rdf:type |
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lifeskim:mentions |
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pubmed:issue |
38
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pubmed:dateCreated |
2001-9-17
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pubmed:abstractText |
Interleukin (IL)-15 is able to regulate tight junction formation in intestinal epithelial cells. However, the mechanisms that regulate the intestinal barrier function in response to IL-15 and the involved subunits of the IL-15 ligand-receptor system are unknown. We determined the IL-2Rbeta subunit and IL-15-dependent regulation of tight junction-associated proteins in the human intestinal epithelial cell line T-84. The IL-2Rbeta subunit was expressed and induced signal transduction in caveolin enriched rafts in intestinal epithelial cells. IL-15-mediated tightening of intestinal epithelial monolayers correlated with the enhanced recruitment of tight junction proteins into Triton X-100-insoluble protein fractions. IL-15-mediated up-regulation of ZO-1 and ZO-2 expression was independent of the IL-2Rbeta subunit, whereas the phosphorylation of occludin and enhanced membrane association of claudin-1 and claudin-2 by IL-15 required the presence of the IL-2Rbeta subunit. Recruitment of claudins and hyperphosphorylated occludin into tight junctions resulted in a more marked induction of tight junction formation in intestinal epithelial cells than the up-regulation of ZO-1 and ZO-2 by itself. The regulation of the intestinal epithelial barrier function by IL-15 involves IL-2Rbeta-dependent and -independent signaling pathways leading to the recruitment of claudins, hyperphosphorylated occludin, ZO-1, and ZO-2 into the tight junctional protein complex.
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pubmed:grant |
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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/CAV1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Caveolin 1,
http://linkedlifedata.com/resource/pubmed/chemical/Caveolins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-15,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin-2,
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 |
Sep
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
35571-80
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11466322-Base Sequence,
pubmed-meshheading:11466322-Caveolin 1,
pubmed-meshheading:11466322-Caveolins,
pubmed-meshheading:11466322-DNA Primers,
pubmed-meshheading:11466322-Humans,
pubmed-meshheading:11466322-Interleukin-15,
pubmed-meshheading:11466322-Intestinal Mucosa,
pubmed-meshheading:11466322-Membrane Proteins,
pubmed-meshheading:11466322-Phosphoproteins,
pubmed-meshheading:11466322-Phosphorylation,
pubmed-meshheading:11466322-Receptors, Interleukin-2,
pubmed-meshheading:11466322-Signal Transduction,
pubmed-meshheading:11466322-Tight Junctions,
pubmed-meshheading:11466322-Transfection,
pubmed-meshheading:11466322-Tumor Cells, Cultured,
pubmed-meshheading:11466322-Up-Regulation
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pubmed:year |
2001
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pubmed:articleTitle |
Interleukin-2 receptor beta subunit-dependent and -independent regulation of intestinal epithelial tight junctions.
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pubmed:affiliation |
Gastrointestinal Unit, Department of Medicine, Center for the Study of Inflammatory Bowel Disease, Massachusetts General Hospital & Harvard Medical School, Boston, Massachusetts 02114, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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