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Caspase Cascade

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Description

Caspases are a family of cysteine proteases that act in concert in a cascade triggered by apoptosis signaling. The culmination of this cascade is the cleavage of a number of proteins in the cell, followed by cell disassembly, cell death, and, ultimately, the phagocytosis and removal of the cell debris. The Caspase cascade is activated by two distinct routes: one from cell surface and the other from mitochondria (Ref.1). The pathway leading to Caspase activation varies according to the apoptotic stimulus. Initiator Caspases (including 8, 9, 10 and 12) are closely coupled to pro-apototic signals. Pro-apoptotic stimuli include the FasL (Fas Ligand), TNF (Tumor Necrosis Factor), Granzyme-B, GRB (Growth Factor Receptor-Bound Protein), DNA damage, Ca2+ (Calcium) channels and ER (Endoplasmic [...]

References:

1.Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization.
Srinivasula SM, Ahmad M, Fernandes-Alnemri T, Alnemri ES.
Mol Cell. 1998 Jun;1(7):949-57.
2.Mitomycin C induces apoptosis and caspase-8 and -9 processing through a caspase-3 and Fas-independent pathway.
Pirnia F, Schneider E, Betticher DC, Borner MM.
Cell Death Differ. 2002 Sep;9(9):905-14.
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