, Volume 7, Issue 4, pp 321–328

Poly(ADP-ribose) polymerase-1 cleavage during apoptosis: An update

  • C. Soldani
  • A. I. Scovassi

DOI: 10.1023/A:1016119328968

Cite this article as:
Soldani, C. & Scovassi, A.I. Apoptosis (2002) 7: 321. doi:10.1023/A:1016119328968


Poly(ADP-ribosylation) is a post-translational modification of proteins playing a crucial role in many processes, including DNA repair and cell death. The best known poly(ADP-ribosylating) enzime, PARP-1, is a DNA nick sensor and uses βNAD+ to form polymers of ADP-ribose which are further bound to nuclear protein acceptors. To strictly regulate poly(ADP-ribose) turnover, its degradation is assured by the enzyme poly(ADP-ribose) glycohydrolase (PARG). During apoptosis, PARP-1 plays two opposite roles: its stimulation leads to poly(ADP-ribose) synthesis, whereas caspases cause PARP-1 cleavage and inactivation. PARP-1 proteolysis produces an 89 kDa C-terminal fragment, with a reduced catalytic activity, and a 24 kDa N-terminal peptide, which retains the DNA binding domains. The fate and the possible role of these fragments during apoptosis will be discussed.

apoptosis autoimmunity caspases PARP-1 

Copyright information

© Kluwer Academic Publishers 2002

Authors and Affiliations

  • C. Soldani
    • 1
  • A. I. Scovassi
    • 2
  1. 1.Dipartimento di Biologia AnimaleUniversity of PaviaPiazza Botta 10Italy
  2. 2.Istituto di Genetica Molecolare CNRPaviaItaly

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