ADP-Ribosylation: Approach to Molecular Basis of Aging

  • Paul Mandel
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 296)


About 25 years ago we observed1 that a liver nuclear extract is able to produce from NAD a polyadenosine polymer. Chemical and enzymatic degradation followed by methylatioh experiments lead us to conclude that the polymer synthesized was polyadenosine diphosphate ribose (polyADPR) (Fig. 1). We called the enzyme present in the nuclear extract polyADP-ribose polymerase (polyADP-R)P. The enzymatic activity was expressed only in the presence of DNA. The structure of the polymer was confirmed one year later by Nishizuka et al.2 and by Sugimura et al.3. We have also demonstrated the activity of the polymerase in vivo.4 A fundamental step in our understanding of the biological role of this enzyme was the demonstration of its capacity to produce a transfer of polyADPR to nuclear proteins and thus a post-translational modification similar to that already well established: phosphorylation, methylation and acetylation 5,6. Later oligo and mono ADPR transferases (ADPRT) were discovered in cytoplasm, in mitochondria7,8,9,10 in erythrocyte supernatant and in the plasma membrane12 as well as in ribonucleoprotein particles carrying messenger RNA13 (mRNP) (see also for review14,15,l6,17,l8). Procedures for the purification of the nuclear (polyADP-R)P from bovine thymus were developed in our laboratory19 and in others (see for review14), providing an enzyme clearly DNA-dependent.


Lens Epithelial Cell Bovine Lens Diphosphate Ribose Adenosine Diphosphate Ribose Glycohydrolase Activity 
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Copyright information

© Plenum Press, New York 1991

Authors and Affiliations

  • Paul Mandel
    • 1
  1. 1.Centre de Neurochimie du CNRSStrasbourg CedexFrance

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