Expression of glutathione S-transferase-π messenger rna in human esophageal cancers

Ishioka, Chikashi; Kanamaru, Ryunosuke; Shibata, Hiroyuki; Konishi, Yoko; Ishikawa, Akira; Wakui, A; Sato, Toshiaki; Nishihira, Tetsuro

doi:10.1002/1097-0142(19910515)67:10<2560::aid-cncr2820671028>3.0.co;2-m

Cited by 23 publications

(11 citation statements)

References 10 publications

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“…However, we have found that the level of GST-P1 in cancerous tissue was significantly lower than the level in normal oesophageal tissue (Figure 3). This was contrary to what others have found (Tsuchida et al, 1989;Ishioka et al, 1991) although they determined blood and not tissue levels. However, our results were not unexpected since a phenomenon was observed in cancer, where GST-P1 was extruded into the blood as the inactive monomer (Kura et al, 1996).…”

Section: Resultsmentioning

confidence: 95%

“…What is the case then in oesophageal cancer? In 80% of the patients, the resected primary oesophageal cancer showed that the RNA transcript levels of GST-P1 were significantly elevated (Ishioka et al, 1991). However, in contrast, Sasano et al (1993) found that with both in situ hybridization and immunohisto chemistry assessments, GST-P1 was detected as strongly in normal oesophageal mucosa as in cancer.…”

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confidence: 99%

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Glutathione-linked enzymes in benign and malignant oesophageal tissue

et al. 1999

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Oxyradicals are involved in multiple mutational events and can contribute to the conversion of healthy cells to cancer cells. Glutathione (GSH) and the GSH-replenishing enzymes keep the antioxidant status of normal cells at a level where they can avert oxyradical derived mutations. The aim of this study was to determine whether in cancer cells the GSH-replenishing, GSH antioxidant and GSH-depleting enzymes were not at appropriate levels and therefore not able to protect cancer cells adequately against oxyradical-induced mutations. Cancer of the oesophagus was chosen since it is the most common gastrointestinal malignancy in South African Blacks. Biopsies and blood from 31 patients with cancer of the oesophagus and 29 non-cancer patients were assessed for these enzymes. The mean activity of the antioxidant and depleting enzyme GSH-peroxidase was elevated significantly by twofold in the cancer tissue compared to normal tissue. However, the activity of the replenishing enzyme GSSG-reductase and the level of the depleting enzyme GSH-s-transferase P1-isoenzyme were significantly reduced by 23% and 33% respectively. As in a previous paper we found that GSH was depleted and γ-glutamine transpeptidase was diminished in oesophageal cancer. There can be two reasons for GSH depletion. Firstly, elevated GSH–peroxidase will use more GSH in an attempt to cope with the excessive production of oxyradicals as revealed by elevated lipid peroxidation; this was, as shown by us before, elevated sixfold in oesophageal cancer. Secondly, if little replenishment of GSH occurred the level of GSH would become lower. This was confirmed by our findings that the activities of the replenishing enzymes were significantly diminished in oesophageal cancer tissue. Contrary to what was expected, the other depleting enzyme GSH-s-transferase P1 was not elevated in cancer tissue but was significantly lower. However, in the blood of the same patients it was significantly elevated. An explanation for this phenomenon is that, although the production of GST-P1 was enhanced in cancer, it did not show because it was rapidly extruded into the blood by an unknown mechanism operational only in cancer cells. © 1999 Cancer Research Campaign

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Section: Resultsmentioning

confidence: 95%

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confidence: 99%

Glutathione-linked enzymes in benign and malignant oesophageal tissue

et al. 1999

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“…In addition, since GSTs are involved in modulation of expression of other drug metabolizing proteins, polymorphism in GST may influence other defense mechanisms, thereby indirectly conferring a differential risk for development of cancer. [19] GSTs, particularly its class-Pi are predominantly expressed in human epithelial cells in the normal squamous esophagus epithelium [16,[20][21][22] and it has been used as the marker of gastrointestinal (G.I) carcinoma. Earlier we reported that the level of class P GST is elevated in tissue biopsies obtained from SCC patients who underwent surgery or upper gastro-digestive endoscopic operation when compared to normal samples.…”

Section: Discussionmentioning

confidence: 99%

Relationship between genetic polymorphism of glutathione S-transferase-p1 and p53 protein accumulation in Iranian esophageal squamous cell carcinoma patients

et al. 2008

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“…Among the isozymes, the pi class enzyme GSTP1-1 is the most widely distributed and has been well studied in cancer. Increased expression of GSTP1-1 has been reported in a number of cancer types, including colon (Mulder et al, 1995), stomach (Peters et al, 1990), oesophagal (Ishioka et al, 1991), head and neck (Wang et al, 1997). An association between increased GSTP1-1 expression and resistance to cytotoxic drugs has also been established with breast cancer cells (Batist et al, 1986).…”

Section: Introductionmentioning

confidence: 99%

Detailed methylation analysis of the glutathione S-transferase π (GSTP1) gene in prostate cancer

et al. 1999

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Glutathione-S-Transferases (GSTs) comprise a family of isoenzymes that provide protection to mammalian cells against electrophilic metabolites of carcinogens and reactive oxygen species. Previous studies have shown that the CpG-rich promoter region of the p-class gene GSTP1 is methylated at single restriction sites in the majority of prostate cancers. In order to understand the nature of abnormal methylation of the GSTP1 gene in prostate cancer we undertook a detailed analysis of methylation at 131 CpG sites spanning the promoter and body of the gene. Our results show that DNA methylation is not con®ned to speci®c CpG sites in the promoter region of the GSTP1 gene but is extensive throughout the CpG island in prostate cancer cells. Furthermore we found that both alleles are abnormally methylated in this region. In normal prostate tissue, the entire CpG island was unmethylated, but extensive methylation was found outside the island in the body of the gene. Loss of GSTP1 expression correlated with DNA methylation of the CpG island in both prostate cancer cell lines and cancer tissues whereas methylation outside the CpG island in normal prostate tissue appeared to have no e ect on gene expression.

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Expression of glutathione S-transferase-π messenger rna in human esophageal cancers

Cited by 23 publications

References 10 publications

Glutathione-linked enzymes in benign and malignant oesophageal tissue

Glutathione-linked enzymes in benign and malignant oesophageal tissue

Relationship between genetic polymorphism of glutathione S-transferase-p1 and p53 protein accumulation in Iranian esophageal squamous cell carcinoma patients

Detailed methylation analysis of the glutathione S-transferase π (GSTP1) gene in prostate cancer

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