Source:http://linkedlifedata.com/resource/pubmed/id/17917069
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-3
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pubmed:dateCreated |
2007-10-5
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pubmed:abstractText |
Host defense against many invading Gram-negative bacteria (GNB) depends on innate immune recognition of endotoxin (lipopolysaccharides, LPS), unique surface glycolipids of GNB. Host responses to endotoxin must be highly sensitive but self-limited. In mammals, optimal sensitivity is achieved by ordered interactions of endotoxin with several different extracellular and cell surface proteins-the LPS-binding protein (LBP), CD14, MD-2, and Toll-like receptor (TLR) 4-reflecting the requirement for specific protein-endotoxin and protein-protein interactions. This complex reaction pathway also provides many ways to attenuate endotoxin-driven inflammation and can explain how differences in endotoxin structure, either intrinsic among GNB or induced by metabolic remodeling, can alter host responsiveness and thus the outcome of host-GNB interactions. Major goals of our research are to better understand: (1) the structural bases of specific host-endotoxin interactions; (2) functional diversity among host endotoxin-binding proteins; and (3) how the actions of various endotoxin-binding proteins are regulated to permit optimal host responses to GNB infection. In addition, the identification of a water-soluble endotoxin:MD-2 complex that, depending on the structure of endotoxin or MD-2, has potent TLR4 agonist or antagonist properties suggests novel pharmacologic approaches to immuno-modulation.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD14,
http://linkedlifedata.com/resource/pubmed/chemical/Endotoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Lymphocyte Antigen 96,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Toll-Like Receptors,
http://linkedlifedata.com/resource/pubmed/chemical/endotoxin binding proteins
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pubmed:status |
MEDLINE
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pubmed:issn |
0257-277X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
39
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
249-60
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:17917069-Animals,
pubmed-meshheading:17917069-Antigens, CD14,
pubmed-meshheading:17917069-Endotoxins,
pubmed-meshheading:17917069-Gram-Negative Bacteria,
pubmed-meshheading:17917069-Gram-Negative Bacterial Infections,
pubmed-meshheading:17917069-Humans,
pubmed-meshheading:17917069-Immunity, Innate,
pubmed-meshheading:17917069-Lipopolysaccharides,
pubmed-meshheading:17917069-Lymphocyte Antigen 96,
pubmed-meshheading:17917069-Membrane Proteins,
pubmed-meshheading:17917069-Signal Transduction,
pubmed-meshheading:17917069-Toll-Like Receptors
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pubmed:year |
2007
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pubmed:articleTitle |
Regulation of interactions of Gram-negative bacterial endotoxins with mammalian cells.
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pubmed:affiliation |
The Inflammation Program, Roy J. and Lucille A. Carver College of Medicine, University of Iowa, 2501 Crosspark Rd, Coralville, Iowa City, IA 52241, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Review,
Research Support, N.I.H., Extramural
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