http://www.cnr.it/ontology/cnr/individuo/prodotto/ID27668
Leukocyte Elastase Inhibitor: a new regulator of PARP-1. (Articolo in rivista)
- Type
- Label
- Leukocyte Elastase Inhibitor: a new regulator of PARP-1. (Articolo in rivista) (literal)
- Anno
- 2009-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1111/j.1749-6632.2009.04701 (literal)
- Alternative label
Lepretre C, Sidoli G, Scovassi AI, Torriglia A. (2009)
Leukocyte Elastase Inhibitor: a new regulator of PARP-1.
in Annals of the New York Academy of Sciences
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Lepretre C, Sidoli G, Scovassi AI, Torriglia A. (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Note
- Scopus (literal)
- ISI Web of Science (WOS) (literal)
- PubMe (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- IGM, INSERM, Parigi, Francia (literal)
- Titolo
- Leukocyte Elastase Inhibitor: a new regulator of PARP-1. (literal)
- Abstract
- Poly(ADP-ribose) polymerase-1 (PARP-1) is an important regulator of apoptosis. Its over-activation at the onset of apoptosis can inhibit the action of apoptotic endonucleases like Caspase-activated DNase and DNAS1L3. Therefore, controlled PARP-1 proteolysis during caspase-dependent apoptosis is considered essential to promote DNA degradation. Yet, little is known about the interplay of PARP-1 and endonucleases that operate during caspase-independent cell death. Here we show that in the long-term cultured HeLa cells which undergo caspase-independent death, PARP-1 co-immunoprecipitates with Leukocyte Elastase Inhibitor-derived DNase II (L-DNaseII), an acid DNase implicated in this death pathway and activated by serine proteases. Our results indicate that, despite having putative poly(ADP-ribose)-acceptor sites, LEI/L-DNase II is neither significantly poly(ADP-ribosyl)ated nor inhibited by PARP-1 during caspase-independent apoptosis. Unexpectedly, caspase-independent apoptosis induced by Hexa-methylene amiloride, LEI/L-DNase II can activate PARP-1 and promote its auto-poly(ADP-ribosyl)ation, thus inhibiting PARP-1 activity. Moreover, overexpression of LEI blocks the pro-survival effect of PARP-1 in this model of cell death. Our results provide the original evidence for a new mechanism of PARP-1 activity regulation in the caspase-independent death pathway involving LEI/L-DNase II. (literal)
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