Apoptosis is a cell death process generally described as involving a cascade of caspase activation， death receptors and/or pro- and antiapoptotic molecules from the BcL-2 family. But about 20 years ago， a caspase-independent apoptotic pathway has been described. Regarding this pathway， we can learn a lot from parasites. Indeed， these parasitic protozoa enter， in response to different stimuli， in a form of cell death phenotypically similar to mammalian apoptosis but without involving caspases or death receptors. So far， only two proteins have been clearly identified as being involved in -regulated cell death: the metacaspase and the endonuclease G. We report here the identification of a new protei... More
Apoptosis is a cell death process generally described as involving a cascade of caspase activation， death receptors and/or pro- and antiapoptotic molecules from the BcL-2 family. But about 20 years ago， a caspase-independent apoptotic pathway has been described. Regarding this pathway， we can learn a lot from parasites. Indeed， these parasitic protozoa enter， in response to different stimuli， in a form of cell death phenotypically similar to mammalian apoptosis but without involving caspases or death receptors. So far， only two proteins have been clearly identified as being involved in -regulated cell death: the metacaspase and the endonuclease G. We report here the identification of a new protein modeled as a potential hydrolase， highly conserved among species and absent in the very close parasite . This protein is involved in -regulated cell death induced by curcumin， miltefosine and pentamidine， after gene overexpression and/or protein translocation to the nucleus. The identification of proteins involved in -regulated cell death will provide a better understanding of nonconventional apoptotic pathways in higher eukaryotes. It will also allow the development of new therapeutic tools via the identification of new specific targets.
