Collagen fibrillogenesis in tissues, in a solution and from modeling: a synthesis.

Collagen fibrillogenesis in tissues, in a solution and from modeling: a synthesis.
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组织中、溶液中和建模中的胶原纤维生成:合成。

DOI:
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发表时间:
1982
影响因子:
6.5
通讯作者:
Frederick H. Silver
Frederick H. Silver
中科院分区:
医学1区
文献类型:
--
作者:
R. Trelstad;David E. Birk;Frederick H. Silver

文献摘要

被引文献

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用光镜和电镜研究了组织中胶原纤维的形成;用光散射和显微镜观察溶液;以及基于I型胶原蛋白氨基酸序列的建模。综上所述,这些研究表明胶原原纤维的组装涉及到中间聚集体的逐步形成,其中每个中间聚集体都是由早期聚集体形成的。在这个序列中,单体胶原蛋白只有助于早期聚集体的形成;原纤维的长度是通过在亚原纤维末端添加中间聚集体而增加的,宽度是通过亚原纤维的外侧包裹而增加的。基于氨基酸序列数据的分子间电荷-电荷相互作用模型显示了促进线性聚集和促进线性聚集的两种不同的相互作用。不同的胶原和共受体(如糖蛋白和蛋白聚糖)的作用可以通过它们对中间亚组件特性的影响来解释。胚胎角膜和肌腱2个组织的超微结构数据表明,原纤维生长和组装的位置在细胞表面。
Collagen fibril formation has been studied in tissues by light and electron microscopy; in solution by light scattering and microscopy; and from modeling based on the amino acid sequence of type I collagen. Taken together these studies indicate that collagen fibril assembly involves a stepwise formation of intermediate aggregates in which each intermediate is formed from earlier aggregates. In this sequence, monomeric collagen contributes only to the formation of early aggregates; and fibrils grow in length by the addition of intermediate aggregates to the end of a subfibril and in width by lateral wrapping of subfibrils. Modeling based on amino acid sequence data of possible intermolecular charge-charge interactions indicate 2 different kinds, one which promotes linear aggregation and the other which promotes linear aggregation. The effects of different collagens and coprecipitants such as glycoproteins and proteoglycans can begin to be explained by their influence on the character of intermediate subassemblies. Ultrastructural data from 2 tissues, embryonic cornea and tendon, indicate that the site of fibril growth and assembly is at the cell surface.