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Magnitude and significance of NAD turnover in human cell line D98/AH2


IN the oxidation–reduction metabolism of a cell the pyridine nucleotide NAD is used catalytically; any NAD that is reduced is reoxidised. But NAD is consumed in certain metabolic reactions in which it serves as a substrate. In eukaryotic cells, the most intriguing of these reactions is the cleavage of NAD to form nicotinamide and a unique polymer, poly adenosine diphosphoribose (poly ADPR) (Fig. 1); the reaction is catalysed by the enzyme poly ADPR synthetase1–4. Other well studied reactions involving the destruction of NAD include the cleavage of NAD to form AMP and NMN by bacterial DNA ligases5,6 and the breakdown of NAD (with the concomitant inactivation of protein synthesis) by diphtheria toxin7,8.

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  1. Chambon, P., Weill, J., and Mandel, P., Biochem. biophys. Res. Commun., 11, 39–43 (1963).

    Article  CAS  Google Scholar 

  2. Chambon, P., Weill, J., Doly, J., Strosser, M., and Mandel, P., Biochem. biophys Res. Commun., 25, 634–643 (1966).

    Article  Google Scholar 

  3. Sugimura, T., Prog. Nucleic Acid Res. molec. Biol., 13, 127–151 (1973).

    Article  CAS  Google Scholar 

  4. Honjo, T., and Hayaishi, O., Curr. Top. cell. Reg., 7, 87–127 (1973).

    Article  CAS  Google Scholar 

  5. Olivera, B., and Lehman, I., Proc. natn. Acad. Sci. U.S.A., 57, 1426–1433 (1967).

    Article  ADS  CAS  Google Scholar 

  6. Zimmerman, S., Little, B., Oshinsky, J., and Gellert, C., Proc. natn. Acad. Sci. U.S.A., 57, 1841–1848 (1967).

    Article  ADS  CAS  Google Scholar 

  7. Collier, R., and Pappenheimer, A. M., J. exp. Med., 120, 1019–1039 (1964).

    Article  CAS  Google Scholar 

  8. Collier, R., J. molec. Biol., 25, 83–98 (1967).

    Article  CAS  Google Scholar 

  9. Matsuya, Y., and Green, H., Science, 163, 697–698 (1969).

    Article  ADS  CAS  Google Scholar 

  10. Rechsteiner, M., Hillyard, D., and Olivera, B., J. cell. Physiol., (in the press).

  11. Hillyard, D., Rechsteiner, M., and Olivera, B., J. cell. Physiol., 82, 165–179 (1973).

    Article  CAS  Google Scholar 

  12. Rechsteiner, M., and Catanzarite, V., J. cell. Physiol., 84, 409–422 (1974).

    Article  CAS  Google Scholar 

  13. Prescott, D., Myerson, D., and Wallace, J., Expl Cell. Res., 71, 480–485 (1971).

    Article  Google Scholar 

  14. Rechsteiner, M., Lund, K., Hillyard, D., and Olivera, B., J. cell. Physiol., 83, 389–400 (1974).

    Article  CAS  Google Scholar 

  15. Hogeboom, G., and Schneider, W., J. Biol. Chem., 197, 611–620 (1952).

    CAS  PubMed  Google Scholar 

  16. Siebert, G., and Humphrey, G., Adv. Enzymol., 21, 239–288 (1965).

    Google Scholar 

  17. Ueda, K., Reeder, R., Honjo, T., Nishizuka, Y., and Hayaishi, O., Biochem. biophys. Res. Commun., 31, 379–385 (1968).

    Article  CAS  Google Scholar 

  18. Smith, J., and Stocken, L., Biochem. biophys. Res. Commun., 54, 297–300 (1973).

    Article  CAS  Google Scholar 

  19. Shall, S., Brightwell, M., O'Farrell, M., Stone, P., and Whish, W., Z. physiol. Chem., 353, 846–847 (1972).

    Google Scholar 

  20. Futai, M., Mizuno, D., and Sugimara, T., J. biol. Chem., 243, 6325–6329 (1968).

    CAS  PubMed  Google Scholar 

  21. Miwa, M., and Sugimura, T., J. biol. Chem., 246, 6362–6364 (1971).

    CAS  PubMed  Google Scholar 

  22. Gholson, R. K., Nature, 212, 933–935 (1966).

    Article  ADS  CAS  Google Scholar 

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RECHSTEINER, M., HILLYARD, D. & OLIVERA, B. Magnitude and significance of NAD turnover in human cell line D98/AH2. Nature 259, 695–696 (1976).

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