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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
2007-10-4
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pubmed:abstractText |
Ephs and ephrins are a family of membrane-bound proteins that function as receptor-ligand pairs. Members of the Eph-ephrin-B family have recently been reported to regulate the paracellular permeability of epithelial cells. In this study, we analyzed the expression and the function of ephrin-B1 in glomeruli. Using immunofluorescence (IF), we found that ephrin-B1 was expressed along the glomerular capillary loop. Immunoelectron microscopy revealed that ephrin-B1 expression was restricted at the slit diaphragm. Dual labeled IF showed ephrin-B1 colocalized with the slit diaphragm proteins nephrin and CD2-associated protein. Ephrin-B1 colocalized with nephrin at the late capillary loop stage of kidney development. Additionally, injection of rats with a nephritogenic anti-nephrin antibody (ANA) reduced ephrin-B1 expression. When podocytes were cultured in vitro, they extruded processes that co-stained for ephrin-B1 and for CD2-associated protein. When these podocytes were treated in culture with small interfering RNA for ephrin-B1, CD2-associated protein was reduced in the processes, with a remaining faint perinuclear staining. We suggest that ephrin-B1 has a role in maintaining barrier function at the slit diaphragm.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Anti-Idiotypic,
http://linkedlifedata.com/resource/pubmed/chemical/CD2-associated protein,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ephrin-B1,
http://linkedlifedata.com/resource/pubmed/chemical/Ephrin-B2,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering,
http://linkedlifedata.com/resource/pubmed/chemical/nephrin
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0085-2538
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
72
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
954-64
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pubmed:meshHeading |
pubmed-meshheading:17667985-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:17667985-Amino Acid Sequence,
pubmed-meshheading:17667985-Animals,
pubmed-meshheading:17667985-Antibodies, Anti-Idiotypic,
pubmed-meshheading:17667985-Cells, Cultured,
pubmed-meshheading:17667985-Cytoskeletal Proteins,
pubmed-meshheading:17667985-Ephrin-B1,
pubmed-meshheading:17667985-Ephrin-B2,
pubmed-meshheading:17667985-Female,
pubmed-meshheading:17667985-Gene Expression Regulation,
pubmed-meshheading:17667985-Kidney Diseases,
pubmed-meshheading:17667985-Kidney Glomerulus,
pubmed-meshheading:17667985-Membrane Proteins,
pubmed-meshheading:17667985-Molecular Sequence Data,
pubmed-meshheading:17667985-Podocytes,
pubmed-meshheading:17667985-RNA, Small Interfering,
pubmed-meshheading:17667985-Rats,
pubmed-meshheading:17667985-Rats, Wistar
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pubmed:year |
2007
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pubmed:articleTitle |
Ephrin-B1 localizes at the slit diaphragm of the glomerular podocyte.
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pubmed:affiliation |
Department of Cell Biology, Institute of Nephrology, Niigata University Graduate School of Medical and Dental Sciences, Niigata, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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