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Opticin is a glycoprotein encoded by the OPTC gene and belongs to the small leucine-rich repeat protein (SLRP) family, primarily localizing to the extracellular matrix of the eye, especially in the vitreous, but also present in the cornea, iris, ciliary body, optic nerve, and retina. It noncovalently binds to collagen fibrils, regulating their arrangement and inhibiting angiogenesis by competing with integrin-mediated binding, which restricts neovascularization. Altered or mutant opticin has been implicated in several degenerative and developmental eye disorders, particularly certain forms of glaucoma and age-related eye diseases. Outside the eye, a unique, unglycosylated form is specifically overexpressed in leukemic cells of chronic lymphocytic leukemia. No drugs target opticin, and its mechanism of action is focused on regulation of extracellular matrix structure and inhibition of pathologic vessel growth[1][2][4][5][7].
Not targeted by drugs; acts as an endogenous inhibitor of angiogenesis by binding collagen and preventing integrin-mediated endothelial cell interaction with collagen[3][7]
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