Abstract
NAD is a coenzyme required for the oxidation-reduction reaction in respiratory chain as well as the substrate for cellular ADP-ribosylation reactions (1-3). Pyridine nucleotide metabolism plays an important role in regulating cell growth through ATP synthesis. Regulating mechanisms of cellular NAD levels have not been clarified. The depletion of cellular NAD levels and activation of poly(ADP-ribose) polymerase after the treatment of DNA damaging agents in vitro and in vivo is well known (4,5). Many data suggest that poly(ADP-ribosyl)ation of nuclear proteins play an important role in DNA repair processes. Mono ADP-ribosyl transferase in cytoplasm might be involved in regulation of activation of G regulatory proteins (6). Thus various proteins within nuclei and cytoplasm should interact with NAD and regulate a wide variety of cellular functions.
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Miwa, M., Uchida, M., Akiyama, T., Uchida, K. (1992). Detection and Analysis of NAD Binding Proteins Including Poly(ADP-Ribose) Polymerase Immobilized on the Membrane. In: Poirier, G.G., Moreau, P. (eds) ADP-Ribosylation Reactions. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-8718-1_20
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DOI: https://doi.org/10.1007/978-1-4419-8718-1_20
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