Source:http://linkedlifedata.com/resource/pubmed/id/18513742
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2008-6-27
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pubmed:abstractText |
Claudin-5 is a transmembrane cell junction protein that is a component of tight junctions in endothelial cell layers. We have previously shown that claudin-5 also localizes to lateral membranes of murine cardiomyocytes at their junction with the extracellular matrix. Claudin-5 levels are specifically reduced in myocytes from a mouse model of muscular dystrophy with cardiomyopathy. To establish whether claudin-5 is similarly specifically reduced in human cardiomyopathy, we compared the levels of claudin-5 with other cell junction proteins in 62 cardiomyopathic end-stage explant samples. We show that claudin-5 levels are reduced in at least 60% of patient samples compared with non-failing controls. Importantly, claudin-5 reductions can be independent of connexin-43, a gap junction protein previously reported to be reduced in failing heart samples. Other cell junction proteins including alpha-catenin, beta-catenin, gamma-catenin, desmoplakin, and N-cadherin are reduced in only a small number of failing samples and only in combination with reduced claudin-5 or connexin-43 levels. We also show that reduced claudin-5 levels can be present independently from dystrophin alterations, which are known to be capable of causing and resulting from cardiomyopathy. These data are the first to show alterations of a tight junction protein in human cardiomyopathy samples and suggest that claudin-5 may participate in novel mechanisms in the pathway to end-stage heart failure.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/CDH2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CLDN5 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cadherins,
http://linkedlifedata.com/resource/pubmed/chemical/Catenins,
http://linkedlifedata.com/resource/pubmed/chemical/Connexin 43,
http://linkedlifedata.com/resource/pubmed/chemical/Desmoplakins,
http://linkedlifedata.com/resource/pubmed/chemical/GJA1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Muscle Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1095-8584
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
45
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
81-7
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pubmed:meshHeading |
pubmed-meshheading:18513742-Animals,
pubmed-meshheading:18513742-Antigens, CD,
pubmed-meshheading:18513742-Cadherins,
pubmed-meshheading:18513742-Cardiomyopathies,
pubmed-meshheading:18513742-Catenins,
pubmed-meshheading:18513742-Connexin 43,
pubmed-meshheading:18513742-Desmoplakins,
pubmed-meshheading:18513742-Female,
pubmed-meshheading:18513742-Gap Junctions,
pubmed-meshheading:18513742-Humans,
pubmed-meshheading:18513742-Male,
pubmed-meshheading:18513742-Membrane Proteins,
pubmed-meshheading:18513742-Mice,
pubmed-meshheading:18513742-Muscle Proteins,
pubmed-meshheading:18513742-Myocytes, Cardiac,
pubmed-meshheading:18513742-Tight Junctions
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pubmed:year |
2008
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pubmed:articleTitle |
Claudin-5 levels are reduced in human end-stage cardiomyopathy.
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pubmed:affiliation |
Department of Molecular and Cellular Biochemistry, College of Medicine, The Ohio State University, Columbus, OH 43210, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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