GSTO1

Glutathione S-transferase omega 1
PDB rendering based on 1eem.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1EEM​, 3LFL​, 3VLN​, 4IS0​
Identifiers
Symbols	GSTO1 ; GSTO 1-1; GSTTLp28; HEL-S-21; P28; SPG-R
External IDs	OMIM: 605482 MGI: 1342273 HomoloGene: 37971 ChEMBL: 3174 GeneCards: GSTO1 Gene
EC number	1.20.4.2, 1.8.5.1, 2.5.1.18
Gene ontology Molecular function • glutathione transferase activity • protein binding • oxidoreductase activity • glutathione dehydrogenase (ascorbate) activity • methylarsonate reductase activity Cellular component • basement membrane • cytoplasm • cytosol • axon • nuclear membrane • myelin sheath • cell body • extracellular exosome Biological process • glutathione metabolic process • xenobiotic metabolic process • regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum • regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion • positive regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion • L-ascorbic acid metabolic process • L-ascorbic acid biosynthetic process • xenobiotic catabolic process • small molecule metabolic process • oxidation-reduction process • negative regulation of ryanodine-sensitive calcium-release channel activity • positive regulation of ryanodine-sensitive calcium-release channel activity • cellular response to arsenic-containing substance • glutathione derivative biosynthetic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	9446	14873
Ensembl	ENSG00000148834	ENSMUSG00000025068
UniProt	P78417	O09131
RefSeq (mRNA)	NM_001191002	NM_010362
RefSeq (protein)	NP_001177931	NP_034492
Location (UCSC)	Chr 10: 104.24 – 104.27 Mb	Chr 19: 47.85 – 47.86 Mb
PubMed search

Glutathione S-transferase omega-1 is an enzyme that in humans is encoded by the GSTO1 gene.^[1][2][3]

This gene encodes a member of the theta class glutathione S-transferase-like (GSTTL) protein family. In mouse, the encoded protein acts as a small stress response protein, likely involved in cellular redox homeostasis.^[3] This protein has dehydroascorbate reductase activity and may function in the glutathione-ascorbate cycle as part of antioxidant metabolism.^[4]

References

1. Board PG, Coggan M, Chelvanayagam G, Easteal S, Jermiin LS, Schulte GK, Danley DE, Hoth LR, Griffor MC, Kamath AV, Rosner MH, Chrunyk BA, Perregaux DE, Gabel CA, Geoghegan KF, Pandit J (Sep 2000). "Identification, characterization, and crystal structure of the Omega class glutathione transferases". J Biol Chem 275 (32): 24798–806. doi:10.1074/jbc.M001706200. PMID 10783391.
2. Whitbread AK, Tetlow N, Eyre HJ, Sutherland GR, Board PG (Mar 2003). "Characterization of the human Omega class glutathione transferase genes and associated polymorphisms". Pharmacogenetics 13 (3): 131–44. doi:10.1097/01.fpc.0000054062.98065.6e. PMID 12618591.
3. "Entrez Gene: GSTO1 glutathione S-transferase omega 1".
4. Whitbread AK, Masoumi A, Tetlow N, Schmuck E, Coggan M, Board PG (2005). "Characterization of the omega class of glutathione transferases". Meth. Enzymol. Methods in Enzymology 401: 78–99. doi:10.1016/S0076-6879(05)01005-0. ISBN 978-0-12-182806-6. PMID 16399380.

