16H04580  2016.04 - 2019.03

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (B)  Grant-in-Aid for Scientific Research (B)

    Futami Junichiro

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    Grant amount：\17810000 （ Direct expense: \13700000 、 Indirect expense：\4110000 ）

    We have developed the technology for analysis of antitumor immune response by using anti-cancer antigen autoantibody biomarkers. This technology employed luminex technology combined with S-cationization techniques to expose linear epitopes. This antibody detection system was successfully demonstrated that sensitive autoantibody detection relating to the activation of cancer immunity cycles.

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  • 変性タンパク質の可溶化技術を活 用したがん抗原抗体検査試薬の開発

    2015.06 - 2016.03

    (公財）岡山工学振興会  岡山工学振興会学術研究助成 

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    Authorship：Principal investigator 

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  • Development of membrane protein reconstitution technique in vivo.

    Grant number：24656506  2012.04 - 2014.03

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research Grant-in-Aid for Challenging Exploratory Research  Grant-in-Aid for Challenging Exploratory Research

    FUTAMI JUNICHIRO

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    Grant amount：\4160000 （ Direct expense: \3200000 、 Indirect expense：\960000 ）

    Combining protein transduction and in cell folding techniques, we tried to develop a novel in cell folding techniques for membrane protein in living cells. In order to achieve this technology, in cell folding technique was drastically improved in this study. Using denatured and reversibly cationized precursor protein, protein maturation events were observed in human cells without translation machinery.

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  • 高純度・水溶性がん抗原タンパク質の調製技術の確立とリソースの整備

    2011.07 - 2012.03

    JST  知財活用促進ハイウェイ 

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  • Application of protein cationization techniques for cancer immunotherapy

    Grant number：23360370  2011.04 - 2014.03

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (B)  Grant-in-Aid for Scientific Research (B)

    JUNICHIRO FUTAMI, KAKIMI Kazuhiro

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    Grant amount：\18330000 （ Direct expense: \14100000 、 Indirect expense：\4230000 ）

    This study aimed development of chemical protein cationization techniques for cancer antigens. Since most of cancer antigen proteins are flexible and unstable, solubilization with protein cationization techniques were useful methodology to prepare water-soluble and full-length cancer antigens. Using these cationized antigens, antigen antibodies for cancer antigens raised in cancer patients were successfully detected with a highly sensitive assay. Combining these developed techniques and enhanced cancer antigen production resource, we have successfully developed tools for cancer immunotherapy.

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  • がん治療遺伝子REICによるナノバイオ標的医療の創成

    2010.06 - 2013.03

    特別 

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    Authorship：Coinvestigator(s) 

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  • タンパク質カチオン化技術を活用した細胞再生医療への応用研究

    2009.04 - 2010.03

    財団法人山陽放送学術文化財団 

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  • タンパク質カチオン化技術を活用した医用工学の基盤技術開発

    2008.04 - 2010.05

    NEDO  産業技術研究助成 

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  • 変性タンパク質の可溶化技術を活用した細胞内イメージング技術の開発

    Grant number：20650070  2008 - 2009

    日本学術振興会  科学研究費助成事業 挑戦的萌芽研究  挑戦的萌芽研究

    山田 秀徳, 二見 淳一郎

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    Grant amount：\3300000 （ Direct expense: \3300000 ）

    (1) N末端特異的な蛍光標識による高精細な細胞内イメージング
    平成20年度に細胞内イメージングのモデルタンパク質としてN末端特異的に蛍光基を標識したβアクチンタンパク質を可逆的変性カチオン化法により高い水溶性を保持した蛍光標識プローブを調製することに成功していた。本年度はマイクロインジェクション法で細胞内への注入を試みたが、培地中で蛍光標識プローブが重合しやすく極めて困難であった。そこで蛍光標識プローブの溶解度向上に向けた諸条件を検討した結果、新規カチオン化試薬:TAP3S-Sulfonateの利用で高い溶解性が得られた。また、逆相HPLCで高純度に精製することで、純水および生理食塩水中で高い溶解度を維持できることを見出し、本手法に適した蛍光標識プローブの調製方法を確立した。
    (2) 細胞内分泌経路のイメージングに関する技術開発
    可逆的変性カチオン化により可溶化した分泌シグナル付きの前駆体の酵素タンパク質を生細胞内に導入すると、一部が培養上清中に活性構造の成熟型の酵素タンパク質が再分泌されることを酵素活性レベルで確認していたが、その収量はごく微量であった。この効率を改善するため、エンドソームから細胞質内への放出を促進する両親媒性ペプチドの併用条件を検討し、再分泌量が大幅に向上する条件を得た。さらにこの手法で回収された成熟型タンパク質を逆相HPLCを用いて高度に精製し、N末端配列を確認したところ、正しくプロセッシングを受けていることが確認され、翻訳系を伴わないpost-translational経路によるタンパク質の成熟化が可能なことを立証できた。

