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Leukocyte Elastase Inhibitor
Author(s) -
Leprêtre Chloé,
Sidoli Giuseppina,
Scovassi A. Ivana,
Torriglia Alicia
Publication year - 2009
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.2009.04701.x
Subject(s) - poly adp ribose polymerase , nad+ kinase , apoptosis , chemistry , caspase , parp inhibitor , endonuclease , polymerase , cleavage (geology) , microbiology and biotechnology , programmed cell death , biochemistry , enzyme , biology , paleontology , fracture (geology)
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.