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{{Infobox_gene}}
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'''Glutathione S-transferase A2''' is an [[enzyme]] that in humans is encoded by the ''GSTA2'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GSTA2 glutathione S-transferase A2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2939| accessdate = }}</ref>
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{{GNF_Protein_box
| image = PBB_Protein_GSTA2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ags.
| PDB = {{PDB2|1ags}}, {{PDB2|1gsd}}, {{PDB2|1gse}}, {{PDB2|1gsf}}, {{PDB2|1guh}}, {{PDB2|1k3l}}, {{PDB2|1k3o}}, {{PDB2|1k3y}}, {{PDB2|1pkw}}, {{PDB2|1pkz}}, {{PDB2|1pl1}}, {{PDB2|1pl2}}, {{PDB2|1usb}}, {{PDB2|1xwg}}, {{PDB2|1ydk}}
| Name = Glutathione S-transferase A2
| HGNCid = 4627
| Symbol = GSTA2
| AltSymbols =; GST2; GSTA2-2; GTA2; GTH2; MGC10525
| OMIM = 138360
| ECnumber = 
| Homologene = 47952
| MGIid = 
| Function = {{GNF_GO|id=GO:0004364 |text = glutathione transferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0008152 |text = metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2939
    | Hs_Ensembl = ENSG00000096087
    | Hs_RefseqProtein = NP_000837
    | Hs_RefseqmRNA = NM_000846
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 6
    | Hs_GenLoc_start = 52722856
    | Hs_GenLoc_end = 52736326
    | Hs_Uniprot = P09210
    | Mm_EntrezGene = 
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = 
    | Mm_RefseqProtein = 
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Glutathione S-transferase A2''', also known as '''GSTA2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GSTA2 glutathione S-transferase A2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2939| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. These enzymes function in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding these enzymes 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 some drugs. 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-tranferase belonging to the alpha class. The alpha class genes, located in a cluster mapped to chromosome 6, are the most abundantly expressed glutathione S-transferases in liver. In addition to metabolizing bilirubin and certain anti-cancer drugs in the liver, the alpha class of these enzymes exhibit glutathione peroxidase activity thereby protecting the cells from reactive oxygen species and the products of peroxidation.<ref name="entrez">{{cite web | title = Entrez Gene: GSTA2 glutathione S-transferase A2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2939| accessdate = }}</ref>
| summary_text = Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. These enzymes function in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding these enzymes 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 some drugs. 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-tranferase belonging to the alpha class. The alpha class genes, located in a cluster mapped to chromosome 6, are the most abundantly expressed glutathione S-transferases in liver. In addition to metabolizing bilirubin and certain anti-cancer drugs in the liver, the alpha class of these enzymes exhibit glutathione peroxidase activity thereby protecting the cells from reactive oxygen species and the products of peroxidation.<ref name="entrez">{{cite web | title = Entrez Gene: GSTA2 glutathione S-transferase A2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2939| accessdate = }}</ref>
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Röhrdanz E, Nguyen T, Pickett CB |title=Isolation and characterization of the human glutathione S-transferase A2 subunit gene. |journal=Arch. Biochem. Biophys. |volume=298 |issue= 2 |pages= 747-52 |year= 1992 |pmid= 1329668 |doi=  }}
*{{cite journal  |vauthors=Röhrdanz E, Nguyen T, Pickett CB |title=Isolation and characterization of the human glutathione S-transferase A2 subunit gene. |journal=Arch. Biochem. Biophys. |volume=298 |issue= 2 |pages= 747–52 |year= 1992 |pmid= 1329668 |doi=10.1016/0003-9861(92)90475-C }}
