SELECTIVE BINDING OF ANCHORIN-CII (ANNEXIN-V) TO TYPE-II AND X-COLLAGEN AND TO CHONDROCALCIN (C-PROPEPTIDE OF TYPE-II COLLAGEN) - IMPLICATIONS FOR ANCHORING FUNCTION BETWEEN MATRIX VESICLES AND MATRIX PROTEINS
SELECTIVE BINDING OF ANCHORIN-CII (ANNEXIN-V) TO TYPE-II AND X-COLLAGEN AND TO CHONDROCALCIN (C-PROPEPTIDE OF TYPE-II COLLAGEN) - IMPLICATIONS FOR ANCHORING FUNCTION BETWEEN MATRIX VESICLES AND MATRIX PROTEINS
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DOI：
10.1016/0014-5793(92)81316-e
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发表时间：
1992-09-28
期刊：
影响因子：
3.5
通讯作者：
PFAFFLE, M
中科院分区：
文献类型：
--
作者：
KIRSCH, T;PFAFFLE, M
锚定蛋白CII是膜联蛋白家族的胶原结合蛋白，与软骨细胞、成骨细胞和许多其他细胞的质膜相关。作为软骨源性基质囊泡的主要成分，它已被证明与天然II型和X型胶原蛋白结合。根据这一观察，在这里，我们显示锚定蛋白CII的定位在细胞外基质的钙化软骨在胎儿人生长板，它被限制在软骨细胞表面的增殖和休息软骨。此外，我们提出的证据，使用狭缝印迹分析，锚定蛋白CII不仅结合到本地II型和X型胶原蛋白，但也软骨钙蛋白，羧基末端延伸的II型前胶原蛋白，在钙的非依赖性的方式。胃蛋白酶消化II型胶原蛋白导致锚定蛋白CII结合的损失，证实了我们先前的概念，即II型胶原蛋白的端肽区域携带锚定蛋白CII结合位点。
Anchorin CII is a collagen binding protein of the annexin family associated with plasma membranes of chondrocytes, osteoblasts, and many other cells. As a major constituent of cartilage-derived matrix vesicles it has been shown to bind to native type II and X collagen. In accordance with this observation, here we show the localization of anchorin CII in the extracellular matrix of calcifying cartilage in the fetal human growth plate, and that it was restricted to the chondrocyte surface in proliferating and resting cartilage. Furthermore, we present evidence, using a slot blot assay, that anchorin CII not only binds to native type II and X collagen, but also to chondrocalcin, the carboxy-terminal extension of type II procollagen, in a calcium-independent manner. Pepsin digestion of type II collagen results in loss of anchorin CII binding, confirming our previous notion that the telopeptide region of type II collagen carries anchorin CII binding sites.