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Apoptotic death sensor: an organelle's alter ego?
Author(s): Bratton SB, Cohen GM
Source: TRENDS IN PHARMACOLOGICAL SCIENCES    Volume: 22    Issue: 6    Pages: 306-315    Published: JUN 2001  
Times Cited: 104     References: 81     
Abstract: Caspases are intracellular cysteine proteases that are primarily responsible for the stereotypic morphological and biochemical changes that are associated with apoptosis. Caspases are often activated by the apoptotic protease-activating factor 1 (APAF-1) apoptosome. a complex that is formed following mitochondrial release of cytochrome cin response to many death-inducing stimuli. Both pro- and anti-apoptotic BCL-2 family members regulate apoptosis, primarily by their effects on mitochondria. whereas me ny inhibitor of apoptosis proteins (IAPs) regulate apoptosis by directly inhibiting distinct caspases. Exposure of cells to chemicals and radiation, as well as loss of trophic stimuli, perturb cellular homeostasis and, depending on the type of cellular stress, particular or multiple organelles appear to 'sense' the damage and signal the cell to undergo apoptosis by stimulating the formation of unique and/or common caspase-activating complexes.
Document Type: Review
Language: English
Reprint Address: Bratton, SB (reprint author), Univ Leicester, MRC, Toxicol Unit, Hodgkin Bldg,POB 138,Lancaster Rd, Leicester LE1 9HN, Leics England
Addresses:
1. Univ Leicester, MRC, Toxicol Unit, Leicester LE1 9HN, Leics England
Publisher: ELSEVIER SCIENCE LONDON, 84 THEOBALDS RD, LONDON WC1X 8RR, ENGLAND
Subject Category: Pharmacology & Pharmacy
IDS Number: 444BT
ISSN: 0165-6147
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