Modulation of collagen fibrillogenesis by tenascin-X and type VI collagen
Modulation of collagen fibrillogenesis by tenascin-X and type VI collagen
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DOI：
10.1016/j.yexcr.2004.04.030
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发表时间：
2004-08-01
影响因子：
3.7
通讯作者：
Matsumoto, K
中科院分区：
文献类型：
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作者：
Minamitani, T;Ikuta, T;Matsumoto, K
Tenascin-X （TNX）是细胞外基质糖蛋白。我们之前证明TNX调节VI型胶原的表达。在本研究中，我们研究了TNX与I型胶原和VI型胶原的结合，以及这些蛋白对I型胶原纤维形成的影响。使用在哺乳动物细胞培养物中表达并纯化的全长重组TNX和从牛胎盘中纯化的VI型胶原。固相测定显示TNX或VI型胶原与I型胶原结合，尽管TNX不与VI型胶原、纤维连接蛋白或层粘连蛋白结合。TNX的存在显著增加了胶原纤维的形成速度和数量（以浊度的增加来衡量），而VI型胶原没有增加胶原纤维的形成速度，而是加速了胶原纤维的形成速度。两者联合治疗对胶原纤维的形成率有叠加效应。此外，TNX的表皮生长因子样（EGF）结构域或纤维蛋白原样结构域的缺失降低了胶原纤维形成的初始速率。最后，我们在电子显微镜下观察到TNX缺陷小鼠（TNX-/-）发育过程中皮肤中异常大的胶原原纤维。这些发现证明了TNX和VI型胶原在体内和体外调节胶原纤维形成中的基本作用。(C) 2004爱思唯尔公司版权所有。
Tenascin-X (TNX) is an extracellular matrix glycoprotein. We previously demonstrated that TNX regulates the expression of type VI collagen. In this study, we investigated the binding of TNX to type I collagen as well as to type VI collagen and the effects of these proteins on fibrillogenesis of type I collagen. Full-length recombinant TNX, which is expressed in and purified from mammalian cell cultures, and type VI collagen purified from bovine placenta were used. Solid-phase assays revealed that TNX or type VI collagen bound to type I collagen, although TNX did not bind to type VI collagen, fibronectin, or laminin. The rate of collagen fibril formation and its quantity, measured as increased turbidity, was markedly increased by the presence of TNX, whereas type VI collagen did not increase the quantity but accelerated the rate of collagen fibril formation. Combined treatment of both had an additive effect on the rate of collagen fibril formation. Furthermore, deletion of the epidermal growth factor-like (EGF) domain or fibrinogen-like domain of TNX attenuated the initial rate of collagen fibril formation. Finally, we observed abnormally large collagen fibrils by electron microscopy in the skin from TNX-deficient (TNX-/-) mice during development. These findings demonstrate a fundamental role for TNX and type VI collagen in regulation of collagen fibrillogenesis in vivo and in vitro. (C) 2004 Elsevier Inc. All rights reserved.