DECORIN-TYPE-I COLLAGEN INTERACTION - PRESENCE OF SEPARATE CORE PROTEIN-BINDING DOMAINS
DECORIN-TYPE-I COLLAGEN INTERACTION - PRESENCE OF SEPARATE CORE PROTEIN-BINDING DOMAINS
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DOI：
10.1074/jbc.270.15.8877
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发表时间：
1995-04-14
影响因子：
4.8
通讯作者：
KRESSE, H
中科院分区：
文献类型：
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作者：
SCHONHERR, E;HAUSSER, H;KRESSE, H
小硫酸皮肤素蛋白聚糖核心蛋白聚糖和I型胶原的核心蛋白之间的相互作用被认为影响胶原原纤维形成的动力学和原纤维的直径和原纤维之间的距离。多种重组核心蛋白片段在大肠杆菌中表达，从包涵体中提取，并在牛血清白蛋白的存在下复性，这是获得功能活性所必需的。缺乏成熟核心蛋白（P15-329）的前14个氨基酸的重组蛋白与重构的I型胶原原纤维相互作用并抑制胶原原纤维形成，几乎与在非变性条件下从成纤维细胞分泌物纯化的完整核心蛋白聚糖一样有效，包含氨基酸15-183（P15-183）和185-329的肽（P185-329）能够竞争野生型核心蛋白聚糖的结合，其中P15-183比P185-329更有活性，其他几种肽的有效性低得多，使用放射性标记的肽P15-183和P185-329的结合研究给出了两种肽独立结合的直接证据，肽15-183和15-125具有抑制胶原纤维形成的能力，而肽185-329是无活性的，这些数据表明（i）核心蛋白聚糖核心蛋白和I型胶原之间的相互作用至少有两个独立的结合结构域，（ii）结合不一定与胶原原纤维形成的改变相关。
Interactions between the core protein of the small dermatan sulfate proteoglycan decorin and type I collagen have been considered to influence the kinetics of collagen fibrillogenesis and the diameter of and the distance between the fibrils. A variety of recombinant core protein fragments were expressed in Escherichia coli, extracted from inclusion bodies, and renatured in the presence of bovine serum albumin, which was essential for obtaining functional activity. A recombinant protein lacking the first 14 amino acids of the mature core protein (P15-329) interacted with reconstituted type I collagen fibrils and inhibited collagen fibrillogenesis almost as efficiently as intact decorin purified from fibroblast secretions under non-denaturing conditions, Peptides comprising amino acids 15-183 (P15-183) and 185-329 (P185-329) were able to compete for the binding of wild-type decorin, with P15-183 being more active than P185-329, Several other peptides were much less effective, Binding studies using radioactively labeled peptides P15-183 and P185-329 gave direct evidence for the independent binding of both peptides, Peptides 15-183 and 15-125 had the capability of inhibiting collagen fibrillogenesis, whereas peptide 185-329 was inactive, These data suggest (i) that there are at least two separate binding domains for the interaction between decorin core protein and type I collagen and (ii) that binding is not necessarily correlated with an alteration of collagen fibrillogenesis.