Search results for "Statin"

showing 10 items of 545 documents

Tick Salivary Sialostatin L Represses the Initiation of Immune Responses by Targeting IRF4-Dependent Transcription in Murine Mast Cells

2015

Abstract Coevolution of ticks and the vertebrate immune system has led to the development of immunosuppressive molecules that prevent immediate response of skin-resident immune cells to quickly fend off the parasite. In this article, we demonstrate that the tick-derived immunosuppressor sialostatin L restrains IL-9 production by mast cells, whereas degranulation and IL-6 expression are both unaffected. In addition, the expression of IL-1β and IRF4 is strongly reduced in the presence of sialostatin L. Correspondingly, IRF4- or IL-1R–deficient mast cells exhibit a strong impairment in IL-9 production, demonstrating the importance of IRF4 and IL-1 in the regulation of the Il9 locus in mast cel…

Transcription GeneticCell DegranulationInterleukin-1betaImmunologyBiologyArticleCell DegranulationHost-Parasite InteractionsMiceImmune systemImmunityAnimalsImmunology and AllergyInterleukin 9Mast CellsPromoter Regions GeneticMice KnockoutRegulation of gene expressionMice Inbred BALB CBinding SitesInterleukin-6Interleukin-9DegranulationReceptors Interleukin-1CystatinsAsthmaImmunity InnateMice Inbred C57BLGene Expression RegulationInterferon Regulatory FactorsImmunologySignal transductionImmunosuppressive AgentsProtein BindingSignal TransductionInterferon regulatory factors
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Role of hepatocyte nuclear factor 3γ in the expression of human CYP2C genes

2004

Hepatocyte nuclear factor 3 gamma (HNF-3 gamma) is an important transcription factor for the maintenance of specific liver functions. However, its relevance in the expression of human cytochrome P450 (CYP) genes has not yet been explored. Several HNF3 putative binding sites can be identified in human CYP2C 5'-flanking regions. Gene reporter experiments with proximal promoters revealed that HNF-3 gamma transactivated CYP2C8, CYP2C9, and CYP2C19 (25-, 4-, and 4-fold, respectively), but it did not transactivate CYP2C18. However, overexpression of HNF-3 gamma in hepatoma cells by means of a recombinant adenovirus induced CYP2C9, CYP2C18, and CYP2C19 mRNA (4.5-, 20-, and 50-fold, respectively) b…

Transcriptional ActivationRecombinant Fusion ProteinsGenetic VectorsBiophysicsBiologyHydroxamic AcidsTransfectionBiochemistryGene Expression Regulation EnzymologicAdenoviridaeCytochrome P-450 Enzyme SystemSp3 transcription factorCell Line TumormedicineHumansRNA MessengerEnzyme InhibitorsLuciferasesPromoter Regions GeneticMolecular BiologyTranscription factorBinding SitesNuclear ProteinsPromoterMolecular biologyDNA-Binding ProteinsHistone Deacetylase InhibitorsHepatocyte nuclear factorsTrichostatin AHepatocyte nuclear factor 4Hepatocyte nuclear factor 4 alphaHepatocytesFOXA2Transcription Initiation SiteHepatocyte Nuclear Factor 3-gammaHeLa CellsTranscription Factorsmedicine.drugArchives of Biochemistry and Biophysics
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Transcriptional Regulation of Human CYP3A4 Basal Expression by CCAAT Enhancer-Binding Protein α and Hepatocyte Nuclear Factor-3γ

2003

Cytochrome P450 3A4 (CYP3A4) is involved in the metabolism of more than 50% of currently used therapeutic drugs, yet the mechanisms that control CYP3A4 basal expression in liver are poorly understood. Several putative binding sites for CCAAT/enhancer-binding protein (C/EBP) and hepatic nuclear factor 3 (HNF-3) were found by computer analysis in CYP3A4 promoter. The use of reporter gene assays, electrophoretic mobility shift assays, and site-directed mutagenesis revealed that one proximal and two distal C/EBP alpha binding sites are essential sites for the trans-activation of CYP3A4 promoter. No trans-activation was found in similar reporter gene experiments with a HNF-3 gamma expression vec…