*{{cite journal  | author=Stenberg G, Björnestedt R, Mannervik B |title=Heterologous expression of recombinant human glutathione transferase A1-1 from a hepatoma cell line. |journal=Protein Expr. Purif. |volume=3 |issue= 1 |pages= 80-4 |year= 1992 |pmid= 1330133 |doi=  }}
*{{cite journal  |vauthors=Stenberg G, Björnestedt R, Mannervik B |title=Heterologous expression of recombinant human glutathione transferase A1-1 from a hepatoma cell line. |journal=Protein Expr. Purif. |volume=3 |issue= 1 |pages= 80–4 |year= 1992 |pmid= 1330133 |doi=10.1016/1046-5928(92)90060-A }}
*{{cite journal  | author=Klöne A, Hussnätter R, Sies H |title=Cloning, sequencing and characterization of the human alpha glutathione S-transferase gene corresponding to the cDNA clone pGTH2. |journal=Biochem. J. |volume=285 ( Pt 3) |issue=  |pages= 925-8 |year= 1992 |pmid= 1497629 |doi=  }}
*{{cite journal  |vauthors=Klöne A, Hussnätter R, Sies H |title=Cloning, sequencing and characterization of the human alpha glutathione S-transferase gene corresponding to the cDNA clone pGTH2. |journal=Biochem. J. |volume=285 |issue=  3|pages= 925–8 |year= 1992 |pmid= 1497629 |doi=  | pmc=1132883  }}
*{{cite journal  | author=Bogaards JJ, van Ommen B, van Bladeren PJ |title=Purification and characterization of eight glutathione S-transferase isoenzymes of hamster. Comparison of subunit composition of enzymes from liver, kidney, testis, pancreas and trachea. |journal=Biochem. J. |volume=286 ( Pt 2) |issue=  |pages= 383-8 |year= 1992 |pmid= 1530570 |doi=  }}
*{{cite journal  |vauthors=Bogaards JJ, van Ommen B, van Bladeren PJ |title=Purification and characterization of eight glutathione S-transferase isoenzymes of hamster. Comparison of subunit composition of enzymes from liver, kidney, testis, pancreas and trachea. |journal=Biochem. J. |volume=286 |issue=  2|pages= 383–8 |year= 1992 |pmid= 1530570 |doi= | pmc=1132909 }}
*{{cite journal | author=Strange RC, Fryer AA, Matharoo B, ''et al.'' |title=The human glutathione S-transferases: comparison of isoenzyme expression in normal and astrocytoma brain. |journal=Biochim. Biophys. Acta |volume=1139 |issue= 3 |pages= 222-8 |year= 1992 |pmid= 1627661 |doi=  }}
*{{cite journal   |vauthors=Strange RC, Fryer AA, Matharoo B, etal |title=The human glutathione S-transferases: comparison of isoenzyme expression in normal and astrocytoma brain. |journal=Biochim. Biophys. Acta |volume=1139 |issue= 3 |pages= 222–8 |year= 1992 |pmid= 1627661 |doi=  10.1016/0925-4439(92)90138-D}}
*{{cite journal  | author=Hayes JD, Kerr LA, Cronshaw AD |title=Evidence that glutathione S-transferases B1B1 and B2B2 are the products of separate genes and that their expression in human liver is subject to inter-individual variation. Molecular relationships between the B1 and B2 subunits and other Alpha class glutathione S-transferases. |journal=Biochem. J. |volume=264 |issue= 2 |pages= 437-45 |year= 1990 |pmid= 2604726 |doi=  }}
*{{cite journal  |vauthors=Hayes JD, Kerr LA, Cronshaw AD |title=Evidence that glutathione S-transferases B1B1 and B2B2 are the products of separate genes and that their expression in human liver is subject to inter-individual variation. Molecular relationships between the B1 and B2 subunits and other Alpha class glutathione S-transferases. |journal=Biochem. J. |volume=264 |issue= 2 |pages= 437–45 |year= 1990 |pmid= 2604726 |doi=  | pmc=1133600  }}
*{{cite journal  | author=Board PG, Webb GC |title=Isolation of a cDNA clone and localization of human glutathione S-transferase 2 genes to chromosome band 6p12. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 8 |pages= 2377-81 |year= 1987 |pmid= 3031680 |doi=  }}
*{{cite journal  |vauthors=Board PG, Webb GC |title=Isolation of a cDNA clone and localization of human glutathione S-transferase 2 genes to chromosome band 6p12. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 8 |pages= 2377–81 |year= 1987 |pmid= 3031680 |doi=10.1073/pnas.84.8.2377  | pmc=304654 }}
*{{cite journal  | author=Rhoads DM, Zarlengo RP, Tu CP |title=The basic glutathione S-transferases from human livers are products of separate genes. |journal=Biochem. Biophys. Res. Commun. |volume=145 |issue= 1 |pages= 474-81 |year= 1987 |pmid= 3036131 |doi=  }}
