Search results for "heme oxygenase-1"

showing 10 items of 57 documents

Cajaninstilbene acid (CSA) exerts cytoprotective effects against oxidative stress through the Nrf2-dependent antioxidant pathway.

2013

Cajaninstilbene acid (CSA), an active compound separated from pigeon pea leaves, possesses the highly efficient antioxidant activities. Transcription factor nuclear factor-erythroid 2-related factor 2 (Nrf2) is an important regulator of cellular oxidative stress. This study examined the role of Nrf2 in CSA-mediated antioxidant effects on human hepatocarcinoma (HepG2) cell line. The generation of reactive oxygen species (ROS) upon H2O2 and CSA treatment was lower than that of H2O2 alone. CSA activated Nrf2 as evaluated by Western blotting. A luciferase reporter assay also demonstrated that CSA-activated signaling resulted in the increased transcriptional activity of Nrf2 through binding to t…

MAPK/ERK pathwayAntioxidantNF-E2-Related Factor 2medicine.medical_treatmentBlotting WesternBiologyToxicologymedicine.disease_causeenvironment and public healthAntioxidantsStilbenesmedicineNAD(P)H Dehydrogenase (Quinone)HumansProtein kinase BTranscription factorPI3K/AKT/mTOR pathwaychemistry.chemical_classificationReactive oxygen speciesGeneral MedicineHep G2 Cellsrespiratory systemAntioxidant Response ElementsSalicylatesOxidative StressBiochemistrychemistryCytoprotectionNAD+ kinaseOxidative stressHeme Oxygenase-1Signal TransductionToxicology letters
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The SGLT2 inhibitor empagliflozin improves the primary diabetic complications in ZDF rats

2017

Hyperglycemia associated with inflammation and oxidative stress is a major cause of vascular dysfunction and cardiovascular disease in diabetes. Recent data reports that a selective sodium-glucose co-transporter 2 inhibitor (SGLT2i), empagliflozin (Jardiance®), ameliorates glucotoxicity via excretion of excess glucose in urine (glucosuria) and significantly improves cardiovascular mortality in type 2 diabetes mellitus (T2DM). The overarching hypothesis is that hyperglycemia and glucotoxicity are upstream of all other complications seen in diabetes. The aim of this study was to investigate effects of empagliflozin on glucotoxicity, β-cell function, inflammation, oxidative stress and endothel…

Male0301 basic medicineendocrine system diseasesDiabetic CardiomyopathiesFPS-ZM1 RAGE inhibitorClinical BiochemistryAorta ThoracicRAGE receptor for AGEICAM-1 intercellular adhesion molecule-1ECL enhanced chemiluminescence030204 cardiovascular system & hematologyDPP-4 dipeptidyl peptidase-4medicine.disease_causeTNF-α tumor necrosis factor-αBiochemistryeNOS endothelial •NO synthase (type 3)0302 clinical medicineGlucosidesecSOD extracellular superoxide dismutaseInsulin-Secreting CellsCCL-2 see MCP-1HyperlipidemiaHyperinsulinemiaGTN glyceryl trinitrate (nitroglycerin)IFN-γ interferon-γDHE dihydroethidineEndothelial dysfunctionEndothelial dysfunctionIL-6 interleukin-6lcsh:QH301-705.5HO-1 heme oxygenase-1lcsh:R5-920ICAM-1NG normoglycemiaDiabetesNox catalytic subunit of NADPH oxidaseSGLT2 inhibitorβ-cell contentL-012 8-amino-5-chloro-7-phenylpyrido[34-d]pyridazine-14-(2H3H)dione sodium saltChIP chromatin immunoprecipitationC-Reactive ProteinCRP C-reactive proteinAGE advanced glycation end productsHbA1c glycohemoglobinlcsh:Medicine (General)Research PaperZucker diabetic fatty ratsmedicine.medical_specialtyDMSO dimethylsulfoxideMCP-1 monocyte-chemoattractant-protein-1qRT-PCR quantitative reverse transcription polymerase chain reactionZDF Zucker diabetic fatty (rat)Low-grade inflammation03 medical and health sciencesROS reactive oxygen speciesSodium-Glucose Transporter 2Physiology (medical)Internal medicineDiabetes mellitusPKC protein kinase CEmpagliflozinmedicineAnimalsHypoglycemic AgentsBenzhydryl CompoundsCOX2 cyclooxygenase-2SGLT2i SGLT2 inhibitorSodium-Glucose Transporter 2 InhibitorsGlycated HemoglobinACh acetylcholinebusiness.industryOrganic Chemistrynutritional and metabolic diseasesType 2 Diabetes Mellitusmedicine.diseaseH2K9me2 histone3 lysine9 dimethylationRatsRats ZuckerDHFR dihydrofolate reductaseSGLT2 sodium-glucose co-transporter-2Oxidative StresssGC soluable guanylyl cyclaseGlucose030104 developmental biologyEndocrinologylcsh:Biology (General)ALDH-2 mitochondrial aldehyde dehydrogenaseEndothelium VascularAGE/RAGE signalingHG hyperglycemiabusinessOxidative stressRedox Biology
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Haem oxygenase-1 down-regulates high mobility group box 1 and matrix metalloproteinases in osteoarthritic synoviocytes

