Faculty Profiles - AOYAMA Eriko

Papers - AOYAMA Eriko

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Design and utility of CCN2 anchor peptide aptamers. Reviewed

Kawaki H, Kubota S, Aoyama E, Fujita N, Hanagata H, Miyauchi A, Nakai K, Takigawa M

Biochimie 92 ( 8 ) 1010 - 1015 2010.8

Thrombopoietic-mesenchymal interaction that may facilitate both endochondral ossification and platelet maturation via CCN2. Reviewed

Sumiyoshi K, Kubota S, Furuta RA, Yasui K, Aoyama E, Kawaki H, Kawata K, Ohgawara T, Yamashiro T, Takigawa M

Journal of cell communication and signaling 4 ( 1 ) 5 - 14 2010.3

N-terminal domains of CCN family 2/connective tissue growth factor bind to aggrecan Reviewed International journal

Aoyama Eriko, Hattori Takako, Hoshijima Mitsuhiro, Araki Daisuke, Nishida Takashi, Kubota Satoshi, Takigawa Masaharu

BIOCHEMICAL JOURNAL 420 ( 3 ) 413 - 420 2009.6

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

CCN2/CTGF (CCN family 2/connective tissue growth factor) is a multi-cellular protein with a broad range of activities. It modulates many cellular functions, including proliferation, migration, adhesion and extracellular matrix production, and it is thus involved in many biological and pathological processes. In particular, CCN2/CTGF is essential for normal skeletal development. To identify CCN2/CTGF-interactive proteins capable of modulating its action in cartilage, we carried out a yeast two-hybrid screening using CCN2/CTGF peptide as a bait and a cDNA library from a chondrocytic cell line, HCS-2/8. In the present paper, we report the identification of aggrecan, which is a major proteoglycan of the extracellular matrix in cartilage, as a CCN2/CTGF-binding protein. Among the four domains of CCN2/CTGF, the IGFBP [IGF (insulin-like growth factor)-binding protein-like] and/or VWC (von Willebrand factor type C) domains had a direct interaction with aggrecan in a yeast two-hybrid assay. The results of a solid-phase-binding assay using aggrecan-coated plates also showed binding to recombinant CCN2/CTGF in a dose-dependent manner. rIGFBP (recombinant IGFBP) and rVWC (recombinant VWC) module peptides had stronger binding to aggrecan compared with rTSP1 (recombinant thrombospondin type 1 repeat) and rCT (recombinant C-terminal cystine knot) module peptides. SPR (surface plasmon resonance) analysis showed the direct interaction between the CCN2/CTGF and aggrecan, and ectopically overexpressed CCN2/CTGF and AgG3 (G3 domain of aggrecan) confirmed their binding In vivo. Indirect immunofluorescence analysis indicated that CCN2/CTGF was extracellularly co-localized with aggrecan on HCS-2/8 cells. The rIGFBP-rVWC peptide effectively enhanced the production and release of aggrecan compared with the rTSP-rCT peptide in chondrocytes. These results indicate that CCN2/CTGF binds to aggrecan through its N-terminal IGFBP and VWC modules, and this binding may be related to the CCN2/CTGF-enhanced production and secretion of aggrecan by chondrocytes.

DOI： 10.1042/BJ20081991

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Regulation of chondrocytic phenotype by micro RNA 18a: Involvement of Ccn2/Ctgf as a major target gene

Toshihiro Ohgawara, Satoshi Kubota, Harumi Kawaki, Seiji Kondo, Takanori Eguchi, Naito Kurio, Eriko Aoyama, Akira Sasaki, Masaharu Takigawa

FEBS LETTERS 583 ( 6 ) 1006 - 1010 2009.3

Language：English Publishing type：Research paper (scientific journal) Publisher：ELSEVIER SCIENCE BV

We searched for miRNAs that were down-regulated in chondrocytic cells and predicted to target CCN2/connective tissue growth factor (CCN2/CTGF) that promotes endochondral ossification. Among them, expression of miR-18a was most strongly repressed in chondrocytic cells. Reporter gene analysis confirmed the functionality of an miR-18a target in the 3'-untranslated region of Ccn2 mRNA, which was predicted in silico. Indeed, introduction of miR-18a efficiently repressed the CCN2 production from chondrocytic cells. Finally, transfected miR-18a significantly repressed the mature chondrocytic phenotype. Our present study revealed a regulatory role for miR-18a in chondrocytic differentiation through CCN2. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

DOI： 10.1016/j.febslet.2009.02.025

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CCN Family 2/Connective Tissue Growth Factor Modulates BMP Signalling as a Signal Conductor, Which Action Regulates the Proliferation and Differentiation of Chondrocytes

Azusa Maeda, Takashi Nishida, Eriko Aoyama, Satoshi Kubota, Karen M. Lyons, Takuo Kuboki, Masaharu Takigawa

