Vasopressin augments TNBS‐induced colitis through enteric neuronal V 1a receptor‐mediated COX‐2‐dependent prostaglandin release from mast cells in mice

2018 ◽  
Vol 31 (2) ◽  
pp. e13493
Author(s):  
Dandan Dou ◽  
Lixin Chen ◽  
Hong Di ◽  
Zhuoran Song ◽  
Shirui Li ◽  
...  
Keyword(s):  
Mast Cells ◽  
Prostaglandin Release ◽  
Cox 2

scholarly journals Topical Spilanthol Inhibits MAPK Signaling and Ameliorates Allergic Inflammation in DNCB-Induced Atopic Dermatitis in Mice

2019 ◽  
Vol 20 (10) ◽  
pp. 2490 ◽  
Author(s):  
Wen-Chung Huang ◽  
Chun-Hsun Huang ◽  
Sindy Hu ◽  
Hui-Ling Peng ◽  
Shu-Ju Wu
Keyword(s):  
Atopic Dermatitis ◽  
Mast Cells ◽  
Protein Kinase ◽  
Allergic Inflammation ◽  
Skin Lesions ◽  
Mapk Signaling ◽  
Mitogen Activated Protein Kinase ◽  
Mapk Pathways ◽  
Mitogen Activated Protein ◽  
Cox 2

Atopic dermatitis (AD) is a recurrent allergic skin disease caused by genetic and environmental factors. Patients with AD may experience immune imbalance, increased levels of mast cells, immunoglobulin (Ig) E and pro-inflammatory factors (Cyclooxygenase, COX-2 and inducible NO synthase, iNOS). While spilanthol (SP) has anti-inflammatory and analgesic activities, its effect on AD remains to be explored. To develop a new means of SP, inflammation-related symptoms of AD were alleviated, and 2,4-dinitrochlorobenzene (DNCB) was used to induce AD-like skin lesions in BALB/c mice. Histopathological analysis was used to examine mast cells and eosinophils infiltration in AD-like skin lesions. The levels of IgE, IgG1 and IgG2a were measured by enzyme-linked immunosorbent assay (ELISA) kits. Western blot was used for analysis of the mitogen-activated protein kinase (MAPK) pathways and COX-2 and iNOS protein expression. Topical SP treatment reduced serum IgE and IgG2a levels and suppressed COX-2 and iNOS expression via blocked mitogen-activated protein kinase (MAPK) pathways in DNCB-induced AD-like lesions. Histopathological examination revealed that SP reduced epidermal thickness and collagen accumulation and inhibited mast cells and eosinophils infiltration into the AD-like lesions skin. These results indicate that SP may protect against AD skin lesions through inhibited MAPK signaling pathways and may diminish the infiltration of inflammatory cells to block allergic inflammation.

scholarly journals Role of mast cells and protease-activated receptor-2 in cyclooxygenase-2 expression in urothelial cells

2009 ◽  
Vol 297 (4) ◽  
pp. R1127-R1135 ◽  
Author(s):  
Zun-Yi Wang ◽  
Peiqing Wang ◽  
Dale E. Bjorling
Keyword(s):  
Mast Cell ◽  
Mast Cells ◽  
Primary Cultures ◽  
Cyclooxygenase 2 ◽  
Protein Abundance ◽  
Urothelial Cells ◽  
Cellular Mechanisms ◽  
Bladder Inflammation ◽  
Cox 2 ◽  
Protease Activated Receptor 2

