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A Caspase‐Independent Cell Clearance Program: The LEI/L‐DNase II Pathway
Author(s) -
TORRIGLIA ALICIA,
PERANI PAOLO,
BROSSAS JEAN YVES,
ALTAIRAC SÉVERINE,
ZEGGAI SAMIA,
MARTIN ELISABETH,
TRÉTON JACQUES,
COURTOIS YVES,
COUNIS MARIEFRANCE
Publication year - 2000
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.1749-6632.2000.tb05612.x
Subject(s) - proteases , caspase , caspase 2 , endonuclease , apoptosis , serine protease , microbiology and biotechnology , protease , programmed cell death , cell , serine , biology , nlrp1 , chemistry , enzyme , biochemistry
A bstract : The discovery of caspase‐mitochondrial pathway counts as one of the most important discovery in apoptosis biochemistry. Today, however, we begin to recognize its limits. Inhibition of caspase does not prevent cell death in many mammalian models. Targeted disruption of caspases does not impair every type of apoptosis. Other pathways, caspase independent, are now described. Here we present one of these pathways. It is a serine‐protease dependent pathway and its key event is the transformation of LEI (a serine protease inhibitor) into L‐DNase II (an endonuclease). When using this apoptotic pathway the cell activates, at the same time, its endonuclease activity (L‐DNase II appears) and its protease activity (there is a release of inhibition of proteases).