Cellular and Molecular Life Sciences CMLS

, Volume 53, Issue 6, pp 539–545

Annexin V interactions with collagen

  • K. von der Mark
  • J. Mollenhauer


Annexin V was originally identified as a collagen-binding protein called anchorin CII and was isolated from chondrocyte membranes by affinity chromatography on native type II collagen. The binding of annexin V to native collagen type II is stable at physiological ionic strength when annexin V is reconstituted in liposomes. The binding to native collagen types II and X, and to some extent to type I as well, was confirmed using recombinant annexin V. A physiological role for annexin V interactions with extracellular collagen is consistent with the localization of annexin V on the outer cell surface of chondrocytes, microvilli of hypertrophic chondrocytes, fibroblasts and osteoblasts. A breakthrough in our understanding of the function of annexin V was made with the discovery of its calcium channel activity. At least one of several putative functions of annexin V became obvious from studies on matrix vesicles derived from calcifying cartilage. It was found that calcium uptake by matrix vesicles depend on collagen type II and type X binding to annexin V in the vesicles and was lost when collagens were digested with collagenase; calcium influx was reconstituted after adding back native collagen II or V. These findings indicate that annexin V plays a major role in matrix vesicle-initiated cartilage calcification as a collagen-regulated calcium channel.

Key words. Cartilage; collagen binding; annexin V; calcium flux. 


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Copyright information

© Birkhäuser Verlag Basel, 1997

Authors and Affiliations

  • K. von der Mark
    • 1
  • J. Mollenhauer
    • 2
  1. 1.Institute of Experimental Medicine, Friedrich-Alexander University of Erlangen-Nürnberg, D-91054 Erlangen (Germany), Fax +49 9131 85 6341, e-mail: kvdmark@EXPMED.UNI-ERLANGEN.DEDE
  2. 2.Department of Biochemistry, Rush-Presbyterian-St. Luke's Medical Center, Chicago (Illinois 60612, (USA)US

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