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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
1986-5-14
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pubmed:abstractText |
The nontumorigenic ARL-15C1 and tumorigenic gamma-glutamyl transpeptidase-containing ARL-16T2 cell lines were found to contain approximately equal amounts of glutathione, cysteine, and cystine, 65.6, 3.5, and 5 nmol/mg of protein for ARL-16C1, and 61.5, 3, and 3 nmol/mg of protein for ARL-16T2, respectively. The half-life for glutathione in these cell lines was 3.2 and 3.8 h in the ARL-15C1 and 16T2, respectively. In ARL-15C1 cells, the cysteine half-life was 0.2 h and that of cystine 2.0 h compared to 2.0 h and 0.5 h, respectively, in the ARL-16T2. The turnover of glutathione in the ARL-15C1 could be accounted for by efflux into the medium whereas only 10% of the glutathione expected from ARL-16T2 cells appeared in the medium. The ARL-16T2 cells appear to support glutathione synthesis by conservation and recycling of cysteine residues. Inhibition of gamma-glutamyl transpeptidase by AT-125 (acivicin) caused extensive loss of intracellular glutathione from ARL-16T2 cells but produced no effect on GSH levels in ARL-15C1 cells. No metabolism of medium glutathione by gamma-glutamyl transpeptidase was detected, independent of AT-125 treatment. AT-125 treatment caused a transient increase in intracellular GSH in the ARL-16T2 but not the ARL-15C1, further suggesting that the enzyme catalyzes intracellular GSH recycling to supply cysteine for cellular functions in the tumorigenic ARL-16T2 cell line. Transport of cysteine, cystine, and methionine was not altered by AT-125 treatment. These data are consistent with an intracellular orientation of gamma-glutamyl transpeptidase in this cell line and not participation in extracellular processes.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Cystine,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione,
http://linkedlifedata.com/resource/pubmed/chemical/Isoxazoles,
http://linkedlifedata.com/resource/pubmed/chemical/acivicin,
http://linkedlifedata.com/resource/pubmed/chemical/gamma-Glutamyltransferase
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
261
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4986-92
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2870063-Animals,
pubmed-meshheading:2870063-Cell Line,
pubmed-meshheading:2870063-Chromatography, High Pressure Liquid,
pubmed-meshheading:2870063-Cysteine,
pubmed-meshheading:2870063-Cystine,
pubmed-meshheading:2870063-Glutathione,
pubmed-meshheading:2870063-Half-Life,
pubmed-meshheading:2870063-Isoxazoles,
pubmed-meshheading:2870063-Kinetics,
pubmed-meshheading:2870063-Liver,
pubmed-meshheading:2870063-Liver Neoplasms, Experimental,
pubmed-meshheading:2870063-Rats,
pubmed-meshheading:2870063-gamma-Glutamyltransferase
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pubmed:year |
1986
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pubmed:articleTitle |
Intracellular glutathione cycling by gamma-glutamyl transpeptidase in tumorigenic and nontumorigenic cultured rat liver cells.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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