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Title: Tissue transglutaminase catalyzes the deamidation of glutamines in lens betaB(2)- and betaB(3)-crystallins.
Author(s): Boros, S. ; Wilmarth, P.A.; Kamps, B.; Jong, W.W.W. de ; Bloemendal, H. ; Lampi, K.; Boelens, W.C.
Publication year: 2008
Source: Experimental Eye Research, vol. 86, iss. 2, (2008), pp. 383-393
ISSN: 0014-4835
DOI: https://doi.org/10.1016/j.exer.2007.11.011
Publication type: Article / Letter to editor

Please use this identifier to cite or link to this item : https://hdl.handle.net/2066/70612   https://hdl.handle.net/2066/70612

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Subject: Bio-Molecular Chemistry
IGMD 9: Renal disorder
NCMLS 2: Metabolism, transport and motion
UMCN 5.4: Renal disorders
Organization: Physiology
Biomolecular Chemistry
Journal title:
Experimental Eye Research
Volume: vol. 86
Issue: iss. 2
Page start: p. 383
Page end: p. 393
Abstract:
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.

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