CT domain of CCN2/CTGF directly interacts with fibronectin and enhances cell adhesion of chondrocytes through integrin α5β1
CT domain of CCN2/CTGF directly interacts with fibronectin and enhances cell adhesion of chondrocytes through integrin α5β1
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DOI：
10.1016/j.febslet.2006.01.061
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发表时间：
2006-02-01
期刊：
影响因子：
3.5
通讯作者：
Takigawa, M
中科院分区：
文献类型：
--
作者：
Hoshijima, M;Hattori, T;Takigawa, M
通过酵母双杂交筛选寻找CCN家族蛋白2/结缔组织生长因子（CCN2/CTGF）相互作用蛋白，我们在软骨肉瘤来源的软骨细胞系HCS - 2/8中鉴定出纤连蛋白1基因产物是CCN2/CTGF的主要结合伴侣。只有CCN2/CTGF的CT结构域直接与纤连蛋白（FN）结合。CCN2/CTGF及其CT结构域以剂量依赖的方式增强HCS - 2/8细胞对FN的黏附。抗α5β1整合素（α5β1）的阻断抗体可消除CCN2/CTGF对细胞黏附FN的增强作用，但抗αvβ3整合素的抗体则无此作用。这些发现首次表明，CCN2/CTGF通过其C末端CT结构域与FN的直接相互作用增强软骨细胞对FN的黏附，并且α5β1参与这种黏附。（c）2006欧洲生物化学学会联合会。由爱思唯尔公司出版。保留所有权利。
Searching for CCN family protein 2/connective tissue growth factor (CCN2/CTGF) interactive proteins by yeast-two-hybrid screening, we identified fibronectin 1 gene product as a major binding partner of CCN2/CTGF in the chondrosarcoma-derived chondrocytic cell line HCS-2/8. Only the CT domain of CCN2/CTGF bound directly to fibronectin (FN). CCN2/CTGF and its CT domain enhanced the adhesion of HCS-2/8 cells to FN in a dose-dependent manner. The CCN2/CTGF-enhancing effect on cell adhesion to FN was abolished by a blocking antibody against alpha 5 beta 1 integrin (alpha 5 beta 1), but not by one against anti-alpha v beta 3 integrin. These findings suggest for the first time that CCN2/CTGF enhances chondrocyte adhesion to FN through direct interaction of its C-terminal CT domain with FN, and that alpha 5 beta 1 is involved in this adhesion. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.