BINDING OF LAMININ TO TYPE-IV COLLAGEN - A MORPHOLOGICAL-STUDY
BINDING OF LAMININ TO TYPE-IV COLLAGEN - A MORPHOLOGICAL-STUDY
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DOI：
10.1083/jcb.100.6.1848
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发表时间：
1985-01-01
影响因子：
7.8
通讯作者：
FURTHMAYR, H
中科院分区：
文献类型：
--
作者：
CHARONIS, AS;TSILIBARY, EC;FURTHMAYR, H
使用 C/Pt 和 EM 通过旋转阴影分析层粘连蛋白和 IV 型[鼠]胶原蛋白的混合物。层粘连蛋白被发现与 IV 型胶原蛋白形成独特的复合物；一个相互作用位点位于距 COOH 末端非胶原 (NC1) 结构域 140 nm 处，另一个位点位于 NH2 末端区域内。这些分离的 IV 型胶原蛋白 NC1 片段似乎不与层粘连蛋白相互作用，而胃蛋白酶处理的 IV 型胶原蛋白缺乏 NC1 结构域，保留了与层粘连蛋白形成复合物的能力。对层粘连蛋白 IV 型复合物的分析表明，层粘连蛋白通过其 4 个臂中任一臂的球状区域与 IV 型胶原蛋白结合。这一发现得到了使用层粘连蛋白片段 P1 的实验的支持，该片段缺乏球状区域并且不以特定方式与 IV 型胶原蛋白结合。此外，层粘连蛋白热变性后，没有观察到特异性结合。
A mixture of laminin and type IV [murine] collagen was analyzed by rotary shadowing using C/Pt and EM. Laminin was found to form distinct complexes with type IV collagen; one site of interaction is located 140 nm from the COOH-terminal, noncollagenous (NC1) domain and the other is located within the NH2-terminal region. These isolated NC1 fragment of type IV collagen does not appear to interact with laminin, while pepsin-treated type IV collagen, which lacks the NC1 domain, retains its ability to form complexes with laminin. Analysis of the laminin-type IV complexes indicates that laminin binds to type IV collagen via the globular regions of either of its 4 arms. This finding is supported by experiments using fragment P1 of laminin which lacks the globular regions and which does not bind to type IV collagen in a specific way. In addition, after heat-denaturation of laminin no specific binding is observed.