Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2001-3-29
pubmed:abstractText
Bacterial lipopolysaccharide (LPS), the major structural component of the outer wall of Gram-negative bacteria, is a potent initiator of an inflammatory response and serves as an indicator of bacterial infection. Although CD14 has been identified as the main LPS receptor, accumulating evidence has suggested the possible existence of other functional receptor(s). In this study, using affinity chromatography, peptide mass fingerprinting and fluorescence resonance energy transfer, we have identified four new proteins that form an activation cluster after LPS ligation and are involved in LPS signal transduction. Here we present evidence that implicates heat shock proteins 70 and 90, chemokine receptor 4 and growth differentiation factor 5 as the main mediators of activation by bacterial lipopolysaccharide.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD14, http://linkedlifedata.com/resource/pubmed/chemical/Bone Morphogenetic Proteins, http://linkedlifedata.com/resource/pubmed/chemical/GDF5 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Growth Differentiation Factor 5, http://linkedlifedata.com/resource/pubmed/chemical/Growth Substances, http://linkedlifedata.com/resource/pubmed/chemical/HSP70 Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/HSP90 Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-6, http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, CXCR4, http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1529-2908
pubmed:author
pubmed:issnType
Print
pubmed:volume
2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
338-45
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:11276205-Animals, pubmed-meshheading:11276205-Antigens, CD14, pubmed-meshheading:11276205-Bacterial Infections, pubmed-meshheading:11276205-Bone Morphogenetic Proteins, pubmed-meshheading:11276205-CHO Cells, pubmed-meshheading:11276205-Cell Line, pubmed-meshheading:11276205-Chromatography, Affinity, pubmed-meshheading:11276205-Cricetinae, pubmed-meshheading:11276205-Energy Transfer, pubmed-meshheading:11276205-Growth Differentiation Factor 5, pubmed-meshheading:11276205-Growth Substances, pubmed-meshheading:11276205-HSP70 Heat-Shock Proteins, pubmed-meshheading:11276205-HSP90 Heat-Shock Proteins, pubmed-meshheading:11276205-Humans, pubmed-meshheading:11276205-Interleukin-6, pubmed-meshheading:11276205-Lipopolysaccharides, pubmed-meshheading:11276205-Peptide Mapping, pubmed-meshheading:11276205-Receptor Aggregation, pubmed-meshheading:11276205-Receptors, CXCR4, pubmed-meshheading:11276205-Signal Transduction, pubmed-meshheading:11276205-Tumor Necrosis Factor-alpha
pubmed:year
2001
pubmed:articleTitle
A CD14-independent LPS receptor cluster.
pubmed:affiliation
University of Essex, Department of Biological Sciences, Central Campus, Wivenhoe Park, Colchester CO4 3SQ, UK. kathy.triantafilou@port.ac.uk
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't