Trp-Arg-Trp-Trp-Trp-Trp antagonizes formyl peptide receptor like 2-mediated signaling

Shin, Eun Ha; Lee, Ha-Young; Kim, Sang Doo; Jo, Seong Ho; Park, Kyoung Sun; Lee, Hyuck; Bae, Yoe‐Sik

doi:10.1016/j.bbrc.2006.01.098

Cited by 20 publications

(21 citation statements)

References 21 publications

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“…4A ), indicating that FPR1 does not play a major role in neutrophil stimulation by SLUSH peptides. However, the FPR2 inhibitor WRW4 (31) blocked neutrophil responses to all three SLUSH peptides completely indicating that neutrophils sense SLUSH peptides mainly via FPR2 (Fig. 4 A ).…”

Section: Resultsmentioning

confidence: 94%

Neutrophil responses to staphylococcal pathogens and commensals via the formyl peptide receptor 2 relates to phenol‐soluble modulin release and virulence

et al. 2010

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The mechanisms used by the immune system to discriminate between pathogenic and commensal bacteria have remained largely unclear. Recently, we have shown that virulence of Staphylococcus aureus depends on secretion of phenol-soluble modulin (PSM) peptides that disrupt neutrophils at micromolar concentrations. Moreover, all S. aureus PSMs stimulate and attract neutrophils at nanomolar concentrations via interaction with the formyl-peptide receptor 2 (FPR2). Here, we demonstrate that FPR2 allows neutrophils to adjust their responses in relation to the aggressiveness of staphylococcal species, which differ largely in their capacity to infect or colonize humans and animals. PSM-related peptides were detected in all human and animal pathogenic staphylococci, but were absent from most commensal species. Three PSMβ-like peptides produced by the serious human pathogen Staphylococcus lugdunensis were identified as the previously described S. lugdunensis-synergistic hemolysins (SLUSHs). SLUSHs attracted and stimulated human leukocytes in a FPR2-dependent manner, indicating that FPR2 is a general receptor for all PSM-like peptide toxins. Remarkably, the release of PSMs correlated closely with the apparent capacity of staphylococcal species to cause invasive infections and with their ability to activate FPR2. These findings suggest that the innate immune system may be able to respond in different ways to pathogenic or innocuous staphylococci by monitoring the presence of PSMs via FPR2.

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Section: Resultsmentioning

confidence: 94%

Neutrophil responses to staphylococcal pathogens and commensals via the formyl peptide receptor 2 relates to phenol‐soluble modulin release and virulence

et al. 2010

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“…LXA 4 itself did not modify the number of released EMVs (results not shown). To establish receptor dependence of this effect, we exposed HUVECs to WRW 4 , a selective ALX/FPR2 antagonist (42). As illustrated in Fig.…”

Section: Resultsmentioning

confidence: 99%

Lipoxin A₄stimulates endothelial miR‐126–5p expression and its transfer via microvesicles

et al. 2017

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The proresolution lipid mediator lipoxin (LX)A bestows protective bioactions on endothelial cells. We examined the impact of LXA on transcellular endothelial signaling microRNA (miR)-containing microvesicles. We report LXA inhibition of MV release by TNF-α-treated HUVECs, associated with the down-regulation of 18 miR in endothelial microvesicles (EMVs) and the up-regulation of miR-126-5p, both in HUVECs and in EMVs. LXA up-regulated miR-126-5p by ∼5-fold in HUVECs and promoted a release of microvesicles (LXA-EMVs) that enhanced miR-126-5p by ∼7-fold in recipient HUVECs. In these cells, LXA-EMVs abrogated the up-regulation of VCAM-1, induced in recipient HUVECs by EMVs released by untreated or TNF-α-treated HUVECs. LXA-EMVs also reduced by ∼40% the expression of SPRED1, which we validated as an miR-126-5p target, whereas they stimulated monolayer repair in an wound assay. This effect was lost when the EMVs were depleted of miR-126-5p. These results provide evidence that changes in miR expression and microvesicle packaging and transfer represent a mechanism of action of LXA, which may be relevant in vascular biology and inflammation.-Codagnone, M., Recchiuti, A., Lanuti, P., Pierdomenico, A. M., Cianci, E., Patruno, S., Mari, V. C., Simiele, F., Di Tomo, P., Pandolfi, A., Romano, M. Lipoxin A stimulates endothelial miR-126-5p expression and its transfer microvesicles.

