ArticleBiochemistry2006
Effect of site-directed mutagenesis of methylglyoxal-modifiable arginine residues on the structure and chaperone function of human alphaA-crystallin.
Article in Biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 48 citations in OpenAlex.
- Lens aging and disease: Molecular mechanisms, functional consequences, and pharmacological implications.Progress in retinal and eye research · 2026Review
- Article
- Methylglyoxal Induced Modifications to Stabilize Therapeutic Proteins: A Review.The protein journal · 2024Review
- Oxysterol Compounds in Mouse Mutant αA- and αB-Crystallin Lenses Can Improve the Optical Properties of the Lens.Investigative ophthalmology & visual science · 2022Article
- Structural and functional analysis of SNP rs76740365 G>A in exon-3 of the alpha A-crystallin gene in lens epithelial cells.Molecular vision · 2022Article
- Substrate Protein Interactions and Methylglyoxal Modifications Reduce the Aggregation Propensity of Human Alpha-A-Crystallin G98R Mutant.Frontiers in molecular biosciences · 2022Article
- Creatine kinase/α-crystallin interaction functions in cataract development.Biochemistry and biophysics reports · 2020Article
- Alpha-crystallin mutations alter lens metabolites in mouse models of human cataracts.PloS one · 2020Article
- Characterization of an N-terminal mutant of αA-crystallin αA-R21Q associated with congenital cataract.Experimental eye research · 2018Article
- Probing the changes in gene expression due to α-crystallin mutations in mouse models of hereditary human cataract.PloS one · 2018Article
- Differential role of arginine mutations on the structure and functions of α-crystallin.Biochimica et biophysica acta · 2016Review
- The combined effect of acetylation and glycation on the chaperone and anti-apoptotic functions of human α-crystallin.Biochimica et biophysica acta · 2013Article
- Article
- The small heat-shock protein HspL is a VirB8 chaperone promoting type IV secretion-mediated DNA transfer.The Journal of biological chemistry · 2010Article
- Hydroimidazolone modification of human alphaA-crystallin: Effect on the chaperone function and protein refolding ability.Biochimica et biophysica acta · 2010Article
- The anti-apoptotic function of human αA-crystallin is directly related to its chaperone activity.Cell death & disease · 2010Article
- AlphaA-crystallin R49Cneo mutation influences the architecture of lens fiber cell membranes and causes posterior and nuclear cataracts in mice.BMC ophthalmology · 2009Article
- Deletion of (54)FLRAPSWF(61) residues decreases the oligomeric size and enhances the chaperone function of alphaB-crystallin.Biochemistry · 2009Article
- Role of cysteine residues in the enhancement of chaperone function in methylglyoxal-modified human alpha A-crystallin.Molecular and cellular biochemistry · 2009Article
- Inhibition of crystallin ascorbylation by nucleophilic compounds in the hSVCT2 mouse model of lenticular aging.Investigative ophthalmology & visual science · 2008Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
We reported previously that chemical modification of human alphaA-crystallin by a metabolic dicarbonyl compound, methylglyoxal (MGO), enhances its chaperone-like function, a phenomenon which we attributed to formation of argpyrimidine at arginine residues (R) 21, 49, and 103. This structural change removes the positive charge on the arginine residues. To explore this mechanism further, we replaced these three R residues with a neutral alanine (A) residue one at a time or in combination and examined the impact on the structure and chaperone function. Measurement of intrinsic tryptophan fluorescence and near-UV CD spectra revealed alteration of the microenvironment of aromatic amino acid residues in mutant proteins. When compared to wild-type (wt) alphaA-crystallin, the chaperone function of R21A and R103A mutants increased 20% and 18% as measured by the insulin aggregation assay and increased it as much as 39% and 28% when measured by the citrate synthase (CS) aggregation assay. While the R49A mutant lost most of its chaperone function, R21A/R103A and R21A/R49A/R103A mutants had slightly better function (6-14% and 10-14%) than the wt protein in these assays. R21A and R103A mutants had higher surface hydrophobicity than wt alphaA-crystallin, but the R49A mutant had lower hydrophobicity. R21A and R103A mutants, but not the R49A mutant, were more efficient than wt protein in refolding guanidine hydrochloride-treated malate dehydrogenase to its native state. Our findings indicate that the positive charges on R21, R49, and R103 are important determinants of the chaperone function of alphaA-crystallin and suggest that chemical modification of arginine residues may play a role in protein aggregation during lens aging and cataract formation.
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