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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
19
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pubmed:dateCreated |
2005-5-9
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pubmed:abstractText |
Nucleotide oligomerization domain 2 (NOD2) functions as a mammalian cytosolic pathogen recognition molecule, and variants have been associated with risk for Crohn disease. We recently demonstrated that NOD2 functions as an anti-bacterial factor limiting survival of intracellular invasive bacteria. To gain further insight into the mechanism of NOD2 activation and signal transduction, we performed yeast two-hybrid screening. We demonstrate that GRIM-19, a protein with homology to the NADPH dehydrogenase complex, interacts with endogenous NOD2 in HT29 cells. GRIM-19 is required for NF-kappaB activation following NOD2-mediated recognition of bacterial muramyl dipeptide. GRIM-19 also controls pathogen invasion of intestinal epithelial cells. GRIM-19 expression is decreased in inflamed mucosa of patients with inflammatory bowel diseases. GRIM-19 may be a key component in NOD2-mediated innate mucosal responses and serve to regulate intestinal epithelial cell responses to microbes.
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pubmed:grant |
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pubmed:commentsCorrections |
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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/Apoptosis Regulatory Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GRIM19 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Luciferases,
http://linkedlifedata.com/resource/pubmed/chemical/NADH, NADPH Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/NOD2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Nod2 Signaling Adaptor Protein,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering
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pubmed:status |
MEDLINE
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pubmed:month |
May
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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 |
13
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pubmed:volume |
280
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
19021-6
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pubmed:dateRevised |
2008-5-13
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pubmed:meshHeading |
pubmed-meshheading:15753091-Animals,
pubmed-meshheading:15753091-Apoptosis Regulatory Proteins,
pubmed-meshheading:15753091-COS Cells,
pubmed-meshheading:15753091-Caco-2 Cells,
pubmed-meshheading:15753091-Cell Line,
pubmed-meshheading:15753091-Cell Line, Tumor,
pubmed-meshheading:15753091-Cytosol,
pubmed-meshheading:15753091-Epithelial Cells,
pubmed-meshheading:15753091-Escherichia coli,
pubmed-meshheading:15753091-Genes, Reporter,
pubmed-meshheading:15753091-Humans,
pubmed-meshheading:15753091-Immunoblotting,
pubmed-meshheading:15753091-Immunoprecipitation,
pubmed-meshheading:15753091-Intestinal Mucosa,
pubmed-meshheading:15753091-Intestines,
pubmed-meshheading:15753091-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:15753091-Luciferases,
pubmed-meshheading:15753091-Microscopy, Confocal,
pubmed-meshheading:15753091-NADH, NADPH Oxidoreductases,
pubmed-meshheading:15753091-NF-kappa B,
pubmed-meshheading:15753091-Nod2 Signaling Adaptor Protein,
pubmed-meshheading:15753091-Plasmids,
pubmed-meshheading:15753091-Protein Binding,
pubmed-meshheading:15753091-Protein Structure, Tertiary,
pubmed-meshheading:15753091-RNA, Small Interfering,
pubmed-meshheading:15753091-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:15753091-Salmonella,
pubmed-meshheading:15753091-Signal Transduction,
pubmed-meshheading:15753091-Two-Hybrid System Techniques
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pubmed:year |
2005
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pubmed:articleTitle |
GRIM-19 interacts with nucleotide oligomerization domain 2 and serves as downstream effector of anti-bacterial function in intestinal epithelial cells.
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pubmed:affiliation |
Gastrointestinal Unit, Department of Medicine, Center for the Study of Inflammatory Bowel Disease, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts 02114, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, N.I.H., Extramural
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