title: Aspirin prevents the nonenzymatic glycosylation and carbamylation of the human eye lens crystallins in vitro.
abstract: When the human eye lens homogenate which was incubated with [14C]-acetylsalicylic acid (aspirin) and separated into alpha-, beta-, and gamma - crystallins by Sepharose 6B gel-filtration, the radiolabel was found in all the three crystallins. The significant decreases in the free zeta-amino groups of aspirin treated crystallins as compared to the untreated ones indicate the probable sites of acetylation in the crystallins. The inhibition of the binding of [14C]-glucose and [14C]-cyanate to the aspirin pre-treated crystallins suggests that prior acetylation with aspirin prevents the occurrence of the nonenzymatic glycosylation and carbamylation of the lens crystallins in vitro.
authors: Department of Ophthalmology, Emory University School of Medicine, Atlanta, GA 30322.
authors: G N
authors: GN
authors: Rao
authors: E
authors: E
authors: Cotlier
mesh_terms: D000107:Acetylation; D001241:Aspirin / Q000494:pharmacology*; D002850:Chromatography, Gel; D003459:Crystallins / Q000378:metabolism*; D003485:Cyanates / Q000378:metabolism; D005947:Glucose / Q000378:metabolism; D006031:Glycosylation; D006801:Humans; D007908:Lens, Crystalline / Q000187:drug effects / Q000378:metabolism*
chemical_list: D003459:Crystallins; D003485:Cyanates; D005947:Glucose; D001241:Aspirin