| Early processing of Bid and caspase-6, -8, -10, -14 in the canine brain during cardiac arrest and resuscitation. | |
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MedLine Citation:
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PMID: 15380478 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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A clinically relevant model of transient global brain ischemia involving cardiac arrest followed by resuscitation in dogs was utilized to study the expression and proteolytic processing of apoptosis-regulatory proteins. In the hippocampus, an increase in pro-apoptotic Bcl-2 family proteins Bcl-XS and Bak was detected, concomitant with proteolysis of Bcl-XL and Bcl-2, following ischemia-reperfusion injury. Also, biphasic cleavage of Bid was found in this region of the brain, with early generation of tBid-p11 within 10 min of cardiac arrest, followed by generation of tBid-p15 within 30-min reperfusion, consistent with activation of this pro-apoptotic protein. In addition, cardiac arrest and resuscitation induced early, reperfusion-dependent proteolytic processing of pro-caspase-6, -8, -10, and -14, which preceded caspase-3 activation. Immunohistochemical analysis using antibodies, which preferentially recognize processed caspase-3, -6, -8, and -10, provided evidence of time-dependent activation of these proteases in both neurons and glia in ischemia-sensitive regions of the brain. In conclusion, extremely rapid, cell-selective processing of apoptosis-regulatory proteins occurs in a clinically relevant model of ischemic brain injury caused by cardiac arrest and resuscitation. The early cleavage of Bid and rapid depletion of 32-kDa pro-caspase-14 from the canine hippocampus after induction of ischemia suggests the involvement of calpains in the processing of these proteins. Demonstration of in vitro cleavage of recombinant mouse caspase-14 by calpain I in the present study lends support to this hypothesis, further implicating cross-talk between different protease families in the pathophysiology of ischemic neural cell death. |
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Authors:
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Maryla Krajewska; Robert E Rosenthal; Jowita Mikolajczyk; Henning R Stennicke; Thomas Wiesenthal; Juergen Mai; Mikihiko Naito; Guy S Salvesen; John C Reed; Gary Fiskum; Stan Krajewski |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Experimental neurology Volume: 189 ISSN: 0014-4886 ISO Abbreviation: Exp. Neurol. Publication Date: 2004 Oct |
Date Detail:
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Created Date: 2004-09-21 Completed Date: 2004-10-28 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 0370712 Medline TA: Exp Neurol Country: United States |
Other Details:
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Languages: eng Pagination: 261-79 Citation Subset: IM |
Affiliation:
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The Burnham Institute, La Jolla, CA 92037, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Apoptosis / physiology* BH3 Interacting Domain Death Agonist Protein Brain Ischemia / enzymology*, physiopathology Calpain / metabolism Carrier Proteins / metabolism* Caspase 14 Caspases / metabolism* Disease Models, Animal Dogs Female Heart Arrest, Induced Hippocampus / enzymology*, physiopathology Membrane Proteins / metabolism Nerve Degeneration / enzymology, physiopathology Proto-Oncogene Proteins c-bcl-2 / metabolism Reaction Time / physiology Reperfusion Injury / enzymology*, physiopathology Resuscitation bcl-2 Homologous Antagonist-Killer Protein bcl-X Protein |
| Grant Support | |
ID/Acronym/Agency:
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NS34152/NS/NINDS NIH HHS; NS36821/NS/NINDS NIH HHS; NS37878/NS/NINDS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/BH3 Interacting Domain Death Agonist Protein; 0/Carrier Proteins; 0/Membrane Proteins; 0/Proto-Oncogene Proteins c-bcl-2; 0/bcl-2 Homologous Antagonist-Killer Protein; 0/bcl-X Protein; EC 3.4.22.-/Calpain; EC 3.4.22.-/Casp14 protein, mouse; EC 3.4.22.-/Caspase 14; EC 3.4.22.-/Caspases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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