Scientific background: |
Tissue transglutaminase, also called TGC, is a 78-kDa, calcium dependent enzyme of the protein-glutamine gamma-glutamyltransferases family. By fluorescence in situ hybridization (FISH), this gene is mapped in 20q11.23. Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. The protein encoded by this gene acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. Finally, the encoded protein is the autoantigen implicated in celiac disease. |
References: |
1. Antonyak, M. A., Jansen, J. M., Miller, A. M., Ly, T. K., Endo, M., Cerione, R. A. Two isoforms of tissue transglutaminase mediate opposing cellular fates. Proc. Nat. Acad. Sci. 103: 18609-18614, 2006.
2. Mastroberardino, P. G., Iannicola, C., Nardacci, R., Bernassola, F., de Laurenzi, V., Melino, G., Moreno, S., Pavone, F., Oliverio, S., Fesus, L., Piacentini, M. 'Tissue' transglutaminase ablation reduces neuronal death and prolongs survival in a mouse model of Huntington's disease. Cell Death Differ. 9: 873-880, 2002.
3. Priglinger, S. G., May, C. A., Neubauer, A. S., Alge, C. S., Schoenfeld, C.-L., Kampik, A., Welge-Lussen, U. Tissue transglutaminase as a modifying enzyme of the extracellular matrix in PVR membranes. Invest. Ophthal. Vis. Sci. 44: 355-364, 2003.
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