Human S100A9 potentiates IL‐8 production in response to GM‐CSF or fMLP via activation of a different set of transcription factors in neutrophils

Simard, Jean-Christophe; Noël, Claudie; Tessier, Philippe A.; Girard, Denis

doi:10.1016/j.febslet.2014.04.027

Cited by 36 publications

(26 citation statements)

References 34 publications

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“…In Simard et al [24], a low level of tyrosine phosphorylation of intracellular substrates in neutrophils exposed to a higher concentration of S100A9 (40 mg/ml) for the same length of time, 30 min, was also reported. We provide evidence that S100A9 is not a direct activator of the production of IL-1b in human neutrophils, an observation that corroborates the report by Simard et al [31].…”

Section: Discussionsupporting

confidence: 92%

“…Together, these data suggest that S100A9 primes neutrophils to express and activate the inflammasome in response to MSUs. It is of note that the priming property of S100A9 was previously reported in neutrophils for their response to pathogenic agonists, such as Escherichia coli and the bacterial Nformylated tripeptide fMLP [24,31]. The preincubation of human neutrophils with S100A9 primed their production of CXCL8/IL-8 in response to fMLP and their bactericidal activity toward E. coli.…”

Section: Discussionmentioning

confidence: 55%

“…Moreover, the phosphorylation of p38, a protein known to be involved in the priming of ROS production by human neutrophils in response to other stimuli, was also enhanced by S100A9 [27]. Regarding the molecular mechanisms underlying the priming of MSU-induced IL-1 production, S100A9 alone does not induce Ik B kinase-a/b phosphorylation in neutrophils, leading to incomplete activation of the NF-kB [31] necessary for the induced expression of NLRP3 and pro-IL-1b. Together, these data suggest that S100A9 primes neutrophils to express and activate the inflammasome in response to MSUs.…”

Section: Discussionmentioning

confidence: 95%

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S100A9 potentiates the activation of neutrophils by the etiological agent of gout, monosodium urate crystals

Rousseau

Paré

Lachhab

et al. 2017

Journal of Leukocyte Biology

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Gout is one of the most painful types of arthritis that arises when the body mounts an acute inflammatory reaction against a crystallized form of uric acid known as monosodium urate crystals (MSUs). Although MSUs are known to activate neutrophils, the most abundant leukocyte in the synovial fluid of patients with gout, few studies have investigated the effect on neutrophils of the simultaneous stimulation with MSU and proinflammatory mediators in the inflamed joint. Herein, we focused on a protein that is highly expressed in the synovium in gout, S100A9. The predominant expression of S100A9 in and around blood vessels suggests it may prime neutrophils during their migration toward the inflamed joint. Using a combination of functional and signaling assays, we found that S100A9 enhances the production of radical oxygen species as well as IL-1 and IL-8 release by human neutrophils activated with MSU. Moreover, upstream and downstream signaling events activated by MSUs in human neutrophils were also potentiated by S100A9, including the mobilization of intracellular calcium stores, tyrosine phosphorylation, the serine phosphorylation of PKC substrates, Akt, and p38. We also show that S100A9 alone increases glycolysis in human neutrophils, which is suggestive of an additional mechanism through which neutrophils can be primed. Together, our observations indicate a novel way in which S100A9 may contribute to the pathogenesis of gout, by priming neutrophils to respond to MSUs.

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Section: Discussionsupporting

confidence: 92%

Section: Discussionmentioning

confidence: 55%

Section: Discussionmentioning

confidence: 95%

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S100A9 potentiates the activation of neutrophils by the etiological agent of gout, monosodium urate crystals

Rousseau

Paré

Lachhab

et al. 2017

Journal of Leukocyte Biology

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“…Therefore, it is possible that the accumulated neutrophils in the depleted mice are the main source of inflammatory cytokines in synovial fluid, as neutrophils are capable of secreting IL-1, IL-6, and TNF-α. In addition, neutrophils can also produce IL-8, a potent chemokine for themselves, recruiting more granulocytes to inflammatory sites (34–36). Although IL-10, an anti-inflammatory molecule, was also found to be up-regulated in the synovial fluid in our model, its concentration may not be sufficient to counteract the catabolic effects of pro-inflammatory cytokines on the joint due to its relative low quantities compared to IL-1β (about 10-fold less).…”

Section: Discussionmentioning

confidence: 99%

Conditional Macrophage Depletion Increases Inflammation and Does Not Inhibit the Development of Osteoarthritis in Obese Macrophage Fas‐Induced Apoptosis–Transgenic Mice

