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.
journal_name
Exp Eye Resjournal_title
Experimental eye researchauthors
Boros S,Wilmarth PA,Kamps B,de Jong WW,Bloemendal H,Lampi K,Boelens WCdoi
10.1016/j.exer.2007.11.011subject
Has Abstractpub_date
2008-02-01 00:00:00pages
383-93issue
2eissn
0014-4835issn
1096-0007pii
S0014-4835(07)00340-5journal_volume
86pub_type
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