Decreased Molecular Chaperone Property of α-Crystallins Due to Posttranslational Modifications
Copyright policy )Decreased Molecular Chaperone Property of α-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.
Adolescent, Age Factors, In Vitro Techniques, Crystallins, Animals, Humans, Cattle, Disulfides, Oxidation-Reduction, Protein Processing, Post-Translational, Aged, Molecular Chaperones
Adolescent, Age Factors, In Vitro Techniques, Crystallins, Animals, Humans, Cattle, Disulfides, Oxidation-Reduction, Protein Processing, Post-Translational, Aged, Molecular Chaperones
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