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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
1995-5-25
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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.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7536794-1281215,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7536794-1698311,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7536794-227936,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7536794-2402637,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7536794-2471708,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7536794-2477488,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7536794-2854151,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7536794-3123100,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7536794-3281933,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7536794-4970220,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7536794-6208133,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7536794-6225125,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7536794-6802835,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7536794-7037642,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7536794-7505800,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7536794-7519640,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7536794-7519994,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7536794-8064223,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7536794-8132678,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7536794-8207264,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7536794-8225591,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7536794-8265667,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7536794-8324886
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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/Acute-Phase Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD14,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation...,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, HDL,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/lipopolysaccharide-binding protein
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0022-1007
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
181
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1743-54
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:7536794-Acute-Phase Proteins,
pubmed-meshheading:7536794-Antigens, CD,
pubmed-meshheading:7536794-Antigens, CD14,
pubmed-meshheading:7536794-Antigens, Differentiation, Myelomonocytic,
pubmed-meshheading:7536794-Biological Transport,
pubmed-meshheading:7536794-Carrier Proteins,
pubmed-meshheading:7536794-Humans,
pubmed-meshheading:7536794-Lipopolysaccharides,
pubmed-meshheading:7536794-Lipoproteins, HDL,
pubmed-meshheading:7536794-Membrane Glycoproteins,
pubmed-meshheading:7536794-Molecular Weight
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pubmed:year |
1995
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pubmed:articleTitle |
Soluble CD14 acts as a shuttle in the neutralization of lipopolysaccharide (LPS) by LPS-binding protein and reconstituted high density lipoprotein.
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pubmed:affiliation |
Laboratory of Cellular Physiology and Immunology, Rockefeller University, New York 10021, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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