I型胶原对人中性粒细胞的激活作用。两种不同序列的需求。
Activation of human neutrophils by type I collagen. Requirement of two different sequences.
作者信息
Monboisse J C, Bellon G, Randoux A, Dufer J, Borel J P
机构信息
Laboratory of Biochemistry, CNRS URA 610, UFR Medicine, Reims, France.
出版信息
Biochem J. 1990 Sep 1;270(2):459-62. doi: 10.1042/bj2700459.
Abstract
Contact between type I collagen purified from several species and human polymorphonuclear neutrophils (PMNs) triggers the production of O2.- by these cells. The activity of collagen is located in the alpha 1(I)-CB6 cyanogen bromide-cleaved (CB)-peptide, which is the C-terminal CB-peptide of the alpha 1(I) chain. Experiments based on the competitive inhibition of O2.- production by simultaneous incubation of PMNs with type I collagen and synthetic peptides identical to the conserved sequences of this collagen demonstrated that the binding of collagen to PMNs and the subsequent activation of these cells depend on the simultaneous presence of two sequences: Arg-Gly-Asp [residues 915, 916 and 917 of the complete alpha 1(I) chain, located in the helical part] Asp-Gly-Gly-Arg-Tyr-Tyr (residues 1034-1039, located in the C-terminal non-helical telopeptide).
摘要
从多个物种中纯化得到的I型胶原蛋白与人类多形核中性粒细胞（PMN）之间的接触会触发这些细胞产生超氧阴离子（O2-）。胶原蛋白的活性位于α1（I）-CB6溴化氰裂解（CB）肽中，该肽是α1（I）链的C末端CB肽。通过将PMN与I型胶原蛋白以及与该胶原蛋白保守序列相同的合成肽同时孵育来竞争性抑制O2-产生的实验表明，胶原蛋白与PMN的结合以及随后这些细胞的激活取决于两个序列的同时存在：精氨酸-甘氨酸-天冬氨酸[完整α1（I）链的第915、916和917位残基，位于螺旋部分] 天冬氨酸-甘氨酸-甘氨酸-精氨酸-酪氨酸-酪氨酸（第1034-1039位残基，位于C末端非螺旋端肽）。
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