| Roles of caspases in the programmed cell death of motoneurons in vivo. | |
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MedLine Citation:
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PMID: 11838706 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Cysteine proteases comprising the caspase family have been considered one of the major executioners of programmed cell death. However, detailed analyses of the programmed cell death of developing motoneurons in mice following the genetic deletion of two key caspases, casp-3 and casp-9, and in the chick embryo following treatment with caspase inhibitors, indicate that normal amounts of cell loss occur although the death process is delayed. Motoneurons undergoing programmed cell death without caspase activities exhibit a nonapoptotic morphology in which nuclear changes such as chromatin condensation are absent or reduced and which exhibit extensive cytoplasmic vacuolization such as is rarely observed in degenerating control neurons. These results suggest that caspases are involved in, but are not indispensable for, the developmental death of motoneurons, and that one function of caspases may be to facilitate the removal of cells that are destined to die. Possible alternative caspase-independent pathways for the programmed death of motoneurons are discussed. |
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Authors:
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H Yaginuma; N Sato; S Homma; R W Oppenheim |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Review |
Journal Detail:
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Title: Archives of histology and cytology Volume: 64 ISSN: 0914-9465 ISO Abbreviation: Arch. Histol. Cytol. Publication Date: 2001 Dec |
Date Detail:
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Created Date: 2002-02-12 Completed Date: 2002-08-21 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 8806082 Medline TA: Arch Histol Cytol Country: Japan |
Other Details:
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Languages: eng Pagination: 461-74 Citation Subset: IM |
Affiliation:
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Department of Anatomy, School of Medicine, Fukushima Medical University, Japan. h-yaginm@fmu.ac.jp |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Apoptosis / physiology* Apoptosis Inducing Factor Autophagy / physiology Caspase 3 Caspase 9 Caspases / physiology* Chick Embryo Cytoskeletal Proteins / metabolism Flavoproteins / metabolism Kinetics Membrane Proteins / metabolism Mice Mice, Knockout Motor Neurons / physiology* Oligopeptides / chemistry* Signal Transduction |
| Chemical | |
Reg. No./Substance:
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0/Apoptosis Inducing Factor; 0/Cytoskeletal Proteins; 0/Flavoproteins; 0/Membrane Proteins; 0/Oligopeptides; 0/Pdcd8 protein, mouse; 0/acetyl-aspartyl-glutamyl-valyl-aspartal; EC 3.4.22.-/Casp3 protein, mouse; EC 3.4.22.-/Casp9 protein, mouse; EC 3.4.22.-/Caspase 3; EC 3.4.22.-/Caspase 9; EC 3.4.22.-/Caspases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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