Programmed cell death: many ways for cells to die decently.
Apoptosis, a cell death programme mediated by the caspase family of cysteine proteases, is essential for appropriate removal of excess cells in many developmental and physiological settings. It would, however, be very dangerous for the organism to depend on a single protease family for clearance of unwanted and potentially dangerous cells. Indeed, the exclusive role of caspases in the execution of programmed cell death (PCD) has been challenged recently, and the understanding of the molecular control of alternative death pathways is emerging. Here, I review recently discovered triggers and molecular regulators of caspase-independent cell death programmes and discuss their potential as therapeutic targets for the treatment of cancer.
Jäättelä
Marja
M
Apoptosis Laboratory, Institute of Cancer Biology, Danish Cancer Society, Strandhoulevarden 49, DK-2100 Copenhagen, Denmark. mhj@biobase.dk
D017209:Apoptosis / Q000502:physiology*; D051033:Apoptosis Inducing Factor; D020169:Caspases / Q000502:physiology*; D002403:Cathepsins / Q000502:physiology; D003546:Cysteine Endopeptidases / Q000502:physiology; D005420:Flavoproteins / Q000502:physiology; D006801:Humans; D008565:Membrane Proteins / Q000502:physiology; D008928:Mitochondria / Q000502:physiology; D019253:Proto-Oncogene Proteins c-bcl-2; D018160:Receptors, Cytoplasmic and Nuclear / Q000502:physiology; D012697:Serine Endopeptidases / Q000502:physiology; D015398:Signal Transduction / Q000502:physiology
C494829:AIFM1 protein, human; D051033:Apoptosis Inducing Factor; D005420:Flavoproteins; D008565:Membrane Proteins; D019253:Proto-Oncogene Proteins c-bcl-2; D018160:Receptors, Cytoplasmic and Nuclear; D002403:Cathepsins; D012697:Serine Endopeptidases; D020169:Caspases; D003546:Cysteine Endopeptidases