ArticleThe Biochemical journal2003
Biochemical and genetic characterization of a murine class Kappa glutathione S-transferase.
Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Human mitochondrial glutathione transferases: Kinetic parameters and accommodation of a mitochondria-targeting group in substrates.Bioorganic & medicinal chemistry · 2024Article
- The mammalian peroxisomal membrane is permeable to both GSH and GSSG - Implications for intraperoxisomal redox homeostasis.Redox biology · 2023Article
- Functional Analysis of GSTK1 in Peroxisomal Redox Homeostasis in HEK-293 Cells.Antioxidants (Basel, Switzerland) · 2023Article
- Selective Disruption of Mitochondrial Thiol Redox State in Cells and In Vivo.Cell chemical biology · 2019Article
- Characterization of visceral and subcutaneous adipose tissue transcriptome in pregnant women with and without spontaneous labor at term: implication of alternative splicing in the metabolic adaptations of adipose tissue to parturition.Journal of perinatal medicine · 2016Article
- Endoplasmic reticulum (ER) localization is critical for DsbA-L protein to suppress ER stress and adiponectin down-regulation in adipocytes.The Journal of biological chemistry · 2015Article
- Article
- Growth hormone alters the glutathione S-transferase and mitochondrial thioredoxin systems in long-living Ames dwarf mice.The journals of gerontology. Series A, Biological sciences and medical sciences · 2014Article
- Effects of insulin-like growth factor 1 on glutathione S-transferases and thioredoxin in growth hormone receptor knockout mice.Age (Dordrecht, Netherlands) · 2014Article
- A disulfide-bond A oxidoreductase-like protein (DsbA-L) regulates adiponectin multimerization.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Thioredoxin-like domain of human kappa class glutathione transferase reveals sequence homology and structure similarity to the theta class enzyme.Protein science : a publication of the Protein Society · 2005Article
- Modelling and bioinformatics studies of the human Kappa-class glutathione transferase predict a novel third glutathione transferase family with similarity to prokaryotic 2-hydroxychromene-2-carboxylate isomerases.The Biochemical journal · 2004Article
- Marine glutathione S-transferases.Marine biotechnology (New York, N.Y.)Review
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5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The class Kappa family of glutathione S-transferases (GSTs) currently comprises a single rat subunit (rGSTK1), originally isolated from the matrix of liver mitochondria [Harris, Meyer, Coles and Ketterer (1991) Biochem. J. 278, 137-141; Pemble, Wardle and Taylor (1996) Biochem. J. 319, 749-754]. In the present study, an expressed sequence tag (EST) clone has been identified which encodes a mouse class Kappa GST (designated mGSTK1). The EST clone contains an open reading frame of 678 bp, encoding a protein composed of 226 amino acid residues with 86% sequence identity with the rGSTK1 polypeptide. The mGSTK1 and rGSTK1 proteins have been heterologously expressed in Escherichia coli and purified by affinity chromatography. Both mouse and rat transferases were found to exhibit GSH-conjugating and GSH-peroxidase activities towards model substrates. Analysis of expression levels in a range of mouse and rat tissues revealed that the mRNA encoding these enzymes is expressed predominantly in heart, kidney, liver and skeletal muscle. Although other soluble GST isoenzymes are believed to reside primarily within the cytosol, subcellular fractionation of mouse liver demonstrates that this novel murine class Kappa GST is associated with mitochondrial fractions. Through the use of bioinformatics, the genes encoding the mouse and rat class Kappa GSTs have been identified. Both genes comprise eight exons, the protein coding region of which spans approx. 4.3 kb and 4.1 kb of DNA for mGSTK1 and rGSTK1 respectively. This conservation in primary structure, catalytic properties, tissue-specific expression, subcellular localization and gene structure between mouse and rat class Kappa GSTs indicates that they perform similar physiological functions. Furthermore, the association of these enzymes with mitochondrial fractions is consistent with them performing a specific conserved biological role within this organelle.
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