anisomycin and Inflammation

anisomycin has been researched along with Inflammation* in 11 studies

Other Studies

11 other study(ies) available for anisomycin and Inflammation

ArticleYear
The protective effects of glutamine against bronchopulmonary dysplasia are associated with MKP-1/MAPK/cPLA2 signalingmediated NF-kappaB pathway.
    General physiology and biophysics, 2023, Volume: 42, Issue:3

    Glutamine is proven to have potential therapeutic effects on decreasing hyperoxia-induced acute pulmonary injury. The aim of this study is to investigate the effects and mechanism of glutamine on bronchopulmonary dysplasia (BPD) induced by hyperoxia in rat alveolar type II epithelial cells (AECIIs) RLE-6TN. Following hyperoxia induction and glutamine treatment, ROS levels were detected by DCFH-DA assay and TUNEL staining was performed to detect cell apoptosis. The levels of inflammatory indicators and expression of apoptosis-related proteins were detected through ELISA and Western blot, respectively. Besides, the expression of related proteins in mitogen-activated protein kinase phosphatase-1 (MKP-1)/mitogen-activated protein kinases (MAPK)/cytoplasmic phospholipase A2 (cPLA2) signaling was also detected by Western blot. To further analyze the role of MKP-1/MAPK/cPLA2 signaling, MKP-1 was silenced and anisomycin was used to treat cells, respectively. It was shown that glutamine significantly decreased inflammation, oxidative stress and apoptosis in hyperoxia-induced cells while MKP-1 interference and anisomycin were able to reverse these effects, suggesting that the protective effects of glutamine on BPD induced by hypoxia were related to MKP-1/MAPK/cPLA2 signaling. To sum up, glutamine protected against BPD by decreasing inflammation, oxidative stress and apoptosis via MKP-1/MAPK/cPLA2 signaling.

    Topics: Animals; Anisomycin; Bronchopulmonary Dysplasia; Glutamine; Hyperoxia; Inflammation; Mitogen-Activated Protein Kinases; NF-kappa B; Phospholipases A2; Rats

2023
Dexmedetomidine alleviates hyperalgesia in arthritis rats through inhibition of the p38MAPK signaling pathway.
    Immunopharmacology and immunotoxicology, 2022, Volume: 44, Issue:4

    Dexmedetomidine (DEX) has showed significant analgesic effects in neuropathic pain, but the underlying mechanism has remained elusive. Our present study aimed to explore the effect of DEX on hyperalgesia with the involvement of p38MAPK signaling pathway in a rat model of monoarthritis (MA).. MA rat model was induced by injection of Complete Freund's Adjuvant (CFA). Pathological changes of MA rats were observed by HE staining and Safranin-O/Fast Green staining. Ankle circumference, paw withdrawal latency (PWL) and paw withdrawal threshold (PWT) were measured to judge the degree of hyperalgesia in MA rats. Immunohistochemistry and ELISA were applied to observe the degree of inflammation in rats. Western blot analysis was conducted to detect expression of p38MAPK signaling pathway-related factors. The mechanism of p38MAPK signaling pathway in MA rats was observed. After 8 h of CFA induction, joint swelling and hyperalgesia occurred in rats. There were obvious pathological changes in the joint cavity, the joint cavity space became narrow and synovial bursa became rough. A large number of inflammatory cell infiltration was observed under microscope. After injection of DEX and SB203580, PWT and PWL were prolonged, the expression of serum inflammatory factors was decreased, and the expression of p38MAPK signaling pathway-related factors was decreased; while all the detected indexes were recovered in MA rats after treated with DEX and Anisomycin.. Our study provided evidence that DEX could alleviate hyperalgesia in arthritis rats through inhibition of the p38MAPK signaling pathway.

