Essential contribution of caspase 3/CPP32 to apoptosis and its associated nuclear changes
Article Abstract:
Caspase 3, or CPP32, is necessary for programmed cell death, apoptosis, and associated changes in the nucleus. It is very stimulus- and system-dependent. If CPP32 is inactivated, apoptosis in various settings has been shown to be greatly reduced. One such setting is inactivation-induced cell death of peripheral T cells, another apoptosis brought on by chemotherapy of oncogenically transformed CPP32-/- mouse embryonic fibroblasts (MEFs). In some settings, CPP32 is necessary for some apoptotic events and not others. Drugs that oppose CPP32 action may work against certain kinds of cell death preferentially.
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 1998
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Apaf1 is required for mitochondrial pathways of apoptosis and brain development
Article Abstract:
Apaf1 is a key element in the mitochondrial pathways of programmed cell death induced in response to a wide range of apoptotic stimuli. However, Fas-mediated programmed cell death in thymocytes and activated T cells is not linked with Apaf1. It has not been possible to prove a link between Casp2 and Apaf1, but Casp2 could also be a downstream effector of Apaf1. It appears that other CED-4/Apaf1-like molecules exist. Research on this subject may give more information about mitochondrial pathways of programmed cell death.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1998
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Negative regulation of PKB/Akt-dependent cell survival by the tumor suppressor PTEN
Article Abstract:
The role of the PTEN tumor suppressor gene was investigated to correlate it with normal cell development and tumorigenesis. The N-terminal domain of PTEN has extensive homology to tensin which is a protein related with the actin cytoskeleton. Also, PTEN has the ability to dephosphorylate position D of phosphatidylinositol (3,4,5) triphosphate. Results revealed that overexpression of the mPTEN gene in transgenic mice induced the suppressed apoptotic function of protein kinase B/Akt and regulated basic cellular processes.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1998
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