Updated on 2026/03/05

写真a

 
Abe Tadashi
 
Organization
Department of Comprehensive Technical Solutions Senior Technical Manager
Position
Senior Technical Manager
External link

Research Areas

  • Life Science / Medical biochemistry

Research History

  • Okayama University   Medical School

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Professional Memberships

 

Papers

  • Vesicular Glutamate Transporter 3 Is Involved in Glutamatergic Signalling in Podocytes. International journal

    Naoko Nishii, Tomoko Kawai, Hiroki Yasuoka, Tadashi Abe, Nanami Tatsumi, Yuika Harada, Takaaki Miyaji, Shunai Li, Moemi Tsukano, Masami Watanabe, Daisuke Ogawa, Jun Wada, Kohji Takei, Hiroshi Yamada

    International journal of molecular sciences   26 ( 6 )   2025.3

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

    Glomerular podocytes act as a part of the filtration barrier in the kidney. The activity of this filter is regulated by ionotropic and metabotropic glutamate receptors. Adjacent podocytes can potentially release glutamate into the intercellular space; however, little is known about how podocytes release glutamate. Here, we demonstrated vesicular glutamate transporter 3 (VGLUT3)-dependent glutamate release from podocytes. Immunofluorescence analysis revealed that rat glomerular podocytes and an immortal mouse podocyte cell line (MPC) express VGLUT1 and VGLUT3. Consistent with this finding, quantitative RT-PCR revealed the expression of VGLUT1 and VGLUT3 mRNA in undifferentiated and differentiated MPCs. In addition, the exocytotic proteins vesicle-associated membrane protein 2, synapsin 1, and synaptophysin 1 were present in punctate patterns and colocalized with VGLUT3 in MPCs. Interestingly, approximately 30% of VGLUT3 colocalized with VGLUT1. By immunoelectron microscopy, VGLUT3 was often observed around clear vesicle-like structures in differentiated MPCs. Differentiated MPCs released glutamate following depolarization with high potassium levels and after stimulation with the muscarinic agonist pilocarpine. The depletion of VGLUT3 in MPCs by RNA interference reduced depolarization-dependent glutamate release. These results strongly suggest that VGLUT3 is involved in glutamatergic signalling in podocytes and may be a new drug target for various kidney diseases.

    DOI： 10.3390/ijms26062485

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  • Direct Binding of Synaptopodin 2-Like Protein to Alpha-Actinin Contributes to Actin Bundle Formation in Cardiomyocytes Reviewed

    Hiroshi Yamada, Hirona Osaka, Nanami Tatsumi, Miu Araki, Tadashi Abe, Keiko Kaihara, Ken Takahashi, Eizo Takashima, Takayuki Uchihashi, Keiji Naruse, Kohji Takei

    Cells   13 ( 16 )   1373 - 1373   2024.8

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

    Synaptopodin 2-like protein (SYNPO2L) is localized in the sarcomere of cardiomyocytes and is involved in heart morphogenesis. However, the molecular function of SYNPO2L in the heart is not fully understood. We investigated the interaction of SYNPO2L with sarcomeric α-actinin and actin filaments in cultured mouse cardiomyocytes. Immunofluorescence studies showed that SYNPO2L colocalized with α-actinin and actin filaments at the Z-discs of the sarcomere. Recombinant SYNPO2La or SYNPO2Lb caused a bundling of the actin filaments in the absence of α-actinin and enhanced the α-actinin-dependent formation of actin bundles. In addition, high-speed atomic force microscopy revealed that SYNPO2La directly bound to α-actinin via its globular ends. The interaction between α-actinin and SYNPO2La fixed the movements of the two proteins on the actin filaments. These results strongly suggest that SYNPO2L cooperates with α-actinin during actin bundle formation to facilitate sarcomere formation and maintenance.

    DOI： 10.3390/cells13161373

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  • 腎糸球体ポドサイトにおける細胞骨格ダイナミクスの解明

    竹居 孝二, 阿部 匡史, 竹田 哲也, 田邊 克幸, 山田 浩司

    日本生化学会大会プログラム・講演要旨集   96回   [2P - 659]   2023.10

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    Language：Japanese   Publisher：(公社)日本生化学会  

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  • TRPV2の細胞膜移行におけるダイナミン1による微小管制御の役割

    山田 浩司, 阿部 匡史, 竹田 哲也, 竹居 孝二

    日本生化学会大会プログラム・講演要旨集   96回   [2P - 660]   2023.10

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    Language：Japanese   Publisher：(公社)日本生化学会  

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  • 脂質膜結合活性が低下しているダイナミン2のCMT変異体は、ポドサイトにおけるアクチン線維の配向とアクチンバンドル形成を異常にする。

    山田 浩司, 阿部 匡史, 内橋 貴之, 成田 哲博, 竹田 哲也, 竹居 孝二

    日本生化学会大会プログラム・講演要旨集   95回   3P - 147   2022.11

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  • Recruitment of Irgb6 to the membrane is a direct trigger for membrane deformation

    Hiroshi Yamada, Tadashi Abe, Hikaru Nagaoka, Eizo Takashima, Ryo Nitta, Masahiro Yamamoto, Kohji Takei

    Frontiers in Cellular and Infection Microbiology   12   2022.9

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    Publishing type：Research paper (scientific journal)   Publisher：Frontiers Media SA  

    Irgb6 is a member of interferon γ-induced immunity related GTPase (IRG), and one of twenty “effector” IRGs, which coordinately attack parasitophorous vacuole membrane (PVM), causing death of intracellular pathogen. Although Irgb6 plays a pivotal role as a pioneer in the process of PVM disruption, the direct effect of Irgb6 on membrane remained to be elucidated. Here, we utilized artificial lipid membranes to reconstitute Irgb6-membrane interaction in vitro, and revealed that Irgb6 directly deformed the membranes. Liposomes incubated with recombinant Irgb6 were drastically deformed generating massive tubular protrusions in the absence of guanine nucleotide, or with GMP-PNP. Liposome deformation was abolished by incubating with Irgb6-K275A/R371A, point mutations at membrane targeting residues. The membrane tubules generated by Irgb6 were mostly disappeared by the addition of GTP or GDP, which are caused by detachment of Irgb6 from membrane. Binding of Irgb6 to the membrane, which was reconstituted in vitro using lipid monolayer, was stimulated at GTP-bound state. Irgb6 GTPase activity was stimulated by the presence of liposomes more than eightfold. Irgb6 GTPase activity in the absence of membrane was also slightly stimulated, by lowering ionic strength, or by increasing protein concentration, indicating synergistic stimulation of the GTPase activity. These results suggest that membrane targeting of Irgb6 and resulting membrane deformation does not require GTP, but converting into GTP-bound state is crucial for detaching Irgb6 from the membrane, which might coincident with local membrane disruption.

