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| Apoptotic death sensor: an organelle's alter ego? |
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| 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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| |  |  |  |  | | | | Record from Web of Science® | |  |  | | | | | | |