Poly(ADP-ribose) degradation by post-nuclear extracts from human cells

Laura Rossi, Marco Denegri, Mauro Torti, Guy G. Poirier, A. Ivana Scovassi

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

The nuclear metabolism of poly(ADP-ribose) is mainly regulated by poly(ADP-ribose) polymerase-1 (PARP-1) and by poly(ADP-ribose) glycohydrolase (PARG). A PARP-like enzyme, V-PARP, and a PARC isoform are present in the extra-nuclear compartment of mammalian cells, even if poly(ADP-ribose) has never been detected therein. In this work, we demonstrate the ability of post-nuclear extracts from HeLa and HL60 cells to degrade synthetic 32P-polymers of ADP-ribose to ADP-ribose and, further, to AMP. This reaction implies the combined action of PARG and of an ADP-ribose-degrading activity, possibly corresponding to a phosphodiesterase and/or to an ADP-ribose pyrophosphatase. The inhibition of PARG or ADP-ribose-degrading enzymes allowed the demonstration that in vitro synthesized 32P-poly(ADP-ribose) is first digested to ADP-ribose monomers by a typical PARG reaction, and that ADP-ribose is further rapidly converted into AMP by an Mg2+-dependent activity. Collectively, our results demonstrate the ability of the human cell post-nuclear fraction to convert synthetic poly (ADP-ribose) into utilizable AMP units by the concerted action of PARG and ADP-ribose-degrading activities.

Original languageEnglish
Pages (from-to)1229-1235
Number of pages7
JournalBiochimie
Volume84
Issue number12
Publication statusPublished - Dec 1 2002

Fingerprint

Adenosine Diphosphate Ribose
Poly Adenosine Diphosphate Ribose
Cell Extracts
Cells
Degradation
Adenosine Monophosphate
Pyrophosphatases
Poly(ADP-ribose) Polymerases
HL-60 Cells
Phosphoric Diester Hydrolases
Enzymes
HeLa Cells
Metabolism
Polymers
Protein Isoforms
Demonstrations
Monomers
poly ADP-ribose glycohydrolase

Keywords

  • (ADP-ribose) pyrophosphatase
  • Phosphodiesterase
  • Poly(ADP-ribose) glycohydrolase (PARG)
  • Poly(ADP-ribosylation)

ASJC Scopus subject areas

  • Biochemistry

Cite this

Rossi, L., Denegri, M., Torti, M., Poirier, G. G., & Scovassi, A. I. (2002). Poly(ADP-ribose) degradation by post-nuclear extracts from human cells. Biochimie, 84(12), 1229-1235.

Poly(ADP-ribose) degradation by post-nuclear extracts from human cells. / Rossi, Laura; Denegri, Marco; Torti, Mauro; Poirier, Guy G.; Scovassi, A. Ivana.

In: Biochimie, Vol. 84, No. 12, 01.12.2002, p. 1229-1235.

Research output: Contribution to journalArticle

Rossi, L, Denegri, M, Torti, M, Poirier, GG & Scovassi, AI 2002, 'Poly(ADP-ribose) degradation by post-nuclear extracts from human cells', Biochimie, vol. 84, no. 12, pp. 1229-1235.
Rossi L, Denegri M, Torti M, Poirier GG, Scovassi AI. Poly(ADP-ribose) degradation by post-nuclear extracts from human cells. Biochimie. 2002 Dec 1;84(12):1229-1235.
Rossi, Laura ; Denegri, Marco ; Torti, Mauro ; Poirier, Guy G. ; Scovassi, A. Ivana. / Poly(ADP-ribose) degradation by post-nuclear extracts from human cells. In: Biochimie. 2002 ; Vol. 84, No. 12. pp. 1229-1235.
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