Opticin exerts its anti-angiogenic activity by regulating extracellular matrix adhesiveness

Magali M. Le Goff, Matthew J. Sutton, Mark Slevins, Ayse Latif, Martin J. Humphries, Paul N. Bishop

    Research output: Contribution to journalArticlepeer-review


    Opticin is an extracellular matrix glycoprotein that we identified associated with the collagen network of the vitreous humor of the eye. Recently, we discovered that opticin possesses anti-angiogenic activity using a murine oxygen-induced retinopathy model: here, we investigate the underlying mechanism. Using an ex vivo chick chorioallantoic membrane assay, we show that opticin inhibits angiogenesis when stimulated by a range of growth factors. We show that it suppresses capillary morphogenesis, inhibits endothelial invasion, and promotes capillary network regression in three-dimensional matrices of collagen and Matrigel™. We then show that opticin binds to collagen and thereby competitively inhibits endothelial cell interactions with collagen via α 1β 1 and α 2β 1 integrins, thereby preventing the strong adhesion that is required for proangiogenic signaling via these integrins. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.
    Original languageEnglish
    Pages (from-to)28027-28036
    Number of pages9
    JournalJournal of Biological Chemistry
    Issue number33
    Publication statusPublished - 10 Aug 2012


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