schliessen

Filtern

 

Bibliotheken

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

An increasing body of evidence suggests that glutathione-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 glutathione S-transferase isoenzyme (GST) cont... Full description

Journal Title: Carcinogenesis 1988, Vol.9(9), pp.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:
ID: ISSN: 0143-3334 ; E-ISSN: 1460-2180 ; DOI: http://dx.doi.org/10.1093/carcin/9.9.1617
Zum Text:
SendSend as email Add to Book BagAdd to Book Bag
Staff View
recordid: crossref10.1093/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:
  • Medicine
ispartof: Carcinogenesis, 1988, Vol.9(9), pp.1617-1621
description: An increasing body of evidence suggests that glutathione-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 glutathione S-transferase isoenzyme (GST) content and glutathione 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 pi class, acidic Yf, GST subunit were found in all the samples, with little variation between individuals. The concentration of alpha and mu class subunits was 5- to 10-fold lower and were subject to significant individual variability. The mu class subunit identified had a faster mobility on SDS-PAGE than the hepatic GST mu 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 mu class subunit, and to a lesser extent the alpha class GST subunit. The pi subunit was present in the normal and tumour cells in very similar concentration. The expression of the mu 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 ; E-ISSN: 1460-2180 ; DOI: http://dx.doi.org/10.1093/carcin/9.9.1617
fulltext: fulltext
issn:
  • 01433334
  • 0143-3334
  • 14602180
  • 1460-2180
url: Link


@attributes
ID1915326785
RANK0.07
NO1
SEARCH_ENGINEprimo_central_multiple_fe
SEARCH_ENGINE_TYPEPrimo Central Search Engine
LOCALfalse
PrimoNMBib
record
control
sourcerecordid10.1093/carcin/9.9.1617
sourceidcrossref
recordidTN_crossref10.1093/carcin/9.9.1617
sourceformatXML
sourcesystemPC
pqid78392213
display
typearticle
titleGlutathione S-transferase isoenzymes and glutathione peroxidase activity in normal and tumour samples from human lung
creatorCarmichael, James ; Forrester, Lesley M. ; Lewis, Alexander D. ; Hayes, John D. ; Hayes, Peter C. ; Wolf, C. Roland
ispartofCarcinogenesis, 1988, Vol.9(9), pp.1617-1621
identifier
languageeng
source
lds411988
descriptionAn increasing body of evidence suggests that glutathione-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 glutathione S-transferase isoenzyme (GST) content and glutathione 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 pi class, acidic Yf, GST subunit were found in all the samples, with little variation between individuals. The concentration of alpha and mu class subunits was 5- to 10-fold lower and were subject to significant individual variability. The mu class subunit identified had a faster mobility on SDS-PAGE than the hepatic GST mu 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 mu class subunit, and to a lesser extent the alpha class GST subunit. The pi subunit was present in the normal and tumour cells in very similar concentration. The expression of the mu 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.
subjectMedicine;
version3
lds50peer_reviewed
links
openurl$$Topenurl_article
thumbnail
0$$TPCamazon_thumb
1$$TPCgoogle_thumb
openurlfulltext$$Topenurlfull_article
addlink$$Uhttp://exlibris-pub.s3.amazonaws.com/aboutCrossref.html$$EView_CrossRef_copyright_notice
search
creatorcontrib
0Carmichael, James
1Forrester, Lesley M.
2Lewis, Alexander D.
3Hayes, John D.
4Hayes, Peter C.
5Wolf, C. Roland
titleGlutathione S-transferase isoenzymes and glutathione peroxidase activity in normal and tumour samples from human lung
general
0English
110.1093/carcin/9.9.1617
2Oxford University Press (via CrossRef)
3Oxford University Press (CrossRef)
sourceidcrossref
recordidcrossref10.1093/carcin/9.9.1617
issn
001433334
10143-3334
214602180
31460-2180
rsrctypearticle
addtitleCarcinogenesis
searchscope
0crossref_oup
1CrossRef
2Crossref
3crossref
scope
0crossref_oup
1CrossRef
2Crossref
3crossref
lsr401988
lsr411988
lsr431988
lsr451988
tmp012
tmp022
creationdate1988
startdate19880101
enddate19881231
citationpf 1617 pt 1621 vol 9 issue 9
lsr30VSR-Enriched:[description, subject, pqid]
sort
titleGlutathione S-transferase isoenzymes and glutathione peroxidase activity in normal and tumour samples from human lung
authorCarmichael, James ; Forrester, Lesley M. ; Lewis, Alexander D. ; Hayes, John D. ; Hayes, Peter C. ; Wolf, C. Roland
creationdate19880000
lso0119880000
facets
frbrgroupid2339837693209465285
frbrtype5
languageeng
creationdate1988
collectionOxford University Press (CrossRef)
prefilterarticles
rsrctypearticles
creatorcontrib
0Carmichael, James
1Forrester, Lesley M.
2Lewis, Alexander D.
3Hayes, John D.
4Hayes, Peter C.
5Wolf, C. Roland
jtitleCarcinogenesis
toplevelpeer_reviewed
delivery
delcategoryRemote Search Resource
fulltextfulltext
addata
aulast
0Carmichael
1Forrester
2Lewis
3Hayes
4Wolf
aufirst
0James
1Lesley M.
2Alexander D.
3John D.
4Peter C.
5C. Roland
au
0Carmichael, James
1Forrester, Lesley M.
2Lewis, Alexander D.
3Hayes, John D.
4Hayes, Peter C.
5Wolf, C. Roland
atitleGlutathione S-transferase isoenzymes and glutathione peroxidase activity in normal and tumour samples from human lung
jtitleCarcinogenesis
stitleCarcinogenesis
date1988
risdate1988
adddate1988
volume9
issue9
spage1617
epage1621
pages1617-1621
issn0143-3334
eissn1460-2180
formatjournal
genrearticle
ristypeJOUR
doi10.1093/carcin/9.9.1617
lad012
lad25drop record use citations