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Issue 926 coverMECHANISMS OF CELL DEATH II: THE THIRD ANNUAL CONFERENCE OF THE INTERNATIONAL CELL DEATH SOCIETY Copyright © 2000 by the New York Academy of Sciences
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Annals of the New York Academy of Sciences 926:192-203 (2000)
© 2000 New York Academy of Sciences

A Caspase-Independent Cell Clearance Program: The LEI/L-DNase II Pathway

ALICIA TORRIGLIAa, PAOLO PERANI, JEAN YVES BROSSAS, SÉVERINE ALTAIRAC, SAMIA ZEGGAI, ELISABETH MARTIN, JACQUES TRÉTON, YVES COURTOIS AND MARIE-FRANCE COUNIS

Unité 450 INSERM, Association Claude Bernard, 75016 Paris, France

aAddress for correspondence : Dr. Alicia Torriglia, U 450 INSERM, 29, rue Wilhem, 75016 Paris, France. Voice: 33 (1) 45 25 21 93; fax: 33 (1)40 50 01 95.
torrigli{at}infobiogen.fr

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).

Key Words: Caspases • Apoptosis • Proteases • LEI • L-DNase II




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