Deamidation of Human γS-Crystallin Increases Attractive Protein Interactions: Implications for Cataract.

ABSTRACT: Deamidation of proteins is one of the most prevalent post-translational modifications found upon aging, and in age-onset diseases. Specific asparagine and glutamine residues are often selectively deamidated during this process. In the human lens, deamidation has been shown to occur in many crystallins, but it is not clear how these deamidated proteins lead to lens opacity or cataract. Here we have modeled in vitro the effect of deamidation of specific asparagine and glutamine residues in human recombinant γS-crystallin (HGS) on the solution properties of the protein. The residues selected for deamidation in vitro are those that are found to be deamidated in aged and cataractous lenses in vivo. Two derivatives were prepared, one with Asn76 and Asn143 deamidated (2N-HGS) and the other with t

SUBMITTER: Pande A 

PROVIDER: S-EPMC5760270 | biostudies-literature | 2015 Aug

REPOSITORIES: biostudies-literature