Activation of the apoptotic protease CPP32 by cytotoxic T-cell-derived granzyme B

Article Abstract:

Cytotoxic T lymphocyte (CTL)-regulated granzyme B cleavages and activates the ICE-like protease CPP32, initiating the cleavage of poly(ADP-ribose) polymerase and most likely other substrates as well. Recognition of an intracellular substrate for granzyme B provides a tool to establish the procedure of CTL-controlled cell death. Other sites inside the target cell can exist where cell-regulated immunity may be inhibited. Granzyme B initiates the fragmentation of DNA and apoptosis in target cells.

Cell-mediated cytotoxicity, Cell mediated cytotoxicity, T cells

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Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis

Article Abstract:

A new protease, apopin, appears responsible for poly(ADP-ribose) polymerase's proteolytic breakdown which is essential for the onset of apoptosis. Apopain is derived from CPP-32, a common proenzyme, and contains two subunits that have relative molecular masses of (Mr)17K and 12K. In vitro and in vivo apoptosis is prevented when the active form of the specific interleukin-1beta-converting (ICE)/CED-3-like cystine protease, CPP-32, is inhibited.

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Baiting death inhibitors

Article Abstract:

Issues are presented concerning the influence of enzymes names caspases in the programming of the death of cells. The physiological pathways which are involved in the death of cells are discussed.

Enzymes

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