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Göteborgs universitets publikationer

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

Författare och institution:
C Soldani (-); M C Lazzè (-); M G Bottone (-); Gianluca Tognon (Institutionen för invärtesmedicin); M Biggiogera (-); C E Pellicciari (-); A I Scovassi (-)
Publicerad i:
Experimental cell research, 269 ( 2 ) s. 193-201
Artikel, refereegranskad vetenskaplig
Sammanfattning (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.
Ämne (baseras på Högskoleverkets indelning av forskningsämnen):
Medicinska grundvetenskaper ->
Cell- och molekylärbiologi
Apoptosis, Blotting, Western, Cell Line, Cell Nucleus, metabolism, Cytoplasm, metabolism, DNA Repair, Dactinomycin, pharmacology, Enzyme Activation, Flow Cytometry, Fluorescein-5-isothiocyanate, metabolism, Humans, Immunohistochemistry, Indicators and Reagents, pharmacology, Microscopy, Confocal, Microscopy, Fluorescence, Phosphatidylserines, chemistry, Poly(ADP-ribose) Polymerases, metabolism, Propidium, pharmacology, Protein Binding, Protein Synthesis Inhibitors, pharmacology, Time Factors, Tumor Cells, Cultured
Postens nummer:
Posten skapad:
2013-01-17 16:03

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