Transcriptional ActivationTranscription GeneticGenetic VectorsBiologyTransfectiondigestive systemGene Expression Regulation EnzymologicChromatin remodelingAdenoviridaeCytochrome P-450 Enzyme SystemCCAAT-Enhancer-Binding Protein-alphamedicineCytochrome P-450 CYP3AHumansEnzyme InhibitorsBinding sitePromoter Regions GeneticCells CulturedPharmacologyReporter geneExpression vectorCcaat-enhancer-binding proteinsNuclear ProteinsMolecular biologyChromatinDNA-Binding ProteinsHistone Deacetylase InhibitorsHepatocyte nuclear factorsTrichostatin AHepatocytesMolecular MedicineHepatocyte Nuclear Factor 3-gammaTranscription Factorsmedicine.drugMolecular Pharmacology
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Ionizing radiation-induced E-selectin gene expression and tumor cell adhesion is inhibited by lovastatin and all-trans retinoic acid

2004

E-selectin mediated tumor cell adhesion plays an important role in metastasis. Here we show that ionizing radiation (IR) induces E-selectin gene and protein expression in human endothelial cells at therapeutically relevant dose level. E-selectin expression is accompanied by an increase in the adhesion of human colon carcinoma cells to primary human umbilical vein endothelial cells (HUVEC). The HMG-CoA reductase inhibitor lovastatin impairs IR-stimulated E-selectin expression as analyzed at the level of the protein, mRNA and promoter. Inactivation of Rho GTPases either by use of Clostridium difficile toxin A or by co-expression of dominant-negative Rho blocked IR-induced E-selectin gene indu…

Transcriptional Activationrho GTP-Binding ProteinsCancer ResearchBlotting WesternIntercellular Adhesion Molecule-1Retinoic acidEnzyme-Linked Immunosorbent AssayTretinoinchemistry.chemical_compoundGenes ReporterTretinoinCell Line TumorNeoplasmsRadiation IonizingE-selectinGene expressionCell AdhesionmedicineHumansLovastatinRNA MessengerPromoter Regions GeneticCell adhesionCells CulturedDose-Response Relationship DrugbiologyReverse Transcriptase Polymerase Chain ReactionTumor Necrosis Factor-alphaCell adhesion moleculeNF-kappa BDose-Response Relationship RadiationGeneral MedicineIntercellular Adhesion Molecule-1Gene Expression Regulation Neoplasticchemistrybiology.proteinCancer researchEndothelium VascularLovastatinHydroxymethylglutaryl-CoA Reductase InhibitorsE-Selectinmedicine.drugCarcinogenesis
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From Bench to Bedside—The Bad Berka Experience With First-in-Human Studies

2019

Precision oncology is being driven by rapid advances in novel diagnostics and therapeutic interventions, with treatments targeted to the needs of individual patients on the basis of genetic, biomarker, phenotypic, or psychosocial characteristics that distinguish a given patient from other patients with similar clinical presentations. Inherent in the theranostics paradigm is the assumption that diagnostic test results can precisely determine whether an individual is likely to benefit from a specific treatment. As part and integral in the current era of precision oncology, theranostics in the context of nuclear medicine aims to identify the appropriate molecular targets in neoplasms (diagnost…

Treatment responseNeurotensin receptor 1Somatostatin receptorbusiness.industryContext (language use)First in humanBioinformaticsBench to bedside030218 nuclear medicine & medical imagingBiomarker (cell)Translational Research Biomedical03 medical and health sciences0302 clinical medicine030220 oncology & carcinogenesisRadionuclide therapyAnimalsHumansMedicineRadiology Nuclear Medicine and imagingNuclear MedicineRadiopharmaceuticalsPeptidesbusinessSeminars in Nuclear Medicine
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Synthesis of Combretastatin A-4 and 3′-Aminocombretastatin A-4 derivatives with Aminoacid Containing Pendants and Study of their Interaction with Tub…

2020

Natural product combretastatin A-4 (CA-4) and its nitrogenated analogue 3&prime

Vascular Endothelial Growth Factor ACell cycle checkpoint<i>htert</i>Pharmaceutical ScienceApoptosisAnalytical Chemistrychemistry.chemical_compound0302 clinical medicineDrug DiscoveryStilbenesc-<i>myc</i>Telomerase0303 health sciences<i>vegf</i>biologyNeovascularization PathologicChemistry3′-aminocombretastatin a-4Cell cycle<i>c-Myc</i>VEGFc-MycBiochemistryChemistry (miscellaneous)030220 oncology & carcinogenesisMCF-7 CellsMolecular Medicinecytotoxicitycell cyclehTERTHT29 CellsArticleProto-Oncogene Proteins c-mycmicrotubuleslcsh:QD241-44103 medical and health sciencesStructure-Activity Relationshiplcsh:Organic chemistryMicrotubuleCell Line TumorHumansPhysical and Theoretical Chemistry030304 developmental biologyCell ProliferationCombretastatinCombretastatin A-4Cell growthOrganic ChemistryAntineoplastic Agents PhytogenicTubulintubulinCell cultureA549 Cellsbiology.proteinM Phase Cell Cycle Checkpointscombretastatin a-4Drug Screening Assays AntitumorMolecules
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Salivary protein profiles are linked to bitter taste acceptance in infants

