Association of chondroadherin with collagen type II
Association of chondroadherin with collagen type II
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DOI：
10.1074/jbc.m101680200
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发表时间：
2001-08-31
影响因子：
4.8
通讯作者：
Heinegård, D
中科院分区：
文献类型：
--
作者：
Månsson, B;Wenglén, C;Heinegård, D
软骨粘附素是一种细胞结合，富含亮氨酸的重复蛋白，存在于关节软骨的领土基质中。富含亮氨酸的重复蛋白家族的几个成员存在于例如软骨的细胞外基质中。已显示与胶原蛋白相互作用并影响胶原蛋白原纤维形成。我们发现，复合物的单体II型胶原蛋白和软骨粘附素可以释放在非变性条件下从关节软骨处理的对氨基苯汞乙酸激活居民基质金属蛋白酶。纯化的复合物，以及在体外重组软骨粘附素和II型胶原之间形成的复合物进行了研究，通过电子显微镜。软骨粘附素被证明结合到II型胶原蛋白上的两个位点。的相互作用的特征在于表面等离子体共振分析显示KD值在纳摩尔范围内。软骨粘附素和胶原蛋白与软骨细胞相互作用，部分通过相同的受体，但引起不同的细胞反应。通过彼此相互作用，产生了复杂的系统，其对于细胞与其周围基质之间的通信和/或在胶原原纤维组装的调节中可能具有功能重要性。
Chondroadherin is a cell binding, leucine-rich repeat protein found in the territorial matrix of articular cartilage. Several members of the leucine-rich repeat protein family present in the extracellular matrix of e.g. cartilage. have been shown to interact with collagen and influence collagen fibrillogenesis. We show that complexes of monomeric collagen type II and chondroadherin can be released under non-denaturing conditions from articular cartilage treated with p-aminophenylmercuric acetate to activate resident matrix metalloproteinases. Purified complexes as well as complexes formed in vitro between recombinant chondroadherin and collagen type II were studied by electron microscopy. Chondroadherin was shown to bind to two sites on collagen type II. The interaction was characterized by surface plasmon resonance analysis showing KD values in the nanomolar range. Both chondroadherin and collagen interact with chondrocytes, partly via the same receptor, but give rise to different cellular responses. By also interacting with each other, a complex system is created which may be of functional importance for the communication between the cells and its surrounding matrix and/or in the regulation of collagen fibril assembly.