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

AbstractCataract, 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 IUBMB Life, 61(5): 485–495, 2009

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