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“…N-formylmethionyl-leucyl-phenylalanine (fMLF) has been widely used to study the biological effects of FPRs (47). The cyclic undecapeptide cyclosporin H (CsH) is a potent FPR1 inhibitor (45), whereas the peptide WRW4 is a FPR2 and FPR3 antagonist (4,37). ANXA1 and its peptides bind to all human FPRs.…”

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confidence: 99%

Annexin A1 modulates macula densa function by inhibiting cyclooxygenase 2

Seidel

Neymeyer

Kahl

et al. 2012

American Journal of Physiology-Renal Physiology

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Annexin A1 (ANXA1) exerts anti-inflammatory effects through multiple mechanisms including inhibition of prostaglandin synthesis. Once secreted, ANXA1 can bind to G protein-coupled formyl peptide receptors (Fpr) and activate diverse cellular signaling pathways. ANXA1 is known to be expressed in cells of the juxtaglomerular apparatus, but its relation to the expression of cyclooxygenase 2 (COX-2) in thick ascending limb and macula densa cells has not been elucidated. We hypothesized that ANXA1 regulates the biosynthesis of COX-2. ANXA1 abundance in rat kidney macula densa was extensively colocalized with COX-2 (95%). Furosemide, an established stimulus for COX-2 induction, caused enhanced expression of both ANXA1 and COX-2 with maintained colocalization (99%). In ANXA1-deficient mice, COX-2-positive cells were more numerous than in control mice (+107%; normalized to glomerular number; P < 0.05) and renin expression was increased (+566%; normalized to glomerular number; P < 0.05). Cultured macula densa cells transfected with full-length rat ANXA1 revealed downregulation of COX-2 mRNA (-59%; P < 0.05). Similarly, treatment with dexamethasone suppressed COX-2 mRNA in the cells (-49%; P < 0.05), while inducing ANXA1 mRNA (+56%; P < 0.05) and ANXA1 protein secretion. Inhibition of the ANXA-1 receptor Fpr1 with cyclosporin H blunted the effect of dexamethasone on COX-2 expression. These data show that ANXA1 exerts an inhibitory effect on COX-2 expression in the macula densa. ANXA1 may be a novel intrinsic modulator of renal juxtaglomerular regulation by inhibition of PGE(2) synthesis.

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Trp-Arg-Trp-Trp-Trp-Trp antagonizes formyl peptide receptor like 2-mediated signaling

Cited by 20 publications

References 21 publications

Neutrophil responses to staphylococcal pathogens and commensals via the formyl peptide receptor 2 relates to phenol‐soluble modulin release and virulence

Neutrophil responses to staphylococcal pathogens and commensals via the formyl peptide receptor 2 relates to phenol‐soluble modulin release and virulence

Lipoxin A₄stimulates endothelial miR‐126–5p expression and its transfer via microvesicles

Annexin A1 modulates macula densa function by inhibiting cyclooxygenase 2

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Trp-Arg-Trp-Trp-Trp-Trp antagonizes formyl peptide receptor like 2-mediated signaling

Cited by 20 publications

References 21 publications

Neutrophil responses to staphylococcal pathogens and commensals via the formyl peptide receptor 2 relates to phenol‐soluble modulin release and virulence

Neutrophil responses to staphylococcal pathogens and commensals via the formyl peptide receptor 2 relates to phenol‐soluble modulin release and virulence

Lipoxin A4stimulates endothelial miR‐126–5p expression and its transfer via microvesicles

Annexin A1 modulates macula densa function by inhibiting cyclooxygenase 2

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Lipoxin A₄stimulates endothelial miR‐126–5p expression and its transfer via microvesicles