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Apoptosis and Caspase-8, Rate My Science

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Uploaded on Oct 10, 2008

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Caspase 8 is member of the cysteine-aspartic acid protease (caspase) family. The NH2-terminal region of caspase-8 contains two death effector domains (DEDs), through which it binds the DED of Fas-associated death domain (FADD). The COOH-terminal region of caspase-8 is related to the interleukin-1beta converting enzyme (ICE) family of proteases. FADD mediates the recruitment of caspase-8 to tumor necrosis factor receptor 1 (TNF-R1), where caspase-8 becomes activated, presumably by self-cleavage, and in turn initiates a proteolytic cascade that ultimately leads to apoptosis.

Two important examples of the direct initiation of apoptotic mechanisms in mammals include the TNF-induced (tumour necrosis factor) model and the Fas-Fas ligand-mediated model, both involving receptors of the TNF receptor (TNFR) family coupled to extrinsic signals. TNF is a cytokine produced mainly by activated macrophages, and is the major extrinsic mediator of apoptosis. Most cells in the human body have two receptors for TNF: TNF-R1 and TNF-R2. The binding of TNF to TNF-R1 has been shown to initiate the pathway that leads to caspase activation via the intermediate membrane proteins TNF receptor-associated death domain (TRADD) and Fas-associated death domain protein (FADD).
Design & production: Kosi Gramatikoff, PhD and John C. Reed, MD PhD

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