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Glutathione S-transferase isoenzymes and glutathione peroxidase activity in normal and tumour samples from human lung

An increasing body of evidence suggests that glutatwhione-dependent enzymes are an important factor in determining the sensitivity of tumours to cytotoxic drugs. Ten randomized normal and tumour samples from individuals with lung cancer were analysed for ghitathione S-transferase isoenzyme (GST) con... Full description

Journal Title: Carcinogenesis (New York) 1988-09, Vol.9 (9), p.1617-1621
Main Author: Carmichael, James
Other Authors: Forrester, Lesley M , Lewis, Alexander D , Hayes, John D , Hayes, Peter C , Wolf, C. Roland
Format: Electronic Article Electronic Article
Language: English
Subjects:
Publisher: Oxford: Oxford University Press
ID: ISSN: 0143-3334
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recordid: cdi_crossref_primary_10_1093_carcin_9_9_1617
title: Glutathione S-transferase isoenzymes and glutathione peroxidase activity in normal and tumour samples from human lung
format: Article
creator:
  • Carmichael, James
  • Forrester, Lesley M
  • Lewis, Alexander D
  • Hayes, John D
  • Hayes, Peter C
  • Wolf, C. Roland
subjects:
  • Analytical, structural and metabolic biochemistry
  • Biological and medical sciences
  • Enzyme Induction
  • Enzymes and enzyme inhibitors
  • Female
  • Fundamental and applied biological sciences. Psychology
  • Glutathione Peroxidase - metabolism
  • Glutathione Transferase - metabolism
  • Humans
  • Isoenzymes - metabolism
  • Lung - enzymology
  • Lung Neoplasms - enzymology
  • Male
  • Transferases
ispartof: Carcinogenesis (New York), 1988-09, Vol.9 (9), p.1617-1621
description: An increasing body of evidence suggests that glutatwhione-dependent enzymes are an important factor in determining the sensitivity of tumours to cytotoxic drugs. Ten randomized normal and tumour samples from individuals with lung cancer were analysed for ghitathione S-transferase isoenzyme (GST) content and ghitathione peroxidase (Gpx) activity. The normal tissue samples exhibited a 5.1- and 7.0-fold variation in GST and Gpx activity respectively. High levels of the π class, acidic Yf, GST subunit were found in all the samples, with little variation between individuals. The concentration of α and μ class subunits was 5- to 10-fold lower and were subject to significant individual variability. The μ class subunit identified had a faster mobility on SDS-PAGE than the hepatic GST μ standard and did not appear subject to the genetic polymorphism associated with certain members of this gene family. This suggests the presence of a novel pulmonary protein which may correspond to the rat Yn Yn protein. The normal to tumour ratio for GST activity varied significantly between the samples and tended to follow the relative expression of the μ class subunit, and to a lesser extent the α class GST subunit. The π subunit was present in the normal and tumour cells in very similar concentration. The expression of the μ class GST appeared to follow the differences in GST enzymic activity and although the numbers were small appeared to segregate according to tumour type. Gpx activity was also elevated in certain tumours. Of particular interest were the two adenocarcinomas which had a 20- to 30-fold higher tumour Gpx activity.
language: eng
source:
identifier: ISSN: 0143-3334
fulltext: no_fulltext
issn:
  • 0143-3334
  • 1460-2180
url: Link


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titleGlutathione S-transferase isoenzymes and glutathione peroxidase activity in normal and tumour samples from human lung
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descriptionAn increasing body of evidence suggests that glutatwhione-dependent enzymes are an important factor in determining the sensitivity of tumours to cytotoxic drugs. Ten randomized normal and tumour samples from individuals with lung cancer were analysed for ghitathione S-transferase isoenzyme (GST) content and ghitathione peroxidase (Gpx) activity. The normal tissue samples exhibited a 5.1- and 7.0-fold variation in GST and Gpx activity respectively. High levels of the π class, acidic Yf, GST subunit were found in all the samples, with little variation between individuals. The concentration of α and μ class subunits was 5- to 10-fold lower and were subject to significant individual variability. The μ class subunit identified had a faster mobility on SDS-PAGE than the hepatic GST μ standard and did not appear subject to the genetic polymorphism associated with certain members of this gene family. This suggests the presence of a novel pulmonary protein which may correspond to the rat Yn Yn protein. The normal to tumour ratio for GST activity varied significantly between the samples and tended to follow the relative expression of the μ class subunit, and to a lesser extent the α class GST subunit. The π subunit was present in the normal and tumour cells in very similar concentration. The expression of the μ class GST appeared to follow the differences in GST enzymic activity and although the numbers were small appeared to segregate according to tumour type. Gpx activity was also elevated in certain tumours. Of particular interest were the two adenocarcinomas which had a 20- to 30-fold higher tumour Gpx activity.
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subjectAnalytical, structural and metabolic biochemistry ; Biological and medical sciences ; Enzyme Induction ; Enzymes and enzyme inhibitors ; Female ; Fundamental and applied biological sciences. Psychology ; Glutathione Peroxidase - metabolism ; Glutathione Transferase - metabolism ; Humans ; Isoenzymes - metabolism ; Lung - enzymology ; Lung Neoplasms - enzymology ; Male ; Transferases
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01Present address: University Department of Clinical Oncology, Newcastle General Hospital, Westgate Road, Newcastle-upon-Tyne, UK
14To whom reprint requests should be sent
abstractAn increasing body of evidence suggests that glutatwhione-dependent enzymes are an important factor in determining the sensitivity of tumours to cytotoxic drugs. Ten randomized normal and tumour samples from individuals with lung cancer were analysed for ghitathione S-transferase isoenzyme (GST) content and ghitathione peroxidase (Gpx) activity. The normal tissue samples exhibited a 5.1- and 7.0-fold variation in GST and Gpx activity respectively. High levels of the π class, acidic Yf, GST subunit were found in all the samples, with little variation between individuals. The concentration of α and μ class subunits was 5- to 10-fold lower and were subject to significant individual variability. The μ class subunit identified had a faster mobility on SDS-PAGE than the hepatic GST μ standard and did not appear subject to the genetic polymorphism associated with certain members of this gene family. This suggests the presence of a novel pulmonary protein which may correspond to the rat Yn Yn protein. The normal to tumour ratio for GST activity varied significantly between the samples and tended to follow the relative expression of the μ class subunit, and to a lesser extent the α class GST subunit. The π subunit was present in the normal and tumour cells in very similar concentration. The expression of the μ class GST appeared to follow the differences in GST enzymic activity and although the numbers were small appeared to segregate according to tumour type. Gpx activity was also elevated in certain tumours. Of particular interest were the two adenocarcinomas which had a 20- to 30-fold higher tumour Gpx activity.
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