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Gene Review

TGM4  -  transglutaminase 4

Homo sapiens

Synonyms: Fibrinoligase, Prostate transglutaminase, Prostate-specific transglutaminase, Protein-glutamine gamma-glutamyltransferase 4, TG(P), ...
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Disease relevance of TGM4

  • Deletion mapping of the TGM4 promoter in the transiently transfected human prostate cancer cell line PC346C showed comparable activity of 2.1-, 1.5-, and 0.5-kb promoter fragments [1].
  • It has been reported that approximately one-third of human volunteers, smokers and nonsmokers, exhibit immediate cutaneous hypersensitivity to a glycoprotein antigen (TGP) purified from cured tobacco leaves and present in cigarette smoke [2].
  • In experiments described herein anaphylaxis was induced in the isolated hearts and lungs of rabbits and guinea pigs previously sensitized by immunization with TGP and challenged with TGP isolated from either tobacco leaf or cigarette smoke condensate [2].

High impact information on TGM4


Biological context of TGM4


Anatomical context of TGM4

  • TGP, a phenol-rich glycoprotein which is present in tobacco leaves and cigarette smoke condensate, activates the immune system [9].
  • The prosegment, termed "cementoin," exhibits high homology with the repetitive element of seminal vesicle clotting protein, which is known as a good substrate for prostate transglutaminase [10].
  • To evaluate the usefulness of the TGP1 score, microarray data of rat liver and rat hepatocytes deposited in the TGP database were scored for three biomarker gene sets, i.e., carcinogenesis-related, PPARalpha-regulated and glutathione depletion-related gene sets [11].
  • OBJECTIVES: TGP (thermo-reversible gelation polymer) is a high molecular compound that has so-gel transmitting temperature of 221C Since solid cancer tissue grows in this polymer three-dimensionally, and fibroblasts scarcely grow in it, TGP is suitable for chemosensitivity assays for solid tumors [12].

Associations of TGM4 with chemical compounds


Other interactions of TGM4

  • A method is proposed for assaying fibrinoligase, based on the rate of ammonia production in the presence of casein as substrate [15].

Analytical, diagnostic and therapeutic context of TGM4

  • This paper deals with the molecular cloning and characterization of the cDNA encoding the human prostate TGase (hTGP) [5].
  • Ammonia production during clot retraction and its use in assay of fibrinoligase [15].
  • Fine clots (with little lateral aggregation of the fibrin protofibrils) were found at pH 8.5, ionic strength 0.45; coarse clots (with substantial lateral aggregation) were formed at pH 7.5, ionic strength 0.15; in both cases with and without ligation by fibrinoligase [16].
  • We describe a method which makes it possible to study the expression of the trimeric glycoprotein (TGP, CD 103) on the surface of hairy cells (HCs) by electron microscopy (e.m.). The monoclonal antibody (mAb) Ber-ACT8 was used to identify the TGP [17].


  1. The human prostate-specific transglutaminase gene (TGM4): genomic organization, tissue-specific expression, and promoter characterization. Dubbink, H.J., de Waal, L., van Haperen, R., Verkaik, N.S., Trapman, J., Romijn, J.C. Genomics (1998) [Pubmed]
  2. Cardiac and pulmonary anaphylaxis in guinea pigs and rabbits induced by glycoprotein isolated from tobacco leaves and cigarette smoke condensate. Levi, R., Zavecz, J.H., Burke, J.A., Becker, C.G. Am. J. Pathol. (1982) [Pubmed]
  3. Primary structure of blood coagulation factor XIIIa (fibrinoligase, transglutaminase) from human placenta. Takahashi, N., Takahashi, Y., Putnam, F.W. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  4. Kinetics of ligation of fibrin oligomers. Nelb, G.W., Kamykowski, G.W., Ferry, J.D. J. Biol. Chem. (1980) [Pubmed]
  5. Tissue specific and androgen-regulated expression of human prostate-specific transglutaminase. Dubbink, H.J., Verkaik, N.S., Faber, P.W., Trapman, J., Schröder, F.H., Romijn, J.C. Biochem. J. (1996) [Pubmed]
  6. Organization of the Tgm family of transposable elements in soybean. Rhodes, P.R., Vodkin, L.O. Genetics (1988) [Pubmed]
  7. Localization of the human prostate transglutaminase (type IV) gene (TGM4) to chromosome 3p21.33-p22 by fluorescence in situ hybridization. Gentile, V., Grant, F.J., Porta, R., Baldini, A. Genomics (1995) [Pubmed]
  8. Transamidase kinetics. Amide formation in the enzymic reactions of thiol esters with amines. Stenberg, P., Curtis, C.G., Wing, D., Tong, Y.S., Credo, R.B., Gray, A., Lorand, L. Biochem. J. (1975) [Pubmed]
  9. IL-1, IL-6, and PDGF mRNA expression in alveolar cells following stimulation with a tobacco-derived antigen. Francus, T., Romano, P.M., Manzo, G., Fonacier, L., Arango, N., Szabo, P. Cell. Immunol. (1992) [Pubmed]
  10. Elastase inhibitor elafin is a new type of proteinase inhibitor which has a transglutaminase-mediated anchoring sequence termed "cementoin". Nara, K., Ito, S., Ito, T., Suzuki, Y., Ghoneim, M.A., Tachibana, S., Hirose, S. J. Biochem. (1994) [Pubmed]
  11. Utilization of a one-dimensional score for surveying chemical-induced changes in expression levels of multiple biomarker gene sets using a large-scale toxicogenomics database. Kiyosawa, N., Shiwaku, K., Hirode, M., Omura, K., Uehara, T., Shimizu, T., Mizukawa, Y., Miyagishima, T., Ono, A., Nagao, T., Urushidani, T. The Journal of toxicological sciences (2006) [Pubmed]
  12. New chemosensitivity test using a thermo-reversible gelation polymer for recurrent gynecologic cancer patients and a preliminary study of mechanisms of anticancer drug resistance. Ohara, T., Kiguchi, K., Tsukikawa, S., Sato, S., Kobayashi, Y., Ishizuka, B., Kubota, S. Hum. Cell (2005) [Pubmed]
  13. Alpha-chain domain of fibrinogen controls generation of fibrinoligase (coagulation factor XIIIa). Calcium ion regulatory aspects. Credo, R.B., Curtis, C.G., Lorand, L. Biochemistry (1981) [Pubmed]
  14. Fate of oxidized triglycerides during refining of seed oils. Gomes, T., Caponio, F., Delcuratolo, D. J. Agric. Food Chem. (2003) [Pubmed]
  15. Ammonia production during clot retraction and its use in assay of fibrinoligase. Mousli, S., Wakid, N.W. Clin. Chem. (1977) [Pubmed]
  16. Modification of shear modulus and creep compliance of fibrin clots by fibronectin. Kamykowski, G.W., Mosher, D.F., Lorand, L., Ferry, J.D. Biophys. Chem. (1981) [Pubmed]
  17. Immune electron-microscopy study of the trimeric glycoprotein (CD 103) of hairy cell leukemia using the Ber-ACT8 monoclonal antibody. Frangoulidis, D., Schulz, A., Pralle, H. Ann. Hematol. (1994) [Pubmed]
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