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   <subfield code="a">Effect of nonprotein thiols on protein synthesis in isolated rat hepatocytes</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[M. Asensi, A. Carcía-España, F. Pallardó, J. Viña, J. Estrela]</subfield>
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   <subfield code="a">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. Glutahione depletion, induced by in vivod 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 perturbatin 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 syntheis by increasing intracellular levels of aspartate: 1. Amino-oxyacetate, an inhibitor of pyridoxyal-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-ocycetate, stimulates protein labelling and induces aspartate accumulation, although mot amino acids diminish or remain unchanged.</subfield>
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