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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1993-10-12
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pubmed:abstractText |
Using a photoactivable, radioiodinated lipopolysaccharide probe, [125I]ASD-LPS (derivatized from purified E. coli 0111:B4 S-LPS), we earlier reported the presence of a 73-kDa (p73) predominant LPS-binding protein on mouse lymphocytes and macrophages with specificity for the lipid A region of LPS. Both Re-LPS from Salmonella minnesota and purified lipid A will inhibit the binding of LPS to the p73 LPS receptor. In the studies reported here, we have found that non-toxic diphosphoryl lipid A purified from Rhodo-pseudomonas sphaeroides has the capability to inhibit the binding of [125I]ASD-LPS to the p73 protein. However, using the same LPS probe and photoaffinity cross-linking techniques, our data suggest that a less dominant 38-kDa (p38) LPS-specific binding protein identified on mouse splenocytes, J774.1 macrophage-like cell line, and 70Z/3 pre B-cell line by SDS-PAGE is not inhibited by purified lipid A, even at a concentration in 50-fold excess of that of [125]ASD-LPS. The binding of the LPS probe to the 38 protein could be inhibited in a dose-dependent manner by underivatized native S. minnesota Re-LPS (composed only of Kdo and lipid A). We speculate that this p38 LPS-binding protein may manifest a specificity for inner core oligosaccharide determinants on LPS.
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pubmed:grant |
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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/Affinity Labels,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD14,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lipid A,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/diphosphoryl lipid A,
http://linkedlifedata.com/resource/pubmed/chemical/lipopolysaccharide-binding protein
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0165-2478
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
36
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
245-50
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:7690343-Acute-Phase Proteins,
pubmed-meshheading:7690343-Affinity Labels,
pubmed-meshheading:7690343-Animals,
pubmed-meshheading:7690343-Antigens, CD14,
pubmed-meshheading:7690343-B-Lymphocytes,
pubmed-meshheading:7690343-Carrier Proteins,
pubmed-meshheading:7690343-Cell Line,
pubmed-meshheading:7690343-Cells, Cultured,
pubmed-meshheading:7690343-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:7690343-Female,
pubmed-meshheading:7690343-Lipid A,
pubmed-meshheading:7690343-Lipopolysaccharides,
pubmed-meshheading:7690343-Male,
pubmed-meshheading:7690343-Membrane Glycoproteins,
pubmed-meshheading:7690343-Membrane Proteins,
pubmed-meshheading:7690343-Mice,
pubmed-meshheading:7690343-Mice, Inbred C3H,
pubmed-meshheading:7690343-Molecular Weight,
pubmed-meshheading:7690343-Receptors, Immunologic,
pubmed-meshheading:7690343-Rhodobacter sphaeroides,
pubmed-meshheading:7690343-Spleen
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pubmed:year |
1993
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pubmed:articleTitle |
Lipopolysaccharide (LPS) binding to 73-kDa and 38-kDa surface proteins on lymphoreticular cells: preferential inhibition of LPS binding to the former by Rhodopseudomonas sphaeroides lipid A.
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pubmed:affiliation |
Department of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, Kansas City 66160.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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