    Topics: Animals; Anisomycin; Arthritis; Dexmedetomidine; Freund's Adjuvant; Hyperalgesia; Inflammation; MAP Kinase Signaling System; Rats; Rats, Sprague-Dawley

2022
Lipoxin A4-Mediated p38 MAPK Signaling Pathway Protects Mice Against Collagen-Induced Arthritis.
    Biochemical genetics, 2021, Volume: 59, Issue:1

    The aim of the article was to study the mechanism of Lipoxin A4 (LXA4)-mediated p38 MAPK pathway protecting mice against collagen-induced arthritis (CIA). The impact of LXA4 (0, 5, 10, 15 nM) on synoviocytes proliferation of CIA mice was detected using 3-(4,5-Dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay. CIA mice were treated with LXA4, SB203580 (a p38 inhibitor), and/or anisomycin (a p38 agonist), and the arthritis severity score in each mouse was determined. The gene or protein expressions were detected with Western Blotting, ELISA, or qRT-PCR. LXA4 inhibited the synoviocytes proliferation of CIA mice with decreased levels of TNF-α, IL-6, IL-1β, and IFN-γ and reduced p-p38/total p38 expression in synoviocytes in a dose-dependent manner. LXA4 levels were decreased in synovial tissues and plasma of CIA mice, but p-p38/total p38 expression was increased in synovial tissues. LXA4 could downregulate p-p38/total p38 expression in synovial tissues of CIA mice. Both LXA4 and SB203580 reduced arthritis severity score of CIA mice with the reduction of synovial tissue hyperplasia and inflammatory cell infiltration. CIA mice treated with LXA4 and SB203580 had lower levels of TNF-α, IL-6, IL-1β, and IFN-γ, accompanying decreased MDA as well as increased SOD, CAT,and GPx. However, anisomycin could reverse the protect effects of LXA4 on CIA mice regarding the abovementioned inflammatory factors and oxidative stress indexes. LXA4 protected mice against collagen-induced arthritis via inhibiting p38 MAPK signaling pathway, which may be a potential new therapeutic target for rheumatoid arthritis.

    Topics: Animals; Anisomycin; Arthritis, Experimental; Arthritis, Rheumatoid; Cell Proliferation; Collagen; Female; Imidazoles; Inflammation; Lipoxins; MAP Kinase Signaling System; Mice; Mice, Inbred DBA; Oxidative Stress; p38 Mitogen-Activated Protein Kinases; Pyridines; Signal Transduction; Synovial Membrane

2021
Anisomycin protects against sepsis by attenuating IκB kinase-dependent NF-κB activation and inflammatory gene expression.
    BMB reports, 2021, Volume: 54, Issue:11

    Anisomycin is known to inhibit eukaryotic protein synthesis and has been established as an antibiotic and anticancer drug. However, the molecular targets of anisomycin and its mechanism of action have not been explained in macrophages. Here, we demonstrated the anti-inflammatory effects of anisomycin both in vivo and in vitro. We found that anisomycin decreased the mortality rate of macrophages in cecal ligation and puncture (CLP)- and lipopolysaccharide (LPS)-induced acute sepsis. It also declined the gene expression of proinflammatory mediators such as inducible nitric oxide synthase, tumor necrosis factor-α, and interleukin-1β as well as the nitric oxide and proinflammatory cytokines production in macrophages subjected to LPS-induced acute sepsis. Furthermore, anisomycin attenuated nuclear factor (NF)-κB activation in LPS-induced macrophages, which correlated with the inhibition of phosphorylation of NF-κBinducing kinase and IκB kinase, phosphorylation and IκBα proteolytic degradation, and NF-κB p65 subunit nuclear translocation. These results suggest that anisomycin prevented acute inflammation by inhibiting NF-κB-related inflammatory gene expression and could be a potential therapeutic candidate for sepsis. [BMB Reports 2021; 54(11): 545-550].

    Topics: Animals; Anisomycin; Female; Gene Expression Regulation; I-kappa B Proteins; Inflammation; Inflammation Mediators; Lipopolysaccharides; Mice; Mice, Inbred C57BL; NF-kappa B; Nitric Oxide; Protein Synthesis Inhibitors; Sepsis

2021
Glucocorticoids reduce inflammation in cystic fibrosis bronchial epithelial cells.
    Cellular signalling, 2012, Volume: 24, Issue:5