JOURNAL OF BIOCHEMISTRY 145 ( 2 ) 207 - 216 2009.2

Language：English Publishing type：Research paper (scientific journal) Publisher：OXFORD UNIV PRESS

Both CCN family 2/connective tissue growth factor (CCN2/CTGF) and bone morphogenetic protein (BMP)-2 play an important role in cartilage metabolism. We evaluated whether or not CCN2 would interact with BMP-2, and examined the combination effect of CCN2 with BMP-2 (CCN2-BMP-2) on the proliferation and differentiation of chondrocytes. Immunoprecipitation-western blotting analysis, solid-phase binding assay and surface plasmon resonance (SPR) spectroscopy showed that CCN2 directly interacted with BMP-2 with a dissociation constant of 0.77 nM as evaluated by SPR. An in vivo study revealed that CCN2 was co-localized with BMP-2 at the pre-hypertrophic region in the E18.5 mouse growth plate. Interestingly, CCN2-BMP-2 did not affect the BMP-2/CCN2-induced phosphorylation of p38 MAPK but caused less phosphorylation of ERK1/2 in cultured chondrocytes. Consistent with these results, cell proliferation assay showed that CCN2-BMP-2 stimulated cell growth to a lesser degree than by either CCN2 or BMP-2 alone, whereas the expression of chondrocyte marker genes and proteoglycan synthesis, representing the mature chondrocytic phenotype, was increased collaboratively by CCN2-BMP-2 treatment in cultured chondrocytes. These findings suggest that CCN2 may regulate the proliferating and differentiation of chondrocytes by forming a complex with BMP-2 as a novel modulator of BMP signalling.

DOI： 10.1093/jb/mvn159

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CCN2/CTGFとBMP-2の相互作用が軟骨細胞の増殖と分化を制御する

西田崇, 前田あずさ, 青山絵理子, 久保田聡, 窪木拓男, Lyons Karen, 滝川正春

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 81回・31回 3T13 - 4 2008.11

低密度リポタンパク受容体関連タンパク-1(LRP1)の軟骨細胞分化における機能とその作用機構

河田かずみ, 久保田聡, 江口傑徳, 青山絵理子, 皆木省吾, 滝川正春

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 81回・31回 4T13 - 2 2008.11

CCN2/CTGFによるBMP-2の軟骨細胞増殖・分化促進作用の制御

前田あずさ, 西田崇, 青山絵理子, 川木晴美, 久保田聡, 窪木拓男, ライアン・カレン, 滝川正春

日本骨代謝学会学術集会プログラム抄録集 26回 234 - 234 2008.10

軟骨細胞分化における低密度リポタンパク受容体関連タンパク-1(LRP1)の関与

河田かずみ, 久保田聡, 江口傑徳, 青山絵理子, 皆木省吾, 滝川正春

日本骨代謝学会学術集会プログラム抄録集 26回 234 - 234 2008.10

Distribution, gene expression, and functional role of EphA4 during ossification

Chisa Kuroda, Satoshi Kubota, Kazumi Kawata, Eriko Aoyama, Kumi Sumiyoshi, Morihiko Oka, Miho Inoue, Shogo Minagi, Masaharu Takigawa

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 374 ( 1 ) 22 - 27 2008.9

Language：English Publishing type：Research paper (scientific journal) Publisher：ACADEMIC PRESS INC ELSEVIER SCIENCE

EphA4 receptor tyrosine kinase has been shown to be critically involved in neural tissue development. Here, we found EphA4 was also distributed among hypertrophic chondrocytes and osteoblasts in the growth plate of developing mouse long bones. In vitro evaluation revealed that ephA4 expression was elevated Upon hypertrophic differentiation of chondrocytes and that markedly stronger expression was observed in osteoblastic SaOS-2 than chondrocytic HCS-2/8 cells. Of note, RNAi-mediated silencing of ephA4 in SaOS-2 cells resulted in the repression of osteocalcin gene expression and alkaline phosphatase activity. Interestingly, confocal laser-scanning Microscopic analysis revealed the presence of EphA4 molecules in the nucleus as well as on the surface of SaOS-2 cells. These findings are the first indication of a critical role of EphA4 in ossification, especially at the final stage in which osteoblasts and hypertrophic chondrocytes play major roles. (C) 2008 Elsevier Inc. All rights reserved.

