IMR Press / FBL / Volume 14 / Issue 13 / DOI: 10.2741/3572

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Article
LEI/L-DNase II: interplay between caspase-dependent and independent pathways
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1 Universite Pierre et Marie Curie - Paris 6, Paris, F-75006, France
2 Universite Paris Descartes - Paris 5, Paris, F-75006, France
3 INSERM, Centre de Recherches des Cordeliers, UMR S 872, Paris, F-75006, France

Academic Editor: Catherine Brenner

Front. Biosci. (Landmark Ed) 2009, 14(13), 4836–4847; https://doi.org/10.2741/3572
Published: 1 June 2009
(This article belongs to the Special Issue Apoptosis and mitochondria)
Abstract

Caspase activation has been seen, for several years, as the biochemical marker of apoptosis. However, in 2005 the Nomenclature Committee on Cell Death (NCCD) established that the 'official' classification of cell death had to rely on morphological criteria owing to the absence of a clear-cut equivalence between structural alterations and biochemical pathways. Actually, the controlled destruction of the cell is coordinated by a proteolytic system involving caspases but also other proteases like cathepsins, calpains and serine proteases. These enzymes participate in an activation cascade that culminates in cleavage of a set of proteins resulting in disassembly of the cell. This disassembling also includes the activation of endonucleases that will destroy a potentially harmful DNA. A caspase-activated DNase performs DNA degradation in caspase-dependent apoptosis, but other endonucleases like L-DNase II or GAAD are activated in caspase-independent apoptosis, allowing the complete dismantling of the cell.

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