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dc.contributor.authorBhattacharyya, Jayaeng
dc.contributor.authorSanthoshkumar, Puttureng
dc.contributor.authorSharma, K. Krishnaeng
dc.contributor.authorShipova, Ekaterina V.eng
dc.contributor.authorOrtwerth, Beryl J.eng
dc.date.issued2007eng
dc.description.abstractDuring aging, human lens proteins undergo several post-translational modifications, one of which is glycation. This process leads to the formation of advanced glycation end products (AGEs) which accumulate with time possibly leading to the formation of cataract. [alpha]B-Crystallin, a predominant protein in the lens, is a member of the small heat shock proteins (sHSPs) which are a ubiquitous class of molecular chaperones that interact with partially denatured proteins to prevent aggregation. This chaperone function is considered to be vital for the maintenance of lens transparency and in the prevention of cataract. In the present study, we introduced an analog of the advanced glycation end product, OP-lysine, at the 90th position of a mutated human [alpha]B-crystallin (K90C) by covalent modification of the cysteine residue with N-(2-bromoethyl)-3-oxidopyridinium hydrobromide. The AGE-modified K90C-[alpha]B-crystallin is termed as K90C-OP. We compared the structural and functional properties of K90C-OP with the original K90C mutant, with K90C chemically modified back to a lysine analog (K90C-AE), and with wild-type human [alpha]B-crystallin. Modified K90C-OP showed decreased intrinsic tryptophan fluorescence and bis-ANS binding without significant alterations in either the secondary, tertiary, or quaternary structure. K90C-OP, however, exhibited a reduced efficiency in the chaperoning ability with alcohol dehydrogenase, insulin, and citrate synthase as substrates compared to the other [alpha]-crystallin proteins. Therefore, introduction of a single AGE near the chaperone site of human [alpha]B-crystallin can alter the chaperoning ability of the protein with only minor changes in the local environment of the protein.eng
dc.identifier.citationBiochemistry, 2007, 46 (50), pp 14682-14692eng
dc.identifier.urihttp://hdl.handle.net/10355/3247eng
dc.languageEnglisheng
dc.publisherAmerican Chemical Societyeng
dc.relation.ispartofProteomics Center publications (MU)eng
dc.relation.ispartofcommunityUniversity of Missouri-Columbia. Christopher S. Bond Life Sciences Center. Proteomics Centereng
dc.rightsOpenAccesseng
dc.rights.licenseThis work is licensed under a Creative Commons Attribution-NonCommerical-NoDerivs 3.0 License.
dc.subjectvisioneng
dc.subjectcrystallineng
dc.subjectglycationeng
dc.subjectproteineng
dc.subject.disciplineLife scienceseng
dc.subject.lcshGlycosylationeng
dc.subject.lcshCataracteng
dc.subject.lcshCrystalline lenseng
dc.subject.lcshProteomicseng
dc.subject.lcshVision -- Researcheng
dc.titleEffect of a single AGE modification on the structure and chaperone activity of human alphaB-Crystallineng
dc.typeArticleeng


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