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Z. Cao, Y. Li, D.D. Hunter, M. Koch, C. Liu, L. Yeh, F.–T. Liu, D.K. Hsu, W.J. Brunken, N. Panjwani; Laminin 5, Netrin–4 and Lumican have Potential to Serve as Counterreceptors of Galectin–3 . Invest. Ophthalmol. Vis. Sci. 2005;46(13):2133.
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© ARVO (1962-2015); The Authors (2016-present)
Purpose: We have previously shown that : (i) a carbohydrate–binding protein, galectin–3, is expressed in corneal epithelium, (ii) re–epithelialization of corneal wounds is significantly slower in galectin–3 deficient mice compared to the wild type mice, and (iii) the exogenous addition of galectin–3 stimulates re–epithelialization of corneal wounds in a mouse animal model (J. Biol. Chem. 277:42299–42305, 2002). Cell–matrix interactions play a key role in re–epithelialization of corneal wounds, and it is well established that galectin–3 contains binding sites for some ECM molecules such as laminin 1. Laminin 5 (α3ß3γ2), netrin and lumican are among ECM molecules known to be present in corneal epithelial basement membrane and play a role in re–epithelialzation of corneal wounds or epithelial cell migration. Since these ECM molecules are glycosylated, it is logical to hypothesize that they may serve as counterreceptors of galectin–3 and that, galectin–3 may influence re–epithelialization of corneal wounds by binding to and modulating the function of one or more of these counterreceptors. Therefore, the goal of the present study was to determine whether galectin–3 binds to laminin 5, netrin–4 or lumican. Methods: Dot blots and/or electrophoresis blots of purified laminin 5, heterologously expressed netrin–4, a fragment of the laminin γ2 chain and affinity–purified lumican from amniotic membranes were probed with peroxidase–conjugated galectin–3 in the presence and absence of a competing disaccharide, ß–lactose. The blots were developed by a chemiluminescence detection system (PerkinElmer, Life Sciences). Results: Galectin–3 bound to laminin 5, γ2 chain of laminin 5, netrin–4 and lumican. The binding was abolished by a competing disaccharide, ß–lactose, but not by a non–competing disaccharide, sucrose. Also, as expected, galectin–3 did not bind to bovine serum albumin, which was used as a negative control. Conclusions: Galectin–3 may influence re–epithelialization of corneal wounds by modulating the function of key ECM molecules (laminin 5, netrin–4 and/or lumican) known to play a role in cell migration.
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