Poly(ADP-ribose) polymerase cleavage during apoptosis: when and where? (Articolo in rivista)

Type
Label
  • Poly(ADP-ribose) polymerase cleavage during apoptosis: when and where? (Articolo in rivista) (literal)
Anno
  • 2001-01-01T00:00:00+01:00 (literal)
Alternative label
  • Soldani C, Lazze MC, Bottone MG, Tognon G, Biggiogera M, Pellicciari CE, Scovassi AI. (2001)
    Poly(ADP-ribose) polymerase cleavage during apoptosis: when and where?
    in Experimental cell research
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Soldani C, Lazze MC, Bottone MG, Tognon G, Biggiogera M, Pellicciari CE, Scovassi AI. (literal)
Pagina inizio
  • 193 (literal)
Pagina fine
  • 201 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 269 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • IGM; UNIPV (literal)
Titolo
  • Poly(ADP-ribose) polymerase cleavage during apoptosis: when and where? (literal)
Abstract
  • Poly(ADP-ribose) polymerase-1 (PARP-1) plays the active role of \"nick sensor\" during DNA repair and apoptosis, when it synthesizes ADP-ribose from NAD(+) in the presence of DNA strand breaks. Moreover, PARP-1 becomes a target of apoptotic caspases, which originate two proteolytic fragments of 89 and 24 kDa. The precise relationship between PARP-1 activation and degradation during apoptosis is still a matter of debate. In human Hep-2 cells driven to apoptosis by actinomycin D, we have monitored PARP-1 activity by the mAb 10H, which is specific for the ADP-ribose polymers, and we have observed that poly(ADP-ribose) synthesis is a very early response to the apoptotic stimulus. The analysis of the presence and fate of the p89 proteolytic fragment revealed that PARP-1 proteolysis by caspases is concomitant with poly(ADP-ribose) synthesis and that p89 migrates from the nucleus into the cytoplasm in late apoptotic cells with advanced nuclear fragmentation. Copyright 2001 Academic Press. (literal)
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