Source:http://linkedlifedata.com/resource/pubmed/id/12928411
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
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| pubmed:dateCreated |
2003-8-20
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| pubmed:abstractText |
C1 inhibitor (C1INH) is beneficial in animal models of endotoxemia and sepsis. However, the mechanism(s) of C1INH protection remain(s) ill-defined. In this study, we demonstrated that both active C1INH and reactive center-cleaved, inactive C1INH protected mice from lethal Gram-negative endotoxemia. Both forms of C1INH blocked the LPS-binding protein-dependent binding of Salmonella typhimurium LPS to the murine macrophage cell line, RAW 264.7, and suppressed LPS-induced TNF-alpha mRNA expression. Inhibition of LPS binding to RAW 264.7 cells was reversed with anti-C1INH Ab and was more efficient when C1INH was incubated first with LPS rather than with the cells. C1INH also suppressed LPS-induced up-regulation of TNF-alpha mRNA in whole human blood. The interaction of C1INH with LPS was directly demonstrated both by ELISA and by nondenaturing PAGE, but deletion of the amino-terminal 97-aa residues abrogated this binding. Therefore, C1INH, in addition to its function as a serine protease inhibitor, has a novel anti-inflammatory function mediated via its heavily glycosylated amino-terminal non-serpin domain.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
AIM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Complement C1 Inactivator Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Inflammation Mediators,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments
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| pubmed:status |
MEDLINE
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| pubmed:month |
Sep
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| pubmed:issn |
0022-1767
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
1
|
| pubmed:volume |
171
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
2594-601
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:12928411-Animals,
pubmed-meshheading:12928411-Binding, Competitive,
pubmed-meshheading:12928411-Cell Line,
pubmed-meshheading:12928411-Complement C1 Inactivator Proteins,
pubmed-meshheading:12928411-Disease Models, Animal,
pubmed-meshheading:12928411-Endotoxemia,
pubmed-meshheading:12928411-Female,
pubmed-meshheading:12928411-Inflammation Mediators,
pubmed-meshheading:12928411-Injections, Intraperitoneal,
pubmed-meshheading:12928411-Injections, Intravenous,
pubmed-meshheading:12928411-Lipopolysaccharides,
pubmed-meshheading:12928411-Macrophages,
pubmed-meshheading:12928411-Male,
pubmed-meshheading:12928411-Mice,
pubmed-meshheading:12928411-Mice, Inbred C57BL,
pubmed-meshheading:12928411-Peptide Fragments,
pubmed-meshheading:12928411-Protein Structure, Tertiary,
pubmed-meshheading:12928411-Survival Analysis
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| pubmed:year |
2003
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| pubmed:articleTitle |
C1 inhibitor prevents endotoxin shock via a direct interaction with lipopolysaccharide.
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| pubmed:affiliation |
Center for Blood Research, Children's Hospital, Harvard Medical School, 800 Huntington Avenue, Boston, MA 02115, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|