Source:http://linkedlifedata.com/resource/pubmed/id/16054019
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
2005-8-1
|
| pubmed:abstractText |
The precise mechanism of the progression of advanced heart failure is unknown. We assessed a new scheme in two heart failure models: (I) congenital dilated cardiomyopathy (DCM) in TO-2 strain hamsters lacking delta-sarcoglycan (SG) gene and (II) administration of a high-dose of isoproterenol, as an acute heart failure in normal rats. In TO-2 hamsters, we followed the time course of the histological, physiological and metabolic the progressions of heart failure to the end stage. Dystrophin localization detected by immunostaining age-dependently to the myoplasm and the in situ sarcolemma fragility evaluated by Evans blue entry was increased in the same cardiomyocytes. Western blotting revealed a limited cleavage of the dystrophin protein at the rod domain, strongly suggesting a contribution of endogenous protease(s). We found a remarkable up-regulation of the amount of calpain-1 and -2, and no change of their counterpart, calpastatin. After supplementing TO-2 hearts with the normal delta-SG gene in vivo, these pathological alterations and the animals' survival improved. Furthermore, dystrophin but not delta-SG was disrupted by a high dose of isoproterenol, translocated from the sarcolemma to the myoplasm and fragmented. These results of heart failure, irrespective of the hereditary or acquired origin, indicate a vicious cycle formed by the increased sarcolemma permeability, preferential activation of calpain over calpastatin, and translocation and cleavage of dystrophin would commonly lead to advanced heart failure.
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| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calpain,
http://linkedlifedata.com/resource/pubmed/chemical/Dystrophin,
http://linkedlifedata.com/resource/pubmed/chemical/Isoproterenol,
http://linkedlifedata.com/resource/pubmed/chemical/Sarcoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/calpastatin
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| pubmed:status |
MEDLINE
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| pubmed:month |
Aug
|
| pubmed:issn |
0006-3002
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
1
|
| pubmed:volume |
1751
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
73-81
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| pubmed:dateRevised |
2007-11-15
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| pubmed:meshHeading |
pubmed-meshheading:16054019-Animals,
pubmed-meshheading:16054019-Calcium-Binding Proteins,
pubmed-meshheading:16054019-Calpain,
pubmed-meshheading:16054019-Cardiomyopathy, Dilated,
pubmed-meshheading:16054019-Cell Membrane Permeability,
pubmed-meshheading:16054019-Cricetinae,
pubmed-meshheading:16054019-Dependovirus,
pubmed-meshheading:16054019-Disease Models, Animal,
pubmed-meshheading:16054019-Dystrophin,
pubmed-meshheading:16054019-Enzyme Activation,
pubmed-meshheading:16054019-Gene Therapy,
pubmed-meshheading:16054019-Heart Failure,
pubmed-meshheading:16054019-Isoproterenol,
pubmed-meshheading:16054019-Mesocricetus,
pubmed-meshheading:16054019-Models, Biological,
pubmed-meshheading:16054019-Rats,
pubmed-meshheading:16054019-Sarcoglycans,
pubmed-meshheading:16054019-Sarcolemma
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| pubmed:year |
2005
|
| pubmed:articleTitle |
A novel scheme of dystrophin disruption for the progression of advanced heart failure.
|
| pubmed:affiliation |
Division of Pharmacy, Niigata University of Medical and Dental Hospital, Niigata, 951-8520, Japan.
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| pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
|