Modulation of α-crystallin chaperone activity: A target to prevent or delay cataract?

Abstract

Cataract, loss of eye lens transparency, is the leading cause of blindness worldwide. α-Crystallin, initially known as one of the major structural proteins of the eye lens, is composed of two homologous subunits αA- and αB-crystallins. It is convincingly established now that α-crystallin functions like a chaperone and plays a decisive role in the maintenance of eye lens transparency. The functional ability of α-crystallin subunits is to act in cooperation as molecular chaperones to prevent the cellular aggregation and/or inactivation of client proteins under variety of stress conditions. However, chaperone-like activity of α-crystallin could be deteriorated or lost during aging or under certain clinical conditions because of various genetic and environmental factors. This review will focus specifically on relevance of α-crystallin chaperone function to lens transparency. In particular, we reviewed the studies that demonstrate the modulation of α-crystallin chaperone-like activity and discussed the possibility of chaperone-like activity of α-crystallin as a potential target to prevent or delay the cataractogenesis. © 2009 IUBMB.