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Leukocyte Elastase Inhibitor

A New Regulator of PARP-1

Authors


Address for correspondence: Alicia Torriglia, Centre de Recherches des Cordeliers, UMRS 872 Eq. 17, 15, rue de l’Ecole de Médecine, 75006 Paris, France. Voice: +33-1-40-46-78-50; fax: +33-1-40-46-78-65. alicia.torriglia@inserm.fr or A. Ivana Scovassi, Istituto di Genetica Molecolare del CNR, Via Abbiategrasso 207, 27100 Pavia, Italy. Voice: +39-0382-546334; fax: +39-0382-422286. scovassi@igm.cnr.it

Abstract

Poly(ADP-ribose) polymerase-1 (PARP-1) uses NAD+ as a substrate to form ADP-ribose. During apoptosis, caspases cleave PARP-1 to avoid excessive NAD consumption. Because PARP-1 is a key regulator of the activity of DNases involved in caspase-dependent apoptosis, its cleavage is required to promote DNA degradation. To explore the situation in caspase-independent cell death, we investigated the effect of PARP-1 on the acid endonuclease leukocyte elastase inhibitor (LEI)–derived DNase II (L-DNase II). We found for the first time an association between PARP-1 and LEI/L-DNase II. Unexpectedly, we observed that LEI influenced the automodification of PARP-1.

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