6533b855fe1ef96bd12b133c

RESEARCH PRODUCT

Regulation of glutathione metabolism in Ehrlich ascites tumour cells.

Jose ViñaMiguel AsensiI R PuertesJ M EstrelaR. HernandezP Terradez

subject

MaleGPX1Glutathione reductaseProtein metabolismMice Inbred StrainsBiologyGlucosephosphate DehydrogenaseBiochemistrychemistry.chemical_compoundMiceMethionineReference ValuesAnimalsAmino AcidsCarcinoma Ehrlich TumorMolecular BiologyCells CulturedGlutathione Transferasechemistry.chemical_classificationGlutathione PeroxidaseGlutathione DisulfideGlutathione peroxidaseCell BiologyGlutathioneGlutathioneAcetylcysteineRatsKineticsGlutathione ReductasechemistryBiochemistryLiverCancer cellGlutathione disulfidesense organsCell DivisionCysteineSubcellular FractionsResearch Article

description

Glutathione metabolism was studied in cancer cells during the growth of an Ehrlich ascites tumour. GSH, but not GSSG, content decreases when cell proliferation and the rate of protein synthesis in the tumour decrease. This change correlates with a decrease in the rate of GSH synthesis and an increase in glutathione peroxidase and glutathione S-transferase activities. Glutathione efflux from tumour cells seems to co-ordinate with the rate of GSH synthesis. Cysteine, and not methionine, promotes GSH synthesis in tumour cells. However, changes in the rate of GSH synthesis are not due to limitations in the supply of blood cysteine or to changes in the intracellular amino acid pool of the cancer cells. Our data suggest that changes in protein metabolism accompanying tumour growth in vivo can modulate glutathione content in cancer cells.

10.1042/bj2860257https://pubmed.ncbi.nlm.nih.gov/1520278