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Type: Journal article
Title: Characterization of the human Omega class glutathione transferase genes and associated polymorphisms
Author: Whitbread, A.
Tetlow, N.
Eyre, H.
Sutherland, G.
Board, P.
Citation: Pharmacogenetics and Genomics (Print Edition), 2003; 13(3):131-144
Publisher: Lippincott Williams & Wilkins
Issue Date: 2003
ISSN: 1744-6872
Abstract: The Omega class glutathione transferases (GSTs) have been identified in many organisms, including human, mouse, rat, pig, Caenorhabditis elegans 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 Ca2+ release by ryanodine receptors. An investigation of the genomic organization of human GSTO1 identified a second actively transcribed member of the Omega class (GST02). Both GSTO1 and GST02 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 (GST03p) 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 GST02 mRNA was seen in a range of tissues, including the liver, kidney, skeletal muscle and prostate. The strongest GST02 expression was in the testis, which also expresses a larger transcript than other tissues. Characterization of recombinant GST02 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.
Keywords: glutathione transferase omega; polymorphism; methylarsonate; thioltransferase
Description: © 2003 Lippincott Williams & Wilkins, Inc.
RMID: 0020032100
DOI: 10.1097/00008571-200303000-00003
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Appears in Collections:Molecular and Biomedical Science publications

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