Decreased molecular chaperone property of alpha-crystallins due to posttranslational modifications.
We studied the effect of oxidation, mixed disulfide formation and glycation of alpha-crystallins on their molecular chaperone property. The ability of alpha-crystallins to protect heat-induced denaturation and aggregation of beta L-crystallin was significantly diminished by these modifications. alpha-Crystallin from senile human lenses also showed significant loss of chaperone-like property. Age-dependent increase in posttranslationally modified alpha-crystallins is the likely cause for this change.
Cherian
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Department of Biochemistry and Molecular Biology, Medical College of Georgia, Augusta 30912-2100.
Abraham
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EC
D000293:Adolescent; D000367:Age Factors; D000368:Aged; D000818:Animals; D002417:Cattle; D003459:Crystallins / Q000378:metabolism*; D004220:Disulfides; D006801:Humans; D066298:In Vitro Techniques; D018832:Molecular Chaperones; D010084:Oxidation-Reduction; D011499:Protein Processing, Post-Translational
D003459:Crystallins; D004220:Disulfides; D018832:Molecular Chaperones