ArticleThe Biochemical journal1994
Variability of glutathione S-transferase isoenzyme patterns in matched normal and cancer human breast tissue.
Article in The Biochemical journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 43 citations in OpenAlex.
- Role of human glutathione transferases in biotransformation of the nitric oxide prodrug JS-K.Scientific reports · 2021Article
- Association analysis of rs1695 and rs1138272 variations in GSTP1 gene and breast cancer susceptibility.Asian Pacific journal of cancer prevention : APJCP · 2020Article
- Estrogen metabolism and exposure in a genotypic-phenotypic model for breast cancer risk prediction.Cancer epidemiology, biomarkers & prevention : a publication of the American Association for Cancer Research, cosponsored by the American Society of Preventive Oncology · 2011Article
- Genetic polymorphisms in the catechol estrogen metabolism pathway and breast cancer risk.Cancer epidemiology, biomarkers & prevention : a publication of the American Association for Cancer Research, cosponsored by the American Society of Preventive Oncology · 2009Article
- Glutathione-S-transferase M1, T1 and P1 polymorphisms, and breast cancer risk, in BRCA1/2 mutation carriers.British journal of cancer · 2008Article
- Polymorphisms in drug metabolism genes, smoking, and p53 mutations in breast cancer.Molecular carcinogenesis · 2008Article
- Characterization of S-hexylglutathione-binding proteins of human hepatocellular carcinoma: separation of enoyl-CoA isomerase from an Alpha class glutathione transferase form.The Biochemical journal · 1997Article
- Quantitative profiling of tissue- and gender-related expression of glutathione S-transferase isoenzymes in the mouse.The Biochemical journal · 1997Article
- Evidence for an essential serine residue in the active site of the Theta class glutathione transferases.The Biochemical journal · 1995Article
- Delta 3, delta 2-enoyl-CoA isomerase is the protein that copurifies with human glutathione S-transferases from S-hexylglutathione affinity matrices.The Biochemical journal · 1994Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The determination of GST levels in blood has been proposed to a marker of tumour burden in general, whereas level of the P1 isoenzyme has been identified as a prognostic factor for breast-cancer patients receiving no adjuvant chemotherapy. Particular glutathione S-transferase (GST) isoenzymes differ in their substrate specificity, however, and their presence or absence might therefore account for the resistance of tumours to particular chemotherapeutic drugs, as already established for cultured cell lines. Determination of the GST isoenzyme profile of a cancer tissue could have prognostic value in the selection of treatment if the levels of expression/activity show a degree of variation comparable with that exhibited by actual patient responses. Using reversed-phase h.p.l.c. to quantify affinity-isolated GSTs, we have analysed full isoenzyme profiles in the first large sample of matched normal and cancer human tissues (18 breast-cancer patients). In no patients did the tumour tissues express any isoenzymes that were not found in normal breast tissue. In addition to the GSTs, another enzyme, identified as enoyl-CoA isomerase, was regularly found in breast tissue cytosol following elution from a hexyl-glutathione affinity column. In most cases, the average level of GST was substantially elevated in the cancer tissues above the levels in normal breast tissue from the same patient. Furthermore, the relative levels of the isoenzymes were substantially more variable in the cancer samples than in the normal breast tissue, providing a plausible mechanism for the well established variable response to treatment.
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