*{{cite journal  |vauthors=Rhoads DM, Zarlengo RP, Tu CP |title=The basic glutathione S-transferases from human livers are products of separate genes. |journal=Biochem. Biophys. Res. Commun. |volume=145 |issue= 1 |pages= 474–81 |year= 1987 |pmid= 3036131 |doi=10.1016/0006-291X(87)91345-3 }}
*{{cite journal | author=Chow NW, Whang-Peng J, Kao-Shan CS, ''et al.'' |title=Human glutathione S-transferases. The Ha multigene family encodes products of different but overlapping substrate specificities. |journal=J. Biol. Chem. |volume=263 |issue= 26 |pages= 12797-800 |year= 1988 |pmid= 3138230 |doi=  }}
*{{cite journal   |vauthors=Chow NW, Whang-Peng J, Kao-Shan CS, etal |title=Human glutathione S-transferases. The Ha multigene family encodes products of different but overlapping substrate specificities. |journal=J. Biol. Chem. |volume=263 |issue= 26 |pages= 12797–800 |year= 1988 |pmid= 3138230 |doi=  }}
*{{cite journal  | author=Tu CP, Qian B |title=Nucleotide sequence of the human liver glutathione S-transferase subunit 1 cDNA. |journal=Biochem. Soc. Trans. |volume=15 |issue= 4 |pages= 734-6 |year= 1988 |pmid= 3678589 |doi=  }}
*{{cite journal  |vauthors=Tu CP, Qian B |title=Nucleotide sequence of the human liver glutathione S-transferase subunit 1 cDNA. |journal=Biochem. Soc. Trans. |volume=15 |issue= 4 |pages= 734–6 |year= 1988 |pmid= 3678589 |doi=  }}
*{{cite journal  | author=Tu CP, Qian B |title=Human liver glutathione S-transferases: complete primary sequence of an Ha subunit cDNA. |journal=Biochem. Biophys. Res. Commun. |volume=141 |issue= 1 |pages= 229-37 |year= 1987 |pmid= 3800996 |doi=  }}
*{{cite journal  |vauthors=Tu CP, Qian B |title=Human liver glutathione S-transferases: complete primary sequence of an Ha subunit cDNA. |journal=Biochem. Biophys. Res. Commun. |volume=141 |issue= 1 |pages= 229–37 |year= 1987 |pmid= 3800996 |doi=10.1016/S0006-291X(86)80358-8 }}
*{{cite journal  | author=Satoh K, Kitahara A, Sato K |title=Identification of heterogeneous and microheterogeneous subunits of glutathione S-transferase in rat liver cytosol. |journal=Arch. Biochem. Biophys. |volume=242 |issue= 1 |pages= 104-11 |year= 1985 |pmid= 3901925 |doi=  }}
*{{cite journal  |vauthors=Satoh K, Kitahara A, Sato K |title=Identification of heterogeneous and microheterogeneous subunits of glutathione S-transferase in rat liver cytosol. |journal=Arch. Biochem. Biophys. |volume=242 |issue= 1 |pages= 104–11 |year= 1985 |pmid= 3901925 |doi=10.1016/0003-9861(85)90484-9 }}
*{{cite journal | author=Zeng K, Rose JP, Chen HC, ''et al.'' |title=A surface mutant (G82R) of a human alpha-glutathione S-transferase shows decreased thermal stability and a new mode of molecular association in the crystal. |journal=Proteins |volume=20 |issue= 3 |pages= 259-63 |year= 1995 |pmid= 7892174 |doi= 10.1002/prot.340200306 }}
*{{cite journal   |vauthors=Zeng K, Rose JP, Chen HC, etal |title=A surface mutant (G82R) of a human alpha-glutathione S-transferase shows decreased thermal stability and a new mode of molecular association in the crystal. |journal=Proteins |volume=20 |issue= 3 |pages= 259–63 |year= 1995 |pmid= 7892174 |doi= 10.1002/prot.340200306 }}
*{{cite journal | author=Anttila S, Hirvonen A, Vainio H, ''et al.'' |title=Immunohistochemical localization of glutathione S-transferases in human lung. |journal=Cancer Res. |volume=53 |issue= 23 |pages= 5643-8 |year= 1994 |pmid= 8242618 |doi=  }}
*{{cite journal   |vauthors=Anttila S, Hirvonen A, Vainio H, etal |title=Immunohistochemical localization of glutathione S-transferases in human lung. |journal=Cancer Res. |volume=53 |issue= 23 |pages= 5643–8 |year= 1994 |pmid= 8242618 |doi=  }}
*{{cite journal  | author=Suzuki T, Johnston PN, Board PG |title=Structure and organization of the human alpha class glutathione S-transferase genes and related pseudogenes. |journal=Genomics |volume=18 |issue= 3 |pages= 680-6 |year= 1994 |pmid= 8307579 |doi=  }}
*{{cite journal  |vauthors=Suzuki T, Johnston PN, Board PG |title=Structure and organization of the human alpha class glutathione S-transferase genes and related pseudogenes. |journal=Genomics |volume=18 |issue= 3 |pages= 680–6 |year= 1994 |pmid= 8307579 |doi=10.1016/S0888-7543(05)80373-8 }}
