来自Descemet膜的与弹性蛋白交联的胶原蛋白与VIII型胶原蛋白无关。

The collagenous protein with elastin crosslinks from Descemet's membrane is not related to type VIII collagen.

作者信息

Davis P F, Ryan P A, Kittelberger R, Greenhill N S

机构信息

Malaghan Institute of Medical Research, Wellington School of Medicine, New Zealand.

出版信息

Biochem Biophys Res Commun. 1990 Aug 31;171(1):260-5. doi: 10.1016/0006-291x(90)91386-7.

DOI:10.1016/0006-291x(90)91386-7

PMID:2393394

Abstract

A collagen-like insoluble protein containing the elastin cross-links (desmosine and isodesmosine) has been isolated from Descemet's membrane. Recently type VIII collagen (endothelial collagen) has been shown to be a major constituent of this membrane. Biochemical studies suggest that these two proteins are unrelated. The cyanogen bromide peptide maps show negligible similarity. Antiserum raised against oxalic acid digests of elastin (alpha-elastin) did not react against an oxalic acid digests of type VIII collagen but did show some reaction against the cross-linked preparation. Immunofluorescent localization has demonstrated the presence of type VIII collagen in trachea but a desmosine cross-linked collagen could not be isolated from this tissue.

摘要

一种含有弹性蛋白交联键（锁链素和异锁链素）的类胶原蛋白不溶性蛋白质已从Descemet膜中分离出来。最近，VIII型胶原蛋白（内皮胶原蛋白）已被证明是该膜的主要成分。生化研究表明这两种蛋白质没有关联。溴化氰肽图谱显示相似性可忽略不计。针对弹性蛋白（α-弹性蛋白）草酸消化物产生的抗血清与VIII型胶原蛋白的草酸消化物不发生反应，但对交联制剂有一定反应。免疫荧光定位已证明气管中存在VIII型胶原蛋白，但无法从该组织中分离出锁链素交联的胶原蛋白。