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  • ナノ構造体内部への高密度タンパク質封入に向けたタンパク質可溶化試薬の開発

    2007.06 - 2008.02

    特別電源所在県科学技術振興事業 

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  • Development of analytical and production method for problematic protein by artificial control of physical property of protein

    Grant number：19206085  2007 - 2010

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (A)  Grant-in-Aid for Scientific Research (A)

    YAMADA Hidenori, FUTAMI Jyunichirou, SENOO Masaharu, TADA Hiroko, KOSAKA Megumi

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    Grant amount：\40820000 （ Direct expense: \31400000 、 Indirect expense：\9420000 ）

    This study aimed development of handling technology especially for problematic protein using chemical conjugation techniques and protein crystallization methodology. Novel chemical modification reagent and optimization of protein preparation techniques provided improved transduction of transcription factor protein into cells, and solubilization of total cellular protein from cancer cells. Together with a newly developed protein crystallization tag sequence, these technologies will give a useful methodology for structure and functional analysis of proteins and their medical applications.

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  • Development and application of in cell folding technology based on reversible cationization of denatured proteins.

    Grant number：17360399  2005 - 2006

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (B)  Grant-in-Aid for Scientific Research (B)

    YAMADA Hidenori, FUTAMI Junichiro, SENO Masaharu, TADA Hiroko, KOSAKA Megumi

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    Grant amount：\15100000 （ Direct expense: \15100000 ）

    This project aimed for the development of two methodologies; first is efficient solubilization of denatured proteins with reversible protein chemical cationization techniques, and second is intracellular delivery of reversibly cationized proteins followed by simultaneous folding to the active conformations, called in cell folding techniques. As a model protein, we investigated human tumor-suppressor p53. Bacterially expressed p53 protein as insoluble inclusion body was successfully solubilized by introduction of polyethylenimine 600 (PEI600, molecular weight: 600) via disulfide bond. The analysis of resulted PEI600-SS-p53 revealed that six cysteins were conjugated by PEI600, but remaining four cysteins failed in conjugation of PEI600, probably because of steric hindrance. This result indicated that reversible blocking of remaining free sulfidryl groups by a small molecule of aminopropyl methanethiosulfonate is important for preparation of chemically stable samples. The 'in cell folding' of p53 was successfully demonstrated by treatment of p53-null Saos-2 cells with reversibly cationized p53. PEI600-SS-p53 treated cells revealed that all events examined as indications of the activation of p53 in cells, such as reduction of disulfide bonds followed by tetramer formation, localization into the nucleus, induction of p53 target genes, and induction of apoptosis of cells, occurred. Cationic charge dependent protein transduction efficiency was seen on the comparison between APS-SS-p53 (net charge: +6) and PEI600-SS-p53 (net charge: +81.6) because more cationic PEI600-SS-p53 showed more efficient induction of p53 targeted gene expression. This project also revealed that most of denatured proteins possessing cysteine residues can be solubilized by introduction of excess cationic charges. Furthermore, protein transduction and induction of their biological functions in living cells by using in cell folding techniques were confirmed by using at least 6 kinds of proteins.

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  • 細胞内ネットワークのダイナミズム解析技術開発

    2002.10 - 2007.03

    NEDO 

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    Authorship：Coinvestigator(s) 

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  • ヒト由来タンパク質をベースとした細胞特異的増殖阻害剤のデザイン

    Grant number：99J07764  1999 - 2001

    日本学術振興会  科学研究費助成事業 特別研究員奨励費  特別研究員奨励費

    二見 淳一郎

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    Grant amount：\4100000 （ Direct expense: \4100000 ）

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  • ヒト膵由来型リボヌクレアーゼの生理学的意義の解明と細胞特異的増殖阻害剤への応用

    Grant number：97J08759  1998

    日本学術振興会  科学研究費助成事業 特別研究員奨励費  特別研究員奨励費

    二見 淳一郎

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    Grant amount：\900000 （ Direct expense: \900000 ）

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  • Analytical Chemistry 2 （2020academic year） Second semester  - 水3,水4

  • Analytical Chemistry 2 （2020academic year） Fourth semester  - 水3～4

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  • English for Chemistry and Biotechnology 1 （2020academic year） 1st semester  - 水3,水4

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  • Physical Chemistry and Exercises 1 （2020academic year） 1st semester  - 月3,月4,水1,水2

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