Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1993-2-22
pubmed:abstractText
The serum protein lipopolysaccharide (LPS)-binding protein (LBP) seems to play an important role in regulating host responses to LPS. Complexes of LPS and LBP form in serum and stimulate monocytes, macrophages, or polymorphonuclear leukocytes after binding to CD14. Previous reports have described the structure and properties of LBP from human and rabbit sera. Since mice are used in some experimental models of endotoxemia or gram-negative bacterial infections, information is needed about the properties of murine LBP. Murine LBP was purified by ion-exchange chromatography and high-pressure liquid chromatography; its NH2-terminal sequence (TNPGLVTRIT) was very similar to those of human and rabbit LBPs (80 to 90% amino acid identity). Murine LBP resembled LBPs from other species in that it promoted the binding of LPS to monocytes and enhanced the sensitivity of monocytes to LPS at least 100-fold. Mouse LBP, like rabbit and human LBPs, was found to be an acute-phase protein. Further in vivo studies with mice and anti-CD14 or anti-LBP reagents should help determine the role of LBP in response to LPS challenges.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/7678583-1375247, http://linkedlifedata.com/resource/pubmed/commentcorrection/7678583-1402386, http://linkedlifedata.com/resource/pubmed/commentcorrection/7678583-1698311, http://linkedlifedata.com/resource/pubmed/commentcorrection/7678583-1716284, http://linkedlifedata.com/resource/pubmed/commentcorrection/7678583-2307935, http://linkedlifedata.com/resource/pubmed/commentcorrection/7678583-2349103, http://linkedlifedata.com/resource/pubmed/commentcorrection/7678583-2402637, http://linkedlifedata.com/resource/pubmed/commentcorrection/7678583-2403458, http://linkedlifedata.com/resource/pubmed/commentcorrection/7678583-2427635, http://linkedlifedata.com/resource/pubmed/commentcorrection/7678583-2722846, http://linkedlifedata.com/resource/pubmed/commentcorrection/7678583-3042431, http://linkedlifedata.com/resource/pubmed/commentcorrection/7678583-3049617, http://linkedlifedata.com/resource/pubmed/commentcorrection/7678583-3138236, http://linkedlifedata.com/resource/pubmed/commentcorrection/7678583-3543052, http://linkedlifedata.com/resource/pubmed/commentcorrection/7678583-3782828, http://linkedlifedata.com/resource/pubmed/commentcorrection/7678583-388439, http://linkedlifedata.com/resource/pubmed/commentcorrection/7678583-3899551, http://linkedlifedata.com/resource/pubmed/commentcorrection/7678583-3949385, http://linkedlifedata.com/resource/pubmed/commentcorrection/7678583-5432063, http://linkedlifedata.com/resource/pubmed/commentcorrection/7678583-6945311
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0019-9567
pubmed:author
pubmed:issnType
Print
pubmed:volume
61
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
378-83
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:7678583-Acute-Phase Proteins, pubmed-meshheading:7678583-Amino Acid Sequence, pubmed-meshheading:7678583-Animals, pubmed-meshheading:7678583-Antigens, CD, pubmed-meshheading:7678583-Antigens, CD14, pubmed-meshheading:7678583-Antigens, Differentiation, Myelomonocytic, pubmed-meshheading:7678583-Carrier Proteins, pubmed-meshheading:7678583-Cells, Cultured, pubmed-meshheading:7678583-Humans, pubmed-meshheading:7678583-Hydrogen-Ion Concentration, pubmed-meshheading:7678583-Lipopolysaccharides, pubmed-meshheading:7678583-Membrane Glycoproteins, pubmed-meshheading:7678583-Mice, pubmed-meshheading:7678583-Mice, Inbred Strains, pubmed-meshheading:7678583-Molecular Sequence Data, pubmed-meshheading:7678583-Monocytes, pubmed-meshheading:7678583-Rabbits, pubmed-meshheading:7678583-Temperature
pubmed:year
1993
pubmed:articleTitle
Purification and characterization of murine lipopolysaccharide-binding protein.
pubmed:affiliation
Department of Internal Medicine, CHUV-Lausanne, Switzerland.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't