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

The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.

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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Research works printed but not linked: 5

  1. Strange, 1999, IARC Sci Publ, 148, 231
  2. Tew, 1994, Cancer Res, 54, 4313
  3. Hall, 1994, Cancer Res, 54, 5251
  4. Callen, 1990, Ann Genet, 33, 219
  5. Pearson, 1993, Am J Hum Genet, 53, 220

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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
ORCID
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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