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Gene Review

TGM1  -  transglutaminase 1

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Disease relevance of TGM1

  • Hepatitis B surface antigen binds to human serum albumin cross-linked by transglutaminase [1].
  • The transglutaminase-mediated crosslinking of alpha B-crystallin may have implications for its involvement in normal and pathological processes in lens and other tissues [2].
  • The results provide a basis for the suggestion that binding of a peptide to a protein, in connection to its modification to a T cell epitope, might be a general explanation for the role of TG2 in celiac disease and a possible mechanism for the generation of autoantigens [3].

Psychiatry related information on TGM1


High impact information on TGM1

  • Requirement for transglutaminase in the activation of latent transforming growth factor-beta in bovine endothelial cells [5].
  • A hitherto unknown function for transglutaminase (TGase; R-glutaminyl-peptide: amine gamma-glutamyltransferase, EC was found in the conversion of latent transforming growth factor-beta (LTGF-beta) to active TGF-beta by bovine aortic endothelial cells (BAECs) [5].
  • Of particular interest is that antibody TGM-1, unlike TGM-3, bound poorly to homogenates of 19-d embryonic smooth muscles [6].
  • Isolation of transglutaminase-reactive sequences from complex biological systems: a prominent lysine donor sequence in bovine lens [7].
  • Apart from its fluorescent properties, the dansyl hapten offered special advantages as a "handle" for the rapid isolation of transglutaminase targets even in the complex system of lens cortical homogenate [7].

Biological context of TGM1


Anatomical context of TGM1


Associations of TGM1 with chemical compounds


Physical interactions of TGM1


Other interactions of TGM1


Analytical, diagnostic and therapeutic context of TGM1


  1. Hepatitis B surface antigen binds to human serum albumin cross-linked by transglutaminase. Thung, S.N., Wang, D.F., Fasy, T.M., Hood, A., Gerber, M.A. Hepatology (1989) [Pubmed]
  2. The carboxy-terminal lysine of alpha B-crystallin is an amine-donor substrate for tissue transglutaminase. Groenen, P.J., Bloemendal, H., de Jong, W.W. Eur. J. Biochem. (1992) [Pubmed]
  3. Deamidation and cross-linking of gliadin peptides by transglutaminases and the relation to celiac disease. Skovbjerg, H., Koch, C., Anthonsen, D., Sjöström, H. Biochim. Biophys. Acta (2004) [Pubmed]
  4. Transglutaminase catalyzes the formation of sodium dodecyl sulfate-insoluble, Alz-50-reactive polymers of tau. Dudek, S.M., Johnson, G.V. J. Neurochem. (1993) [Pubmed]
  5. Requirement for transglutaminase in the activation of latent transforming growth factor-beta in bovine endothelial cells. Kojima, S., Nara, K., Rifkin, D.B. J. Cell Biol. (1993) [Pubmed]
  6. Localization and topography of antigenic domains within the heavy chain of smooth muscle myosin. Schneider, M.D., Sellers, J.R., Vahey, M., Preston, Y.A., Adelstein, R.S. J. Cell Biol. (1985) [Pubmed]
  7. Isolation of transglutaminase-reactive sequences from complex biological systems: a prominent lysine donor sequence in bovine lens. Lorand, L., Velasco, P.T., Murthy, S.N., Wilson, J., Parameswaran, K.N. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  8. The transglutaminase in vascular cells and tissues could provide an alternate pathway for fibrin stabilization. Greenberg, C.S., Achyuthan, K.E., Borowitz, M.J., Shuman, M.A. Blood (1987) [Pubmed]
  9. Characterization of transglutaminase activity in rabbit tracheal epithelial cells. Regulation by retinoids. Jetten, A.M., Shirley, J.E. J. Biol. Chem. (1986) [Pubmed]
  10. Identification of a substrate site for liver transglutaminase on the aminopropeptide of type III collagen. Bowness, J.M., Folk, J.E., Timpl, R. J. Biol. Chem. (1987) [Pubmed]
  11. Lens transglutaminase selects specific beta-crystallin sequences as substrate. Berbers, G.A., Feenstra, R.W., van den Bos, R., Hoekman, W.A., Bloemendal, H., de Jong, W.W. Proc. Natl. Acad. Sci. U.S.A. (1984) [Pubmed]
  12. Covalent cross-linking of secreted bovine thyroglobulin by transglutaminase. Saber-Lichtenberg, Y., Brix, K., Schmitz, A., Heuser, J.E., Wilson, J.H., Lorand, L., Herzog, V. FASEB J. (2000) [Pubmed]
  13. Epidermal transglutaminase. Identification and purification of a soluble substrate with studies of in vitro cross-linking. Buxman, M.M., Lobitz, C.J., Wuepper, K.D. J. Biol. Chem. (1980) [Pubmed]
  14. Identification of a guanosine triphosphate-binding site on guinea pig liver transglutaminase. Role of GTP and calcium ions in modulating activity. Achyuthan, K.E., Greenberg, C.S. J. Biol. Chem. (1987) [Pubmed]
  15. Stabilization of follicle-stimulating hormone-receptor complexes may involve calcium-dependent transglutaminase activation. Grasso, P., Reichert, L.E. Mol. Cell. Endocrinol. (1992) [Pubmed]
  16. Microfibril-associated glycoprotein binds to the carboxyl-terminal domain of tropoelastin and is a substrate for transglutaminase. Brown-Augsburger, P., Broekelmann, T., Mecham, L., Mercer, R., Gibson, M.A., Cleary, E.G., Abrams, W.R., Rosenbloom, J., Mecham, R.P. J. Biol. Chem. (1994) [Pubmed]
  17. Posttranslational modifications of microfibril associated glycoprotein-1 (MAGP-1). Trask, B.C., Broekelmann, T., Ritty, T.M., Trask, T.M., Tisdale, C., Mecham, R.P. Biochemistry (2001) [Pubmed]
  18. Formation of high molecular weight dermatan sulfate proteoglycan in bovine aortic endothelial cell cultures. Evidence for transglutaminase-catalyzed cross-linking to fibronectin. Kinsella, M.G., Wight, T.N. J. Biol. Chem. (1990) [Pubmed]
  19. Identification and sequence analysis of two new members of the SKALP/elafin and SPAI-2 gene family. Biochemical properties of the transglutaminase substrate motif and suggestions for a new nomenclature. Zeeuwen, P.L., Hendriks, W., de Jong, W.W., Schalkwijk, J. J. Biol. Chem. (1997) [Pubmed]
  20. Cross-linking of osteopontin by tissue transglutaminase increases its collagen binding properties. Kaartinen, M.T., Pirhonen, A., Linnala-Kankkunen, A., Mäenpää, P.H. J. Biol. Chem. (1999) [Pubmed]
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