Characterization of the human Omega class glutathione transferase genes and associated polymorphisms

Whitbread, Astrid K; Tetlow, Natasha; Eyre, Helen J; Sutherland, Grant R; Board, Philip G

doi:10.1097/00008571-200303000-00003

Cited by 181Glutathione Transferases and PolymorphismsPharmacogenetics and Drug MetabolismRedox biology and oxidative stress

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Characterization of the human Omega class glutathione transferase genes and associated polymorphisms

Whitbread, Astrid K, Tetlow, Natasha, Eyre, Helen J, Sutherland, Grant R, Board, Philip G·2003·Pharmacogenetics

DOI 10.1097/00008571-200303000-00003

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Abstract

The Omega class glutathione transferases (GSTs) have been identified in many organisms, including human, mouse, rat, pig, Caenorhabditis eglands and Drosophila melanogaster. These GSTs have poor activity with common GST substrates, but exhibit novel glutathione-dependent thioltransferase, dehydroascorbate reductase and monomethylarsonate reductase activities, and modulate Ca release by ryanodine receptors. An investigation of the genomic organization of human GSTO1 identified a second actively transcribed member of the Omega class (GSTO1). Both GSTO1 and GSTO2 are composed of six exons and are separated by 7.5 kb on chromosome 10q24.3. A third sequence that appears to be a reverse-transcribed pseudogene (GSTO3p) has been identified on chromosome 3. GSTO2 has 64% amino acid identity with GSTO1 and conserves the cysteine residue at position 32, which is thought to be important in the active site of GSTO1. Expression of GSTO2 mRNA was seen in a range of tissues, including the liver, kidney, skeletal muscle and prostate. The strongest GSTO2 expression was in the testis, which also expresses a larger transcript than other tissues. Characterization of recombinant GSTO2 has been limited by its poor solubility. Two functional polymorphisms of GSTO1 have been identified. One alters a splice junction and causes the deletion of E155 and another results in an A140D substitution. Characterization of these variants revealed that the A140D substitution affects neither heat stability, nor activity towards 1-chloro-2,4-dinitrobenzene or hydroxyethyl disulphide. In contrast, deletion of residue E155 appears to contribute towards both a loss of heat stability and increased enzymatic activity.

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Omega-class GSTs have dehydroascorbate reductase, thioltransferase, and monomethylarsenate reductase activities.
“Four omega-class GSTs are present in the urchin genome, closely related to vertebrate and insect omega GSTs with dehydroascorbate reductase, thioltransferase, and monomethylarsenate reductase activities (Whitbread et al., 2003).”
From The chemical defensome: Environmental sensing and response genes in the Strongylocentrotus purpuratus genome (2006) · cites this paper as Whitbread et al., 2003

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Characterization of the Omega Class of Glutathione Transferases
Whitbread, A. K., Masoumi, A., Tetlow, N., Schmuck, E., Coggan, M., & Philip G. Board (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)01005-0 · Cited by 218
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Characterization of the Omega class glutathione transferases
Philip G. Board, Coggan, M., Chelvanayagam, G., Easteal, S., Jermiin, L. S., Schulte, J. T., Danley, D. E., Hoth, L. R., Griffor, M. C., Kamath, A. J., et al. (2001) · ANU Open Research (Australian National University)
Characterization of the monomethylarsonate reductase and dehydroascorbate reductase activities of Omega class glutathione transferase variants: implications for arsenic metabolism and the age-at-onset of Alzheimer's and Parkinson's diseases
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The omega-class glutathione transferases: structure, function, and genetics
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Authors: Whitbread, A. K., Tetlow, N., Eyre, H. J., Sutherland, G. R., & Board, P. G.
Affiliations: Australian National University (AU)
Corresponding author: Board, Philip G
ORCID: Whitbread, Astrid K
Board, Philip G
Venue: Pharmacogenetics
Publisher: Ovid Technologies (Wolters Kluwer Health)
Published: 2003-03
Volume: 13
Issue: 3
Pages: 131-144
ISSN: 0960-314X (ISSN-L)
DOI: 10.1097/00008571-200303000-00003
OpenAlex: W1970831257
Cited by: 181
References: 39
Citations by year: 2026: 3 · 2025: 6 · 2024: 2 · 2023: 3 · 2022: 1 · 2021: 10 · 2020: 3 · 2019: 1 · 2018: 7 · 2017: 5 · 2016: 8 · 2015: 3 · 2014: 8 · 2013: 10 · 2012: 16
FWCI: 4.60
Type: journal article
Language: en
Open access: closed
Locations: Pharmacogenetics (publishedVersion)
PubMed (publishedVersion)
Adelaide Research & Scholarship (AR&S) (University of Adelaide) (submittedVersion)
ANU Open Research (Australian National University) (submittedVersion)
Funders: Incyte
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords: GSTO1, GSTO2, gene structure, tissue expression, thermal stability, dehydroascorbate reductase, genetic polymorphism
MeSH terms: Amino Acid Sequence, Animals, Base Sequence, Chromosome Mapping, Chromosomes, Human, Pair 10, Cloning, Molecular, Exons, Glutathione Transferase, Humans, Molecular Sequence Data, Pseudogenes, Recombinant Proteins, RNA, Messenger, Sequence Homology, Nucleic Acid, Sequence Deletion, Sequence Homology, Amino Acid, DNA, Complementary

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Characterization of the human Omega class glutathione transferase genes and associated polymorphisms

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