    Reduction of lung inflammation is one of the goals of cystic fibrosis (CF) therapy. Among anti-inflammatory molecules, glucocorticoids (GC) are one of the most prescribed. However, CF patients seem to be resistant to glucocorticoid treatment. Several molecular mechanisms that contribute to decrease anti-inflammatory effects of glucocorticoids have been identified in pulmonary diseases, but the molecular actions of glucocorticoids have never been studied in CF. In the cytoplasm, glucocorticoids bind to glucocorticoid receptor (GR) and then, control NF-κB and MAPK pathways through direct interaction with AP-1 and NF-κB in the nucleus. Conversely, MAPK can regulate glucocorticoid activation by targeting GR phosphorylation. Together these pathways regulate IL-8 release in the lung. Using bronchial epithelial cell lines derived from non CF and CF patients, we analyzed GR-based effects of glucocorticoids on NF-κB and MAPK pathways, after stimulation with TNF-α. We demonstrate that the synthetic glucocorticoid dexamethasone (Dex) significantly decreases IL-8 secretion, AP-1 and NF-κB activity in CF cells in a pro-inflammatory context. Moreover, we show that p38 MAPK controls IL-8 release by determining GR activation through specific phosphorylation on serine 211. Finally, we demonstrate a synergistic effect of dexamethasone treatment and inhibition of p38 MAPK inducing more than 90% inhibition of IL-8 production in CF cells. All together, these results demonstrate the good responsiveness to glucocorticoids of CF bronchial epithelial cells and the reciprocal link between glucocorticoids and p38 MAPK in the control of CF lung inflammation.

    Topics: Anisomycin; Anti-Inflammatory Agents; Bronchioles; Cell Line; Cystic Fibrosis; Dexamethasone; Enzyme Induction; Epithelial Cells; Glucocorticoids; Humans; Inflammation; Interleukin-8; NF-kappa B; p38 Mitogen-Activated Protein Kinases; Phosphorylation; Protein Transport; Receptors, Glucocorticoid; Signal Transduction; Transcription Factor AP-1; Transcriptional Activation

2012
Increased cell apoptosis of urothelium mediated by inflammation in interstitial cystitis/painful bladder syndrome.
    Urology, 2012, Volume: 79, Issue:2

    To investigate whether bladder inflammation could directly modulate the signaling pathway of increased urothelial cell apoptosis in interstitial cystitis/painful bladder syndrome (IC/PBS). Chronic inflammation and impaired urothelial homeostasis are possible pathogenesis of IC/PBS.. A total of 29 patients with IC/PBS and 5 control patients were enrolled in the present study. Double stain, protein array analysis, and Western blotting were performed to analyze the alterations of caspase 3, Bad, Bax, phospho-p53, phospho-p38α, and tumor necrosis factor-α (TNF-α) in bladder mucosa specimens from patients with IC/PBS and control patients. The intensities of the proteins in the arrays and Western blots were quantified using ImageJ processing. Inflammatory molecule-treated urothelial cells were analyzed using terminal deoxynucleotidyl transferase-mediated deoxyuridine triphosphate nick end labeling staining and Western blotting for the level of molecules involved in apoptosis.. Phospho-p38 and terminal deoxynucleotidyl transferase-mediated deoxyuridine triphosphate nick end labeling double staining indicated that inflammatory and apoptotic events coexisted in the IC/PBS bladder. Protein-antibody array analysis showed that several inflammatory molecules were increased in the IC/PBS samples. We also found that the levels of pro-apoptotic proteins, including phospho-p53 (Ser 15), Bad, Bax, and cleaved caspase-3 were significantly increased in the IC/PBS bladders. These results were confirmed by immunoblotting and suggested that the tissue damage and abnormal urothelium in the IC/PBS bladder might be regulated concurrently by inflammatory signals, such as p38 mitogen-activated protein kinase and TNF-α. The in vitro analysis also showed that the apoptotic process could be induced by TNF-α treatment and anisomycin stimulation in normal urothelial cells.. Apoptosis of urothelial cells in patients with IC/PBS could result from upregulation of inflammatory signals, including p38 mitogen-activated protein kinase and TNF-α.

    Topics: Anisomycin; Apoptosis; bcl-2-Associated X Protein; bcl-Associated Death Protein; Caspase 3; Cells, Cultured; Cystitis, Interstitial; Female; Gene Expression Regulation; Humans; Inflammation; Mitogen-Activated Protein Kinase 14; Mucous Membrane; Phosphorylation; Protein Processing, Post-Translational; Tumor Necrosis Factor-alpha; Tumor Suppressor Protein p53; Up-Regulation; Urinary Incontinence, Stress; Urothelium

2012
Microsphere-based flow cytometry protease assays for use in protease activity detection and high-throughput screening.
    Current protocols in cytometry, 2010, Volume: Chapter 13

    This protocol describes microsphere-based protease assays for use in flow cytometry and high-throughput screening. This platform measures a loss of fluorescence from the surface of a microsphere due to the cleavage of an attached fluorescent protease substrate by a suitable protease enzyme. The assay format can be adapted to any site or protein-specific protease of interest and results can be measured in both real time and as endpoint fluorescence assays on a flow cytometer. Endpoint assays are easily adapted to microplate format for flow cytometry high-throughput analysis and inhibitor screening.

