0000000000084837

AUTHOR

Fernando Rodríguez-pascual

showing 7 related works from this author

Tristetraprolin Regulates the Expression of the Human Inducible Nitric-Oxide Synthase Gene

2005

The expression of human inducible NO synthase (iNOS) is regulated both by transcriptional and post-transcriptional mechanisms. Stabilization of mRNAs often depends on activation of p38 mitogen-activated protein kinase (p38 MAPK). In human DLD-1 cells, inhibition of p38 MAPK by the compound 4-(4-fluorophenyl)-2-(4-methylsulfinylphenyl)-5-(4-pyridyl)1H-imidazole (SB203580) or by overexpression of a dominant-negative p38 MAPKalpha protein resulted in a reduction of human iNOS mRNA and protein expression, whereas human iNOS promoter activity was not affected. An important RNA binding protein regulated by the p38 MAPK pathway and involved in the regulation of the stability of several mRNAs is tr…

ImmunoprecipitationRNA Stabilityp38 mitogen-activated protein kinasesTristetraprolinNitric Oxide Synthase Type IIRNA-binding proteinGene Expression Regulation EnzymologicCell LineImmediate-Early ProteinsTristetraprolinEnzyme StabilityHumansRNA MessengerProtein kinase APharmacologyRegulation of gene expressionbiologyChemistryZinc FingersTransfectionMolecular biologyDNA-Binding ProteinsNitric oxide synthasebiology.proteinMolecular MedicineNitric Oxide SynthaseMolecular Pharmacology
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Epithelial contribution to the profibrotic stiff microenvironment and myofibroblast population in lung fibrosis

2017

The contribution of epithelial-to-mesenchymal transition (EMT) to the profibrotic stiff microenvironment and myofibroblast accumulation in pulmonary fibrosis remains unclear. We examined EMT-competent lung epithelial cells and lung fibroblasts from control (fibrosisfree) donors or patients with idiopathic pulmonary fibrosis (IPF), which is a very aggressive fibrotic disorder. Cells were cultured on profibrotic conditions including stiff substrata and TGF-β1, and analyzed in terms of morphology, stiffness, and expression of EMT/myofibroblast markers and fibrillar collagens. All fibroblasts acquired a robust myofibroblast phenotype on TGF-β1 stimulation. Yet IPF myofibroblasts exhibited highe…

Adult0301 basic medicineEpithelial-Mesenchymal TransitionPulmonary FibrosisPopulationmacromolecular substancesEpithelial cellsBiologyEpitheliumPulmonary fibrosisTransforming Growth Factor beta103 medical and health sciencesIdiopathic pulmonary fibrosisMechanobiology0302 clinical medicinePulmonary fibrosismedicineHumansMyofibroblastsFibroblasteducationLungMolecular BiologyCells Culturededucation.field_of_studyCèl·lules epitelialsLungEpithelial CellsFibrosi pulmonarArticlesCell BiologyFibroblastsmusculoskeletal systemmedicine.diseasePhenotype030104 developmental biologymedicine.anatomical_structureCellular MicroenvironmentCell Biology of DiseaseCase-Control Studies030220 oncology & carcinogenesisembryonic structurescardiovascular systemCancer researchMyofibroblastcirculatory and respiratory physiology
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Cytokine induction of NO synthase II in human DLD-1 cells: roles of the JAK-STAT, AP-1 and NF-κB-signaling pathways

1998

1. In human epithelial-like DLD-I cells, nitric oxide synthase (NOS) II expression was induced by interferon-gamma (100 u ml(-1)) alone and, to a larger extent, by a cytokine mixture (CM) consisting of interferon-gamma, interleukin-1beta (50 u ml(-1)) and tumor necrosis factor-alpha (10 ng ml(-1)). 2. CM-induced NOS II expression was inhibited by tyrphostin B42 (mRNA down to 1%; nitrite production down to 0.5% at 300 microM) and tyrphostin A25 (mRNA down to 24%, nitrite production down to 1% at 200 microM), suggesting the involvement of janus kinase 2 (JAK-2). Tyrphostin B42 also blocked the CM-induced JAK-2 phosphorylation (kinase assay) and reduced the CM-stimulated STAT1alpha binding act…

PharmacologyJanus kinase 2biologyKinaseOkadaic acidMolecular biologyNitric oxide synthasechemistry.chemical_compoundPyrrolidine dithiocarbamatechemistryGene expressionbiology.proteinPhenylarsine oxideAnisomycinBritish Journal of Pharmacology
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Complex Contribution of the 3′-Untranslated Region to the Expressional Regulation of the Human Inducible Nitric-oxide Synthase Gene