DOI： 10.1016/j.bbrc.2008.06.089

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Differentiation of murine B cells induced by chondroitin sulfate B

Ritsuko Yoshihara, Eriko Aoyama, Yusuke Kadota, Saeko Kawai, Tomomi Goto, Ming Zhong, Eiichi Gohda

CELLULAR IMMUNOLOGY 250 ( 1-2 ) 14 - 23 2007.11

Language：English Publishing type：Research paper (scientific journal) Publisher：ACADEMIC PRESS INC ELSEVIER SCIENCE

A two-step culture system was used to investigate the role of chondroitin sulfate (CS) B, which is mitogenic to B cells, in differentiation of B cells. Mouse spleen B cells were incubated for 3 days with CSB in the presence of interleukin (IL)-4 and IL-5. After washing, the cells were replated at 10(5) viable cells/well and recultured without CSB in the presence of IL-4 and IL-5. CSB dose-dependently increased IgM production, the greatest enhancement being 450%. Dextran sulfate had a similar effect, whereas other glycosaminoglycans, CSA, CSC, heparin and hyaluronic acid, were marginally effective. Treatment of B cells with CSB resulted in increases in the number of IgM-secreting cells and numbers of CD138-positive cells and CD45R/B220-negative cells. CSB-induced IgM production was inhibited by the protein kinase C (PKC) inhibitor GF109203X but not by the phosphatidylinositol 3-kinase (PI3K) inhibitor wortmannin. These results demonstrated that CSB promoted differentiation of B cells in the presence of IL-4 and IL-5 and suggested that PKC but not PI3K is crucial for CSB-induced IgM production. (c) 2007 Elsevier Inc. All rights reserved.

DOI： 10.1016/j.cellimm.2007.12.002

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結合組織成長因子(CCN2/CTGF)とアグリカンとの結合についての解析(Analysis of binding between CCN2/CTGF and aggrecan)

青山絵理子, 服部高子, 荒木大介, 星島光博, 滝川正春

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 80回・30回 2T22 - 13 2007.11

PKC- and PI3K-dependent but ERK-independent proliferation of murine splenic B cells stimulated by chondroitin sulfate B

E Aoyama, R Yoshihara, A Tai, Yamamoto, I, E Gohda

IMMUNOLOGY LETTERS 99 ( 1 ) 80 - 84 2005.6

Language：English Publishing type：Research paper (scientific journal) Publisher：ELSEVIER SCIENCE BV

High molecular weight polyanions such as dextran sulfate are known to be weak polyclonal activators of murine B cells, but the molecular mechanism of their mitogenic activitiy is not fully elucidated. Although chondroitin sulfate A (CSA), B (CSB) and C (CSC) are highly charged polyanions, little is known about their effects on the proliferation of B cells. In this study, we demonstrated that CSB stimulated proliferation of murine B cells as markedly as did anti-IgM antibody, more markedly than did dextran sulfate and much more markedly than did CSA, CSC, heparin and hyaluronic acid. CSB caused translocation of protein kinase C (PKC) isoform beta from cytosol to membrane fractions and increased phosphorylation of Akt but not phosphorylation of extracellular signal-regulated kinase (ERK) of B cells. CSB-induced B cell proliferation was almost completely blocked by either the phosphatidylinositol 3-kinase (PI3K) inhibitor LY294002 or the PKC inhibitor GF109203X but was not significantly inhibited by the ERK kinase inhibitor PD98059. The mitogenic effect of anti-IgM was significantly inhibited by all the three inhibitors, while the mitogenic effect of LPS was inhibited only by LY294002. These findings indicate that CSB stimulated proliferation of murine B cells more markedly than did dextran sulfate and suggest that PKC and PI3K are crucial but that ERK is less important for the mitogenic activity of CSB, the signaling pathways of which may be at least partly distinct from those of anti-IgM and LPS. (c) 2005 Elsevier B.V. All rights reserved.

DOI： 10.1016/j.imlet.2005.01.005

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Augmentation by 2-mercaptoethanol of in vitro anti-TNP antibody production induced by butyrate plus IL-2 in murine splenic B cells

E Gohda, T Okamura, E Aoyama, Yamamoto, I

IMMUNOPHARMACOLOGY AND IMMUNOTOXICOLOGY 25 ( 4 ) 539 - 550 2003

Language：English Publishing type：Research paper (scientific journal) Publisher：MARCEL DEKKER INC

We previously reported that anti-trinitrophenyl (TNP) antibody production in murine splenic B cells stimulated with TNP-lipopolysaccharide in vitro was promoted by sodium butyrate (NaBu) in an IL-2-dependent manner. In the present study, we found that the effect of NaBu plus IL-2 was markedly augmented by 2-mercaptoethanol (2-ME), which showed a slight or null effect on the response of untreated, IL-2-treated or NaBu-treated B cells, as assessed by both anti-TNP plaque-forming cell assay and anti-TNP IgM ELISA. Other thiol compounds such as dithiothreitol, cysteamine and reduced glutathione (GSH) also had this activity. 2-ME enhanced the anti-TNP antibody production induced by other short-chain fatty acids with three to five carbon atoms plus IL-2. The proliferation of B cells was significantly inhibited by NaBu or NaBu plus IL-2, and the proliferation was completely restored by the simultaneous addition of 2-ME. These results demonstrate that 2-ME markedly enhanced anti-TNP antibody production in murine B cells induced by NaBu plus IL-2 and suggest that the effect of 2-ME is at least partly due to its blocking activity of the growth-inhibitory action of NaBu.

DOI： 10.1081/IPH-120026439

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