Transglutaminases (TGMs) catalyze the formation of lysine isodipeptide crosslinks in proteins between the gamma-amide of a donor glutamine and the epsilon-NH2 of an acceptor lysine. The result is a stable, insoluble macromolecular structure, a process used widely throughout the plant and animal kingdoms.
Pathology
Epidermal transglutaminase (TGM3) is the autoantigen of dermatitis herpetiformis. (11901200)
Expression of transglutaminase 3 (TGM3) was significantly down-regulated in cancer and correlated with loss of histological differentiation.
Hypermethylation of TGM3 gene CpG islands was observed in 12 oral squamous cell carcinoma (OSCC) cell lines with reduced TGM3 expression.
Epigenetic silencing of TGM3 plays certain roles in the process of oral carcinogenesis.
See also
References
Quantitative proteomics using formalin-fixed paraffin-embedded tissues of oral squamous cell carcinoma. Negishi A, Masuda M, Ono M, Honda K, Shitashige M, Satow R, Sakuma T, Kuwabara H, Nakanishi Y, Kanai Y, Omura K, Hirohashi S, Yamada T. Cancer Sci. 2009 Sep;100(9):1605-11. PMID: 19522851
Transglutaminase 3 as a prognostic biomarker in esophageal cancer revealed by proteomics. Uemura N, Nakanishi Y, Kato H, Saito S, Nagino M, Hirohashi S, Kondo T. Int J Cancer. 2009 May 1;124(9):2106-15. PMID: 19142970
Sardy, M.; Karpati, S.; Merkl, B.; Paulsson, M.; Smyth, N. : Epidermal transglutaminase (TGase 3) is the autoantigen of dermatitis herpetiformis. J. Exp. Med. 195: 747-757, 2002. PubMed ID : 11901200