Published in

Elsevier, Journal of Biological Chemistry, 33(287), p. 28027-28036, 2012

DOI: 10.1074/jbc.m111.331157

Links

Tools

Export citation

Search in Google Scholar

Opticin Exerts Its Anti-angiogenic Activity by Regulating Extracellular Matrix Adhesiveness*

Journal article published in 2012 by Magali M. Le Goff, Matthew J. Sutton Mark Slevin Ayse Latif Martin J. Humphries,and Paul N. Bishop • Magali M. Le Goff, Matthew J. Sutton, Mark Slevin, Ayse Latif ORCID, Martin J. Humphries, Paul N. Bishop
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

Full text: Download

Green circle
Preprint: archiving allowed
Upload
Green circle
Postprint: archiving allowed
Upload
Green circle
Published version: archiving allowed
Upload
Policy details
Data provided by SHERPA/RoMEO

Abstract

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(TM). We then show that opticin binds to collagen and thereby competitively inhibits endothelial cell interactions with collagen via α(1)β(1) and α(2)β(1) integrins, thereby preventing the strong adhesion that is required for proangiogenic signaling via these integrins.