| pubmed-article:7536794 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7536794 | lifeskim:mentions | umls-concept:C0023821 | lld:lifeskim |
| pubmed-article:7536794 | lifeskim:mentions | umls-concept:C1749467 | lld:lifeskim |
| pubmed-article:7536794 | lifeskim:mentions | umls-concept:C0023810 | lld:lifeskim |
| pubmed-article:7536794 | lifeskim:mentions | umls-concept:C1367477 | lld:lifeskim |
| pubmed-article:7536794 | lifeskim:mentions | umls-concept:C0065054 | lld:lifeskim |
| pubmed-article:7536794 | lifeskim:mentions | umls-concept:C1416801 | lld:lifeskim |
| pubmed-article:7536794 | lifeskim:mentions | umls-concept:C1446680 | lld:lifeskim |
| pubmed-article:7536794 | lifeskim:mentions | umls-concept:C1551336 | lld:lifeskim |
| pubmed-article:7536794 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:7536794 | pubmed:dateCreated | 1995-5-25 | lld:pubmed |
| pubmed-article:7536794 | pubmed:abstractText | We have recently shown that lipopolysaccharide (LPS)-binding protein (LBP) is a lipid transfer protein that catalyzes two distinct reactions: movement of bacterial LPS (endotoxin) from LPS micelles to soluble CD14 (sCD14) and movement of LPS from micelles to reconstituted high density lipoprotein (R-HDL) particles. Here we show that LBP facilitates a third lipid transfer reaction: movement of LPS from LPS-sCD14 complexes to R-HDL particles. This action of LBP is catalytic, with one molecule of LBP enabling the movement of multiple LPS molecules into R-HDL. LBP-catalyzed movement of LPS from LPS-sCD14 complexes to R-HDL neutralizes the capacity of LPS to stimulate polymorphonuclear leukocytes. Our findings show that LPS may be transferred to R-HDL either by the direct action of LBP or by a two-step reaction in which LPS is first transferred to sCD14 and subsequently to R-HDL. We have observed that the two-step pathway of LPS transfer to R-HDL is strongly favored over direct transfer. Neutralization of LPS by LBP and R-HDL was accelerated more than 30-fold by addition of sCD14. Several observations suggest that sCD14 accelerates this reaction by serving as a shuttle for LPS: addition of LBP and sCD14 to LPS micelles resulted in LPS-sCD14 complexes that could diffuse through a 100-kD cutoff filter; LPS-sCD14 complexes appeared transiently during movement of LPS to R-HDL facilitated by purified LBP; and sCD14 could facilitate transfer of LPS to R-HDL without becoming part of the final LPS-R-HDL complex. Complexes of LPS and sCD14 were formed transiently when LPS was incubated in plasma, suggesting that these complexes may play a role as intermediates in the neutralization of LPS under physiological conditions. These findings detail a new activity for sCD14 and suggest a novel mechanism for lipid transfer by LBP. | lld:pubmed |
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| pubmed-article:7536794 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:7536794 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7536794 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7536794 | pubmed:month | May | lld:pubmed |
| pubmed-article:7536794 | pubmed:issn | 0022-1007 | lld:pubmed |
| pubmed-article:7536794 | pubmed:author | pubmed-author:WrightS DSD | lld:pubmed |
| pubmed-article:7536794 | pubmed:author | pubmed-author:HailmanEE | lld:pubmed |
| pubmed-article:7536794 | pubmed:author | pubmed-author:WurfelM MMM | lld:pubmed |
| pubmed-article:7536794 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7536794 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:7536794 | pubmed:volume | 181 | lld:pubmed |
| pubmed-article:7536794 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7536794 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7536794 | pubmed:pagination | 1743-54 | lld:pubmed |
| pubmed-article:7536794 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:7536794 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7536794 | pubmed:articleTitle | Soluble CD14 acts as a shuttle in the neutralization of lipopolysaccharide (LPS) by LPS-binding protein and reconstituted high density lipoprotein. | lld:pubmed |
| pubmed-article:7536794 | pubmed:affiliation | Laboratory of Cellular Physiology and Immunology, Rockefeller University, New York 10021, USA. | lld:pubmed |
| pubmed-article:7536794 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7536794 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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