2010

Objectives. Activation of osteoarthritic synoviocytes by pro-inflammatory cytokines results in the release of biochemical mediators such as MMPs and high mobility group box 1 (HMGB1). Extracellular HMGB1 can play an important role in joint diseases as a mediator of synovitis. We have shown previously that haem oxygenase-1 (HO-1) exerts protective effects during inflammatory responses. In this study, we have examined whether HO-1 induction would be an effective strategy to control MMP and HMGB1 production in osteoarthritic synoviocytes. Methods. Osteoarthritic synoviocytes were obtained by digestion with collagenase and cultured until third passage. HO-1 was induced by cobalt protoporphyrin …

MaleAnalysis of VarianceSmall interfering RNASynovial MembraneDown-RegulationTransfectionBiologyMatrix metalloproteinaseHMGB1COPPMolecular biologyMatrix MetalloproteinasesRheumatologyOsteoarthritisGene expressionbiology.proteinHumansGene silencingInterstitial collagenaseFemalePharmacology (medical)HMGB1 ProteinCells CulturedHeme Oxygenase-1AgedRheumatology
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Induction of hepatic heme oxygenase-1 by diclofenac in rodents: role of oxidative stress and cytochrome P-450 activity

2003

Abstract Background/Aims : The role of oxidative stress in diclofenac hepatotoxicity is still not clear. This study examined whether the drug induced heme oxygenase-1 (HO-1), a stress protein. Methods : HO-1 mRNA and HO activity were measured in mouse liver and in rat hepatocytes after treatment with diclofenac parallel to release of serum alanine aminotransferase (ALT) and sorbitol dehydrogenase (SDH) as a marker of hepatic damage. Results : HO-1 was transcriptionally and dose-dependently induced by diclofenac in mouse liver and rat hepatocytes. HO-1 mRNA, ALT and SDH peaked at the same time. Mechanistic studies revealed that the drug synergized with buthionine sulfoximine (BSO) in lowerin…

MaleCarcinoma HepatocellularDiclofenacCytochromeMice Inbred StrainsOxidative phosphorylationPharmacologymedicine.disease_causeMicechemistry.chemical_compoundCytochrome P-450 Enzyme SystemCell Line TumormedicineAnimalsCytochrome P-450 Enzyme InhibitorsHumansButhionine sulfoximineEnzyme InhibitorsButhionine SulfoximineDose-Response Relationship DrugHepatologybiologyLiver NeoplasmsMembrane ProteinsCytochrome P450GlutathioneAcetylcysteineRatsHeme oxygenaseOxidative Stressstomatognathic diseasesmedicine.anatomical_structureLiverchemistryBiochemistryEnzyme InductionHepatocyteHeme Oxygenase (Decyclizing)Hepatocytesbiology.proteinFemaleHeme Oxygenase-1Oxidative stressJournal of Hepatology
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Control of Cell Migration and Inflammatory Mediators Production by CORM-2 in Osteoarthritic Synoviocytes

2011

Background Osteoarthritis (OA) is the most widespread degenerative joint disease. Inflamed synovial cells contribute to the release of inflammatory and catabolic mediators during OA leading to destruction of articular tissues. We have shown previously that CO-releasing molecules exert anti-inflammatory effects in animal models and OA chondrocytes. We have studied the ability of CORM-2 to modify the migration of human OA synoviocytes and the production of chemokines and other mediators sustaining inflammatory and catabolic processes in the OA joint. Methodology/Principal Findings OA synoviocytes were stimulated with interleukin(IL)-1β in the absence or presence of CORM-2. Migration assay was…

