Manzanares D, Bauby C, de la Peña R, Garcia J C, Sanchez R, Martinez S, Romay C H, López-Reconde J L, Pino E, Lissi E A
Centro de Investigaciones Biomédicas, Instituto Superior de Ciencias Médicas de la Habana, Cuba.
J Protein Chem. 2001 Apr;20(3):181-9. doi: 10.1023/a:1010996528884.
alpha-Crystallin is a major chaperone lens protein to which has been ascribed antioxidant functions. In the present work we have evaluated the antioxidant and free radical scavenging properties of bovine alpha-crystallin in a series of in vitro models: zimosan-induced, luminol-enhanced chemiluminescence response of polymorphonuclear leukocytes, the autoxidation of brain homogenate, bleaching of 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)-derived radical cations, trapping of peroxyl radicals, and reactivity toward hypochloric acid. In all these systems, the reactivity of alpha-crystallin is higher than or similar to that of bovine serum albumin. It is concluded that, given the high concentrations of ol-crystallin in the lenses, its capacity to interact with free radicals and to remove hypochlorous acid could contribute to the maintenance of the lens functionality.