Source:http://linkedlifedata.com/resource/pubmed/id/18197414
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2008-2-21
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pubmed:abstractText |
As the only barrier between blood and bile compartments hepatocellular tight junctions play a crucial role in cholestasis-induced increase of biliary permeability. The molecular basis of this reversible defect is not known. We, therefore, examined expression, phosphorylation, distribution and colocalization of the junctional proteins occludin, claudin-1-3, ZO-1 and ZO-2 in rats after bile duct ligation and release of ligation. In control rats, claudin-1 and ZO-2 displayed a lobular gradient with highest expression levels in periportal cells, whereas claudin-2 showed a reciprocal distribution. Other proteins were evenly expressed in the liver lobule. Ligation resulted in upregulation of ZO-2 (2.7-fold), ZO-1 (1.4-fold) and occludin (1.2-fold) but not of claudins. Only ZO-2 showed increased phosphorylation. Distribution patterns were unchanged except for a strong accumulation of ZO-2 in perivenous hepatocytes. Colocalization analysis demonstrated that perivenous ZO-2 was the only protein examined revealing strongly increased overlap with occludin and ZO-1, whereas claudins and other proteins displayed a decrease. All changes were partially reversed by release of ligation. We conclude that differential expression of claudin-1-2 and ZO-2 has functional implications for bile formation. The moderately increased ZO-1 and occludin levels account for the known elongation of tight junction strands. The highly increased expression and changed distribution of ZO-2 suggests that ZO-1 is partly substituted by ZO-2, an alteration possibly causing impaired barrier function.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cldn2 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/claudin 1,
http://linkedlifedata.com/resource/pubmed/chemical/claudin 3,
http://linkedlifedata.com/resource/pubmed/chemical/occludin,
http://linkedlifedata.com/resource/pubmed/chemical/zonula occludens-1 protein,
http://linkedlifedata.com/resource/pubmed/chemical/zonula occludens-2 protein
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0948-6143
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
129
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
289-99
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pubmed:meshHeading |
pubmed-meshheading:18197414-Animals,
pubmed-meshheading:18197414-Bile Ducts,
pubmed-meshheading:18197414-Blotting, Western,
pubmed-meshheading:18197414-Liver,
pubmed-meshheading:18197414-Male,
pubmed-meshheading:18197414-Membrane Proteins,
pubmed-meshheading:18197414-Phosphoproteins,
pubmed-meshheading:18197414-Phosphorylation,
pubmed-meshheading:18197414-Rats,
pubmed-meshheading:18197414-Rats, Sprague-Dawley,
pubmed-meshheading:18197414-Tight Junctions,
pubmed-meshheading:18197414-Up-Regulation
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pubmed:year |
2008
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pubmed:articleTitle |
Bile duct ligation in the rat causes upregulation of ZO-2 and decreased colocalization of claudins with ZO-1 and occludin.
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pubmed:affiliation |
Department of Anatomy, University of Basel, Switzerland. I-P.Maly@unibas.ch
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pubmed:publicationType |
Journal Article
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