MaleChemokineAnatomy and PhysiologyInterleukin-1betalcsh:MedicineGene ExpressionMatrix metalloproteinaseBiochemistryCell MovementDrug Discoverylcsh:ScienceMusculoskeletal SystemCells CulturedChemokine CCL2MultidisciplinarybiologyReverse Transcriptase Polymerase Chain ReactionSynovial MembraneNF-kappa BInterleukinCell migrationmedicine.anatomical_structureMedicineFemaleMatrix Metalloproteinase 3Inflammation MediatorsMatrix Metalloproteinase 1Mitogen-Activated Protein KinasesResearch ArticleCell PhysiologyBlotting WesternRheumatologySynovitisOsteoarthritisOrganometallic CompoundsmedicineHumansInterleukin 8BiologyAgedCell ProliferationChemokine CCL20lcsh:RInterleukin-8medicine.diseaseTranscription Factor AP-1CCL20Oxidative StressSmall MoleculesImmunologyCancer researchbiology.proteinlcsh:QSynovial membraneHeme Oxygenase-1PLoS ONE
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Heme oxygenase-1: a novel key player in the development of tolerance in response to organic nitrates.

2007

Objective— Nitrate tolerance is likely attributable to an increased production of reactive oxygen species (ROS) leading to an inhibition of the mitochondrial aldehyde dehydrogenase (ALDH-2), representing the nitroglycerin (GTN) and pentaerythrityl tetranitrate (PETN) bioactivating enzyme, and to impaired nitric oxide bioactivity and signaling. We tested whether differences in their capacity to induce heme oxygenase-1 (HO-1) might explain why PETN and not GTN therapy is devoid of nitrate and cross-tolerance. Methods and Results— Wistar rats were treated with PETN or GTN (10.5 or 6.6 μg/kg/min for 4 days). In contrast to GTN, PETN did not induce nitrate tolerance or cross-tolerance as assess…

MaleEndotheliumPharmacologySensitivity and SpecificityNitric oxidechemistry.chemical_compoundNitroglycerinRandom AllocationDrug toleranceReference ValuesmedicineAnimalsPentaerythritol TetranitrateRats WistarHemeCyclic GMPChromatography High Pressure LiquidProbabilitychemistry.chemical_classificationReactive oxygen speciesbiologyDrug ToleranceFree Radical ScavengersAldehyde DehydrogenaseRatsHeme oxygenaseFerritinDisease Models Animalmedicine.anatomical_structurechemistryBiochemistrycardiovascular systembiology.proteinEndothelium VascularCardiology and Cardiovascular MedicineReactive Oxygen SpeciesHeme Oxygenase-1HeminArteriosclerosis, thrombosis, and vascular biology
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Hemin, an inducer of heme oxygenase-1, lowers intraocular pressure in rabbits.

2007

Carbon monoxide (CO) generated from heme may induce vasodilation and exert cyto-protective properties in the eye. This study was undertaken to investigate the effects of hemin, a potent inducer of heme oxygenase-1 (HO-1), on models of ocular hypertension in rabbits.Ocular hypertension was induced by injecting alpha-chymotrypsin in both eyes under local anesthesia. Only rabbits with an intraocular pressure (IOP) of 25 mmHg or more were used. The dose-response study of the hemin effect on IOP was made by an intravenous injection of the drug (50, 75, and 100 mg/kg) and subsequent IOP monitoring every 6 h. A separate set of animals was pretreated with the HO-1 inhibitor, zinc protoporphyrin-IX …

MaleIntraocular pressuregenetic structuresmedicine.drug_classOcular hypertensionProtoporphyrinsVasodilationPharmacologyBetamethasonechemistry.chemical_compoundRandom AllocationmedicineAnimalsChymotrypsinPharmacology (medical)Enzyme inducerIntraocular PressurePharmacologyAnalysis of VariancebiologyDose-Response Relationship Drugmedicine.diseaseeye diseasesHeme oxygenaseOphthalmologyDisease Models AnimalchemistryAnesthesiaEnzyme InductionInjections Intravenousbiology.proteinCorticosteroidBetamethasoneHeminOcular Hypertensionsense organsRabbitsHeme Oxygenase-1Heminmedicine.drugJournal of ocular pharmacology and therapeutics : the official journal of the Association for Ocular Pharmacology and Therapeutics
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Expression of heme oxygenase-1 and regulation by cytokines in human osteoarthritic chondrocytes

2003

Heme oxygenase-1 (HO-1) is implicated in the protection against tissue injury. We investigated the expression of this protein in cartilage sections and chondrocytes obtained from osteoarthritic patients. HO-1 was immunodetected in preparations from cartilage and also in chondrocytes cultured in the absence of stimulation. We found that HO-1 can be modulated by cytokines since the pro-inflammatory cytokines interleukin (IL)-1beta, IL-17 and tumour necrosis factor-alpha (TNF-alpha) down-regulated this protein, whereas the anti-inflammatory cytokine IL-10 exerted the opposite effect. Our results suggest a role for HO-1 as part of protective mechanisms against tissue injury in human cartilage.

