ArticleThe Biochemical journal1991
Heterologous expression of the allelic variant mu-class glutathione transferases mu and psi.
Article in The Biochemical journal, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 2 of them syntheses that pooled it.
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Who cites it
22 citing papers in PubMed, 2 syntheses or guidelines pooled it, 92 citations in OpenAlex.
- Association of GSTT1 gene polymorphisms with the risk of prostate cancer: an updating meta-analysis.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2013Pooled it
- Meta-analysis and pooled analysis of GSTM1 and CYP1A1 polymorphisms and oral and pharyngeal cancers: a HuGE-GSEC review.Genetics in medicine : official journal of the American College of Medical Genetics · 2008Pooled it
- Effects of GSTT1 and GSTM1 polymorphisms in glutathione levels and breast cancer development in Brazilian patients.Molecular biology reports · 2021Article
- Role of GSTM1 in resistance to lung inflammation.Free radical biology & medicine · 2012Review
- Polymorphisms in the CYP2E1 and GSTM1 genes as possible protection factors for leprosy patients.PloS one · 2012Article
- Pharmacogenomics of cisplatin-induced ototoxicity.Pharmacogenomics · 2011Review
- Population-specific GSTM1 copy number variation.Human molecular genetics · 2009Article
- Human pharmacogenomic variations and their implications for antifungal efficacy.Clinical microbiology reviews · 2006Review
- Cancer drugs, genetic variation and the glutathione-S-transferase gene family.American journal of pharmacogenomics : genomics-related research in drug development and clinical practice · 2003Review
- Perspectives on the chemical etiology of breast cancer.Environmental health perspectives · 2002Review
- Structural determinants in domain II of human glutathione transferase M2-2 govern the characteristic activities with aminochrome, 2-cyano-1,3-dimethyl-1-nitrosoguanidine, and 1,2-dichloro-4-nitrobenzene.Protein science : a publication of the Protein Society · 1999Article
- Comparison of the mRNA sequences for Pi class glutathione transferases in different hamster species and the corresponding enzyme activities with anti-benzo[a]pyrene-7,8-dihydrodiol 9,10-epoxide.The Biochemical journal · 1996Article
- Molecular basis of polymorphic drug metabolism.Journal of molecular medicine (Berlin, Germany) · 1995Review
- Isothiocyanates as substrates for human glutathione transferases: structure-activity studies.The Biochemical journal · 1995Article
- Genotyping for polymorphisms in xenobiotic metabolism as a predictor of disease susceptibility.Environmental health perspectives · 1994Article
- Detoxication of base propenals and other alpha, beta-unsaturated aldehyde products of radical reactions and lipid peroxidation by human glutathione transferases.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- Identification of class-mu glutathione transferase genes GSTM1-GSTM5 on human chromosome 1p13.American journal of human genetics · 1993Article
- Deduced amino acid sequence, gene structure and chromosomal location of a novel human class Mu glutathione S-transferase, GSTM4.The Biochemical journal · 1993Article
- Participation of the phenolic hydroxyl group of Tyr-8 in the catalytic mechanism of human glutathione transferase P1-1.The Biochemical journal · 1992Article
- Contribution of five amino acid residues in the glutathione-binding site to the function of human glutathione transferase P1-1.The Biochemical journal · 1992Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
cDNA encoding the more acidic form, glutathione transferase (GST) psi, of the polymorphic Mu-class GSTs discovered in liver, was mutated in the 5'-end to create an NcoI site, facilitating cloning into the expression plasmid pKK233-2. The protein expressed from this construct has a point mutation Pro-2----Ala-2, but gives a catalytically functional protein. Back-mutation of the codon for amino acid residue 2 gave rise to a plasmid expressing the wild-type enzyme GST psi, or GST Mu1b-1b. A variant cDNA, differing only in specifying lysine rather than asparagine in position 173 of the coding region, was generated by site-directed mutagenesis. The variant sequence corresponds to another cDNA clone isolated from a human liver cDNA library and expresses the near-neutral GST mu, or GST Mu1a-1a. The two recombinant proteins GST Mu1a-1a and GST Mu1b-1b, by physicochemical as well as kinetic criteria, were found to be indistinguishable from GST mu and GST psi respectively, isolated from human liver. It is therefore concluded that the recombinant proteins correspond to the allelic variants observed in the human population. The two forms have different isoelectric points and correspond to the allelic variants observed in the human population. The two forms have different isoelectric points and their protein subunits can be separated by h.p.l.c. on a reverse-phase column. With standard substrates and inhibitors no differences in kinetic parameters between the two variants were detected. The mutated GST Mu1b-1b (Pro-2----Ala) was not significantly different in catalytic properties from the wild-type enzyme, even though Pro-2 is a well conserved amino acid residue in the known Mu-class GSTs.
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