ArticleThe Biochemical journal1997
Quantitative profiling of tissue- and gender-related expression of glutathione S-transferase isoenzymes in the mouse.
Article in The Biochemical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 78 citations in OpenAlex.
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- Developmental and activity-dependent expression of LanCL1 confers antioxidant activity required for neuronal survival.Developmental cell · 2014Article
- Genetic or pharmacologic activation of Nrf2 signaling fails to protect against aflatoxin genotoxicity in hypersensitive GSTA3 knockout mice.Toxicological sciences : an official journal of the Society of Toxicology · 2014Article
- Role of GSTM1 in resistance to lung inflammation.Free radical biology & medicine · 2012Review
- The effects of the Chinese medicine ZiBu PiYin recipe on the hippocampus in a rat model of diabetes-associated cognitive decline: a proteomic analysis.Diabetologia · 2011Article
- In vivo induction of phase II detoxifying enzymes, glutathione transferase and quinone reductase by citrus triterpenoids.BMC complementary and alternative medicine · 2010Article
- Sex-specific gene expression in the BXD mouse liver.Physiological genomics · 2010Article
- Glutathione-S-transferase A3 knockout mice are sensitive to acute cytotoxic and genotoxic effects of aflatoxin B1.Toxicology and applied pharmacology · 2010Article
- Glutathione S-transferase-micro1 regulates vascular smooth muscle cell proliferation, migration, and oxidative stress.Hypertension (Dallas, Tex. : 1979) · 2009Article
- Induction of hepatic glutathione S-transferases in male mice by prototypes of various classes of microsomal enzyme inducers.Toxicological sciences : an official journal of the Society of Toxicology · 2008Article
- Mechanistic basis for inflammation and tumor promotion in lungs of 2,6-di-tert-butyl-4-methylphenol-treated mice: electrophilic metabolites alkylate and inactivate antioxidant enzymes.Chemical research in toxicology · 2007Article
- Loss of the Nrf2 transcription factor causes a marked reduction in constitutive and inducible expression of the glutathione S-transferase Gsta1, Gsta2, Gstm1, Gstm2, Gstm3 and Gstm4 genes in the livers of male and female mice.The Biochemical journal · 2002Article
- Method for non-invasively recording electrocardiograms in conscious mice.BMC physiology · 2001Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Cytosolic glutathione S-transferase (GST) isoenzymes from brain, heart, lung, liver, kidney and gonads of male and female CD-1 mice were identified and quantified with a combination of affinity purification, electrospray ionization MS, Edman microsequencing, Western blot analysis and reverse-phase HPLC. The three principal hepatic GST subunits, mGSTA3 (25271 Da), mGSTP1 (23478 Da), and mGSTM1 (25839 Da), were isolated from liver, lung, kidney, testes and female heart, whereas brain, ovaries and male heart contained mGSTM1 and mGSTP1. Additional isoenzymes were detected in tissues, including mu class subunits mGSTM2 (25580 Da) and mGSTM3 (25570 Da), an N-terminally blocked Alpha subunit (25480 Da) assigned as mGSTA4, and proteins of molecular masses 25490, 22540, 24493, 24378 and 25383 Da. Distinct gender differences in expression of GST subunits were observed for liver, heart, kidney and gonads, whereas GST expression was similar in brain and lung for both genders. In contrast with patterns of expression in liver (high ratio of mGSTA3 to mGSTP1 in females relative to males), mGSTP1 was the most abundant subunit in female gonads, whereas mGSTA3 was not present in detectable quantities. The profile of GST expression in kidney was similar to that in liver; however, male kidneys expressed 30% more soluble GST than female kidneys. A striking gender-related difference in GST expression was found in cardiac tissue, where female animals expressed 50% more soluble GST than male tissues, and the GST isoenzyme with the greatest documented activity towards lipid hydroperoxides, mGSTA3, was present in female tissue yet absent from male tissue. These results point to complex gender- and tissue-dependent expression of individual mouse GST isoenzymes.
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