| pubmed-article:3667623 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3667623 | lifeskim:mentions | umls-concept:C0023418 | lld:lifeskim |
| pubmed-article:3667623 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:3667623 | lifeskim:mentions | umls-concept:C0017817 | lld:lifeskim |
| pubmed-article:3667623 | lifeskim:mentions | umls-concept:C0031453 | lld:lifeskim |
| pubmed-article:3667623 | lifeskim:mentions | umls-concept:C0702240 | lld:lifeskim |
| pubmed-article:3667623 | lifeskim:mentions | umls-concept:C0591833 | lld:lifeskim |
| pubmed-article:3667623 | pubmed:issue | 31 | lld:pubmed |
| pubmed-article:3667623 | pubmed:dateCreated | 1987-12-10 | lld:pubmed |
| pubmed-article:3667623 | pubmed:abstractText | Murine L1210 leukemia cells resistant to the antineoplastic agent L-phenylalanine mustard have a 1.5-2.0-fold elevation in their cellular GSH and GSSG content as compared to drug-sensitive cells. Cellular uptake of L-[U-14C]cystine and its incorporation into GSH of the resistant tumor are correspondingly elevated. Synthesis of gamma-glutamylcysteine, GSH, and GSSG is elevated 1.5-2.0-fold in cell-free preparations of the resistant tumor. This increased synthesis of GSH is attributed to increased cellular content (1.6-fold) of gamma-glutamylcysteine synthetase. GSH synthetase activity is equivalent in both drug-sensitive and -resistant cells. Investigation into the hydrolysis of selected peptides by cell-free preparations of both sensitive and resistant tumors suggest that aminopeptidase M participates in the formation of L-cysteine from L-Cys-Gly. This is supported by the observation that these preparations readily degrade L-Leu-p-nitroanilide and L-Ala-L-Ala-L-Ala, known substrates for aminopeptidase M, but not dipeptidase. The failure of the tumors to degrade Gly-D-Ala, a dipeptidase substrate, and the marked inhibition of L-Ala-Gly, L-Cys-Gly, and L-Ala-L-Ala-L-Ala hydrolysis by Bestatin further support a role for aminopeptidase M in the generation of L-cysteine from L-Cys-Gly. These results suggest that the drug-resistant tumor cell has developed an efficient mechanism for maintenance of elevated GSH which involves both gamma-glutamyl transpeptidase-initiated catabolism of GSH to cysteine and its reutilization by gamma-glutamylcysteine synthetase. | lld:pubmed |
| pubmed-article:3667623 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3667623 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3667623 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3667623 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3667623 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3667623 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3667623 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:3667623 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3667623 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3667623 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:3667623 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:3667623 | pubmed:author | pubmed-author:OkineLL | lld:pubmed |
| pubmed-article:3667623 | pubmed:author | pubmed-author:VisticaD TDT | lld:pubmed |
| pubmed-article:3667623 | pubmed:author | pubmed-author:AhmadSS | lld:pubmed |
| pubmed-article:3667623 | pubmed:author | pubmed-author:LiFF | lld:pubmed |
| pubmed-article:3667623 | pubmed:author | pubmed-author:NajarianPP | lld:pubmed |
| pubmed-article:3667623 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3667623 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:3667623 | pubmed:volume | 262 | lld:pubmed |
| pubmed-article:3667623 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3667623 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3667623 | pubmed:pagination | 15048-53 | lld:pubmed |
| pubmed-article:3667623 | pubmed:dateRevised | 2003-11-14 | lld:pubmed |
| pubmed-article:3667623 | pubmed:meshHeading | pubmed-meshheading:3667623-... | lld:pubmed |
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| pubmed-article:3667623 | pubmed:meshHeading | pubmed-meshheading:3667623-... | lld:pubmed |
| pubmed-article:3667623 | pubmed:meshHeading | pubmed-meshheading:3667623-... | lld:pubmed |
| pubmed-article:3667623 | pubmed:meshHeading | pubmed-meshheading:3667623-... | lld:pubmed |
| pubmed-article:3667623 | pubmed:meshHeading | pubmed-meshheading:3667623-... | lld:pubmed |
| pubmed-article:3667623 | pubmed:meshHeading | pubmed-meshheading:3667623-... | lld:pubmed |
| pubmed-article:3667623 | pubmed:meshHeading | pubmed-meshheading:3667623-... | lld:pubmed |
| pubmed-article:3667623 | pubmed:meshHeading | pubmed-meshheading:3667623-... | lld:pubmed |
| pubmed-article:3667623 | pubmed:meshHeading | pubmed-meshheading:3667623-... | lld:pubmed |
| pubmed-article:3667623 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:3667623 | pubmed:articleTitle | Elevation of glutathione in phenylalanine mustard-resistant murine L1210 leukemia cells. | lld:pubmed |
| pubmed-article:3667623 | pubmed:affiliation | Laboratory of Pharmacology and Experimental Therapeutics, National Cancer Institute, Bethesda, Maryland 20892. | lld:pubmed |
| pubmed-article:3667623 | pubmed:publicationType | Journal Article | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3667623 | lld:pubmed |
