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  • Title: Effect of nonprotein thiols on protein synthesis in isolated rat hepatocytes.
    Author: Asensi M, Garcia-España A, Pallardó FV, Vina J, Estrela JM.
    Journal: Experientia; 1996 Feb 15; 52(2):111-4. PubMed ID: 8608810.
    Abstract:
    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.
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