Identification of a new basement membrane collagen by the aid of a large fragment resistant to bacterial collagenase
Identification of a new basement membrane collagen by the aid of a large fragment resistant to bacterial collagenase
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借助抗细菌胶原酶大片段鉴定新的基底膜胶原
DOI：
10.1016/0014-5793(79)81022-4
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发表时间：
1979
期刊：
影响因子：
3.5
通讯作者：
H. Bächinger
中科院分区：
文献类型：
--
作者：
R. Timpl;J. Risteli;H. Bächinger
IV型胶原已被确定为在多种组织中发现的基底膜的主要组分[11]。最近的研究[2-61]表明，基底膜胶原蛋白不是一种单一的蛋白质，而是一组相关的蛋白质，类似于间质胶原组织的I、II和III型胶原蛋白。可移植的小鼠肿瘤[7]！~作为一种方便的来源，可用于纯化和制备可溶性基底膜胶原。它由二硫键连接的多肽链组成（mol. wt 16- 18 X 104）并且类似于前胶原样蛋白[Xl.胃蛋白酶将该物质降解为几个三螺旋片段，产生5个不同的多肽链（mol.重量27-72 X 103）。数据表明，这些片段来源于两种不同的IV型胶原[4]。从不溶性肿瘤胶原蛋白制备的胃蛋白酶消化物含有与可溶性胶原蛋白相同的片段和一些额外的组分[4]，表明基底膜胶原蛋白的性质甚至更复杂。在这里，我们描述了一个大的胶原蛋白片段的肿瘤的分离Col I（IV）抵抗胃蛋白酶和胶原酶消化。Co 11（1V）的化学和免疫学性质表明，它来源于迄今未被认识到的IV型胶原的另外种类。
Type IV collagen has been identified as the major component of basement membranes found in a variety of tissues [11. Recent studies [2-61 have indicated that basement membrane collagen is not a single protein but rather a group of related proteins, similar to the collagen types I, II and 111 of interstitial COIIIICC-tive tissue. A transplantable mouse tumor [7]!~ a< been used as a convenient source to purify and cbaracterize a soluble fortn of basement membrane collagen. It consisted of disulfide-bonded polypeptide chains (mol. wt 16-I 8 X 104) and resembled a procollagenlike protein [Xl. Pepsin degraded this material to several triple helical fragments giving rise to 5 distinct polypeptide chains (mol. wt 27-72 X 103). The data indicated that these fragments originate from two different type IV collagens [4]. A pepsin digest prepared from the insoluble tumor collagen contained the same fragments as found with the soluble collagen and some additional components [4] suggesting an even more complex nature of basement membrane collagen. Here we describe the isolation from the tumor of a large collagenous fragment Col I (IV) which resisted digestion with pepsin and collagenase. The chemical and immunological properties of Co1 l (1V) show that it is derived from a hitherto unrecognized additional species of type IV collagen.