RRC ID 43226
Author Boros S, Wilmarth PA, Kamps B, de Jong WW, Bloemendal H, Lampi K, Boelens WC.
Title Tissue transglutaminase catalyzes the deamidation of glutamines in lens betaB(2)- and betaB(3)-crystallins.
Journal Exp Eye Res
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.
Volume 86(2)
Pages 383-93
Published 2008-2-1
DOI 10.1016/j.exer.2007.11.011
PII S0014-4835(07)00340-5
PMID 18184610
MeSH Aging / metabolism Amides / metabolism Animals Catalysis Cattle Fetus / metabolism GTP-Binding Proteins / pharmacology* Glutamine / metabolism* Humans In Vitro Techniques Lens, Crystalline / drug effects* Lens, Crystalline / embryology Lens, Crystalline / metabolism Middle Aged Protein Glutamine gamma Glutamyltransferase 2 Proteome / drug effects Transglutaminases / pharmacology* beta-Crystallin B Chain / metabolism*
IF 3.011
Times Cited 16
WOS Category OPHTHALMOLOGY
Resource
Human and Animal Cells anti-αB-crystallin(RCB1304)