    Topics: Animals; Biotinylation; Flow Cytometry; Fluorescence Resonance Energy Transfer; Green Fluorescent Proteins; High-Throughput Screening Assays; Humans; Inflammation; Kinetics; Microspheres; Peptide Hydrolases; Peptides; Reproducibility of Results; Temperature

2010
Protein synthesis inhibitors enhance the expression of mRNAs for early inducible inflammatory genes via mRNA stabilization.
    Biochimica et biophysica acta, 2008, Volume: 1779, Issue:2

    Expression of inflammatory genes is regulated at multiple steps, including transcriptional activation and mRNA stabilization. During an investigation into the requirement of de novo protein synthesis for the induction of inflammatory genes, it was revealed that protein synthesis inhibitors unexpectedly potentiated the induction of mRNAs for primary response genes, while the inhibitors suppressed the induction of secondary inducible genes as previously described. Stimulus-induced nuclear translocation and promoter recruitment of NF-kappaB, which is responsible for the transcriptional activation of many inflammatory genes, were largely unaffected by the inhibitors. Instead, these inhibitors prolonged the half-lives of all of the primary inducible mRNAs tested. Thus, these findings emphasize the important contribution of regulated mRNA longevity to gene expression induced by pro-inflammatory stimulation.

    Topics: Active Transport, Cell Nucleus; Animals; Anisomycin; Cell Line; Cycloheximide; Cytokines; Gene Expression Regulation; Half-Life; Inflammation; Lipopolysaccharides; Mice; NF-kappa B; Promoter Regions, Genetic; Protein Synthesis Inhibitors; RNA Stability; RNA, Messenger

2008
C-jun N-terminal kinase mediates tumor necrosis factor-alpha suppression of differentiation in myoblasts.
    Endocrinology, 2006, Volume: 147, Issue:9

    The stress kinase c-jun N-terminal kinase (JNK) was recently shown to be involved in the pathophysiology of major inflammatory conditions, including Alzheimer's disease, stroke, obesity, and type II diabetes. However, the role of JNK in regulating inflammatory events in skeletal muscle is only beginning to be explored. IGF-I is the major hormone that promotes muscle growth and development. Here we used a novel, JNK interacting protein (JIP)-derived JNK peptide inhibitor to establish that JNK suppresses the biological activity of IGF-I in skeletal muscle progenitor cells. In these myoblasts, TNFalpha and its downstream receptor substrates, neutral-sphingomyelinase (N-SMase) and N-acetyl-d-sphingosine (C2-ceramide), induce JNK kinase activity in a time-dependent manner. Consistent with these results, TNFalpha induces JNK binding to insulin receptor substrate 1 (IRS-1) but is unable to inhibit IGF-I-induced IRS-1 tyrosine phosphorylation in myoblasts that are treated with the JNK peptide inhibitor. More importantly, JNK activation induced by TNFalpha, C2-ceramide, and N-SMase is associated with reduced expression of the critical muscle transcription factor myogenin as well as the differentiation marker myosin heavy chain (MHC). The JNK peptide inhibitor, but not the control peptide, completely reverses this inhibition of both myogenin and MHC. In the absence of IGF-I, TNFalpha, C2-ceramide, N-SMase and the JNK inhibitor are inactive, as shown by their inability to affect IRS tyrosine phosphorylation and protein expression of myogenin and MHC. These results establish that the resistance of muscle progenitor cells to IGF-I, which is caused by inflammatory stimuli, is mediated by the JNK stress kinase pathway.

