Parkin J Des, San Antonio James D, Persikov Anton V, Dagher Hayat, Dalgleish Raymond, Jensen Shane T, Jeunemaitre Xavier, Savige Judy
From the University of Melbourne Department of Medicine (Northern Health), Melbourne, VIC, Australia.
Operations, Stryker Global Quality and Operations, Malvern, PA, United States of America.
PLoS One. 2017 Jul 13;12(7):e0175582. doi: 10.1371/journal.pone.0175582. eCollection 2017.
Collagen III is critical to the integrity of blood vessels and distensible organs, and in hemostasis. Examination of the human collagen III interactome reveals a nearly identical structural arrangement and charge distribution pattern as for collagen I, with cell interaction domains, fibrillogenesis and enzyme cleavage domains, several major ligand-binding regions, and intermolecular crosslink sites at the same sites. These similarities allow heterotypic fibril formation with, and substitution by, collagen I in embryonic development and wound healing. The collagen III fibril assumes a "flexi-rod" structure with flexible zones interspersed with rod-like domains, which is consistent with the molecule's prominence in young, pliable tissues and distensible organs. Collagen III has two major hemostasis domains, with binding motifs for von Willebrand factor, α2β1 integrin, platelet binding octapeptide and glycoprotein VI, consistent with the bleeding tendency observed with COL3A1 disease-causing sequence variants.
Ⅲ型胶原蛋白对于血管和可扩张器官的完整性以及止血过程至关重要。对人类Ⅲ型胶原蛋白相互作用组的研究表明，其结构排列和电荷分布模式与Ⅰ型胶原蛋白几乎相同，在相同位点具有细胞相互作用结构域、纤维形成和酶切结构域、几个主要的配体结合区域以及分子间交联位点。这些相似性使得在胚胎发育和伤口愈合过程中，Ⅲ型胶原蛋白能够与Ⅰ型胶原蛋白形成异型纤维并被其替代。Ⅲ型胶原蛋白纤维呈现出“柔性杆”结构，其中柔性区域与杆状结构域相间分布，这与该分子在年轻、柔韧组织和可扩张器官中的突出作用相一致。Ⅲ型胶原蛋白具有两个主要的止血结构域，带有与血管性血友病因子、α2β1整合素、血小板结合八肽和糖蛋白VI的结合基序，这与COL3A1致病序列变异所观察到的出血倾向一致。
