Heat shock protein 90 mediates macrophage activation by Taxol and bacterial lipopolysaccharide

Byrd, Cynthia A.; Bornmann, William G.; Erdjument‐Bromage, Hediye; Tempst, Paul; Pavletich, Nikola P.; Rosen, Neal; Nathan, Carl; Ding, Aihao

doi:10.1073/pnas.96.10.5645

Cited by 190 publications

(147 citation statements)

References 51 publications

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“…Hsp60 might signal through CD14, TLR-2 and TLR-4 [61,62], probably binding to a different molecule [63]. It was also suggested that Hsp90 and Hsp70 bound to LPS [64,65], and the latter could activate the innate immune response by a TLR4-mediated signal pathway [66]. In fish, beta-propiolactone (BPL) e inactivated VHSV was able to activate the expression of genes involved in the innate immune response in vitro [67], and some genes related to early immune response, such as IL-1b, TGF-b, IL-8 and iNOS, were simultaneously up-regulated in rainbow trout challenged with VHSV [68].…”

Section: Discussionmentioning

confidence: 99%

Differential expression of three Paralichthys olivaceus Hsp40 genes in responses to virus infection and heat shock☆

Caiwen

Zhang

et al. 2006

Fish & Shellfish Immunology

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Section: Discussionmentioning

confidence: 99%

Differential expression of three Paralichthys olivaceus Hsp40 genes in responses to virus infection and heat shock☆

Caiwen

Zhang

et al. 2006

Fish & Shellfish Immunology

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“…The critical role of Raf-1 is also supported by the results showing that LPS-induced NO production was significantly inhibited in RAW cells transfected with the Raf-1 antisense oligonucleotide. Recently, Byrd et al (24) reported that HSP90 can bind LPS and mediates macrophage activation by LPS. However, the exact action of LPS on Raf-1/HSP90 complex has not yet been clarified.…”

Section: Discussionmentioning

confidence: 99%

“…Therefore, it is reasonable that SA abrogates the Erk1/2 MAP kinase pathway through the loss of Raf-1 in LPS-stimulated RAW cells. Of particular interest are a series of recent reports implicating HSP90 and its associated proteins in signal transduction of macrophage activation (24,25). Raf-1 protein exists in native complexes with HSP90 that can be formed in vitro by reticulocyte lysate, and its catalytic domain is sufficient for HSP90 binding (29,30).…”

Section: Discussionmentioning

confidence: 99%

“…Three components of the MAP kinase signaling system (Src, Raf, and Mek) are found in association with HSP90, and Raf-1 is stabilized by forming heteromeric complexes with HSP90 (23). Further, NO production is known to be mediated in part through HSP90 signaling (24). Therefore, it was of interest to determine whether SA affects the formation of Raf-1/HSP90 heteromeric complexes (Fig.…”

Section: Sa Does Not Affect the Expression Level Of Hsp90 Which Formmentioning

confidence: 99%

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The Inhibitory Action of Sodium Arsenite on Lipopolysaccharide-Induced Nitric Oxide Production in RAW 267.4 Macrophage Cells: A Role of Raf-1 in Lipopolysaccharide Signaling

Chakravortty

Kato

Sugiyama

et al. 2001

The Journal of Immunology

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The effect of sodium arsenite (SA) on LPS-induced NO production in RAW 267.4 murine macrophage cells was studied. SA pretreatment of LPS-stimulated RAW cells resulted in a striking reduction in NO production. No significant difference in LPS binding was observed between RAW cells pretreated with SA and control untreated RAW cells, suggesting that SA might impair the intracellular signal pathway for NO production. SA inhibited LPS-induced NF-κB activation by preventing loss of IκB-α and -β. Furthermore, SA blocked phosphorylation of extracellular signal-regulated kinase 1/2 (Erk1/2), but not phosphorylation of p38 and c-Jun N-terminal kinase. SA treatment resulted in the disappearance of Raf-1, suggesting that it might cause the inhibition of the Erk1/2 mitogen-activated protein (MAP) kinase pathway. The SA-mediated loss of Raf-1 also abolished LPS-induced NF-κB activation as well as the Erk1/2 pathway. The dominant negative mutant of MAP kinase kinase 1 inhibited both NO production and NF-κB activation in LPS-stimulated RAW cells. Taken together, these results indicate that the inhibitory action of SA on NO production in LPS-stimulated macrophages might be due to abrogation of inducible NO synthase induction, and it might be closely related to inactivation of the NF-κB and Erk1/2 MAP kinase pathways through loss of Raf-1.

