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

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 PARG 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 Mg(2+)-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.

journal_name

Biochimie

journal_title

Biochimie

authors

Rossi L,Denegri M,Torti M,Poirier GG,Ivana Scovassi A

doi

10.1016/s0300-9084(02)00017-2

keywords:

subject

Has Abstract

pub_date

2002-12-01 00:00:00

pages

1229-35

issue

12

eissn

0300-9084

issn

1638-6183

pii

S0300908402000172

journal_volume

84

pub_type

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