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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1997-7-15
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pubmed:abstractText |
To characterize the cyst-lining cells in human autosomal dominant polycystic kidney disease (ADPKD), we performed immunohistological studies with specific antibodies against human aquaporin-2 (AQP-2, the vasopressin-regulated water channel) and aquaporin-3 (AQP-3), which are expressed only in collecting duct cells in the normal kidney. The polycystic kidney samples were obtained from 2 hemodialysis patient at uninephrectomy. Immunohistochemical studies revealed two types of staining of cyst-lining cells. Approximately 30% of all the cysts were simultaneously immunostained by both antibodies. Among these AQP-positive cysts, more than 90% of the cysts were intensely stained, with well-polarized localization of AQP-2 and AQP-3. In fewer than 10% of AQP-positive cysts, by contrast, immunostaining for AQP-2 and AQP-3 was faint and no clearly polarized localization of the channels was observed. We examined the immunostaining in further detail by electron microscopy. Staining specific for AQP-2 was mainly observed in the apical membrane of cyst-lining cells. Moreover, staining specific for AQP-3 was observed in all of the AQP-2-positive cysts. It appeared unlikely that the variations in immunostaining observed under the light microscope had been induced by total disruption of water-channel polarity. The present study suggests that about 30% of the cysts in our cases of ADPKD were derived from the collecting duct cells and that the cyst-lining cells were well differentiated in terms of AQP expression.
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pubmed:commentsCorrections | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/AQP2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/AQP3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Aquaporin 2,
http://linkedlifedata.com/resource/pubmed/chemical/Aquaporin 3,
http://linkedlifedata.com/resource/pubmed/chemical/Aquaporin 6,
http://linkedlifedata.com/resource/pubmed/chemical/Aquaporins,
http://linkedlifedata.com/resource/pubmed/chemical/Ion Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments
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pubmed:status |
MEDLINE
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pubmed:issn |
0028-2766
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
75
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
321-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9069455-Aquaporin 2,
pubmed-meshheading:9069455-Aquaporin 3,
pubmed-meshheading:9069455-Aquaporin 6,
pubmed-meshheading:9069455-Aquaporins,
pubmed-meshheading:9069455-Gene Expression,
pubmed-meshheading:9069455-Humans,
pubmed-meshheading:9069455-Immunohistochemistry,
pubmed-meshheading:9069455-Ion Channels,
pubmed-meshheading:9069455-Kidney Cortex,
pubmed-meshheading:9069455-Microscopy, Electron,
pubmed-meshheading:9069455-Peptide Fragments,
pubmed-meshheading:9069455-Polycystic Kidney, Autosomal Dominant
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pubmed:year |
1997
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pubmed:articleTitle |
Expression and localization of the water channels in human autosomal dominant polycystic kidney disease.
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pubmed:affiliation |
Department of Internal Medicine, Keio University, School of Medicine, Shinjuku-ku, Tokyo, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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