GSTM4

GSTM4
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4GTU
Identifiers
Aliases	GSTM4 , GSTM4-4, GTM4, glutathione S-transferase mu 4
External IDs	OMIM: 138333 MGI: 95862 HomoloGene: 37357 GeneCards: GSTM4
Gene location (Human) Chr. Chromosome 1 (human) [1] Band 1p13.3 Start 109,656,099 bp [1] End 109,674,836 bp [1]
Gene location (Mouse) Chr. Chromosome 3 (mouse) [2] Band 3|3 F2.3 Start 107,947,724 bp [2] End 107,952,210 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gastrocnemius muscle rectum right lobe of liver right lobe of thyroid gland duodenum gastric mucosa Right adrenal gland left lobe of thyroid gland stromal cell of endometrium nucleus accumbens Top expressed in yolk sac left lobe of liver duodenum proximal tubule facial motor nucleus brown adipose tissue white adipose tissue skeletal muscle tissue intercostal muscle respiratory epithelium More reference expression data BioGPS n/a
Gene ontology Molecular function transferase activity enzyme binding glutathione transferase activity protein binding protein homodimerization activity glutathione binding Cellular component cytoplasm cytosol intercellular bridge Biological process metabolism glutathione metabolic process glutathione derivative biosynthetic process nitrobenzene metabolic process xenobiotic catabolic process long-chain fatty acid biosynthetic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2948 14865 Ensembl ENSG00000168765 ENSMUSG00000027890 UniProt Q03013 Q8R5I6 RefSeq (mRNA) NM_000850 NM_147148 NM_147149 NM_001160411 NM_026764 RefSeq (protein) NP_000841 NP_671489 NP_001153883 NP_081040 Location (UCSC) Chr 1: 109.66 – 109.67 Mb Chr 3: 107.95 – 107.95 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Glutathione S-transferase Mu 4 is an enzyme that in humans is encoded by the GSTM4 gene. ^{[5] [6]}

Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are organized in a gene cluster on chromosome 1p13.3 and are known to be highly polymorphic. These genetic variations can change an individual's susceptibility to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs. Diversification of these genes has occurred in regions encoding substrate-binding domains, as well as in tissue expression patterns, to accommodate an increasing number of foreign compounds. Multiple transcript variants, each encoding a distinct protein isoform, have been identified. ^[6]

In the August 2009 issue of Oncogene journal, researchers at Huntsman Cancer Institute (HCI) at the University of Utah demonstrated that expression levels of GSTM4 could predict response to chemotherapy in patients with Ewing sarcoma. The study found that patients who did not respond to chemotherapy had high levels of GSTM4. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000168765 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000027890 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Ross VL, Board PG, Webb GC (Feb 1994). "Chromosomal mapping of the human Mu class glutathione S-transferases to 1p13". Genomics. 18 (1): 87–91. doi:10.1006/geno.1993.1429. PMID   8276420.
6. "Entrez Gene: GSTM4 glutathione S-transferase M4".
7. OncoGenetics.Org (August 2009). "New hope for deadly childhood bone cancer". OncoGenetics.Org. Archived from the original on 2015-09-24. Retrieved 2009-08-31.

Further reading

• Bogaards JJ, van Ommen B, van Bladeren PJ (1992). "Purification and characterization of eight glutathione S-transferase isoenzymes of hamster. Comparison of subunit composition of enzymes from liver, kidney, testis, pancreas and trachea". Biochem. J. 286 (2): 383–8. doi:10.1042/bj2860383. PMC   1132909 . PMID   1530570.
• Taylor JB, Oliver J, Sherrington R, Pemble SE (1991). "Structure of human glutathione S-transferase class Mu genes". Biochem. J. 274 (2): 587–93. doi:10.1042/bj2740587. PMC   1150179 . PMID   2006920.
• Seidegård J, Vorachek WR, Pero RW, Pearson WR (1988). "Hereditary differences in the expression of the human glutathione transferase active on trans-stilbene oxide are due to a gene deletion". Proc. Natl. Acad. Sci. U.S.A. 85 (19): 7293–7. Bibcode:1988PNAS...85.7293S. doi: 10.1073/pnas.85.19.7293 . PMC   282172 . PMID   3174634.
• Comstock KE, Widersten M, Hao XY, et al. (1994). "A comparison of the enzymatic and physicochemical properties of human glutathione transferase M4-4 and three other human Mu class enzymes". Arch. Biochem. Biophys. 311 (2): 487–95. doi:10.1006/abbi.1994.1266. PMID   8203914.
• Rozell B, Hansson HA, Guthenberg C, et al. (1994). "Glutathione transferases of classes alpha, mu and pi show selective expression in different regions of rat kidney". Xenobiotica. 23 (8): 835–49. doi:10.3109/00498259309059412. PMID   8284940.
• Comstock KE, Johnson KJ, Rifenbery D, Henner WD (1993). "Isolation and analysis of the gene and cDNA for a human Mu class glutathione S-transferase, GSTM4". J. Biol. Chem. 268 (23): 16958–65. doi: 10.1016/S0021-9258(19)85287-0 . PMID   8349586.
• Ross VL, Board PG (1993). "Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript". Biochem. J. 294 (2): 373–80. doi:10.1042/bj2940373. PMC   1134464 . PMID   8373352.
• Zhong S, Spurr NK, Hayes JD, Wolf CR (1993). "Deduced amino acid sequence, gene structure and chromosomal location of a novel human class Mu glutathione S-transferase, GSTM4". Biochem. J. 291 (1): 41–50. doi:10.1042/bj2910041. PMC   1132478 . PMID   8471052.
• Patskovsky YV, Patskovska LN, Listowsky I (2000). "An asparagine-phenylalanine substitution accounts for catalytic differences between hGSTM3-3 and other human class mu glutathione S-transferases". Biochemistry. 38 (49): 16187–94. doi:10.1021/bi991714t. PMID   10587441.
• Beuckmann CT, Fujimori K, Urade Y, Hayaishi O (2000). "Identification of mu-class glutathione transferases M2-2 and M3-3 as cytosolic prostaglandin E synthases in the human brain". Neurochem. Res. 25 (5): 733–8. doi:10.1023/A:1007579507804. PMID   10905636. S2CID   36490150.
• Liloglou T, Walters M, Maloney P, et al. (2003). "A T2517C polymorphism in the GSTM4 gene is associated with risk of developing lung cancer". Lung Cancer. 37 (2): 143–6. doi:10.1016/S0169-5002(02)00078-8. PMID   12140136.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . PMID   12477932.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC   528928 . PMID   15489334.
• Stelzl U, Worm U, Lalowski M, et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl: 11858/00-001M-0000-0010-8592-0 . PMID   16169070. S2CID   8235923.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID   16189514. S2CID   4427026.
• Denson J, Xi Z, Wu Y, et al. (2006). "Screening for inter-individual splicing differences in human GSTM4 and the discovery of a single nucleotide substitution related to the tandem skipping of two exons". Gene. 379: 148–55. doi:10.1016/j.gene.2006.05.012. PMID   16854533.

External links

• Overview of all the structural information available in the PDB for UniProt : Q03013 (Glutathione S-transferase Mu 4) at the PDBe-KB .