Document Detail


Apoptosis caused by cathepsins does not require Bid signaling in an in vivo model of progressive myoclonus epilepsy (EPM1).
MedLine Citation:
PMID:  12934064     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Apoptosis can be mediated by mechanisms other than the traditional caspase-mediated cleavage cascade. There is growing recognition that alternative proteolytic enzymes such as the lysosomal cathepsin proteases can initiate or propagate proapoptotic signals, but it is currently unclear how cathepsins achieve these actions. Recent in vitro evidence suggests that cathepsins cleave the proapoptotic Bcl-2 family member Bid, thereby activating it and allowing it to induce the mitochondrial release of cytochrome c and subsequent apoptosis. We have tested this hypothesis in vivo by breeding mice that lack cathepsin inhibition (cystatin B-deficient mice) to Bid-deficient mice, to determine whether the apoptosis caused by cathepsins is dependent on Bid signaling. We found that cathepsins are still able to promote apoptosis even in the absence of Bid, indicating that these proteases mediate apoptosis via a different pathway, or that some other molecule can functionally substitute for Bid in this system.
Authors:
M K Houseweart; A Vilaythong; X-M Yin; B Turk; J L Noebels; R M Myers
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Cell death and differentiation     Volume:  10     ISSN:  1350-9047     ISO Abbreviation:  Cell Death Differ.     Publication Date:  2003 Dec 
Date Detail:
Created Date:  2003-11-19     Completed Date:  2004-07-13     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  9437445     Medline TA:  Cell Death Differ     Country:  England    
Other Details:
Languages:  eng     Pagination:  1329-35     Citation Subset:  IM    
Affiliation:
Department of Genetics, School of Medicine, Stanford University, 300 Pasteur Drive, Stanford, CA 94305-5120, USA.
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MeSH Terms
Descriptor/Qualifier:
Age Factors
Animals
Apoptosis*
Ataxia
BH3 Interacting Domain Death Agonist Protein
Blotting, Western
Carrier Proteins / metabolism*
Cathepsins / metabolism*
Cell Death
Cerebellum / metabolism
Cystatin B
Cystatins / genetics
Cytochromes c / metabolism
Disease Models, Animal
Electroencephalography
Genotype
In Situ Nick-End Labeling
Lysosomes / metabolism
Mice
Mice, Knockout
Mitochondria / metabolism
Myoclonic Epilepsies, Progressive / metabolism,  pathology*
Phenotype
Proto-Oncogene Proteins c-bcl-2 / metabolism
Signal Transduction*
Grant Support
ID/Acronym/Agency:
CA 83817/CA/NCI NIH HHS; NS29709/NS/NINDS NIH HHS
Chemical
Reg. No./Substance:
0/BH3 Interacting Domain Death Agonist Protein; 0/Bid protein, mouse; 0/Carrier Proteins; 0/Cstb protein, mouse; 0/Cystatins; 0/Proto-Oncogene Proteins c-bcl-2; 88844-95-5/Cystatin B; 9007-43-6/Cytochromes c; EC 3.4.-/Cathepsins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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