Mast cells have been shown to play a role in development and persistence of various inflammatory bladder disorders. Mast cell-derived tryptase specifically activates protease-activated receptor-2 (PAR-2), and PAR-2 is known to be involved in inflammation. We investigated whether mast cells participate in increase of cyclooxygenase-2 (COX-2) protein abundance in urothelium/suburothelium of bladders of mice subsequent to cyclophosphamide (CYP)-induced bladder inflammation. We also used primary cultures of human urothelial cells to investigate cellular mechanisms underlying activation of PAR-2 resulting in increased COX-2 expression. We found that treatment of mice with CYP (150 mg/kg ip) increased COX-2 protein abundance in bladder urothelium/suburothelium 3, 6, and 24 h after CYP ( P < 0.01), and increased COX-2 protein abundance was prevented by treatment of mice with the mast cell stabilizer sodium cromolyn (10 mg/kg ip) for 4 consecutive days before CYP treatment. Incubation of freshly isolated mouse urothelium/suburothelium with a selective PAR-2 agonist, 2-furoyl-LIGRLO-amide (3 μM), also increased COX-2 protein abundance ( P < 0.05). We further demonstrated that 2-furoyl-LIGRLO-amide (3 μM) increased COX-2 mRNA expression and protein abundance in primary cultures of human urothelial cells ( P < 0.01), and the effects of PAR-2 activation were mediated primarily by the ERK1/2 MAP kinase pathway. These data indicate that there are functional interactions among mast cells, PAR-2 activation, and increased expression of COX-2 in bladder inflammation.

scholarly journals Cross-linking of the high-affinity IgE receptor induces the expression of cyclo-oxygenase 2 and attendant prostaglandin generation requiring interleukin 10 and interleukin 1β in mouse cultured mast cells

1996 ◽  
Vol 320 (3) ◽  
pp. 965-973 ◽  
Author(s):  
Musharraf ASHRAF ◽  
Makoto MURAKAMI ◽  
Ichiro KUDO
Keyword(s):  
Mast Cells ◽  
Mrna Level ◽  
Interleukin 10 ◽  
Second Phase ◽  
Mouse Bone Marrow ◽  
Cox 2 ◽  
The Individual ◽  
High Affinity Ige Receptor ◽  
Delayed Phase ◽  
Cox 1

When mouse bone marrow-derived mast cells (BMMC) developed in interleukin (IL)-3 were activated with IgE and antigen (IgE/antigen) in the presence of both IL-10 and IL-1β, two sequential phases of prostaglandin (PG)D2 generation were elicited, in which the first phase occurred by 1 h and the second phase from 2 to 10 h. The delayed phase of PGD2 generation was accompanied by a marked induction of cyclo-oxygenase (COX)-2 mRNA, which reached a peak at 1–2 h, followed by that of its protein from 2–10 h, with a peak at 5 h. The immediate phase of PGD2 generation was completely abrogated by the irreversible inhibition of pre-exisiting COX-1 by aspirin pretreatment, whereas the delayed phase of PGD2 generation was almost undetectable in the presence of the COX-2 inhibitor NS-398. A detailed analysis of the individual effects of IgE/antigen, IL-10 and IL-1β on COX-2 expression revealed that IgE/antigen and IL-10 each initiated and stabilized COX-2 mRNA expression, leading to an increase in the expression of its protein. Conversely, IL-1β stabilized the COX-2 protein without affecting its mRNA level. The induction of COX-2 by IgE/antigen with IL-10 and IL-1β preceded the induction of transcripts for endogenous cytokines such as IL-6, IL-1β and IL-10. The inhibition of PGD2 generation by indomethacin did not affect the induction of COX-2 or these cytokines. Thus the two major delayed-phase responses of BMMC after IgE-dependent activation, namely COX-2-dependent PGD2 generation and cytokine production, are regulated independently.

scholarly journals Differential usage of COX-1 and COX-2 in prostaglandin production by mast cells and basophils

2017 ◽  
Vol 10 ◽  
pp. 82-87 ◽  
Author(s):  
Tomoyuki Bando ◽  
Setsuko Fujita ◽  
Naoko Nagano ◽  
Soichiro Yoshikawa ◽  
Yoshinori Yamanishi ◽  
...  
Keyword(s):  
Mast Cells ◽  
Prostaglandin Production ◽  
Cox 2 ◽  
Cox 1

scholarly journals Resident peritoneal macrophages and mast cells are important cellular sites of COX-1 and COX-2 activity during acute peritoneal inflammation

