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Gene Review

GSTM2  -  glutathione S-transferase mu 2 (muscle)

Homo sapiens

Synonyms: GST class-mu 2, GST4, GSTM, GSTM2-2, GTHMUS, ...
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Disease relevance of GSTM2


High impact information on GSTM2


Biological context of GSTM2

  • For the mu family, 90% of the lines had GSTM2, 68% had GSTM3, but only 28% were positive for the M1 phenotype [5].
  • The N-terminal amino acid sequence of GST6 was found to be identical with that of GST4 previously purified from human muscle [6].
  • This complex binds with extraordinary affinity to the active site of all these dimeric enzymes; GSTA1-1 shows the strongest interaction (KD congruent with 10-10 m), whereas GSTM2-2 and GSTP1-1 display similar and slightly lower affinities (KD congruent with 10-9 m) [4].
  • Other isoenzymes with fast anodal mobilities were also identified in several tissues; these are believed to be GST3 isoenzymes that have undergone posttranslational modification rather than products of the putative GST4 locus [7].
  • We also identified regions of conserved synteny, each containing the Gstm2 gene, on mouse chromosome 3 and human chromosome 1 [8].

Anatomical context of GSTM2

  • In colon fibroblasts, butyrate (4 mM, 72 h) also induced GSTM2 protein (1.7-fold) and GST activity (1.4-fold) [9].
  • An hGSTM2-2-like protein was isolated from rabbit skeletal muscle and sheep heart, at concentrations of approximately 17-93muM [10].
  • When added to the cytoplasmic side of RyRs, hGSTM2-2 and GST isolated from skeletal or cardiac muscle, modified channel activity in an RyR isoform-specific manner [10].

Associations of GSTM2 with chemical compounds

  • However, butyrate, an important luminal component produced from fermentation of dietary fibers, is an efficient inducer of GSTs and especially of GSTM2 [9].
  • GSTM2-2 and 3-3 may play crucial roles in temperature regulation, nociception, and sleep-wake regulation by producing PGE2 in the brain [11].
  • Michaelis-Menten constants and turnover numbers for PGH2 were 141 microM and 10.8 min(-1) for GSTM2-2 and 1.5 mM and 130 min(-1) for GSTM3-3, respectively [11].
  • Cloning, expression, and characterization of a class-mu glutathione transferase from human muscle, the product of the GST4 locus [1].
  • CDNA-derived amino acid sequence analysis revealed that mfaGSTM1 and mfaGSTM2 share 97% and 96% homology with the human mu-class GSTs hGSTM4 and hGSTM2, respectively [12].

Regulatory relationships of GSTM2

  • GSTM2 transcript was expressed in all patients in contradistinction to GSTM5, which was not detected in any sample [13].

Other interactions of GSTM2


Analytical, diagnostic and therapeutic context of GSTM2

  • The three-dimensional structure of ligand-free hGSTM2-2 determined by x-ray crystallography suggests that Arg(107) maintains an electrostatic interaction with the Asp(161) side chain (3 A apart), but is distant from the GSH-binding site [16].
  • Human muscle specific glutathione S-transferase (RX: glutathione R-transferase, EC (GST-4) and liver GST-1 have been purified and subjected to N-terminal sequence analysis [17].


