A caspase-independent cell clearance program. The LEI/L-DNase II pathway.
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).
Torriglia
A
A
Unité 450 INSERM, Association Claude Bernard, 75016 Paris, France. torrigli@infobiogen.fr
Perani
P
P
Brossas
J Y
JY
Altairac
S
S
Zeggai
S
S
Martin
E
E
Tréton
J
J
Courtois
Y
Y
Counis
M F
MF
D000818:Animals; D017209:Apoptosis / Q000235:genetics / Q000502:physiology*; D020169:Caspases / Q000378:metabolism; D004706:Endodeoxyribonucleases / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D011499:Protein Processing, Post-Translational; D012697:Serine Endopeptidases / Q000378:metabolism; D015842:Serine Proteinase Inhibitors / Q000737:chemistry / Q000378:metabolism*; D015843:Serpins / Q000737:chemistry / Q000378:metabolism*; D015398:Signal Transduction
D015842:Serine Proteinase Inhibitors; D015843:Serpins; D004706:Endodeoxyribonucleases; C019329:deoxyribonuclease II; D012697:Serine Endopeptidases; D020169:Caspases