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

FEBS Letters

Pfäffle, Michael¹  Kirsch, Thorsten² 

[1] Max-Planck-Society, Clinical Research Units for Rheumatology at the University of Sandoz, Basel, Switzerland;Max-Planck-Society, Clinical Research Units for Rheumatology at the University of Erlangen-Nürnberg, Erlangen, Germany

关键词: Anchorin CII (annexin V);    Collagen binding;    Chondrocalcin binding;    Cartilage calcification;   

DOI  :  10.1016/0014-5793(92)81316-E

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 calcuim-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.

【 授权许可】

Unknown