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PMID:10623794
| Citation |
Ohashi, K, Burkart, V, Flohé, S and Kolb, H (2000) Cutting edge: heat shock protein 60 is a putative endogenous ligand of the toll-like receptor-4 complex. J. Immunol. 164:558-61 |
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| Abstract |
Human heat shock protein 60 (hsp60) elicits a potent proinflammatory response in cells of the innate immune system and therefore has been proposed as a danger signal of stressed or damaged cells. We report here that macrophages of C3H/HeJ mice, carrying a mutant Toll-like-receptor (Tlr) 4 are nonresponsive to hsp60. Both the induction of TNF-alpha and NO formation were found dependent on a functional Tlr4 whereas stimulation of macrophages by CpG DNA was Tlr4 independent. We conclude that Tlr4 mediates hsp60 signaling. This is the first report of a putative endogenous ligand of the Tlr4 complex. |
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| Keywords |
Animals; Chaperonin 60/metabolism; Chaperonin 60/physiology; Drosophila Proteins; Humans; Ligands; Macromolecular Substances; Macrophages/immunology; Macrophages/metabolism; Membrane Glycoproteins/metabolism; Membrane Glycoproteins/physiology; Mice; Mice, Inbred C3H; Mice, Inbred C57BL; Nitric Oxide/biosynthesis; Receptors, Cell Surface/metabolism; Receptors, Cell Surface/physiology; Signal Transduction/immunology; Toll-Like Receptor 4; Toll-Like Receptors; Tumor Necrosis Factor-alpha/biosynthesis |
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Significance
Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
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