ArticleMolecular and cellular biochemistry2009
Role of cysteine residues in the enhancement of chaperone function in methylglyoxal-modified human alpha A-crystallin.
Article in Molecular and cellular biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- The E156K mutation in theHeliyon · 2024Article
- Protein posttranslational modification (PTM) by glycation: Role in lens aging and age-related cataractogenesis.Experimental eye research · 2021Review
- Article
- The oxidized thiol proteome in aging and cataractous mouse and human lens revealed by ICAT labeling.Aging cell · 2017Article
- Site-directed mutagenesis substituting cysteine for serine in 2-Cys peroxiredoxin (2-Cys Prx A) of Arabidopsis thaliana effectively improves its peroxidase and chaperone functions.Annals of botany · 2015Article
- The role of the cysteine residue in the chaperone and anti-apoptotic functions of human Hsp27.Journal of cellular biochemistry · 2010Article
- Lens aging: effects of crystallins.Biochimica et biophysica acta · 2009Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
We have previously demonstrated that the reaction of a physiological dicarbonyl, methylglyoxal (MGO) enhances the chaperone function of human alpha A-crystallin. MGO can react with cysteine, arginine, and lysine residues in proteins. Although the role of arginine and lysine residues in the enhancement of chaperone function has been investigated, the role of cysteine residues is yet to be determined. In this study, we have investigated the effect of MGO modification on the structure and chaperone function of alpha A-crystallin mutant proteins in which C131 and C142 were replaced either individually or simultaneously with isoleucine. MGO-modification resulted in improved chaperone function in all three alpha A-crystallin mutants, including the cysteine-free double mutant. The enhanced chaperone function was due to increased surface hydrophobicity and increased binding of client proteins. These results suggest that the two cysteine residues, even though they could be modified, do not take part in the MGO-induced improvement in the chaperone function of human alpha A-crystallin.
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