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“…Among the other potential molecules that are likely to be recruited and participate in optimal signaling for gene expression, small G proteins (reviewed in Ref. 65), heat shock protein 90 (66), and others have been implicated in LPS-and/or Taxol-induced macrophage activation. The role of CD11b/CD18 might be analogous to that of CD14, where CD11b/CD18 functions to bind Taxol (via CD18) and LPS, whereas associated TLR4 molecules function as signal transducing receptors.…”

Section: Figurementioning

confidence: 99%

CD11b/CD18 Acts in Concert with CD14 and Toll-Like Receptor (TLR) 4 to Elicit Full Lipopolysaccharide and Taxol-Inducible Gene Expression

Perera

Mayadas

Takeuchi

et al. 2001

The Journal of Immunology

372

285

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Overproduction of inflammatory mediators by macrophages in response to Gram-negative LPS has been implicated in septic shock. Recent reports indicate that three membrane-associated proteins, CD14, CD11b/CD18, and Toll-like receptor (TLR) 4, may serve as LPS recognition and/or signaling receptors in murine macrophages. Therefore, the relative contribution of these proteins in the induction of cyclooxygenase 2 (COX-2), IL-12 p35, IL-12 p40, TNF-α, IFN-inducible protein (IP)-10, and IFN consensus sequence binding protein (ICSBP) genes in response to LPS or the LPS-mimetic, Taxol, was examined using macrophages derived from mice deficient for these membrane-associated proteins. The panel of genes selected reflects diverse macrophage effector functions that contribute to the pathogenesis of septic shock. Induction of the entire panel of genes in response to low concentrations of LPS or Taxol requires the participation of both CD14 and TLR4, whereas high concentrations of LPS or Taxol elicit the expression of a subset of LPS-inducible genes in the absence of CD14. In contrast, for optimal induction of COX-2, IL-12 p35, and IL-12 p40 genes by low concentrations of LPS or by all concentrations of Taxol, CD11b/CD18 was also required. Mitigated induction of COX-2, IL-12 p35, and IL-12 p40 gene expression by CD11b/CD18-deficient macrophages correlated with a marked inhibition of NF-κB nuclear translocation and mitogen-activated protein kinase (MAPK) activation in response to Taxol and of NF-κB nuclear translocation in response to LPS. These findings suggest that for expression of a full repertoire of LPS-/Taxol-inducible genes, CD14, TLR4, and CD11b/CD18 must be coordinately engaged to deliver optimal signaling to the macrophage.

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Heat shock protein 90 mediates macrophage activation by Taxol and bacterial lipopolysaccharide

Abstract: Taxol, a plant-derived antitumor agent, stabilizes microtubules. Taxol

Cited by 190 publications

References 51 publications

Differential expression of three Paralichthys olivaceus Hsp40 genes in responses to virus infection and heat shock☆

Differential expression of three Paralichthys olivaceus Hsp40 genes in responses to virus infection and heat shock☆

The Inhibitory Action of Sodium Arsenite on Lipopolysaccharide-Induced Nitric Oxide Production in RAW 267.4 Macrophage Cells: A Role of Raf-1 in Lipopolysaccharide Signaling

CD11b/CD18 Acts in Concert with CD14 and Toll-Like Receptor (TLR) 4 to Elicit Full Lipopolysaccharide and Taxol-Inducible Gene Expression

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