    Topics: Animals; Anisomycin; Cell Differentiation; Cell Line; Enzyme Activation; Enzyme Inhibitors; Gene Expression; Humans; Inflammation; Insulin Receptor Substrate Proteins; Insulin-Like Growth Factor I; JNK Mitogen-Activated Protein Kinases; Kinetics; Mice; Myoblasts; Myogenin; Phosphoproteins; Phosphorylation; Receptor, IGF Type 1; Recombinant Proteins; Signal Transduction; Sphingomyelin Phosphodiesterase; Sphingosine; Tumor Necrosis Factor-alpha; Tyrosine

2006
Tyrosine phosphorylation of K(ir)3.1 in spinal cord is induced by acute inflammation, chronic neuropathic pain, and behavioral stress.
    The Journal of biological chemistry, 2005, Dec-16, Volume: 280, Issue:50

    Tyrosine phosphorylation is an important means of regulating ion channel function. Our previous gene expression studies using the Xenopus laevis oocyte system suggested that tyrosine phosphorylation of G-protein-gated inwardly rectifying potassium channels (K(ir)3 or GIRK) suppressed basal channel conductance and accelerated channel deactivation. To assess whether similar mechanisms regulate K(ir)3 function in mammalian cells, we developed and characterized a phosphoselective antibody recognizing K(ir)3.1 phosphorylated at tyrosine 12 in the N-terminal domain and then probed for evidence of K(ir)3.1 phosphorylation in cultured mammalian cells and spinal cord. The antibody was found to discriminate between the phospho-Tyr(12) of K(ir)3.1 and the native state in transfected cell lines and in primary cultures of mouse atria. Following either mouse hindpaw formalin injection or sciatic nerve ligation, pY12-K(ir)3.1 immunoreactivity was enhanced unilaterally in the superficial layers of the spinal cord dorsal horn, regions previously described as expressing K(ir)3.1 channels. Mice lacking K 3.1 following targeted gene disruption did not show specific pY12-K(ir)3.1 immunoreactivity after sciatic nerve ligation. Further, mice exposed to repeatedly forced swim stress showed bilateral enhancement in pY12-K(ir)3.1 in the dorsal horn. This study provides evidence that K(ir)3 tyrosine phosphorylation occurred during acute and chronic inflammatory pain and under behavioral stress. The reduction in K(ir)3 channel activity is predicted to enhance neuronal excitability under physiologically relevant conditions and may mediate a component of the adaptive physiological response.

    Topics: Animals; Anisomycin; Antibodies; Behavior; Blotting, Western; Cell Line; Cell Line, Tumor; CHO Cells; Cricetinae; DNA; Dose-Response Relationship, Drug; Electrophysiology; Enzyme-Linked Immunosorbent Assay; Female; G Protein-Coupled Inwardly-Rectifying Potassium Channels; GTP-Binding Proteins; Heart Atria; Heart Ventricles; Humans; Immunoblotting; Immunohistochemistry; Inflammation; Male; Mice; Mice, Inbred C57BL; Microscopy, Confocal; Microscopy, Fluorescence; Muscle Cells; Neurodegenerative Diseases; Neurons; NIH 3T3 Cells; Phosphorylation; Plasmids; Protein Structure, Tertiary; Sciatic Nerve; Spinal Cord; Stress, Physiological; Tyrosine; Xenopus laevis

2005
Glucocorticoids suppress levels of immunoreactive bradykinin in inflamed tissue as evaluated by microdialysis probes.
    Clinical pharmacology and therapeutics, 1990, Volume: 48, Issue:2

    Although circulating bradykinin increases during surgery, concentrations remain unknown in the biologically relevant compartment, the inflamed tissue. We have developed a new method, using microdialysis probes, for collecting tissue samples of immunoreactive bradykinin in both postoperative patients and rats injected with carrageenan. In vitro studies determined optimal flow rate, that dialysate levels of immunoreactive bradykinin were linearly related to external concentrations, and that the probes do not activate bradykinin synthesis. In oral surgery patients, tissue levels of immunoreactive bradykinin peaked approximately 3 hours after surgery. Preoperative administration of methylprednisolone (125 mg) reduced immunoreactive bradykinin levels by 62% (p less than 0.001) compared with placebo. Comparison of bradykinin levels to concurrent pain revealed a counterclockwise hysteresis, suggesting a delay between peak levels of bradykinin in the effect compartment and pain. In rats, dexamethasone suppressed tissue levels of immunoreactive bradykinin. The glucocorticoid suppression was dependent on de novo protein synthesis. Microdialysis appears to be a novel and useful method for measuring the peripheral release of bradykinin and, possibly, other inflammatory mediators.

    Topics: Animals; Anisomycin; Bradykinin; Carrageenan; Dialysis; Female; Glucocorticoids; Humans; Inflammation; Male; Methylprednisolone; Mifepristone; Pain, Postoperative; Radioimmunoassay; Rats; Rats, Inbred Strains; Time Factors

1990