Abstract:
:The discovery of caspase activation counts as one of the most important finds in the biochemistry of apoptosis. However, targeted disruption of caspases does not impair every type of apoptosis. Other proteases can replace caspases and several so called "caspase independent" pathways are now described. Here we review our current knowledge on one of these pathways, the LEI/L-DNase II. It is a serine protease-dependent pathway and its key event is the transformation of LEI (leukocyte elastase inhibitor, a serine protease inhibitor) into L-DNase II (an endonuclease). The molecular events leading to this change of enzymatic function as well as the cross-talk and interactions of this molecule with other apoptotic pathway, including caspases, are discussed.
journal_name
Biochem Pharmacoljournal_title
Biochemical pharmacologyauthors
Torriglia A,Leprêtre C,Padrón-Barthe L,Chahory S,Martin Edoi
10.1016/j.bcp.2008.07.039subject
Has Abstractpub_date
2008-12-01 00:00:00pages
1490-502issue
11eissn
0006-2952issn
1873-2968pii
S0006-2952(08)00502-9journal_volume
76pub_type
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