Disease relevance of Gstm1

• These two murine cDNAs were subcloned into bacterial expression vectors, and enzymatically active GSTs encoded by pmGT10 (mGTmu1) or pmGT2 (mGTmu2) were purified from transformed Escherichia coli lysates [1].
• Immunodetection with a monoclonal antibody of glutathione S-transferase mu in patients with and without carcinomas [2].

Psychiatry related information on Gstm1

• Our results demonstrate that a reduction in several anti-oxidant defense mechanisms, including catalase and glutathione S-transferase mu, correlates with the emergence of the malignant phenotype [3].

High impact information on Gstm1

• We have isolated from a murine cell line (L929) two mu class GST cDNAs, pmGT10 (1.4 kilobases (kb] and pmGT2 (1.1 kb) [1].
• Analysis of the deduced amino acid sequences revealed 93% homology between pmGT10 and the rat Yb1 (subunit 3) gene and 95% homology between pmGT2 and the rat Yb2 (subunit 4) gene [1].
• Consistent with this possibility, associations between the glutathione S-transferase-mu-null phenotype and increased risk for lung, larynx, and bladder cancer have been recently demonstrated in humans [4].
• Our murine studies suggest that the chemopreventive activity of oltipraz may be due in part to its ability to elevate glutathione S-transferase-mu activity [4].
• In 62.5% of the mononuclear blood cells from controls, glutathione S-transferase mu is present [2].

Biological context of Gstm1

• Characterization of phenotypes in Gstm1-null mice by cytosolic and in vivo metabolic studies using 1,2-dichloro-4-nitrobenzene [5].
• In conclusion, Gstm1-null mice showed markedly low ability for glutathione conjugation to DCNB in the cytosol and in vivo and would be useful as a deficient model of GSTM1 for absorption, distribution, metabolism, and excretion/toxicology studies [5].
• The evidence indicated that GST1 is assigned to chromosome 11 in humans [6].
• Gene for glutathione S-transferase-1 (GST1) is on human chromosome 11 [6].
• These findings give evidence that the MDR1-, GST mu- and TOPO IIa-gene products may contribute to drug resistance in HB [7].

Anatomical context of Gstm1

• In the enzymatic study, GST activities toward 1,2-dichloro-4-nitrobenzene (DCNB) and 1-chloro-2,4-dinitrobenzene (CDNB) in the liver and kidney cytosols were markedly lower in Gstm1-null mice than in the wild-type control [5].
• Using a modified immunization and fusion procedure, one stable hybridoma clone secreting an anti-GST antibody (alpha GST-1) was obtained [8].
• The chromosomal location of one of the enzyme forms, GST1, reported recently to be polymorphic, was determined utilizing man-mouse somatic cell hybrids segregating human chromosomes [6].

Associations of Gstm1 with chemical compounds

• Expression analyses for the Gstm1-null mice revealed a deletion of Gstm1 mRNA and a small decrease in glutathione S-transferase alpha 3 mRNA [5].
• With the assay, we tested the effectiveness of a set of 15 phosphorothioate ODNs against rat glutathione S-transferase Mu1 (GSTM1) and/or Mu2 (GSTM2) [9].

Analytical, diagnostic and therapeutic context of Gstm1

• In this study, we generated mice with disrupted glutathione S-transferase Mu 1 gene (Gstm1-null mice) by gene targeting, and characterized the phenotypes by cytosolic and in vivo studies [5].
• Using probes specific for each gene, northern blot analysis demonstrated that pmGT10 and pmGT2 hybridized to a 1.3-1.4-kb mRNA species present in L929 cells [1].

References