Modulation of alpha-crystallin chaperone activity: a target to prevent or delay cataract?
Cataract, loss of eye lens transparency, is the leading cause of blindness worldwide. alpha-Crystallin, initially known as one of the major structural proteins of the eye lens, is composed of two homologous subunits alphaA- and alphaB-crystallins. It is convincingly established now that alpha-crystallin functions like a chaperone and plays a decisive role in the maintenance of eye lens transparency. The functional ability of alpha-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 alpha-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 alpha-crystallin chaperone function to lens transparency. In particular, we reviewed the studies that demonstrate the modulation of alpha-crystallin chaperone-like activity and discussed the possibility of chaperone-like activity of alpha-crystallin as a potential target to prevent or delay the cataractogenesis.
Kumar
Pasupulati Anil
PA
Biochemistry Division, National Institute of Nutrition, Hyderabad, Andhra Pradesh, India.
Reddy
Geereddy Bhanuprakash
GB
D000818:Animals; D002386:Cataract / Q000378:metabolism*; D004032:Diet; D006801:Humans; D007908:Lens, Crystalline / Q000378:metabolism*; D018832:Molecular Chaperones / Q000378:metabolism*; D038201:alpha-Crystallins / Q000378:metabolism*
D018832:Molecular Chaperones; D038201:alpha-Crystallins