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 ID: 11276205 RIS Download
Mesh terms: Animals | Antigens, CD14 | Bacterial Infections | Bone Morphogenetic Proteins | CHO Cells | Cell Line | Chromatography, Affinity | Cricetinae | Energy Transfer | Growth Differentiation Factor 5 | Growth Substances | HSP70 Heat-Shock Proteins | HSP90 Heat-Shock Proteins | Humans | Interleukin-6 | Lipopolysaccharides | Peptide Mapping | Receptor Aggregation | Receptors, CXCR4 | Signal Transduction | Tumor Necrosis Factor-alpha
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