    DOI： 10.3389/fcimb.2022.992198

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  • Pacsin 2-dependent N-cadherin internalization regulates the migration behaviour of malignant cancer cells

    Haymar Wint, Jianzhen Li, Tadashi Abe, Hiroshi Yamada, Yasutomo Nasu, Masami Watanabe, Kohji Takei, Tetsuya Takeda

    2022.8

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  • Imaging‐based evaluation of pathogenicity by novel DNM2 variants associated with centronuclear myopathy Reviewed International journal

    Kenshiro Fujise, Mariko Okubo, Tadashi Abe, Hiroshi Yamada, Kohji Takei, Ichizo Nishino, Tetsuya Takeda, Satoru Noguchi

    Human Mutation   43 ( 2 )   169 - 179   2021.11

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

    A centronuclear myopathy (CNM) is a group of inherited congenital diseases showing clinically progressive muscle weakness associated with the presence of centralized myonuclei, diagnosed by genetic testing and muscle biopsy. The gene encoding dynamin 2, DNM2, has been identified as a causative gene for an autosomal dominant form of CNM. However, the information of a DNM2 variant alone is not always sufficient to gain a definitive diagnosis as the pathogenicity of many gene variants is currently unknown. In this study, we identified five novel DNM2 variants in our cohort. To establish the pathogenicity of these variants without using clinicopathological information, we used a simple in cellulo imaging-based assay for T-tubule-like structures to provide quantitative data that enable objective determination of pathogenicity by novel DNM2 variants. With this assay, we demonstrated that the phenotypes induced by mutant dynamin 2 in cellulo are well correlated with biochemical gain-of-function features of mutant dynamin 2 as well as the clinicopathological phenotypes of each patient. Our approach of combining an in cellulo assay with clinical information of the patients also explains the course of a disease progression by the pathogenesis of each variant in DNM2-associated CNM.

    DOI： 10.1002/humu.24307

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  • Mutant BIN1-Dynamin 2 complexes dysregulate membrane remodeling in the pathogenesis of centronuclear myopathy. International journal

    Kenshiro Fujise, Mariko Okubo, Tadashi Abe, Hiroshi Yamada, Ichizo Nishino, Satoru Noguchi, Kohji Takei, Tetsuya Takeda

    The Journal of biological chemistry   2020.11

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    Membrane remodeling is required for dynamic cellular processes such as cell division, polarization and motility. BAR domain proteins and dynamins are key molecules in membrane remodeling that work together for membrane deformation and fission. In striated muscles, sarcolemmal invaginations termed T-tubules are required for excitation-contraction coupling. BIN1 and DNM2, which encode a BAR domain protein BIN1 and dynamin 2, respectively, have been reported to be causative genes of centronuclear myopathy (CNM), a hereditary degenerative disease of skeletal muscle, and deformation of T-tubules is often observed in the CNM patients. However, it remains unclear how BIN1 and dynamin 2 are implicated in T-tubule biogenesis, and how mutations in these molecules cause CNM to develop.Here, using an in cellulo reconstitution assay, we demonstrate that dynamin 2 is required for stabilization of membranous structures equivalent to T-tubules. GTPase activity of wild type dynamin 2 is suppressed through interaction with BIN1, whereas that of the disease-associated mutant dynamin 2 remains active due to lack of the BIN1-mediated regulation thus causing aberrant membrane remodeling. Finally, we show that in cellulo aberrant membrane remodeling by mutant dynamin 2 variants is correlated with their enhanced membrane fission activities, and the results can explain severity of the symptoms in patients. Thus, this study provides molecular insights into dysregulated membrane remodeling triggering the pathogenesis of DNM2-related centronuclear myopathy.

    DOI： 10.1074/jbc.RA120.015184

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  • Dynamin 1 is important for microtubule organization and stabilization in glomerular podocytes

    The Mon La, Hiromi Tachibana, Shun‐Ai Li, Tadashi Abe, Sayaka Seiriki, Hikaru Nagaoka, Eizo Takashima, Tetsuya Takeda, Daisuke Ogawa, Shin‐ichi Makino, Katsuhiko Asanuma, Masami Watanabe, Xuefei Tian, Shuta Ishibe, Ayuko Sakane, Takuya Sasaki, Jun Wada, Kohji Takei, Hiroshi Yamada

    The FASEB Journal   34 ( 12 )   16449 - 16463   2020.10

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    Publishing type：Research paper (scientific journal)   Publisher：Wiley  

    DOI： 10.1096/fj.202001240rr

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    Other Link： https://onlinelibrary.wiley.com/doi/full-xml/10.1096/fj.202001240RR

  • Internalization of AMPA-type Glutamate Receptor in the MIN6 Pancreatic β-cell Line. Reviewed

    The Mon La, Hiroshi Yamada, Sayaka Seiriki, Shun-Ai Li, Kenshiro Fujise, Natsuho Katsumi, Tadashi Abe, Masami Watanabe, Kohji Takei

