<h2>Cross-Talk in Cell Death Signaling</h2> Sophie Roy a Merck Frosst Centre for Therapeutic Research, Merck Research Laboratories, P.O. Box 1005, Pointe Claire-Dorval, Quebec H9R 4P8, Canada. Fax: 514-428-4900 Phone: 514-428-8544 and Donald W. Nicholson a a Merck Frosst Centre for Therapeutic Research, Merck Research Laboratories, Pointe Claire-Dorval, Quebec H9R 4P8, Canada Apoptotic cell suicide can be initiated by a plethora of stimuli that generally feed into one of two known cell death signaling pathways ( Fig. 1 ; for review see references ( 1 ) and ( 2 )). Both pathways share many features, including molecular devices that spark caspase activation by proenzyme recruitment, oligomerization, and proximity-induced autocatalytic activation. Beyond this, however, their activities are relatively (but not absolutely) distinct. The ‘intrinsic’ pathway feeds cell death signals through the mitochondrion, which appears to act as a generic damage sensor and monitor of metabolic status. With the assistance of cytochrome c , cell death is initiated by the formation of a macromolecular complex (the apoptosome), which utilizes apoptotic protease activating factor (APAF)-1 to mediate the activation of caspase-9. The ‘extrinsic’ pathway transduces the signals of extracellular ‘death ligands’ belonging to the TNF superfamily (e.g., TNF-α, Fas ligand [FasL]/Apo1L/CD95L, Trail/Apo2L,
The Journal of Experimental Medicine – Rockefeller University Press
Published: Oct 16, 2000
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