| First Author | Le Goff MM | Year | 2012 |
| Journal | J Biol Chem | Volume | 287 |
| Issue | 33 | Pages | 28027-36 |
| PubMed ID | 22669977 | Mgi Jnum | J:188846 |
| Mgi Id | MGI:5442453 | Doi | 10.1074/jbc.M111.331157 |
| Citation | Le Goff MM, et al. (2012) Opticin exerts its anti-angiogenic activity by regulating extracellular matrix adhesiveness. J Biol Chem 287(33):28027-36 |
| abstractText | 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 alpha(1)beta(1) and alpha(2)beta(1) integrins, thereby preventing the strong adhesion that is required for proangiogenic signaling via these integrins. |
