Tissue transglutaminase catalyzes the deamidation of glutamines in lens betaB(2)- and betaB(3)-crystallins.

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Publication year
2008Source
Experimental Eye Research, 86, 2, (2008), pp. 383-93ISSN
Publication type
Article / Letter to editor

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Organization
Physiology
Biomolecular Chemistry
Journal title
Experimental Eye Research
Volume
vol. 86
Issue
iss. 2
Page start
p. 383
Page end
p. 93
Subject
Bio-Molecular Chemistry; IGMD 9: Renal disorder; NCMLS 2: Metabolism, transport and motion; UMCN 5.4: Renal disordersAbstract
Tissue transglutaminase (tTG) is a Ca(2+)-dependent enzyme catalyzing the formation of covalent crosslinks between peptide-bound glutamine and lysine residues. Lens crystallins, including alphaB-crystallin and several beta-crystallins, are in vitro substrates for tTG. In both human and bovine fetal lens extracts treated with commercially available guinea pig liver tTG we detected the formation of high molecular weight (HMW) aggregates containing crosslinked betaB(2)- and betaA(3)-crystallin. More interestingly, 2D-gel electrophoresis combined with mass spectrometry analysis revealed that glutamines present in the N-terminal arms of betaB(2)- and betaB(3)-crystallins deamidate readily in the presence of tTG. We found that both tTG-catalyzed crosslinking and deamidation disrupt the beta-crystallin complex, suggesting that these tTG-catalyzed modifications can influence the macromolecular assembly of lens crystallins. These data together suggest that tTG can contribute to the age-related deamidation of glutamine residues of lens crystallins.
This item appears in the following Collection(s)
- Academic publications [227864]
- Electronic publications [107337]
- Faculty of Medical Sciences [86218]
- Faculty of Science [33774]
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