Collagen-binding proteins in collagenase-released matrix vesicles from cartilage. Interaction between matrix vesicle proteins and different types of collagen.
Collagen-binding proteins in collagenase-released matrix vesicles from cartilage. Interaction between matrix vesicle proteins and different types of collagen.
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发表时间：
1991-01
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影响因子：
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通讯作者：
L. N. Wu;B. Genge;G. C. Lloyd;R. Wuthier
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文献类型：
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作者：
L. N. Wu;B. Genge;G. C. Lloyd;R. Wuthier
最近的证据表明，基质囊泡（MV）与软骨特异性胶原和其他基质蛋白相互作用。II型和X型胶原都与MV结合并共沉积。我们的同伴研究表明，MV也紧密耦合到蛋白多糖连接蛋白（LP）和透明质酸结合区（HABR）在软骨基质。在这里，我们试图确定负责MV和基质胶原蛋白之间的关系，使用亲和层析与I型，II型和X型胶原蛋白-琼脂糖凝胶柱。在非离子去污剂存在下用NaCl阶梯梯度洗脱用于评估MV蛋白和共价连接的胶原之间的亲和力。发现几种MV蛋白与天然I型、II型和X型胶原结合，但没有与变性I型胶原结合。碱性磷酸酶，蛋白多糖LP和HABR，和33-和67-kDa的膜联蛋白，结合不同的亲和力的天然I型，II型和X列。特别是，LP和HABR，67-kDa膜联蛋白，和碱性磷酸酶结合与软骨特异性胶原蛋白的高亲和力，虽然LP，HABR，和一个37-kDa的蛋白质也结合不太紧密的天然I型胶原蛋白。因此，几种MV蛋白特异性结合天然II型和X型胶原，并应促进MV和细胞外基质之间的相互作用。这种相互作用在MV形成或MV介导的矿化中可能是重要的。
Recent evidence indicates that matrix vesicles (MV) interact with cartilage-specific collagens and other matrix proteins. Both type II and X collagens bind to and cosediment with MV. Our companion study shows that MV also are tightly coupled to proteoglycan link proteins (LP) and hyaluronic acid-binding region (HABR) in cartilage matrix. Here we sought to identify proteins responsible for the nexus between MV and matrix collagens using affinity chromatography with types I, II, and X collagen-Sepharose columns. Elution with NaCl step-gradients in the presence of nonionic detergent was used to assess the affinity between the MV proteins and the covalently attached collagens. Several MV proteins were found to bind to native type I, II, and X collagens but none bound to denatured type I collagen. Alkaline phosphatase, proteoglycan LP and HABR, and the 33- and 67-kDa annexins, bound with varying affinities to the native type I, II and X columns. In particular, LP and HABR, the 67-kDa annexin, and alkaline phosphatase bound with high affinity to the cartilage-specific collagens, although LP, HABR, and a 37-kDa protein also bound less tightly to native type I collagen. Thus, several MV proteins bind specifically to native type II and X collagens and should promote interaction between MV and the extracellular matrix. Such interactions may be important in MV formation, or in MV-mediated mineralization.