The role of the main noncollagenous domain (NC1) in type IV collagen self-assembly.
The role of the main noncollagenous domain (NC1) in type IV collagen self-assembly.
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DOI：
10.1083/jcb.103.6.2467
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发表时间：
1986-12
期刊：
影响因子：
--
通讯作者：
Charonis AS
中科院分区：
文献类型：
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作者：
Tsilibary EC;Charonis AS
在生理缓冲液中高温培养的IV型胶原蛋白(a)通过其羧基末端（NC1）结构域，(b)通过其氨基末端（7S）结构域，和(c)横向结合；它形成了一个网络。当用旋转阴影技术检查时，分离结构域NC1被发现沿着IV型胶原蛋白的长度结合到四个不同的位置，每个位置的间隔约为100 nm。完整IV型胶原的NC1结构域在网络形成初期和完整网络中沿胶原分子长度结合的距离相同，为100 nm。IV型胶原溶液中抗nc1 Fab片段的存在抑制了旋转阴影图像中的横向关联和网络形成。在自缔合过程中，IV型胶原蛋白出现浑浊；孤立结构域NC1的加入以浓度依赖的方式抑制浊度的发展。这些发现表明，IV型胶原结构域NC1在自我结合过程中起着重要作用，并提示NC1结构的改变可能部分负责某些病理条件下基底膜功能受损。
Type IV collagen incubated at elevated temperatures in physiologic buffers self-associates (a) via its carboxy-terminal (NC1) domain, (b) via its amino-terminal (7S) domain, and (c) laterally; and it forms a network. When examined with the technique of rotary shadowing, isolated domain NC1 was found to bind along the length of type IV collagen to four distinct sites located at intervals of approximately 100 nm each. The same 100-nm distance was observed in domain NC1 of intact type IV collagen bound along the length of the collagen molecules during initial steps of network formation and in complete networks. The presence of anti-NC1 Fab fragments in type IV collagen solutions inhibited lateral association and network formation in rotary shadow images. During the process of self-association type IV collagen develops turbidity; addition of isolated domain NC1 inhibited the development of turbidity in a concentration-dependent manner. These findings indicate that domain NC1 of type IV collagen plays an important role in the process of self-association and suggest that alterations in the structure of NC1 may be partially responsible for impaired functions of basement membranes in certain pathological conditions.