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

Apoptosis. 2002 Aug;7(4):321-8. 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) enzyme, PARP-1, is a DNA nick sensor and uses betaNAD(+) 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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Apoptosis / physiology*
  • Autoimmune Diseases / etiology
  • Autoimmune Diseases / metabolism
  • Autoimmune Diseases / pathology
  • DNA Repair / physiology
  • Mice
  • Necrosis
  • Peptide Hydrolases / metabolism*
  • Poly(ADP-ribose) Polymerases / metabolism*


  • Poly(ADP-ribose) Polymerases
  • Peptide Hydrolases