    Cell structure and function   45 ( 2 )   121 - 130   2020.8

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    The activity of AMPA-type glutamate receptor is involved in insulin release from pancreatic β-cells. However, the mechanism and dynamics that underlie AMPA receptor-mediated insulin release in β-cells is largely unknown. Here, we show that AMPA induces internalization of glutamate receptor 2/3 (GluR2/3), AMPA receptor subtype, in the mouse β-cell line MIN6. Immunofluorescence experiments showed that GluR2/3 appeared as fine dots that were distributed throughout MIN6 cells. Intracellular GluR2/3 co-localized with AP2 and clathrin, markers for clathrin-coated pits and vesicles. Immunoelectron microscopy revealed that GluR2/3 was also localized at plasma membrane. Surface biotinylation and immunofluorescence measurements showed that addition of AMPA caused an approximate 1.8-fold increase in GluR2/3 internalization under low-glucose conditions. Furthermore, internalized GluR2 largely co-localized with EEA1, an early endosome marker. In addition, GluR2/3 co-immunoprecipitated with cortactin, a F-actin binding protein. Depletion of cortactin by RNAi in MIN6 cells altered the intracellular distribution of GluR2/3, suggesting that cortactin is involved in internalization of GluR2/3 in MIN6 cells. Taken together, our results suggest that pancreatic β-cells adjust the amount of AMPA-type GluR2/3 on the cell surface to regulate the receptive capability of the cell for glutamate.Key words: endocytosis, GluR2, AMPA, cortactin, MIN6.

    DOI： 10.1247/csf.20020

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  • Phosphorylation of cortactin by cyclin-dependent kinase 5 modulates actin bundling by the dynamin 1-cortactin ring-like complex and formation of filopodia and lamellipodia in NG108-15 glioma-derived cells. Reviewed International journal

    Tadashi Abe, The Mon La, Yuuzi Miyagaki, Eri Oya, Fan-Yan Wei, Kento Sumida, Kenshiro Fujise, Tetsuya Takeda, Kazuhito Tomizawa, Kohji Takei, Hiroshi Yamada

    International journal of oncology   54 ( 2 )   550 - 558   2019.2

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    Dynamin copolymerizes with cortactin to form a ring‑like complex that bundles and stabilizes actin filaments. Actin bundle formation is crucial for generation of filopodia and lamellipodia, which guide migration, invasion, and metastasis of cancer cells. However, it is unknown how the dynamin‑cortactin complex regulates actin bundle formation. The present study investigated phosphorylation of cortactin by cyclin‑dependent kinase 5 (CDK5) and its effect on actin bundle formation by the dynamin‑cortactin complex. CDK5 directly phosphorylated cortactin at T145/T219 in vitro. Phosphomimetic mutants in which one or both of these threonine residues was substituted by aspartate were used. The three phosphomimetic mutants (T145D, T219D and T145DT219D) had a decreased affinity for F‑actin. Furthermore, electron microscopy demonstrated that these phosphomimetic mutants could not form a ring‑like complex with dynamin 1. Consistently, the dynamin 1‑phosphomimetic cortactin complexes exhibited decreased actin‑bundling activity. Expression of the phosphomimetic mutants resulted in not only aberrant lamellipodia and short filopodia but also cell migration in NG108‑15 glioma‑derived cells. These results indicate that phosphorylation of cortactin by CDK5 regulates formation of lamellipodia and filopodia by modulating dynamin 1/cortactin‑dependent actin bundling. Taken together, these findings suggest that CDK5 is a potential molecular target for anticancer therapy.

    DOI： 10.3892/ijo.2018.4663

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  • メカノエンザイム・ダイナミンGTPaseによるアクチン線維束化機構の解析

    山田 浩司, 阿部 匡史, 竹田 哲也, 高島 英造, 森田 将之, 竹居 孝二

    日本生物工学会大会講演要旨集   平成30年度   122 - 122   2018.8

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  • Dynamic clustering of dynamin-amphiphysin helices regulates membrane constriction and fission coupled with GTP hydrolysis Reviewed

    Tetsuya Takeda, Toshiya Kozai, Huiran Yang, Daiki Ishikuro, Kaho Seyama, Yusuke Kumagai, Tadashi Abe, Hiroshi Yamada, Takayuki Uchihashi, Toshio Ando, Kohji Takei

    eLife   7   2018.1

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    Language：English   Publishing type：Research paper (scientific journal)   Publisher：eLife Sciences Publications Ltd  

    DOI： 10.7554/eLife.30246

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  • Actin bundling by dynamin 2 and cortactin is implicated in cell migration by stabilizing filopodia in human non-small cell lung carcinoma cells Reviewed

    Hiroshi Yamada, Tetsuya Takeda, Hiroyuki Michiue, Tadashi Abe, Kohji Takei

    INTERNATIONAL JOURNAL OF ONCOLOGY   49 ( 3 )   877 - 886   2016.9

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    DOI： 10.3892/ijo.2016.3592

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  • Possible role of cortactin phosphorylation by protein kinase C in actin-bundle formation at growth cone Reviewed

    Hiroshi Yamada, Tatsuya Kikuchi, Toshio Masumoto, Fan-Yan Wei, Tadashi Abe, Tetsuya Takeda, Teiichi Nishiki, Kazuhito Tomizawa, Masami Watanabe, Hideki Matsui, Kohji Takei

    BIOLOGY OF THE CELL   107 ( 9 )   319 - 330   2015.9

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    DOI： 10.1111/boc.201500032

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  • N '[4-(dipropylamino)benzylidene]-2-hydroxybenzohydrazide is a dynamin GTPase inhibitor that suppresses cancer cell migration and invasion by inhibiting actin polymerization Reviewed

    Hiroshi Yamada, Tadashi Abe, Shun-Ai Li, Shota Tago, Peng Huang, Masami Watanabe, Satoru Ikeda, Naohisa Ogo, Akira Asai, Kohji Takei

    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS   443 ( 2 )   511 - 517   2014.1

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    DOI： 10.1016/j.bbrc.2013.11.118

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  • Stabilization of actin bundles by a dynamin 1/cortactin ring complex is necessary for growth cone filopodia. Reviewed International journal

