RRC ID 43226
著者 Boros S, Wilmarth PA, Kamps B, de Jong WW, Bloemendal H, Lampi K, Boelens WC.
タイトル Tissue transglutaminase catalyzes the deamidation of glutamines in lens betaB(2)- and betaB(3)-crystallins.
ジャーナル 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.
巻・号 86(2)
ページ 383-93
公開日 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
引用数 16
WOS 分野 OPHTHALMOLOGY
リソース情報
ヒト・動物細胞 anti-αB-crystallin(RCB1304)