Four deaths and a funeral: from caspases to alternative mechanisms.
A single family of proteases, the caspases, has long been considered the pivotal executioner of all programmed cell death. However, recent findings of evolutionarily conserved, caspase-independent controlled death mechanisms have opened new perspectives on the biology of cell demise, with particular implications for neurobiology, cancer research and immunological processes.
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H. Lundbeck A/S, Ottiliavej 9, DK-2500 Copenhagen-Valby, Denmark. male@lundbeck.dk
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D000818:Animals; D017209:Apoptosis / Q000187:drug effects / Q000502:physiology*; D017173:Caenorhabditis elegans / Q000502:physiology; D020169:Caspases / Q000502:physiology*; D002843:Chromatin / Q000648:ultrastructure; D015853:Cysteine Proteinase Inhibitors / Q000494:pharmacology; D004789:Enzyme Activation; D005057:Eukaryotic Cells / Q000166:cytology / Q000201:enzymology; D019143:Evolution, Molecular; D005656:Fungal Proteins / Q000502:physiology; D015801:Helminth Proteins / Q000502:physiology; D006801:Humans; D008928:Mitochondria / Q000502:physiology; D009336:Necrosis; D009369:Neoplasms / Q000473:pathology / Q000628:therapy; D009420:Nervous System / Q000166:cytology / Q000196:embryology / Q000254:growth & development; D018124:Receptors, Tumor Necrosis Factor / Q000502:physiology; D012441:Saccharomyces cerevisiae / Q000502:physiology; D015398:Signal Transduction; D019014:fas Receptor / Q000502:physiology
D002843:Chromatin; D015853:Cysteine Proteinase Inhibitors; D005656:Fungal Proteins; D015801:Helminth Proteins; D018124:Receptors, Tumor Necrosis Factor; D019014:fas Receptor; D020169:Caspases