Further reading

• Matoba R, Okubo K, Hori N, et al. (1994). "The addition of 5'-coding information to a 3'-directed cDNA library improves analysis of gene expression". Gene 146 (2): 199–207. doi:10.1016/0378-1119(94)90293-3. PMID 8076819.
• Ishikawa T, Casini AF, Nishikimi M (1998). "Molecular cloning and functional expression of rat liver glutathione-dependent dehydroascorbate reductase". J. Biol. Chem. 273 (44): 28708–12. doi:10.1074/jbc.273.44.28708. PMID 9786866.
• Kodym R, Calkins P, Story M (1999). "The cloning and characterization of a new stress response protein. A mammalian member of a family of theta class glutathione s-transferase-like proteins". J. Biol. Chem. 274 (8): 5131–7. doi:10.1074/jbc.274.8.5131. PMID 9988762.
• Hubbard MJ, McHugh NJ (2001). "Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping". Electrophoresis 21 (17): 3785–96. doi:10.1002/1522-2683(200011)21:17<3785::AID-ELPS3785>3.0.CO;2-2. PMID 11271497.
• Yin ZL, Dahlstrom JE, Le Couteur DG, Board PG (2001). "Immunohistochemistry of omega class glutathione S-transferase in human tissues". J. Histochem. Cytochem. 49 (8): 983–7. doi:10.1177/002215540104900806. PMID 11457926.
• 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Tanaka-Kagawa T, Jinno H, Hasegawa T, et al. (2003). "Functional characterization of two variant human GSTO 1-1s (Ala140Asp and Thr217Asn)". Biochem. Biophys. Res. Commun. 301 (2): 516–20. doi:10.1016/S0006-291X(02)03066-8. PMID 12565892.
• Yu L, Kalla K, Guthrie E, et al. (2004). "Genetic variation in genes associated with arsenic metabolism: glutathione S-transferase omega 1-1 and purine nucleoside phosphorylase polymorphisms in European and indigenous Americans". Environ. Health Perspect. 111 (11): 1421–7. doi:10.1289/ehp.6420. PMC 1241635. PMID 12928150.
• Li YJ, Oliveira SA, Xu P, et al. (2004). "Glutathione S-transferase omega-1 modifies age-at-onset of Alzheimer disease and Parkinson disease". Hum. Mol. Genet. 12 (24): 3259–67. doi:10.1093/hmg/ddg357. PMID 14570706.
• Whitbread AK, Mellick GD, Silburn PA, et al. (2004). "Glutathione transferase Omega class polymorphisms in Parkinson disease". Neurology 62 (10): 1910–1. doi:10.1212/01.wnl.0000125282.09308.b1. PMID 15159516.
• Deloukas P, Earthrowl ME, Grafham DV, et al. (2004). "The DNA sequence and comparative analysis of human chromosome 10". Nature 429 (6990): 375–81. doi:10.1038/nature02462. PMID 15164054.
• 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.
• Kölsch H, Linnebank M, Lütjohann D, et al. (2005). "Polymorphisms in glutathione S-transferase omega-1 and AD, vascular dementia, and stroke". Neurology 63 (12): 2255–60. doi:10.1212/01.wnl.0000147294.29309.47. PMID 15623683.
• Ozturk A, Desai PP, Minster RL, et al. (2005). "Three SNPs in the GSTO1, GSTO2 and PRSS11 genes on chromosome 10 are not associated with age-at-onset of Alzheimer's disease". Neurobiol. Aging 26 (8): 1161–5. doi:10.1016/j.neurobiolaging.2004.11.001. PMID 15917099.
• 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. PMID 16169070.
• Fujihara J, Kunito T, Takeshita H (2007). "Frequency of two human glutathione-S-transferase omega-1 polymorphisms (E155 deletion and E208K) in Ovambo and Japanese populations using the PCR-based genotyping method". Clin. Chem. Lab. Med. 45 (5): 621–4. doi:10.1515/CCLM.2007.128. PMID 17484623.
• Harju TH, Peltoniemi MJ, Rytilä PH, et al. (2007). "Glutathione S-transferase omega in the lung and sputum supernatants of COPD patients". Respir. Res. 8 (1): 48. doi:10.1186/1465-9921-8-48. PMC 1939846. PMID 17617905.
• Kölsch H, Larionov S, Dedeck O, et al. (2007). "Association of the glutathione S-transferase omega-1 Ala140Asp polymorphism with cerebrovascular atherosclerosis and plaque-associated interleukin-1 alpha expression". Stroke 38 (10): 2847–50. doi:10.1161/STROKEAHA.107.484162. PMID 17717316.