BENDAZAC DECREASES IN-VITRO GLYCATION OF HUMAN LENS CRYSTALLINS - DECREASE OF IN-VITRO PROTEIN GLYCATION BY BENDAZAC

Bendazac has been used as an anti-cataractogenic drug. It has been rep orted that this acts by preventing protein denaturation. In this study the ability of bendazac to inhibit in vitro glycation of human lens c rystallins was evaluated. Possible effects of bendazac were detected b y incubation of WS crystallins with the reducing sugars glucose and fr uctose. The efficiency of bendazac was evaluated by means of selected parameters including: browning, glycation (measured as tyrosine conten t) and specific NTP-fluorescence. The results showed clearly that bend azac (bendazac L-lysine and sodium) inhibits the early stages of prote in glycation, as well as the formation of fluorescent advanced glycati on products. Bendazac lysine (20 mM) proved to be more effective in in hibiting fluorescence development (67% inhibition) than the correspond ing sodium salt (35% inhibition). No significant differences were foun d with respect to furosine levels; about 40% inhibition was produced w ith either bendazac lysine or sodium salt bendazac clearly inhibits gl ycation of human lens crystallins, as can be efficiently monitored by following specific changes in lens protein fluorescence. These results may constitute a new and relevant therapeutic approach to monitoring cataract development.