Identification of collagen fibril fusion during vertebrate tendon morphogenesis. The process relies on unipolar fibrils and is regulated by collagen-proteoglycan interaction
Identification of collagen fibril fusion during vertebrate tendon morphogenesis. The process relies on unipolar fibrils and is regulated by collagen-proteoglycan interaction
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DOI：
10.1006/jmbi.1999.3384
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发表时间：
2000-01-28
影响因子：
5.6
通讯作者：
Kadler, KE
中科院分区：
文献类型：
--
作者：
Graham, HK;Holmes, DF;Kadler, KE
含有长（长度类似于mm）胶原纤维的细胞外基质的合成是动物组织正常形态发生的基础。在这项研究中，我们有直接的证据表明，成纤维细胞合成短暂的早期原纤维中间体（类似于1 μ m的长度），相互作用的尖端到尖端融合，以产生长的原纤维在较老的组织。对来自肌腱的早期胶原原纤维的检查表明，存在两种类型的早期原纤维：单极原纤维（具有羧基（C）和氨基（N）末端）和双极原纤维（具有两个N末端）。端对端融合需要单极原纤维的C端。蛋白聚糖包被的原纤维的轴，但不是提示。在缺乏蛋白聚糖的情况下，原纤维通过侧对侧的相互作用聚集。因此，蛋白聚糖促进尖端-尖端融合并抑制侧-侧融合。蛋白聚糖沿着原纤维的这种分布需要在原纤维组装之前胶原和蛋白聚糖的共组装。该研究表明，胶原原纤维形成是一个分级过程，取决于单极原纤维的独特结构和蛋白聚糖的新功能。(C)北京大学出版社.
The synthesis of an extracellular matrix containing long (similar to mm in length) collagen fibrils is fundamental to the normal morphogenesis of animal tissues. In this study we have direct evidence that fibroblasts synthesise transient early fibril intermediates (similar to 1 mu m in length) that interact by tip-to-tip fusion to generate long fibrils seen in older tissues. Examination of early collagen fibrils from tendon showed that two types of early fibrils occur: unipolar fibrils (with carboxyl (C) and amino (N) ends) and bipolar fibrils (with two N-ends). End-to-end fusion requires the C-end of a unipolar fibril. Proteoglycans coated the shafts of the fibrils but not the tips. Ln the absence of proteoglycans the fibrils aggregated by side-to-side interactions. Therefore, proteoglycans promote tip-to-tip fusion and inhibit side-to-side fusion. This distribution of proteoglycan along the fibril required co-assembly of collagen and proteoglycan prior to fibril assembly. The study showed that collagen fibrillogenesis is a hierarchical process that depends on the unique structure of unipolar fibrils and a novel function of proteoglycans. (C) 2000 Academic Press.