    Hiroshi Yamada, Tadashi Abe, Ayano Satoh, Nana Okazaki, Shota Tago, Kinue Kobayashi, Yumi Yoshida, Yoshiya Oda, Masami Watanabe, Kazuhito Tomizawa, Hideki Matsui, Kohji Takei

    The Journal of neuroscience : the official journal of the Society for Neuroscience   33 ( 10 )   4514 - 26   2013.3

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    Dynamin GTPase, a key molecule in endocytosis, mechanically severs the invaginated membrane upon GTP hydrolysis. Dynamin functions also in regulating actin cytoskeleton, but the mechanisms are yet to be defined. Here we show that dynamin 1, a neuronal isoform of dynamin, and cortactin form ring complexes, which twine around F-actin bundles and stabilize them. By negative-staining EM, dynamin 1-cortactin complexes appeared as "open" or "closed" rings depending on guanine nucleotide conditions. By pyrene actin assembly assay, dynamin 1 stimulated actin assembly in mouse brain cytosol. In vitro incubation of F-actin with both dynamin 1 and cortactin led to the formation of long and thick actin bundles, on which dynamin 1 and cortactin were periodically colocalized in puncta. A depolymerization assay revealed that dynamin 1 and cortactin increased the stability of actin bundles, most prominently in the presence of GTP. In rat cortical neurons and human neuroblastoma cell line, SH-SY5Y, both dynamin 1 and cortactin localized on actin filaments and the bundles at growth cone filopodia as revealed by immunoelectron microscopy. In SH-SY5Y cell, acute inhibition of dynamin 1 by application of dynamin inhibitor led to growth cone collapse. Cortactin knockdown also reduced growth cone filopodia. Together, our results strongly suggest that dynamin 1 and cortactin ring complex mechanically stabilizes F-actin bundles in growth cone filopodia. Thus, the GTPase-dependent mechanochemical enzyme property of dynamin is commonly used both in endocytosis and regulation of F-actin bundles by a dynamin 1-cortactin complex.

    DOI： 10.1523/JNEUROSCI.2762-12.2013

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  • Use of liposomes to study vesicular transport. Reviewed International journal

    Kohji Takei, Hiroshi Yamada, Tadashi Abe

    Methods in molecular biology (Clifton, N.J.)   606   531 - 42   2010

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    Liposomes have been utilized for variety of membrane transport studies including clathrin-mediated endocytosis. Here we introduce clathrin-coated structures that are generated on large unilamellar liposomes by incubating with clathrin coat proteins. Large unilamellar liposomes are also used to reconstitute vesicle formation in a cell-free system, and the vesicle formation can be quantified by using dynamic light scattering (DLS). Furthermore, phagocytosis assay using liposome-conjugated styrene beads is demonstrated.

    DOI： 10.1007/978-1-60761-447-0_36

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  • Dynasore, a dynamin inhibitor, suppresses lamellipodia formation and cancer cell invasion by destabilizing actin filaments Reviewed

    Hiroshi Yamada, Tadashi Abe, Shun-Ai Li, Yuki Masuoka, Mihoko Isoda, Masami Watanabe, Yasutomo Nasu, Hiromi Kumon, Akira Asai, Kohji Takei

    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS   390 ( 4 )   1142 - 1148   2009.12

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

    DOI： 10.1016/j.bbrc.2009.10.105

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  • Dynamin 2 is required for actin assembly in phagocytosis in Sertoli cells Reviewed

    Atsushi Otsuka, Tadashi Abe, Masami Watanabe, Hitoshi Yagisawa, Kohji Takei, Hiroshi Yamada

    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS   378 ( 3 )   478 - 482   2009.1

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    DOI： 10.1016/j.bbrc.2008.11.066

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  • Dynamin 2 Cooperates with Amphiphysin 1 in Phagocytosis in Sertoli Cells Reviewed

    Akira Nakanishi, Tadashi Abe, Masami Watanabe, Kohji Takei, Hiroshi Yamada

    ACTA MEDICA OKAYAMA   62 ( 6 )   385 - 391   2008.12

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    DOI： 10.18926/AMO/30954

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  • Amphiphysin 1 is important for actin polymerization During phagocytosis Reviewed

    Hiroshi Yamada, Emiko Ohashi, Tadashi Abe, Norihiro Kusumi, Shun-AI Li, Yumi Yoshida, Masami Watanabe, Kazuhito Tomizawa, Yuji Kashiwakura, Hiromi Kumon, Hideki Matsui, Kohji Takei

    MOLECULAR BIOLOGY OF THE CELL   18 ( 11 )   4669 - 4680   2007.11

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    DOI： 10.1091/mbc.E07-04-0296

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  • Major Cdk5-dependent phosphorylation sites of amphiphysin 1 are implicated in the regulation of the membrane binding and endocytosis Reviewed

    Shuang Liang, Fan-Yan Wei, Yu-Mei Wu, Kenji Tanabe, Tadashi Abe, Yoshiya Oda, Yumi Yoshida, Hiroshi Yamada, Hideki Matsui, Kazuhito Tomizawa, Kohji Takei

    JOURNAL OF NEUROCHEMISTRY   102 ( 5 )   1466 - 1476   2007.9

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    DOI： 10.1111/j.1471-4159.2007.04507.x

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  • The stimulatory action of amphiphysin on dynamin function is dependent on lipid bilayer curvature Reviewed

    Y Yoshida, M Kinuta, T Abe, S Liang, K Araki, O Cremona, G Di Paolo, Y Moriyama, T Yasuda, P De Camilli, K Takei

    EMBO JOURNAL   23 ( 17 )   3483 - 3491   2004.9

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    DOI： 10.1038/sj.emboj.7600355

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  • Formation of meso, N-diphenylprotoporphyrin IX by an aerobic reaction of phenylhydrazine with oxyhemoglobins Reviewed

    A Nakanishi, K Kinuta, T Abe, K Araki, Y Yoshida, S Liang, SA Li, K Takei, M Kinuta