2009 ◽  
Vol 57 (6) ◽  
pp. 459-466 ◽  
Author(s):  
Elzbieta Kolaczkowska ◽  
Anna Goldys ◽  
Elzbieta Kozakiewicz ◽  
Monika Lelito ◽  
Barbara Plytycz ◽  
...  
Keyword(s):  
Mast Cells ◽  
Peritoneal Macrophages ◽  
Peritoneal Inflammation ◽  
Cox 2 ◽  
Cox 1

Differential Regulation of Cyclo-Oxygenase-1 and Cyclo-Oxygenase-2 Gene Expression by Lipopolysaccharide Treatment in vivo in the Rat

1996 ◽  
Vol 90 (4) ◽  
pp. 301-306 ◽  
Author(s):  
Shu Fang Liu ◽  
Robert Newton ◽  
Timothy W. Evans ◽  
Peter J. Barnes
Keyword(s):  
Mrna Expression ◽  
Down Regulation ◽  
Physiological Conditions ◽  
Prostaglandin Release ◽  
Key Enzyme ◽  
Cox 2 ◽  
Oxide Synthase ◽  
Cox 1 ◽  
Inducible Nitric Oxide

1. Prostaglandins are important regulatory mediators of cardiovascular and pulmonary functions which may become disordered in patients with sepsis. The mechanisms controlling their synthesis and release under these circumstances remain unclear. Cyclo-oxygenase (COX, prostaglandin G/H synthase) is a key enzyme in prostaglandin synthesis and has two isoforms (COX-1 and COX-2). COX-1 is constitutively expressed and is probably responsible for prostaglandin release under physiological conditions, whereas COX-2 is expressed at high levels upon induction. 2. We investigated the effect of lipopolysaccharide treatment in vivo on differential COX-1 and COX-2 mRNA expression in the rat. 3. The 2.8 kb COX-1 message was detected in all lungs and seven hearts of eight control rats. In lipopolysaccharide-treated animals, COX-1 expression was reduced by approximately 5-fold in lungs and 2-fold in hearts as quantified by densitometry. In parallel, a marked upregulation of COX-2 mRNA expression was observed. The 4.4 kb COX-2 transcript was absent or expressed at low level in control lungs and hearts, but was increased by approximately 7- and 12-fold in lipopolysaccharide-treated lungs and hearts respectively. Neither the down-regulation of COX-1 nor the upregulation of COX-2 mRNA induced by lipopolysaccharide was significantly affected by pretreatment with dexamethasone in lung and heart, although expression of inducible nitric oxide synthase, induced by lipopolysaccharide, was markedly inhibited in the same tissues. 4. The down-regulation of COX-1 and upregulation of COX-2 may contribute to the multi-organ failure seen in sepsis.

Genetic Evidence for Distinct Roles of COX-1 and COX-2 in the Immediate and Delayed Phases of Prostaglandin Synthesis in Mast Cells

1999 ◽  
Vol 265 (1) ◽  
pp. 205-210 ◽  
Author(s):  
Srinivasa T. Reddy ◽  
Howard F. Tiano ◽  
Robert Langenbach ◽  
Scott G. Morham ◽  
Harvey R. Herschman
Keyword(s):  
Mast Cells ◽  
Prostaglandin Synthesis ◽  
Genetic Evidence ◽  
Cox 2 ◽  
Cox 1

Histamine-dependent prolongation by aldosterone of vasoconstriction in isolated small mesenteric arteries of the mouse

2013 ◽  
Vol 304 (8) ◽  
pp. H1094-H1102 ◽  
Author(s):  
Jeppe Schjerning ◽  
Torben R. Uhrenholt ◽  
Per Svenningsen ◽  
Paul M. Vanhoutte ◽  
Ole Skøtt ◽  
...  
Keyword(s):  
Mast Cells ◽  
Receptor Antagonist ◽  
Vascular Function ◽  
Mesenteric Arteries ◽  
Wild Type ◽  
Rt Pcr ◽  
No Donor ◽  
High K ◽  
Cox 2 ◽  
Cox 1