*{{cite journal  | author=Ahmad H, Singhal SS, Saxena M, Awasthi YC |title=Characterization of two novel subunits of the alpha-class glutathione S-transferases of human liver. |journal=Biochim. Biophys. Acta |volume=1161 |issue= 2-3 |pages= 333-6 |year= 1993 |pmid= 8431482 |doi=  }}
*{{cite journal  |vauthors=Ahmad H, Singhal SS, Saxena M, Awasthi YC |title=Characterization of two novel subunits of the alpha-class glutathione S-transferases of human liver. |journal=Biochim. Biophys. Acta |volume=1161 |issue= 2–3 |pages= 333–6 |year= 1993 |pmid= 8431482 |doi=  10.1016/0167-4838(93)90234-i}}
*{{cite journal  | author=Rowe JD, Nieves E, Listowsky I |title=Subunit diversity and tissue distribution of human glutathione S-transferases: interpretations based on electrospray ionization-MS and peptide sequence-specific antisera. |journal=Biochem. J. |volume=325 ( Pt 2) |issue=  |pages= 481-6 |year= 1997 |pmid= 9230131 |doi=  }}
*{{cite journal  |vauthors=Rowe JD, Nieves E, Listowsky I |title=Subunit diversity and tissue distribution of human glutathione S-transferases: interpretations based on electrospray ionization-MS and peptide sequence-specific antisera |journal=Biochem. J. |volume=325 |issue=  2|pages= 481–6 |year= 1997 |pmid= 9230131 |doi= | pmc=1218585 }}
*{{cite journal | author=Coles BF, Anderson KE, Doerge DR, ''et al.'' |title=Quantitative analysis of interindividual variation of glutathione S-transferase expression in human pancreas and the ambiguity of correlating genotype with phenotype. |journal=Cancer Res. |volume=60 |issue= 3 |pages= 573-9 |year= 2000 |pmid= 10676639 |doi=  }}
*{{cite journal   |vauthors=Coles BF, Anderson KE, Doerge DR, etal |title=Quantitative analysis of interindividual variation of glutathione S-transferase expression in human pancreas and the ambiguity of correlating genotype with phenotype |journal=Cancer Res. |volume=60 |issue= 3 |pages= 573–9 |year= 2000 |pmid= 10676639 |doi=  }}
*{{cite journal  | author=Tetlow N, Liu D, Board P |title=Polymorphism of human Alpha class glutathione transferases. |journal=Pharmacogenetics |volume=11 |issue= 7 |pages= 609-17 |year= 2001 |pmid= 11668220 |doi=  }}
*{{cite journal  |vauthors=Tetlow N, Liu D, Board P |title=Polymorphism of human Alpha class glutathione transferases |journal=Pharmacogenetics |volume=11 |issue= 7 |pages= 609–17 |year= 2001 |pmid= 11668220 |doi=10.1097/00008571-200110000-00007 }}
*{{cite journal | author=Coles BF, Morel F, Rauch C, ''et al.'' |title=Effect of polymorphism in the human glutathione S-transferase A1 promoter on hepatic GSTA1 and GSTA2 expression. |journal=Pharmacogenetics |volume=11 |issue= 8 |pages= 663-9 |year= 2002 |pmid= 11692074 |doi=  }}
*{{cite journal   |vauthors=Coles BF, Morel F, Rauch C, etal |title=Effect of polymorphism in the human glutathione S-transferase A1 promoter on hepatic GSTA1 and GSTA2 expression |journal=Pharmacogenetics |volume=11 |issue= 8 |pages= 663–9 |year= 2002 |pmid= 11692074 |doi=10.1097/00008571-200111000-00004 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=2939}}
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Latest revision as of 09:07, 31 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Glutathione S-transferase A2 is an enzyme that in humans is encoded by the GSTA2 gene.[1]

Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. These enzymes function in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding these enzymes 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 some drugs. 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-tranferase belonging to the alpha class. The alpha class genes, located in a cluster mapped to chromosome 6, are the most abundantly expressed glutathione S-transferases in liver. In addition to metabolizing bilirubin and certain anti-cancer drugs in the liver, the alpha class of these enzymes exhibit glutathione peroxidase activity thereby protecting the cells from reactive oxygen species and the products of peroxidation.[1]

References

  1. ↑ 1.0 1.1 "Entrez Gene: GSTA2 glutathione S-transferase A2".

Further reading



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