    ACTA MEDICA OKAYAMA   57 ( 5 )   249 - 256   2003.10

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    DOI： 10.18926/AMO/32823

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  • Formation of S-[2-carboxy-1-(1H-imidazol-4-yl) ethyl]glutathione, a new metabolite of L-histidine, from cis-urocanic acid and glutathione by the action of glutathione S-transferase Reviewed

    M Kinuta, K Kinuta, H Yamada, T Abe, Y Yoshida, K Araki, SA Li, A Otsuka, A Nakanishi, Y Moriyama, K Takei

    ELECTROPHORESIS   24 ( 18 )   3212 - 3218   2003.9

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    DOI： 10.1002/elps.200305582

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  • Characterization of hydrogen peroxide removal reaction by hemoglobin in the presence of reduced pyridine nucleotides. Reviewed

    Masuoka N, Kodama H, Abe T, Wang DH, Nakano T

    Biochimica et biophysica acta   1637 ( 1 )   46 - 54   2003.1

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  • Phosphatidylinositol 4,5-bisphosphate stimulates vesicle formation from liposomes by brain cytosol Reviewed

    M Kinuta, H Yamada, T Abe, M Watanabe, SA Li, A Kamitani, T Yasuda, T Matsukawa, H Kumon, K Takei

    PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA   99 ( 5 )   2842 - 2847   2002.3

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    DOI： 10.1073/pnas.261715599

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  • Determination of S-[2-carboxy-1-(1H-imidazol-4-yl)ethyl]glutathione, a novel metabolite of L-histidine, in tissue extracts from sunlight-irradiated rat by capillary electrophoresis

    M Kinuta, J Ohta, H Yamada, K Kinuta, T Abe, SA Li, A Otsuka, A Nakanishi, K Takei

    ELECTROPHORESIS   22 ( 16 )   3365 - 3370   2001.10

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    DOI： 10.1002/1522-2683(200109)22:16<3365::AID-ELPS3365>3.0.CO;2-M

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  • Excretion of Sulfate and Taurine in Rats Fed with a High Protein Diet

    Yukihiro Keishi, Tomozawa Masaru, Abe Tadashi, Yao Wen-Bin, Ohta Jun, Ubuka Toshihiko

    Acta Medica Okayama   52 ( 2 )   71 - 75   1998.4

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    Language：English   Publisher：Okayama University Medical School  

    DOI： 10.18926/AMO/31315

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  • Excretion of Taurine and Sulfate in Rats Fed with a Low Protein Diet

    Tomozawa Masaru, Yukihiro Keishi, Yao Wen-Bin, Abe Tadashi, Ohta Jun, Ubuka Toshihiko

    Acta Medica Okayama   52 ( 2 )   77 - 81   1998.4

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    Language：English   Publisher：Okayama University Medical School  

    DOI： 10.18926/AMO/31312

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  • A method for determination of total glutathione and total cysteine as S-carboxymethyl derivatives by using an amino acid analyzer, and its application to samples from rat liver, kidney and blood after intraperitoneal administration of 2-(4-carboxy-D-gluco-tetrahydroxybutyl)thiazolidine-4-carboxylic acid.

    Zhao Yuan-Qing, Kinuta Masahiro, Abe Tadashi, Yao Wen-Bin, Ubuka Toshihiko

    Acta Medica Okayama   49 ( 1 )   35 - 42   1995.2

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    Language：English   Publisher：Okayama University Medical School  

    DOI： 10.18926/AMO/30413

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  • 腎糸球体ポドサイトにおけるアンフィファイジン1の機能

    山田浩司, LA The Mon, 竹田哲也, 阿部匡史, 淺沼克彦, 竹居孝二

    日本生化学会大会(Web)   92nd   2019

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  • 腎糸球体ポドサイトにおけるダイナミンイソフォームの局在と機能

    阿部匡史, LA The Mon, 橘洋美, 竹田哲也, 竹居孝二, 山田浩司

    日本生化学会大会(Web)   92nd   2019

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  • メカノエンザイム・ダイナミンGTPaseによるアクチン線維束化機構の解析

    山田 浩司, 阿部 匡史, 竹田 哲也, 高島 英造, 森田 将之, 竹居 孝二

    日本生物工学会大会講演要旨集   平成30年度   122 - 122   2018.8

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  • ダイナミン2のシャルコー・マリー・トゥース病の原因変異とアクチン再構成との相関

    隅田健斗, LA The Mon, 和木田夏輝, 森田将之, 高島英造, 竹田哲也, 阿部匡史, 竹居孝二, 山田浩司

    日本分子生物学会年会プログラム・要旨集(Web)   41st   2018

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  • エンドサイトーシス生物学の新展開 ダイナミンによる膜切断過程の動態イメージング

    竹田 哲也, 小財 稔矢, 楊 恵然, 石黒 大輝, 背山 佳穂, 熊谷 祐介, 阿部 匡史, 山田 浩司, 内橋 貴之, 安藤 敏夫, 竹居 孝二

    生命科学系学会合同年次大会   2017年度   [4AW17 - 2]   2017.12

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  • ダイナミン2のシャルコー・マリー・トゥース病の原因変異は腎ポドサイトのアクチン再構成を阻害する

    和木田 夏輝, La The Mon, 隅田 健斗, 竹田 哲也, 阿部 匡史, 竹居 孝二, 山田 浩司

    生命科学系学会合同年次大会   2017年度   [2P - 1089]   2017.12

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  • "Clusterase" model of dynamin-mediated membrane fission.

