Acetylation of lens crystallins: a possible mechanism by which aspirin could prevent cataract formation.
The calf eye lens homogenate incubated with [1-14C-acetyl] aspirin and separated into HMW, alpha, beta H, beta L and gamma-crystallins by means of Sepharose 6B and Bio-Gel P2 columns showed radioactivity in all the crystallins. In contrast, no radioactivity was found in the crystallins when the lens homogenate was incubated with [14C-carboxyl] aspirin. These experiments clearly indicated that the eye lens crystallins are acetylated with aspirin. Furthermore, no decrease in the radioactivity in the crystallins after exhaustive dialysis against 0.15M NaCl suggests a covalent type of binding of acetyl moiety of aspirin to the lens crystallins. The significant decrease in the free epsilon-amino groups of aspirin-treated crystallins further suggests the probable sites of acetylation in the crystallins. It may be concluded that acetylation of free epsilon-amino groups of lens crystallins by aspirin may confer protection against crystallin aggregation in cataractogenesis.
D000107:Acetylation; D000818:Animals; D001241:Aspirin / Q000494:pharmacology*; D001665:Binding Sites; D002386:Cataract / Q000517:prevention & control*; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D003459:Crystallins / Q000378:metabolism*; D066298:In Vitro Techniques; D007908:Lens, Crystalline / Q000187:drug effects / Q000378:metabolism
D003459:Crystallins; D001241:Aspirin