Experientia

, 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

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. 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 

Abbreviations

GSH

reduced glutathione

GSSG

oxidized glutathione

GSH ester

glutathione monoethyl ester

BSO

L-buthionine sulfoximine

DEM

diethylmaleate

NAC

N-acetyl cysteine

AOA

amino-oxyacetate

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References

  1. 1.
    Ochoa, S., Archs Biochem. Biophys.223 (1983) 325.Google Scholar
  2. 2.
    Meister, A., Science220(1983) 470.Google Scholar
  3. 3.
    Zehavi-Willner, T., Israel J. med. Sci.9 (1973) 129.PubMedGoogle Scholar
  4. 4.
    Kan, B., London, I. M., and Levin, D. H., J. biol. Chem.263 (1988) 15652.PubMedGoogle Scholar
  5. 5.
    Murthy, M. R. V., Biochim. biophys. Acta119 (1966) 586.PubMedGoogle Scholar
  6. 6.
    Kosower, N. S., and Kosower, E. M., Int. Rev. Cytol.58 (1978) 109.Google Scholar
  7. 7.
    Tateishi, N., Higashi, T., Naruse, A., Nakashima, K., Shiozaki, H., and Sakamoto, Y., J. Nutr.107 (1977) 51.PubMedGoogle Scholar
  8. 8.
    Pocius, P. A., Clark, J. H., and Baumrucker, C. R., J. Dairy Sci.64 (1981) 1551.PubMedGoogle Scholar
  9. 9.
    Szent-Györgyi, A., Együd, L. G., and McLaughlin, J. A., Science155 (1967) 539.Google Scholar
  10. 10.
    Pérez-Sala, D., Bengoa, B., Martín-Requero, A., and Parrilla, R, Biochoem. J.242 (1987) 485.Google Scholar
  11. 11.
    Anderson, A., and Meister, A., Analyt. Biochem.183(1989) 16.PubMedGoogle Scholar
  12. 12.
    Berry, N. M., and Friend, D. S., J. Cell Biol.43 (1969) 506.PubMedGoogle Scholar
  13. 13.
    Zuurendonk, P. F., and Tager, J. M., Biochim. biophys. Acta333 (1974) 393.Google Scholar
  14. 14.
    Asensi, M., Sastre, J., Pallardó, F. V., García de la Asunción, J., Estrela, J. M., and Viña, J., Analyt. Biochem.217 (1994) 323.PubMedGoogle Scholar
  15. 15.
    Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J., J. biol. Chem.193 (1951) 265.PubMedGoogle Scholar
  16. 16.
    Bergmeyer, H. U., and Bernt, E., in: Methods of Enzymatic Analysis, p.574. Ed. H. U. Bermeyer, Verlag Chemie, Weinheim, and Academic Press Inc., New York and London 1974.Google Scholar
  17. 17.
    Estrela, J. M., Gil, F., Vila, J. M., and Viña, J., Am. J. Physiol.255 (1989) E801.Google Scholar
  18. 18.
    Viña, J. R., Palacín, M., Puertes, I. R., Hernández, R., and Viña, J., Am. Physiol.257 (1989) E916.Google Scholar
  19. 19.
    Deneke, S. M., and Famburg, B. L., Am. J. Physiol.257 1989) L163.PubMedGoogle Scholar
  20. 20.
    Griffiths, P. A., and Loyd, J. B., Biochem. biophys. Res. Commun.89 (1979) 428.PubMedGoogle Scholar
  21. 21.
    Boyland, E. L., and Chasseaud, L. F., Biochem. J.104 (1967) 95.PubMedGoogle Scholar
  22. 22.
    Meijer, A. J., Gimpel, J. A., Deleeuw, G., Tischler, M. E., Tager, J. M., and Willamson, J. R., J. biol. Chem.253 (1978) 2308.PubMedGoogle Scholar
  23. 23.
    Rongstd, R., and Katz, J., Biochem. J.116 (1970) 483.PubMedGoogle Scholar
  24. 24.
    Seglen, P. O., and Sollheim, A. E., Biochim. Biophys. Acta520 (1978) 630.PubMedGoogle Scholar
  25. 25.
    Poli, A., Gordon, P. B., Schwarze, P. E., Grinde, B., and Seglen, P. O., J. Cell Sci.48 (1981)1.PubMedGoogle Scholar
  26. 26.
    Tischer, M. E., Hecht, P., and Willamson, J. R., Archs Biochem. Biophys.181 (1977) 278.Google Scholar

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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