    Takeda T, Kozai T, Yang H, Kaho S, Yusuke K, Tadashi A, Hiroshi Y, Uchihashi T, Ando T, Takei K

    MOLECULAR BIOLOGY OF THE CELL   28   .   2017

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  • ダイナミン-コルタクチンらせん状複合体の解析:機械的なアクチン線維束形成とアクチン脱重合保護作用

    阿部匡史, 山田浩司, 竹田哲也, 内橋貴之, 安藤敏夫, 竹居孝二

    日本生化学会大会(Web)   90th   2017

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  • 成長円錐におけるPKCαのコルタクチンリン酸化によるアクチン制御の可能性

    山田 浩司, 菊池 達也, 増本 年男, 魏 范研, 阿部 匡史, 竹田 哲也, 西木 禎一, 富澤 一仁, 渡部 昌実, 松井 秀樹, 竹居 孝二

    日本生化学会大会・日本分子生物学会年会合同大会講演要旨集   88回・38回   [1P1328] - [1P1328]   2015.12

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  • 肺がん細胞株における細胞運動を司るダイナミン2によるアクチン動態制御

    阿部匡史, 山田浩司, 竹田哲也, 竹居孝二

    日本生化学会大会(Web)   87th   2014

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  • Dynaminを標的にした抗がん剤の開発

    岡崎奈奈, 阿部匡史, 有田美香子, 多湖翔太, 永井さや, 池田敏, 小郷尚久, 浅井章良, 山田浩司, 竹居孝二

    日本生化学会大会(Web)   85th   2012

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  • ダイナミンGTPアーゼ/コルタクチン複合体はアクチン線維束を安定化するメカニカルデバイスである

    山田浩司, 阿部匡史, 竹居孝二

    日本生体エネルギー研究会討論会講演要旨集   38th   2012

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  • 成長円錐糸状仮足形成におけるCortactinのPKCalphaによるリン酸化とアクチン制御の可能性

    山田 浩司, 勢井 麻梨, 阿部 匡史, 増本 年男, 菊池 達也, 富澤 一仁, 池田 敏, 松井 秀樹, 竹居 孝二

    日本生化学会大会プログラム・講演要旨集   84回   2P - 0345   2011.9

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  • ダイナミン・コルタクチン複合体はアクチン線維を束化し、この束化は成長円錐の糸状仮足形成に重要である

    山田 浩司, 阿部 匡史, 竹居 孝二

    日本薬学会年会要旨集   131年会 ( 3 )   152 - 152   2011.3

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  • PKC phosphorylation of cortactin is implicated in the regulation of actin dynamics

    H. Yamada, T. Abe, T. Masumoto, M. Sei, T. Kikuchi, K. Tomizawa, S. Ikeda, H. Matsui, K. Takei

    MOLECULAR BIOLOGY OF THE CELL   22   2011

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  • ダイナミン1/コルタクチン複合体はアクチン線維束を形成し、成長円錐フィロポディア形成を支持する(Dynamin 1/cortactin complex mechanically bundles actin filaments and supports the formation of growth cone filopodia)

    竹居 孝二, 阿部 匡史, 川田 慎浩, 山田 浩司

    神経化学   49 ( 2-3 )   501 - 501   2010.8

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  • Dynamin 1/cortactin complex mechanically bundles actin filaments and supports the formation of growth cone filopodia

    Kohji Takei, Tadashi Abe, Yoshihiro Kawada, Hiroshi Yamada

    NEUROSCIENCE RESEARCH   68   E88 - E88   2010

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    DOI： 10.1016/j.neures.2010.07.156

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  • ダイナミン/コルタクチン複合体によるアクチン束化は糸状仮足形成と関連がある(Actin bundling by dynamin/cortactin complex is implicated in filopodia formation)

    山田 浩司, 阿部 匡史, 川田 慎浩, 竹居 孝二

    日本生化学会大会プログラム・講演要旨集   82回   3P - 372   2009.9

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  • ダイナミン/コルタクチン複合体によるアクチン束形成の新しいメカニズム 糸状仮足形成における意義(Novel mechanism of actin bundle formation by dynamin/cortactin complex: its implication in filopodia formation)

    山田 浩司, 阿部 匡史, 吉田 祐実, 竹居 孝二

    日本細胞生物学会大会講演要旨集   61回   175 - 175   2009.5

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  • ダイナミン1は、コルタクチンとともに、アクチンの動態に働く(Dynamin 1 participates in actin dynamics with cortactin)

    信崎 哲郎, 吉田 祐実, 阿部 匡史, 小田 吉哉, 富沢 一仁, 山田 浩司, 竹居 孝二

    日本細胞生物学会大会講演要旨集   60回   100 - 100   2008.6

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  • D_035 Proposal of clustering system to content of complaint receipt

    ABE Tadashi

    5 ( 2 )   81 - 82   2006.8

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  • Analysis of the major cdk5 phosphorylation sites of amphiphysin 1 Reviewed

    Shuang Liang, Yumi Yoshida, Kazuhito Tomizawa, Tadashi Abe, Hiroshi Yamada, Hideki Matsui, Kohji Takei

    CELL STRUCTURE AND FUNCTION   30   70 - 70   2005.6

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  • Stimulatory action of amphiphysin 1 on dynamin function and dependence on bilayer curvature Reviewed

    Yumi Yoshida, Tadashi Abe, Shuang Liang, Kenta Araki, Pietro De Camilli, Kohji Takei, Masahiro Kinuta

    CELL STRUCTURE AND FUNCTION   29   110 - 110   2004.5

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  • Dynamin及びAmphiphysinのリン酸化-脱リン酸化による小胞形成能変化

    絹田 正裕, 荒木 健太, 阿部 匡史, 梁 爽, 吉田 祐美, 山田 浩司, 永松 知洋, 富澤 一仁, 松井 秀樹, 保田 立二, 竹居 孝二

    生化学   76 ( 3 )   307 - 307   2004.3

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  • 小胞形成に対するdynamin及びamphiphysinのリン酸化-脱リン酸化の効果

    荒木 健太, 阿部 匡史, 福田 功, 富澤 一仁, 山田 浩司, 須田 城, 絹田 正裕, 竹居 孝二

    日本細胞生物学会大会講演要旨集   56回   52 - 52   2003.5

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  • Effects of phosphorylation of dynamin and amphiphysin on vesicle formations from liposomes

    M Kinuta, K Tomizawa, T Abe, Fukuta, I, H Matsui, K Takei

    MOLECULAR BIOLOGY OF THE CELL   13   95A - 95A   2002.11

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  • ARF6によるPI(4)P5-kinaseの活性化機構

