Susceptibility of type V collagen to neutral proteases: evidence that the major molecular species is a thrombin-sensitive heteropolymer, [alpha 1(V)]2 alpha 2(V).
Susceptibility of type V collagen to neutral proteases: evidence that the major molecular species is a thrombin-sensitive heteropolymer, [alpha 1(V)]2 alpha 2(V).
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V 型胶原对中性蛋白酶的敏感性：证据表明主要分子种类是凝血酶敏感的杂聚物，[α 1(V)]2 α 2(V)。
DOI：
10.1021/bi00516a017
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发表时间：
1981
期刊：
影响因子：
2.9
通讯作者：
Bornstein,P
中科院分区：
文献类型：
--
作者：
Sage,H;Pritzl,P;Bornstein,P
Helene Sage、Pam Pritzl 和 PaulBornstein* 摘要：研究了人类 V 型胶原蛋白对几种中性蛋白酶的敏感性。凝血酶在34℃下裂解该蛋白的α1(V)和α2(V)链，在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳上产生两对表观分子量分别为95000和10000的片段。较大片段的二维 125I 标记肽图谱表明，上部条带[与 1 (1) 共迁移]源自 a1 (V) 和 a2 (V) 链，而其他组分[与 a2 (I) 共迁移]是单独的 a1 (V) 的产物。 V 型胶原蛋白（含有 a3 (V) 链）与凝血酶的裂解产生了类似的模式，具有三高（与基底膜或细胞表面相关的胶原蛋白（IV 型和 V 型）1）在导致间质胶原蛋白（I、II 和 III 型）裂解的条件下不是人皮肤胶原酶的底物（Woolley 等人，1978 年；Crouch & Bornstein，1979 年；Sage等人，1979；Liotta 等人，1979）这些观察促使人们对其他中性蛋白酶对 IV 型和 V 型胶原的反应性进行了一些研究，并考虑了这种过程在炎症、伤口修复和转移性侵袭中的可能意义，这一概念因对 I 型胶原表现出优先活性的粒细胞胶原酶而存在。与 III 型胶原蛋白相比（Horwitz 等人，1977 年），以及从转移性鼠肿瘤中分离胶原酶，仅裂解 IV 型胶原蛋白（Liotta 等人，
Helene Sage, Pam Pritzl, and PaulBornstein* abstract: Thesusceptibility of human type V collagen to several neutral proteases was examined. Thrombin cleaved both the al (V) and a2 (V) chains of this protein at 34 C, producing two pairs of fragments with apparent molecular weights of 95000 and 10000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Two-dimensional 125I-labeled peptide mapping of the larger fragments demonstrated that the upper band [which comigrated with a 1 (1)] was derived from both the al (V) and a2 (V) chains, while the other com-ponent [which comigrated with a2 (I)] was a product of al (V) alone. Cleavage of type V collagen, containing a3 (V) chains, with thrombin produced an analogous patternwith three high (Collagens associated with basement membranes or with cell surfaces (types IV and V) 1 are not substrates for human skin collagenase under conditions which result in cleavage of in-terstitial collagens (types I, II, and III)(Woolley et al., 1978; Crouch & Bornstein, 1979; Sage et al., 1979; Sage & Bornstein, 1979; Liotta et al., 1979). These observations have prompted several investigations of the reactivities of other neutral proteases toward types IV and V collagens and con-sideration of the possible significance of such processes in inflammation, wound repair, and metastatic invasion. The concept that specific collagenases existfor certain collagen types has been reinforced by the finding of a granulocyte collagenase which exhibited preferential activity toward type I as compared to type III collagen (Horwitz et al., 1977) and by the isolation of a collagenase from a metastatic murine tumor which cleaved only type IV collagen (Liotta et al.,