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Characterization of the human Omega class glutathione transferase genes and associated polymorphisms
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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“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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Glutathione transferases, regulators of cellular metabolism and physiology
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Metadata
- 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
- Venue
- Pharmacogenetics
- Published
- 2003-03
- Volume
- 13
- Issue
- 3
- Pages
- 131-144
- ISSN
- 0960-314X (ISSN-L)
- 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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