    福田 功, 絹田 正裕, 芝 直基, 重歳 正尚, 阿部 匡史, Volker Haucke, 竹居 孝二

    生化学   74 ( 8 )   895 - 895   2002.8

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  • Arf6によるPI(4)P 5-kinaseの活性化機構

    芝 直基, 重歳 正尚, 絹田 正裕, 阿部 匡史, 福田 功, Haucke Volker, 竹居 孝二

    日本細胞生物学会大会講演要旨集   55回   51 - 51   2002.5

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  • PtdIns(4,5)P2の分解とエンドサイトーシス

    山田 浩司, 絹田 正裕, 阿部 匡史, 李 順愛, 渡部 昌美, 紙谷 章弘, 公文 裕巳, 竹居 孝二

    神経化学   40 ( 2-3 )   331 - 331   2001.9

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  • エンドサイトーシスにおけるPtdIns(4,5)P2の分解

    絹田 正裕, 山田 浩司, 阿部 匡史, 李 順愛, 渡部 昌実, 紙谷 章弘, 公文 裕巳, 竹居 孝二

    日本細胞生物学会大会講演要旨集   54回   81 - 81   2001.5

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  • 含硫アミノ酸代謝に関する研究(4) 日本人における硫酸及びタウリンの尿中排泄について

    産賀 敏彦, 中村 博範, 梶川 梨恵, 森野 勝也, 武政 睦子, 阿部 匡史

    日本栄養・食糧学会大会講演要旨集   55回   174 - 174   2001.4

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  • Vesicle formation and membrane lipid kinetics in model synaptic endocytosis using liposomes.

    M Kinuta, H Yamada, T Abe, M Watanabe, J Ohta, K Takei

    MOLECULAR BIOLOGY OF THE CELL   11   326A - 326A   2000.12

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  • 含硫アミノ酸代謝に関する研究(2) ガスクロマトグラフィー及びイオンクロマトグラフィーによる生物試料中H2S及びacid-labile sulfideの定量

    産賀 敏彦, 阿部 匡史

    生化学   72 ( 8 )   770 - 770   2000.8

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  • 細胞膜のダイナミックス エンドサイトーシスにおける細胞膜脂質の動態

    竹居 孝二, 絹田 正裕, 阿部 匡史, 山田 浩司, 太田 潤, 渡部 昌実

    日本細胞生物学会大会講演要旨集   53回   42 - 42   2000.8

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  • リポソームを用いたエンドサイトーシスのモデル実験と膜脂質の動態

    絹田 正裕, 阿部 匡史, 山田 浩司, 太田 潤, 渡部 昌実, ラタナクル・ニシャ, 竹居 孝二

    日本細胞生物学会大会講演要旨集   53回   101 - 101   2000.8

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  • 含硫アミノ酸代謝に関する研究(1) 含硫アミノ酸代謝に対する食餌タンパク質(カゼイン)濃度の影響

    産賀 敏彦, 阿部 匡史, 姚 文彬, 友澤 賢, 行廣 圭史

    日本栄養・食糧学会大会講演要旨集   54回   260 - 260   2000.4

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  • 天然の非タンパク性アミノ酸の代謝におけるγ-グルタミルシステイン合成酵素の役割について

    太田 潤, 阿部 匡史, 益岡 典芳, 絹田 正裕, 児玉 裕敬

    生化学   71 ( 8 )   1012 - 1012   1999.8

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  • 赤血球による過酸化水素の分解について(6) ヘモグロビンによる分解活性の性質

    益岡 典芳, 太田 潤, 阿部 匡史, 中野 琢

    生化学   71 ( 8 )   748 - 748   1999.8

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  • プロパルギルグリシン投与ラット肝臓内に増加するグルタチオン類似体について

    太田 潤, 永峰 昇, 阿部 匡史, 姚 文彬, 益岡 典芳, 絹田 正裕, 児玉 裕敬, 産賀 敏彦

    生化学   70 ( 12 )   1479 - 1479   1998.12

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  • ヒト赤血球によるL-γ-glutamyl-L-propargylglycyl-glycine生成のキネティクス

    永峰 昇, 太田 潤, 阿部 匡史, 姚 文彬, 児玉 裕敬, 産賀 敏彦

    生化学   70 ( 8 )   970 - 970   1998.8

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  • 高蛋白食給餌ラットにおける硫酸塩及びタウリンの排泄

    行廣 圭史, 友澤 賢, 阿部 匡史

    Acta Medica Okayama   52 ( 2 )   71 - 75   1998.4

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    硫酸塩及びタウリンはL-システインの主要代謝産物で尿中に排泄される.排泄されるタウリン/硫酸塩の比率に対する高蛋白食の効果を25%(通常蛋白群,グループA)及び40%(高蛋白群,グループB)カゼインをラットに給餌することにより解析した.その結果,グループAの平均比率が0.30±0.08であるのに対し,グループBの平均比率は0.22±0.07であった.このことから,タウリンと硫酸塩の産生する割合は食餌中の蛋白量によって決定され,高蛋白摂取時は硫酸塩の産生の方が大きいことが示唆された

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  • システイン前駆体に関する研究(4)ラット肝再生に対するGlucose-Cysteine(Glc-Cys)及び N-Acetylcysteine(NAC)の影響

    姚 文彬, 阿部 匡史, 太田 潤, 行廣 圭史, 友澤 賢, 産賀 敏彦, 馬 玉祥, 岡田 茂

    日本分子生物学会年会プログラム・講演要旨集   19   107 - 107   1996.8

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  • ジスルフィドに関する研究 (11)プロテインジスルフィドイソメラーゼ(PDI)による修飾リボヌクレアーゼAの再生

    産賀 敏彦, 黒住 吉篤, 阿部 匡史, 姚 文彬, 友澤 賢, 行廣 圭史

    日本分子生物学会年会プログラム・講演要旨集   19   107 - 107   1996.8

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  • ブロパルギルグリシン投与後のラット肝臓内γ-glutamyl-(propargylglycyl)glycineの変動

