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A chondroitin sulphate receptor

Interactions between cells and extracellular matrix (ECM) components promote cell adhesion and have profound effects on cell physiology. In contrast to many ECM molecules, chondoitin sulphate (CS) proteoglycans inhibit cell adhesion. How do they do this? And what are the cellular proteins involved? Koji Kimata and co-workers have examined the ability of immobilized CS chains to inhibit cell adhesion in centrifugation assays (see p. 3309). They find that, although the chains inhibit cell spreading, they nevertheless allow cell attachment. Concluding that a specific cellular receptor must be involved, the authors used affinity chromatography to identify the CS receptor in fibroblast membrane protein extracts. Surprisingly, it appears to be annexin 6 - a cytosolic protein that binds to acidic phospholipids - and the authors confirm this by showing that A431 cells that lack annexin 6 cannot interact with CS. Kimata and co-workers demonstrate that, although thought to be primarily cytosolic, annexin 6 is in fact exposed on the surface of cells. Given that annexin 6 interacts with lipid rafts, they propose that it could interfere with cell spreading by influencing raft or membrane protein dynamics.

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Annexin 6 is a putative cell surface receptor for chondroitin sulfate chains

Hidekazu Takagi, Yasushi Asano, Naomi Yamakawa, Isamu Matsumoto, and Koji Kimata
JCS 2002 115: 3309-3318. [Abstract] [Full Text]  

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This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?