In arterioles, aldosterone counteracts the rapid dilatation (recovery) following depolarization-induced contraction. The hypothesis was tested that this effect of aldosterone depends on cyclooxygenase (COX)-derived products and/or nitric oxide (NO) synthase (NOS) inhibition. Recovery of the response to high K+ was observed in mesenteric arteries of wild-type and COX-2−/− mice but it was significantly diminished in preparations from endothelial NOS (eNOS)−/− mice. Aldosterone pretreatment inhibited recovery from wild-type and COX-2−/− mice. The NO donor sodium nitroprusside (SNP) restored recovery in arteries from eNOS−/− mice, and this was inhibited by aldosterone. Actinomycin-D abolished the effect of aldosterone, indicating a genomic effect. The effect was blocked by indomethacin and by the COX-1 inhibitor valeryl salicylate but not by NS-398 (10−6 mol/l) or the TP-receptor antagonist S18886 (10−7 mol/l). The effect of aldosterone on recovery in arteries from wild-type mice and the SNP-mediated dilatation in arteries from eNOS−/− mice was inhibited by the histamine H2 receptor antagonist cimetidine. RT-PCR showed expression of mast cell markers in mouse mesenteric arteries. The adventitia displayed granular cells positive for toluidine blue vital stain. Confocal microscopy of live mast cells showed loss of quinacrine fluorescence and swelling after aldosterone treatment, indicating degranulation. RT-PCR showed expression of mineralocorticoid receptors in mesenteric arteries and in isolated mast cells. These findings suggest that aldosterone inhibits recovery by stimulation of histamine release from mast cells along mesenteric arteries. The resulting activation of H2 receptors decreases the sensitivity to NO of vascular smooth muscle cells. Aldosterone may chronically affect vascular function through paracrine release of histamine.

scholarly journals Suppressive role of PPARγ in the IgE-dependent activation of mast cells

2019 ◽  
Author(s):  
Kazuki Nagata ◽  
Kazumi Kasakura ◽  
Ryosuke Miura ◽  
Takuya Yashiro ◽  
Chiharu Nishiyama
Keyword(s):  
Mast Cells ◽  
Expression Level ◽  
Cell Surface Expression ◽  
Mrna Levels ◽  
Cox Inhibitor ◽  
Pparγ Agonist ◽  
Ige Mediated ◽  
Cox 2 ◽  
Cox 1

Abstract Mast cells (MCs) play a central role in IgE-dependent immune responses. PPARγ is a nuclear receptor that is essential for adipocyte differentiation and insulin sensitivity. Although PPARγ is expressed in activated MCs, the effect of PPARγ suppression in IgE-mediated activation of MCs is largely unknown. In the current study, we evaluated the effect of PPARγ knockdown on the function of IgE plus antigen (Ag)-stimulated MCs using siRNA-transfected BMMCs. We found that the mRNA expression level of cytokines in IgE/Ag-stimulated BMMCs was significantly increased in PPARγ knockdown BMMCs, and IgE/Ag-mediated degranulation and the protein production level of TNF-α was moderately increased by PPARγ knockdown, whereas the cell surface expression level of FcεRI was not affected by PPARγ knockdown. Oral administration of pioglitazone (PPARγ agonist) significantly suppressed body temperature change of mice in passive systemic anaphylaxis, supporting the inhibitory functions of PPARγ in IgE/Ag-dependent activation of MCs in vivo. IgE-mediated upregulation of mRNA levels of Ptgs2 (encoding COX-2) was drastically enhanced in PPARγ knockdown BMMCs. Although several prostaglandin (PG) derivatives are known to be ligands for PPARγ, treatment with a COX inhibitor, acetyl salicylic acid, upregulated the IgE-mediated increase of Il13, Tnf, and Ptgs2 mRNA levels in a synergistic manner with PPARγ siRNA. Knockdown of COX-1 and/or COX-2 by siRNA showed that suppression of IgE/Ag-mediated activation was mainly dependent on COX-1. Taken together, these results indicate that PPARγ suppresses IgE/Ag-induced transactivation of cytokine genes and the Ptgs2 gene in MCs in a manner distinguishable from that of PGs.

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