  1. Cloning, expression, and characterization of a class-mu glutathione transferase from human muscle, the product of the GST4 locus. Vorachek, W.R., Pearson, W.R., Rule, G.S. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  2. Identification of class-mu glutathione transferase genes GSTM1-GSTM5 on human chromosome 1p13. Pearson, W.R., Vorachek, W.R., Xu, S.J., Berger, R., Hart, I., Vannais, D., Patterson, D. Am. J. Hum. Genet. (1993) [Pubmed]
  3. Immunohistochemical localization of glutathione S-transferases in human lung. Anttila, S., Hirvonen, A., Vainio, H., Husgafvel-Pursiainen, K., Hayes, J.D., Ketterer, B. Cancer Res. (1993) [Pubmed]
  4. The specific interaction of dinitrosyl-diglutathionyl-iron complex, a natural NO carrier, with the glutathione transferase superfamily: suggestion for an evolutionary pressure in the direction of the storage of nitric oxide. De Maria, F., Pedersen, J.Z., Caccuri, A.M., Antonini, G., Turella, P., Stella, L., Lo Bello, M., Federici, G., Ricci, G. J. Biol. Chem. (2003) [Pubmed]
  5. Glutathione-associated enzymes in the human cell lines of the National Cancer Institute Drug Screening Program. Tew, K.D., Monks, A., Barone, L., Rosser, D., Akerman, G., Montali, J.A., Wheatley, J.B., Schmidt, D.E. Mol. Pharmacol. (1996) [Pubmed]
  6. Purification and characterization of acidic glutathione S-transferase 6 from human brain. Suzuki, T., Shaw, D.C., Board, P.G. Biochem. J. (1991) [Pubmed]
  7. The human glutathione S-transferases: developmental aspects of the GST1, GST2, and GST3 loci. Strange, R.C., Davis, B.A., Faulder, C.G., Cotton, W., Bain, A.D., Hopkinson, D.A., Hume, R. Biochem. Genet. (1985) [Pubmed]
  8. Microarray analysis of rat chromosome 2 congenic strains. McBride, M.W., Carr, F.J., Graham, D., Anderson, N.H., Clark, J.S., Lee, W.K., Charchar, F.J., Brosnan, M.J., Dominiczak, A.F. Hypertension (2003) [Pubmed]
  9. Expression of glutathione S-transferases (GSTs) in human colon cells and inducibility of GSTM2 by butyrate. Ebert, M.N., Klinder, A., Peters, W.H., Schäferhenrich, A., Sendt, W., Scheele, J., Pool-Zobel, B.L. Carcinogenesis (2003) [Pubmed]
  10. The Mu class glutathione transferase is abundant in striated muscle and is an isoform-specific regulator of ryanodine receptor calcium channels. Abdellatif, Y., Liu, D., Gallant, E.M., Gage, P.W., Board, P.G., Dulhunty, A.F. Cell Calcium (2007) [Pubmed]
  11. Identification of mu-class glutathione transferases M2-2 and M3-3 as cytosolic prostaglandin E synthases in the human brain. Beuckmann, C.T., Fujimori, K., Urade, Y., Hayaishi, O. Neurochem. Res. (2000) [Pubmed]
  12. Mu-class GSTs are responsible for aflatoxin B(1)-8, 9-epoxide-conjugating activity in the nonhuman primate macaca fascicularis liver. Wang, C., Bammler, T.K., Guo, Y., Kelly, E.J., Eaton, D.L. Toxicol. Sci. (2000) [Pubmed]
  13. Mu class glutathione S-transferase mRNA isoform expression in acute lymphoblastic leukaemia. Kearns, P.R., Chrzanowska-Lightowlers, Z.M., Pieters, R., Veerman, A., Hall, A.G. Br. J. Haematol. (2003) [Pubmed]
  14. Genotoxicity of 4-hydroxy-2-nonenal in human colon tumor cells is associated with cellular levels of glutathione and the modulation of glutathione S-transferase A4 expression by butyrate. Knoll, N., Ruhe, C., Veeriah, S., Sauer, J., Glei, M., Gallagher, E.P., Pool-Zobel, B.L. Toxicol. Sci. (2005) [Pubmed]
  15. Studies on the developmental expression of glutathione S-transferase isoenzymes in human heart and diaphragm. Hirrell, P.A., Hume, R., Fryer, A.A., Collins, M.F., Drew, R., Bradwell, A.R., Strange, R.C. Biochim. Biophys. Acta (1987) [Pubmed]
  16. The enhanced affinity for thiolate anion and activation of enzyme-bound glutathione is governed by an arginine residue of human Mu class glutathione S-transferases. Patskovsky, Y.V., Patskovska, L.N., Listowsky, I. J. Biol. Chem. (2000) [Pubmed]
  17. Human muscle glutathione S-transferase (GST-4) shows close homology to human liver GST-1. Board, P.G., Suzuki, T., Shaw, D.C. Biochim. Biophys. Acta (1988) [Pubmed]
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