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RESEARCH PRODUCT
Effect of nonprotein thiols on protein synthesis in isolated rat hepatocytes.
A Garcia-españaJose ViñaFederico V. PallardóMiguel AsensiJ M Estrelasubject
AntimetabolitesBiologyCellular and Molecular Neurosciencechemistry.chemical_compoundMethionineMethionine SulfoximineProtein biosynthesisAnimalsButhionine sulfoximineCarbon RadioisotopesCysteineSulfhydryl CompoundsAmino AcidsRats WistarMolecular BiologyButhionine SulfoximineCells CulturedPharmacologychemistry.chemical_classificationMaleatesAminooxyacetic AcidCell BiologyGlutathioneAmino acidRatsKineticsEnzymechemistryBiochemistryLiverProtein BiosynthesisMolecular MedicineNAD+ kinaseLeucineCysteinedescription
The ability of nonprotein thiols to modulate rates of protein synthesis was investigated in isolated rat hepatocytes. Addition of cysteine stimulates protein labelling by [14C]Leucine. Glutathione depletion, induced by in vivo administration of L-buthionine sulfoximine and diethylmaleate, did not alter the effect of cysteine, although it decreased the rate of protein synthesis by 32%. The effect of cysteine on protein synthesis does not seem to be related to a perturbation of the redox state of the NAD+/NADH system or to changes in the rate of gluconeogenic pathway. The following observations indicate that cysteine may stimulate protein synthesis by increasing intracellular levels of aspartate: 1. Amino-oxyacetate, an inhibitor of pyridoxal-dependent enzymes, inhibits protein labelling and decreases aspartate cellular content, whereas most amino acids accumulate or remain unchanged; 2. Cysteine, in the absence or in the presence of amino-oxyacetate, stimulates protein labelling and induces aspartate accumulation, although most amino acids diminish or remain unchanged.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1996-02-01 | Experientia |