2000

Cytokine stimulation of human DLD-1 cells resulted in a marked expression of nitric-oxide synthase (NOS) II mRNA and protein accompanied by only a moderate increase in transcriptional activity. Also, there was a basal transcription of the NOS II gene, which did not result in measurable NOS II expression. The 3′-untranslated region (3′-UTR) of the NOS II mRNA contains four AUUUA motifs and one AUUUUA motif, known to destabilize the mRNAs of proto-oncogenes, nuclear transcription factors, and cytokines. Luciferase reporter gene constructs containing the NOS II 3′-UTR showed a significantly reduced luciferase activity. The embryonic lethal abnormal vision (ELAV)-like protein HuR was found to b…

Regulation of gene expressionMessenger RNAGeneral transcription factorThree prime untranslated regionELAV-Like Protein 1LuciferaseRNA-binding proteinCell BiologyBiologyMolecular BiologyBiochemistryMolecular biologyTranscription factorJournal of Biological Chemistry
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Inhibition of small G proteins of the Rho family by statins orClostridium difficiletoxin B enhances cytokine-mediated induction of NO synthase II

2000

In order to investigate the involvement of Ras and/or Rho proteins in the induction of the inducible isoform of nitric oxide synthase (NOS II) we used HMG-CoA reductase inhibitors (statins) and Clostridium difficile toxin B (TcdB) as pharmacological tools. Statins indirectly inhibit small G proteins by preventing their essential farnesylation (Ras) and/or geranylgeranylation (Rho). In contrast, TcdB is a glucosyltransferase and inactivates Rho-proteins directly. Human A549/8- and DLD-1 cells as well as murine 3T3 fibroblasts were preincubated for 18 h with statins (1–100 μM) or TcdB (0.01–10 ng ml−1). Then NOS II expression was induced by cytokines. NOS II mRNA was measured after 4–8 h by R…

rho GTP-Binding ProteinsG proteinBacterial ToxinsMevalonic AcidNitric Oxide Synthase Type IISmall G ProteinClostridium difficile toxin BBiologyGene Expression Regulation EnzymologicMiceGeranylgeranylationBacterial ProteinsPolyisoprenyl PhosphatesPrenylationGTP-Binding ProteinsGene expressionAtorvastatinTumor Cells CulturedAnimalsHumansDrug InteractionsPyrrolesLovastatinPromoter Regions GeneticPharmacology3T3 CellsTransfectionMolecular biologyHeptanoic AcidsEnzyme InductionPapersCytokinesHydroxymethylglutaryl-CoA Reductase InhibitorsNitric Oxide SynthaseSignal transductionBritish Journal of Pharmacology
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Functional coupling of nitric oxide synthase and soluble guanylyl cyclase in controlling catecholamine secretion from bovine chromaffin cells

1997

This study was designed to evaluate whether the enzymes of the nitric oxide/cyclic-GMP pathway, nitric oxide synthase and soluble guanylyl cyclase, are functionally coupled in controlling catecholamine secretion in primary cultures of bovine chromaffin cells. In immunocytochemical studies, 80-85% of the tyrosine hydroxylase-positive chromaffin cells also possessed phenylethanolamine-N-methyltransferase, f1p4cating their capability to synthesize epinephrine. Immunoreactivity for neuronal-type nitric oxide synthase was found in over 90% of all chromaffin cells. Reverse transcription-polymerase chain reaction also demonstrated neuronal-type nitric oxide synthase messenger RNA. Immunoreactivity…

Tyrosine 3-MonooxygenaseChromaffin CellsPolymerase Chain ReactionNitric oxidechemistry.chemical_compoundCatecholaminesCytosolAdrenal GlandsmedicineAnimalsRNA MessengerCyclic GMPbiologyChemistryPhenylethanolamine N-MethyltransferaseGeneral NeuroscienceNitric oxide synthasemedicine.anatomical_structureBiochemistryGuanylate CyclaseChromaffin cellCatecholaminebiology.proteinCalciumCattleSodium nitroprussideNitric Oxide SynthaseAdrenal medullaSoluble guanylyl cyclaseAcetylcholinemedicine.drugNeuroscience
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Glyceraldehyde-3-phosphate dehydrogenase regulates endothelin-1 expression by a novel, redox-sensitive mechanism involving mRNA stability

2008

17 pages.-- PMID: 18809573 [PubMed].-- Printed version published on Dec 2008.

Untranslated regionUmbilical VeinsRNA StabilityRNA StabilityGlyceraldehyde-3'-phosphate dehydrogenase (GAPDH)Plasma protein bindingstomatognathic systemHumansmRNA stabilityS-Glutathionylation3' Untranslated RegionsMolecular BiologyGlyceraldehyde 3-phosphate dehydrogenaseRegulation of gene expressionMessenger RNAEndothelin-1biologyThree prime untranslated regionGlyceraldehyde-3-Phosphate DehydrogenasesArticlesCell BiologyGlutathioneOxidative StressGene Expression RegulationBiochemistryEndothelin-1 (ET-1)biology.proteinOxidation-ReductionProtein Binding
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