Source:http://linkedlifedata.com/resource/pubmed/id/10508613
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
18
|
pubmed:dateCreated |
2000-2-14
|
pubmed:abstractText |
In multicellular organisms, various compositionally distinct fluid compartments are established by epithelial and endothelial cellular sheets. For these cells to function as barriers, tight junctions (TJs) are considered to create a primary barrier for the diffusion of solutes through the paracellular pathway [1] [2] [3]. In ultrathin sections viewed under electron microscopy, TJs appear as a series of apparent fusions, involving the outer leaflets of plasma membranes of adjacent cells, to form the so-called kissing points of TJs, where the intercellular space is completely obliterated [4]. Claudins are a family of 16 proteins whose members have been identified as major integral membrane proteins localized exclusively at TJs [5] [6] [7] [8]. It remains unclear, however, whether claudins have the cell-adhesion activity that would explain the unusual intercellular adhesion at TJs. Using mouse L-fibroblast transfectants expressing various amounts of claudin-1, -2 or -3, we found that these claudins possess Ca(2+)-independent cell-adhesion activity. Using ultrathin-section electron microscopy, we observed many kissing points of TJs between adjacent transfectants. Furthermore, the cell-adhesion activity of occludin, another integral membrane protein localized at TJs [9] [10] [11], was negligible when compared with that of claudins. Thus, claudins are responsible for TJ-specific obliteration of the intercellular space.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Cldn2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/claudin 1,
http://linkedlifedata.com/resource/pubmed/chemical/claudin 3,
http://linkedlifedata.com/resource/pubmed/chemical/occludin
|
pubmed:status |
MEDLINE
|
pubmed:month |
Sep
|
pubmed:issn |
0960-9822
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
23
|
pubmed:volume |
9
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1035-8
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:10508613-Animals,
pubmed-meshheading:10508613-Calcium,
pubmed-meshheading:10508613-Cell Adhesion,
pubmed-meshheading:10508613-Cell Aggregation,
pubmed-meshheading:10508613-L Cells (Cell Line),
pubmed-meshheading:10508613-Membrane Proteins,
pubmed-meshheading:10508613-Mice,
pubmed-meshheading:10508613-Microscopy, Electron,
pubmed-meshheading:10508613-Recombinant Fusion Proteins,
pubmed-meshheading:10508613-Tight Junctions,
pubmed-meshheading:10508613-Transfection
|
pubmed:year |
1999
|
pubmed:articleTitle |
Ca(2+)-independent cell-adhesion activity of claudins, a family of integral membrane proteins localized at tight junctions.
|
pubmed:affiliation |
Department of Cell Biology Faculty of Medicine Kyoto University Sakyo-ku, Kyoto, 606-8501, Japan.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|