    太田 潤, 産賀 敏彦, 永峰 昇, 児玉 裕敬, 管原 和宣, 姚 文彬, 阿部 匡史

    日本分子生物学会年会プログラム・講演要旨集   19   107 - 107   1996.8

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  • Studies on sulfur-containing amino acids

    UBUKA Toshihiko, YAO Kenzaburoh, MASUOKA Noriyoshi, KINUTA Masahiro, OHTA Jun, YAO Wen-Bin, ABE Tadashi

    Okayama Igakkai Zasshi (Journal of Okayama Medical Association)   103 ( 3 )   55 - 65   1991

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    Studies on sulfur-containing amino acids performed in our department were reviewed. The subjects discussed were: (1) cysteine metabolism via 3-mercaptopyruvate pathway, (2) the chemical modification of a protein with glutathione or cysteine, (3) developments of analytical methods for sulfur compounds and sialic acid, and (4) the sulfur balance in the animal body. In section 1, 3-mercaptolactate-cysteine mixed disulfide (HCETC), mercaptoacetate-cysteine mixed disulfide, &amp;beta;-mercaptolactate cysteine disulfiduria, 3-mercaptopyruvate pathway, biosynthesis of HCETC, sulfate formation in mitochondria and &amp;beta;-[(carboxymethyl) thio]-1H-imidazole-4-propanoic acid were discussed. Preparation and properties of ribonuclease A-glutathione mixed disulfide and ribonuclease A-cysteine mixed disulfide were discussed in section 2.

    DOI： 10.4044/joma1947.103.3_55

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  • 電解質と微量元素の臨床検査ガイド 生体に必要な元素 硫黄(S)

    産賀 敏彦, 益岡 典芳, 阿部 匡史

    臨床検査   34 ( 11 )   1436 - 1441   1990.10

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    DOI： 10.11477/mf.1542900347

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Presentations

  • ダイナミン-コルタクチンらせん状複合体の解析 機械的なアクチン線維束形成とアクチン脱重合保護作用

    阿部 匡史, 山田 浩司, 竹田 哲也, 内橋 貴之, 安藤 敏夫, 竹居 孝二

    生命科学系学会合同年次大会  2017.12 

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  • 肺がん細胞株における細胞運動を司るダイナミン2によるアクチン動態制御

    阿部 匡史, 山田 浩司, 竹田 哲也, 竹居 孝二

    日本生化学会大会プログラム・講演要旨集  2014.10 

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    Language：Japanese   Presentation type：Poster presentation  

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  • N'-(4-(diethylamino(benzylidene)-4-methoxybenzohydrazide)はdynamin GTPase阻害分子でありアクチンの重合抑制により癌細胞の遊走と浸潤を阻害する(N'-(4-(diethylamino)benzylidene)-4-methoxybenzohydrazide is a dynamin GTPase inhibitor and suppresses cancer cell migration and invasion by inhibitin

    阿部 匡史, 渡部 昌実, 池田 敏, 小郷 尚久, 浅井 章良, 竹居 孝二, 山田 浩司

    日本生化学会大会プログラム・講演要旨集  2013.9 

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  • β-アミノ酸代謝に関する研究(3)PR-HPLCによるβ-alanine,β-aminoisobutyric acid,γ-aminobutyric acidの同時定量

    阿部 匡史, 黒住 吉篤, 姚 文彬, 吉田 繁子, 産賀 敏彦

    生化学  1998.8 

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Research Projects

  • 骨形成ネットワークを支えるダイナミンによる新規細胞骨格制御機構の解明

    Grant number：25K12951  2025.04 - 2028.03

    日本学術振興会  科学研究費助成事業  基盤研究(C)

    阿部 匡史, 岡村 裕彦, 池亀 美華, 山田 浩司

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    Grant amount：\4550000 （ Direct expense: \3500000 、 Indirect expense：\1050000 ）

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  • がん細胞の浸潤転移を制御するダイナミンクロスブリッジ機構の解析

    Grant number：22K06580  2022.04 - 2025.03

    日本学術振興会  科学研究費助成事業  基盤研究(C)

    阿部 匡史, 山田 浩司

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    Grant amount：\4030000 （ Direct expense: \3100000 、 Indirect expense：\930000 ）

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  • Elucidation of the function of novel actin-binding factors in neutrophil phagocytosis and extracellular trap formation

    Grant number：19K07084  2019.04 - 2022.03

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

    ABE TADASHI

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    Authorship：Principal investigator 

    Grant amount：\4420000 （ Direct expense: \3400000 、 Indirect expense：\1020000 ）

    Neutrophils play an essential role in the destruction of bacteria in innate immune system. In the process of killing pathogens, neutrophils drastically change their cell shape with accompanying the rearrangement of actin cytoskeleton. We found that expressing dynamin 2 K562E mutant, one of the pathogenic mutations in Charcot-Marie-Tooth disease in cells leads to aberrant actin clusters and stress fibers. The effect of this mutant on actin fibers was analyzed in vitro. Recombinant dynamin 2 K562E showed lower self-assembly ability and membrane binding ability than that of dynamin 2 wildtype. Although dynamin K562E directly bundled actin filaments, the formed bundles showed much less ability to bind to the lipid membranes as compared to dynamin 2 wildtype. In conclusion, dynamin 2-mediated interactions between actin and membranes are critical for actin bundle formation in neutrophil functions.

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  • ドラッグ・リポジショニングによる悪性グリオーマの抗浸潤分子標的薬の開発

    2016.04 - 2019.03

    Japan Society For The Promotion Of Science  Grants-in-Aid for Scientific Research 

    Tadashi Abe

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    Authorship：Principal investigator  Grant type：Competitive

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  • ガン細胞の走化浸潤を担うダイナミンナノクリップ：新たな制ガン剤の分子標的

    2010.04 - 2013.03

    Japan Society For The Promotion Of Science  Grants-in Aid for Scientific Research 

    阿部匡史

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    Authorship：Principal investigator  Grant type：Competitive

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