, Volume 52, Issue 2, pp 111–114 | Cite as

Effect of nonprotein thiols on protein synthesis in isolated rat hepatocytes

  • M. Asensi
  • A. Carcía-España
  • F. V. Pallardó
  • J. Viña
  • J. M. Estrela
Research Articles


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.

Key words

Cysteine glutathione protein synthesis aspartate thiols 



reduced glutathione


oxidized glutathione

GSH ester

glutathione monoethyl ester


L-buthionine sulfoximine




N-acetyl cysteine




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Copyright information

© Birkhäuser Verlag Basel 1996

Authors and Affiliations

  • M. Asensi
    • 1
  • A. Carcía-España
    • 2
  • F. V. Pallardó
    • 1
  • J. Viña
    • 1
  • J. M. Estrela
    • 1
  1. 1.Department de FisiologíaFacultad de MedicinaValencia
  2. 2.Departmento de Bioquímica y Biología MolecularUniversidad de ValenciaValencia(Spain)

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