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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1998-6-18
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pubmed:abstractText |
Occludin is an integral membrane protein that is concentrated at tight junctions (zonulae occludentes) in simple epithelial cells. ZO-1 and ZO-2 are peripheral membrane proteins that are localized at tight junctions in simple epithelial cells and at cadherin-based adherens junctions in nonepithelial cells. In this study, we investigated the expression and subcellular distribution of occludin, ZO-1, and ZO-2 in rodent skin. Immunoblotting detected all of these molecules in isolated epidermis, but the occludin/ZO-1 (or occludin/ZO-2) ratio was significantly lower than that in cultured simple epithelial cells. In the epidermis of adult skin, occludin was concentrated at cell-cell borders only in the most superficial zone of the granular cell layer, whereas ZO-1 and ZO-2 were distributed in a much broader zone from the spinous to the granular layers. During mouse skin development, this peculiar distribution of occludin in the epidermis appeared when the periderm, a simple epithelium bearing typical occludin-based tight junctions, was sloughed off at embryonic day 16.5 of gestation. Freeze-fracture electron microscopy identified the so-called focal strands or maculae occludentes, i.e., spot tight junction-like structures, between adjacent granular cells, and anti-occludin monoclonal antibody exclusively labeled these focal strands. In hair follicles, occludin and ZO-1 were colocalized at cell-cell borders in Henle's layer and the cornifying cuticle of the inner root sheath. In addition, ZO-1 but not occludin were localized weakly at the outer root sheath and intensely at the hair cortex/matrix.
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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/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
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 |
Jun
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pubmed:issn |
0022-202X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
110
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
862-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9620290-Animals,
pubmed-meshheading:9620290-Animals, Newborn,
pubmed-meshheading:9620290-Cells, Cultured,
pubmed-meshheading:9620290-Epithelial Cells,
pubmed-meshheading:9620290-Female,
pubmed-meshheading:9620290-Freeze Fracturing,
pubmed-meshheading:9620290-Frozen Sections,
pubmed-meshheading:9620290-Immunoblotting,
pubmed-meshheading:9620290-Immunohistochemistry,
pubmed-meshheading:9620290-Male,
pubmed-meshheading:9620290-Membrane Proteins,
pubmed-meshheading:9620290-Mice,
pubmed-meshheading:9620290-Microscopy, Fluorescence,
pubmed-meshheading:9620290-Microscopy, Immunoelectron,
pubmed-meshheading:9620290-Phosphoproteins,
pubmed-meshheading:9620290-Skin,
pubmed-meshheading:9620290-Subcellular Fractions,
pubmed-meshheading:9620290-Tight Junctions
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pubmed:year |
1998
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pubmed:articleTitle |
Subcellular distribution of tight junction-associated proteins (occludin, ZO-1, ZO-2) in rodent skin.
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pubmed:affiliation |
Department of Cell Biology, Faculty of Medicine, Kyoto University, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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