2014

Salivary protein profiles are linked to bitter taste acceptance in infants. Séminaire final du projet européen HabEat

[SDV.AEN] Life Sciences [q-bio]/Food and Nutritionsalivastomatognathic systeminfantsbitter tastefood and beveragesureacystatin[SDV.AEN]Life Sciences [q-bio]/Food and Nutritionpsychological phenomena and processesingestive behaviour
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Synthesis and antiproliferative activity of the ring system [1,2]oxazolo[4,5-g]indole.

2012

Brand new ring: A series of 27 derivatives of the new ring system [1,2]oxazolo[4,5-g]indole were conveniently prepared and tested at the NCI for antiproliferative studies. Several of them showed good inhibitory activity toward all tested cell lines, reaching GI50 values generally at the micromolar and sub-micromolar levels and in some cases at nanomolar concentrations. The mean GI50 values, calculated on the full panel, were in the range 0.25-7.08 μM.

antiproliferative activityIndolesStereochemistryhydroxylamine hydrochloridesAntineoplastic AgentsRing (chemistry)Biochemistrychemistry.chemical_compoundStructure-Activity RelationshipCell Line TumorNeoplasms2]oxazolo[4Drug Discoveryantiproliferative activity; combretastatin A-4; enaminoketones; hydroxylamine hydrochlorides; [1; 2]oxazolo[4; 5-g]indolesStructure–activity relationshipHumanscombretastatin A-4General Pharmacology Toxicology and PharmaceuticsOxazolesCell ProliferationPharmacologyCombretastatin A-4Indole testantiproliferative activity combretastatin A-4 enaminoketones hydroxylamine hydrochlorides[12]oxazolo[45-g]indolesOrganic ChemistrySettore CHIM/08 - Chimica Farmaceuticachemistry5-g]indolesenaminoketonesMolecular Medicine[1Drug Screening Assays AntitumorChemMedChem
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Bempedoic acid as adjunct for traditional lipid-lowering therapy in patients with hyperlipidaemia

2020

Statin therapy has been the cornerstone for the reduction of cholesterol and circulating low-density lipoprotein (LDL) in patients with cardiovascular diseases. However, statin monotherapy has disadvantages attributable to myopathies and to the insufficient cholesterol reduction observed in some patients. There is a need for new well-tolerated therapies for lowering LDL. This review will focus on bempedoic acid in combination with traditional statin therapy or other lipid-lowering agents and its emerging role in LDL-C lowering. Bempedoic acid is also a viable alternative for reducing LDL cholesterol in the treatment of some patients suffering from heterozygous familial hypercholesterolemia.

bempedoic acidmedicine.medical_specialtyStatinmedicine.drug_classHyperlipidemiasFamilial hypercholesterolemia030204 cardiovascular system & hematologyLipid-lowering therapystatins03 medical and health scienceschemistry.chemical_compound0302 clinical medicineInternal medicinemedicineHumansDicarboxylic AcidsIn patient030212 general & internal medicineHypolipidemic AgentsClinical Trials as Topiclipid-lowering therapyCholesterolbusiness.industryFatty Acidsnutritional and metabolic diseasesCholesterol LDLGeneral Medicinemedicine.diseaselow-density lipoproteinchemistryDrug Therapy Combinationlipids (amino acids peptides and proteins)Statin therapyHydroxymethylglutaryl-CoA Reductase InhibitorsatherosclerosisCardiology and Cardiovascular MedicinebusinessBempedoic acidLipoproteinCoronary Artery Disease
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The Soluble Interleukin-6 Receptora

2006

biologyChemistryGeneral NeuroscienceLymphokineOncostatin MCiliary neurotrophic factorMolecular biologyGeneral Biochemistry Genetics and Molecular BiologyHistory and Philosophy of Sciencebiology.proteinLeukemia Inhibitory Factor Receptor alpha SubunitInterleukin 6ReceptorPeptide sequenceLeukemia inhibitory factorAnnals of the New York Academy of Sciences
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