Microsomal glutathione S-transferase 1

MGST1
Identifiers
AliasesMGST1, GST12, MGST, MGST-I, microsomal glutathione S-transferase 1
External IDsMGI: 1913850 HomoloGene: 10544 GeneCards: MGST1
Gene location (Human)
Chr.Chromosome 12 (human)[1]
Band12p12.3Start16,347,142 bp[1]
End16,609,259 bp[1]
Orthologs
SpeciesHumanMouse
Entrez

4257

56615

Ensembl

ENSG00000008394

ENSMUSG00000008540

UniProt

P10620

Q91VS7

RefSeq (mRNA)

NM_019946
NM_001347489
NM_001361308
NM_001361309
NM_001361307

RefSeq (protein)

NP_001334418
NP_064330
NP_001348237
NP_001348238
NP_001348236

Location (UCSC)Chr 12: 16.35 – 16.61 MbChr 6: 138.14 – 138.16 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Microsomal glutathione S-transferase 1 is an enzyme that in humans is encoded by the MGST1 gene.[5]

Function

The MAPEG family (Membrane-Associated Proteins in Eicosanoid and Glutathione metabolism) consists of six human proteins, two of which are involved in the production of leukotrienes and prostaglandin E, important mediators of inflammation. Other family members, demonstrating glutathione S-transferase and peroxidase activities, are involved in cellular defense against toxic, carcinogenic, and pharmacologically active electrophilic compounds. This gene encodes a protein that catalyzes the conjugation of glutathione to electrophiles and the reduction of lipid hydroperoxides. This protein is localized to the endoplasmic reticulum and outer mitochondrial membrane where it is thought to protect these membranes from oxidative stress. Four transcript variants of this gene encode one protein isoform.[5]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000008394 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000008540 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. 1 2 "Entrez Gene: MGST1 microsomal glutathione S-transferase 1".

Further reading

  • Jakobsson PJ, Morgenstern R, Mancini J (2000). "Membrane-associated proteins in eicosanoid and glutathione metabolism (MAPEG). A widespread protein superfamily". Am. J. Respir. Crit. Care Med. 161 (2 Pt 2): S20–4. doi:10.1164/ajrccm.161.supplement_1.ltta-5. PMID 10673221.
  • Cholon A, Giaccia AJ, Lewis AD (1992). "What role do glutathione S-transferases play in the cellular response to ionizing radiation?". Int. J. Radiat. Oncol. Biol. Phys. 22 (4): 759–63. PMID 1544849.
  • DeJong JL, Mohandas T, Tu CP (1990). "The gene for the microsomal glutathione S-transferase is on human chromosome 12". Genomics. 6 (2): 379–82. doi:10.1016/0888-7543(90)90580-N. PMID 2307478.
  • DeJong JL, Morgenstern R, Jörnvall H (1988). "Gene expression of rat and human microsomal glutathione S-transferases". J. Biol. Chem. 263 (17): 8430–6. PMID 3372534.
  • Adams MD, Kerlavage AR, Fleischmann RD (1995). "Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence" (PDF). Nature. 377 (6547 Suppl): 3–174. PMID 7566098.
  • Söderström M, Morgenstern R, Hammarström S (1995). "Protein-protein interaction affinity chromatography of leukotriene C4 synthase". Protein Expr. Purif. 6 (3): 352–6. doi:10.1006/prep.1995.1046. PMID 7663172.
  • Kelner MJ, Stokely MN, Stovall NE, Montoya MA (1997). "Structural organization of the human microsomal glutathione S-transferase gene (GST12)". Genomics. 36 (1): 100–3. doi:10.1006/geno.1996.0429. PMID 8812420.
  • Estonius M, Forsberg L, Danielsson O (1999). "Distribution of microsomal glutathione transferase 1 in mammalian tissues. A predominant alternate first exon in human tissues". Eur. J. Biochem. 260 (2): 409–13. doi:10.1046/j.1432-1327.1999.00165.x. PMID 10095775.
  • Lee SH, DeJong J (1999). "Microsomal GST-I: genomic organization, expression, and alternative splicing of the human gene". Biochim. Biophys. Acta. 1446 (3): 389–96. doi:10.1016/S0167-4781(99)00112-8. PMID 10524215.
  • Kelner MJ, Bagnell RD, Montoya MA (2000). "Structural organization of the microsomal glutathione S-transferase gene (MGST1) on chromosome 12p13.1-13.2. Identification of the correct promoter region and demonstration of transcriptional regulation in response to oxidative stress". J. Biol. Chem. 275 (17): 13000–6. doi:10.1074/jbc.275.17.13000. PMID 10777602.
  • Surapureddi S, Svartz J, Magnusson KE (2000). "Colocalization of leukotriene C synthase and microsomal glutathione S-transferase elucidated by indirect immunofluorescence analysis". FEBS Lett. 480 (2–3): 239–43. doi:10.1016/S0014-5793(00)01885-8. PMID 11034337.
  • Iida A, Saito S, Sekine A (2001). "Catalog of 46 single-nucleotide polymorphisms (SNPs) in the microsomal glutathione S-transferase 1 (MGST1) gene". J. Hum. Genet. 46 (10): 590–4. doi:10.1007/s100380170026. PMID 11587073.
  • To-Figueras J, Gené M, Gómez-Catalán J (2003). "Microsomal epoxide hydrolase and glutathione S-transferase polymorphisms in relation to laryngeal carcinoma risk". Cancer Lett. 187 (1–2): 95–101. doi:10.1016/S0304-3835(02)00406-8. PMID 12359356.
  • Strausberg RL, Feingold EA, Grouse LH (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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Ekström L, Lyrenäs L, Jakobsson PJ (2003). "Basal expression of the human MAPEG members microsomal glutathione transferase 1 and prostaglandin E synthase genes is mediated by Sp1 and Sp3". Biochim. Biophys. Acta. 1627 (2–3): 79–84. doi:10.1016/S0167-4781(03)00077-0. PMID 12818425.
  • Lengqvist J, Svensson R, Evergren E (2004). "Observation of an intact noncovalent homotrimer of detergent-solubilized rat microsomal glutathione transferase-1 by electrospray mass spectrometry". J. Biol. Chem. 279 (14): 13311–6. doi:10.1074/jbc.M310958200. PMID 14726533.
  • Gerhard DS, Wagner L, Feingold EA (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.
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