MaleNecrosismedicine.medical_treatmentBiochemistryGene Expression Regulation EnzymologicChondrocytechemistry.chemical_compoundChondrocytesOsteoarthritismedicineHumansHemeAgedPharmacologyRegulation of gene expressionbusiness.industryCartilageInterleukin-17Membrane ProteinsInterleukinInterleukin-10Cell biologyHeme oxygenasemedicine.anatomical_structureCytokinechemistryHeme Oxygenase (Decyclizing)ImmunologyCytokinesFemalemedicine.symptombusinessHeme Oxygenase-1Interleukin-1Biochemical Pharmacology
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Beneficial effect of dipyridyl, a liposoluble iron chelator against focal cerebral ischemia: In vivo and in vitro evidence of protection of cerebral …

2007

Whereas iron chelators were shown to induce neuroprotection against brain injury, the effect of iron chelators on ischemia-induced damage of cerebral endothelium is largely unknown. Our objective was to explore the endothelioprotective effect of the lipophilic iron chelator dipyridyl (DP) (i) in vitro on the death of cerebral endothelial cells (CECs) subjected to intracellular iron loading and (ii) in vivo on the ischemia-induced blood-brain barrier (BBB) disruption. When given shortly after iron exposure or brain ischemia, DP prevented the death of CECs and diminished BBB disruption, respectively, whereas a delayed administration of DP was associated with a lower CECs protection. Interesti…

MaleProgrammed cell deathTime FactorsIronIschemiaPharmacologymedicine.disease_causeBlood–brain barrierIron Chelating AgentsTransfectionNeuroprotectionStatistics NonparametricBrain IschemiaBrain ischemiaMice22'-DipyridylIn vivoIschemiamedicineAnimalsPROTECTIONMolecular BiologyCells CulturedtherapyCell DeathDose-Response Relationship DrugChemistrySuperoxide DismutaseGeneral NeuroscienceLEDEndothelial CellsBrainProteinscellmedicine.diseaseEndothelial stem cellIn VitroDisease Models Animalmedicine.anatomical_structureGene Expression RegulationBlood-Brain BarrierBrain InjuriesImmunologyCELLScardiovascular systemNeurology (clinical)Oxidative stressHeme Oxygenase-1Developmental Biology
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Heme oxygenase-1 regulates the progression of K/BxN serum transfer arthritis.

2012

Background Heme oxygenase-1 (HO-1) is induced in many cell types as a defense mechanism against stress. We have investigated the possible role of endogenous HO-1 in the effector phase of arthritis using the K/BxN serum transfer model of arthritis in HO-1 heterozygous and homozygous knock-out mice. Methodology/Principal Findings Arthritis was induced in C57/Black-6 xFVB (HO-1+/+, HO-1+/− and HO-1−/−) mice by intraperitoneal injection of 150 µl serum from arthritic K/BxN mice at days 0 and 2. Blood was collected and animals were sacrificed at day 10. Histological analysis was performed in ankle sections. The levels of inflammatory mediators were measured in serum and paw homogenates by enzyme…

MaleTime FactorsAnatomy and PhysiologyMouseNon-Clinical MedicineArthritislcsh:MedicineEndogenyBiochemistryAntioxidantsMicechemistry.chemical_compoundDrug Discoverylcsh:ScienceMusculoskeletal SystemHemeRegulation of gene expressionMultidisciplinaryEffectorSystems BiologyAnimal ModelsEnzymesDisease ProgressionMedicineMatrix Metalloproteinase 3Inflammation Mediatorsmedicine.symptomResearch ArticleCell typeOsteocalcinRheumatoid ArthritisInflammationModel OrganismsRheumatologymedicineAnimalsBiologyBlood CellsRANK Ligandlcsh:Rmedicine.diseaseArthritis ExperimentalMolecular biologyMice Inbred C57BLHeme oxygenaseDisease Models AnimalGene Expression RegulationchemistryImmunologylcsh:QAnkle JointHeme Oxygenase-1PLoS ONE
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