McNeill

Goon

et al. 2017

Arthritis & Rheumatology

106

102

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Objective Macrophages are believed to play a critical role in the inflammation associated with the development of osteoarthritis (OA) in obesity. The objective of the study was to investigate whether short-term, systemic depletion of macrophages would mitigate OA following injury in obese mice. Methods CSF-1R–GFP+ Macrophage Fas-Induced Apoptosis (MaFIA) transgenic mice that allow conditional depletion of macrophages were placed on a high-fat diet and underwent surgery to induce knee OA. A small molecule (AP20187) was administrated to deplete macrophages in MaFIA mice. The effect of macrophage depletion on acute joint inflammation, OA severity, and arthritic bone changes were evaluated using histology and microCT. Immunohistochemistry was used to identify various immune cells. Serum and synovial fluid cytokines were also measured. Results Macrophage-depleted mice had significantly fewer M1 and M2 macrophages in the surgical operated-joints relative to controls and exhibited decreased osteophyte formation immediately following depletion. Surprisingly, macrophage depletion did not attenuate OA with obesity; instead, it induced systemic inflammation and led to a massive infiltration of CD3+ T cells and particularly neutrophils, but not B cells, into the injured joints. Macrophage-depleted mice also demonstrated markedly increased pro-inflammatory cytokines including granulocyte-colony stimulating factor (G-CSF), IL-1β, IL-6, IL-8, and TNF-α in both serum and joint synovial fluid, although animals showed trends for decreased serum insulin and leptin levels after depletion. Conclusion Our findings indicate that macrophages are vital in modulating the homeostasis of immune cells in obesity and suggest that more targeted approaches of different macrophage subtypes may be necessary to mitigate inflammation and OA with obesity.

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“…S100A8/A9 (calprotectin) is among the most abundant alarmins under conditions of sterile inflammation that are driven by endogenous danger signals and is used as biomarker for various autoimmune diseases, such as rheumatoid arthritis and Crohn's disease (20)(21)(22). S100A8/A9 signaling results in the production of proinflammatory mediators in a plethora of cell types, including endothelial cells, monocytes, macrophages, and neutrophils (19,(23)(24)(25)(26)(27)(28).…”

mentioning

confidence: 99%

The alarmin S100A9 hampers osteoclast differentiation from human circulating precursors by reducing the expression of RANK

Ceglie¹,

Blom²,

Davar

et al. 2019

FASEB j.

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The alarmin S100A8/A9 is implicated in sterile inflammation‐induced bone resorption and has been shown to increase the bone‐resorptive capacity of mature osteoclasts. Here, we investigated the effects of S100A9 on osteoclast differentiation from human CD14+ circulating precursors. Hereto, human CD14+ monocytes were isolated and differentiated toward osteoclasts with M‐CSF and receptor activator of NF‐κB (RANK) ligand (RANKL) in the presence or absence of S100A9. Tartrate‐resistant acid phosphatase staining showed that exposure to S100A9 during monocyte‐to‐osteoclast differentiation strongly decreased the numbers of multinucleated osteoclasts. This was underlined by a decreased resorption of a hydroxyapatite‐like coating. The thus differentiated cells showed a high mRNA and protein production of proinflammatory factors after 16 h of exposure. In contrast, at d 4, the cells showed a decreased production of the osteoclast‐promoting protein TNF‐α. Interestingly, S100A9 exposure during the first 16 h of culture only was sufficient to reduce osteoclastogenesis. Using fluorescently labeled RANKL, we showed that, within this time frame, S100A9 inhibited the M‐CSF‐mediated induction of RANK. Chromatin immunoprecipitation showed that this was associated with changes in various histone marks at the epigenetic level. This S100A9‐induced reduction in RANK was in part recovered by blocking TNF‐α but not IL‐1. Together, our data show that S100A9 impedes monocyte‐to‐osteoclast differentiation, probably via a reduction in RANK expression.—Di Ceglie, I., Blom, A. B., Davar, R., Logie, C., Martens, J. H. A., Habibi, E., Böttcher, L.‐M., Roth, J., Vogl, T., Goodyear, C. S., van der Kraan, P. M., van Lent, P. L., van den Bosch, M. H. The alarmin S100A9 hampers osteoclast differentiation from human circulating precursors by reducing the expression of RANK. FASEB J. 33, 10104–10115 (2019). http://www.fasebj.org

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Human S100A9 potentiates IL‐8 production in response to GM‐CSF or fMLP via activation of a different set of transcription factors in neutrophils

Cited by 36 publications

References 34 publications

S100A9 potentiates the activation of neutrophils by the etiological agent of gout, monosodium urate crystals

S100A9 potentiates the activation of neutrophils by the etiological agent of gout, monosodium urate crystals

Conditional Macrophage Depletion Increases Inflammation and Does Not Inhibit the Development of Osteoarthritis in Obese Macrophage Fas‐Induced Apoptosis–Transgenic Mice

The alarmin S100A9 hampers osteoclast differentiation from human circulating precursors by reducing the expression of RANK

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