| pubmed-article:12874245 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12874245 | lifeskim:mentions | umls-concept:C0024432 | lld:lifeskim |
| pubmed-article:12874245 | lifeskim:mentions | umls-concept:C0208355 | lld:lifeskim |
| pubmed-article:12874245 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:12874245 | lifeskim:mentions | umls-concept:C0441471 | lld:lifeskim |
| pubmed-article:12874245 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:12874245 | lifeskim:mentions | umls-concept:C0065054 | lld:lifeskim |
| pubmed-article:12874245 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:12874245 | lifeskim:mentions | umls-concept:C0443199 | lld:lifeskim |
| pubmed-article:12874245 | lifeskim:mentions | umls-concept:C1514526 | lld:lifeskim |
| pubmed-article:12874245 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:12874245 | pubmed:dateCreated | 2003-7-22 | lld:pubmed |
| pubmed-article:12874245 | pubmed:abstractText | We have developed a novel LPS probe using a highly purified and homogenous preparation of [(3)H] Escherichia coli LPS from the deep rough mutant, which contains a covalently linked, photoactivable 4-p-(azidosalicylamido)-butylamine group. This cross-linker was used to identify the LPS-binding proteins in membranes of the murine-macrophage-like cell line RAW 264.7. The alpha-subunit (PSMA1 C2, 29.5 kDa) and the beta-subunit (PSMB4 N3, 24.36 kDa) of the 20S proteasome complex were identified as LPS-binding proteins. This is the first report demonstrating LPS binding to enzymes such as the proteasome subunits. Functionally, LPS enhanced the chymotrypsin-like activity of the proteasome to degrade synthetic peptides in vitro and, conversely, the proteasome inhibitor lactacystin completely blocked the LPS-induced proteasome's chymotrypsin activity as well as macrophage TNF-alpha secretion and the expression of multiple inflammatory mediator genes. Lactacystin also completely blocked the LPS-induced expression of Toll-like receptor 2 mRNA. In addition, lactacystin dysregulated mitogen-activated protein kinase phosphorylation in LPS-stimulated macrophages, but failed to inhibit IL-1 receptor-associated kinase-1 activity. Importantly, lactacystin also prevented LPS-induced shock in mice. These data strongly suggest that the proteasome complex regulates the LPS-induced signal transduction and that it may be an important therapeutic target in Gram-negative sepsis. | lld:pubmed |
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| pubmed-article:12874245 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:12874245 | pubmed:citationSubset | AIM | lld:pubmed |
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| pubmed-article:12874245 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12874245 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:12874245 | pubmed:issn | 0022-1767 | lld:pubmed |
| pubmed-article:12874245 | pubmed:author | pubmed-author:QureshiNilofe... | lld:pubmed |
| pubmed-article:12874245 | pubmed:author | pubmed-author:VogelStefanie... | lld:pubmed |
| pubmed-article:12874245 | pubmed:author | pubmed-author:PereraPin-YuP... | lld:pubmed |
| pubmed-article:12874245 | pubmed:author | pubmed-author:MorrisonDavid... | lld:pubmed |
| pubmed-article:12874245 | pubmed:author | pubmed-author:ShenJingJ | lld:pubmed |
| pubmed-article:12874245 | pubmed:author | pubmed-author:SplitterGaryG | lld:pubmed |
| pubmed-article:12874245 | pubmed:author | pubmed-author:ZhangGuochiG | lld:pubmed |
| pubmed-article:12874245 | pubmed:author | pubmed-author:LenschatArndA | lld:pubmed |
| pubmed-article:12874245 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12874245 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:12874245 | pubmed:volume | 171 | lld:pubmed |
| pubmed-article:12874245 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12874245 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12874245 | pubmed:pagination | 1515-25 | lld:pubmed |
| pubmed-article:12874245 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:12874245 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12874245 | pubmed:articleTitle | The proteasome as a lipopolysaccharide-binding protein in macrophages: differential effects of proteasome inhibition on lipopolysaccharide-induced signaling events. | lld:pubmed |
| pubmed-article:12874245 | pubmed:affiliation | Department of Basic Medical Science, School of Medicine and Shock/Trauma Research Center, University of Missouri, Kansas City, MO 64108, USA. qureshi@umkc.edu | lld:pubmed |
| pubmed-article:12874245 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12874245 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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