Search results for "mito"

showing 10 items of 2513 documents

Intravesical mitoxantrone in superficial bladder tumours (Ta-T1)

1993

Abstract 36 patients with histologically proven grade G1–G2, Ta-T1 transitional cell carcinoma of the bladder were introduced, after transurethral resection (TUR), into a study of intravesical chemoprophylaxis with mitoxantrone (20 mg diluted in 50 ml). After a mean follow-up of 23 months, 16 (50%) patients showed a superficial recurrence with a mean recurrence rate of 0.56 per year. In 19 patients with recurring tumours the mean recurrence rate decreased from 1.65 to 0.58 per year. 9 patients (25.7%) suffered from a chemical cystitis that in 2 cases (5.7%) required treatment interruption.

Cancer Researchmedicine.medical_specialtymedicine.medical_treatmentUrologyResectionCystitismedicineHumansCarcinoma Transitional CellMitoxantroneChemotherapyUrinary bladderbusiness.industrymedicine.diseaseSurgeryChemical cystitisAdministration IntravesicalTransitional cell carcinomamedicine.anatomical_structureUrinary Bladder NeoplasmsOncologyTreatment interruptionChemoprophylaxisMitoxantroneNeoplasm Recurrence Localbusinessmedicine.drugEuropean Journal of Cancer
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The oxygen radicals involved in the toxicity induced by parthenolide in MDA-MB-231 cells

2014

It has been shown that the sesquiterpene lactone parthenolide lowers the viability of MDA-MB-231 breast cancer cells, in correlation with oxidative stress. The present report examined the different radical species produced during parthenolide treatment and their possible role in the toxicity caused by the drug. Time course experiments showed that in the first phase of treatment (0-8 h), and in particular in the first 3 h, parthenolide induced dichlorofluorescein (DCF) signal in a large percentage of cells, while dihydroethidium (DHE) signal was not stimulated. Since the effect on DCF signal was suppressed by apocynin and diphenyleneiodonium (DPI), two inhibitors of NADPH oxidase (NOX), we s…

Cancer Researchparthenolide oxygen radicals NADPH oxidase breast cancer cellsCell SurvivalBreast NeoplasmsSuperoxide dismutasechemistry.chemical_compoundSuperoxide Dismutase-1DichlorofluoresceinSuperoxidesCell Line TumorSettore BIO/10 - BiochimicaHumansParthenolidechemistry.chemical_classificationReactive oxygen speciesNADPH oxidasebiologySuperoxideSuperoxide DismutaseAnti-Inflammatory Agents Non-SteroidalNADPH OxidasesGeneral MedicineHydrogen PeroxideMolecular biologyMitochondriaOncologychemistryApocyninbiology.proteinFemaleSesquiterpenesPeroxynitrite
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Apoptosis induced in HepG2 cells by the synthetic cannabinoid WIN: involvement of the transcription factor PPARgamma.

2008

It has recently been shown that cannabinoids induce growth inhibition and apoptosis in different tumour cell lines. In the current study, the effects of WIN 55,212-2 (WIN), a synthetic and potent cannabinoid receptor agonist, are investigated in hepatoma HepG2 cells and a possible signal transduction pathway is proposed. In these cells, WIN induces a clear apoptotic effect which was accompanied by up-regulation of the death-signalling factors Bax, Bcl-X(S), t-Bid and down-regulation of the survival factors survivin, phospho-AKT, Hsp72 and Bcl-2. Moreover, WIN-induced apoptosis is associated with JNK/p38 MAPK pathway activation and mitochondrial depolarisation demonstrated by a cytofluorimet…

Cannabinoid receptorCarcinoma HepatocellularCell SurvivalPyridinesmedicine.medical_treatmentp38 mitogen-activated protein kinasesMorpholinesApoptosisBiologyNaphthalenesBiochemistryReceptor Cannabinoid CB2Membrane Microdomainscannabinoids PPARgamma factor apoptosis cancer cellsSettore BIO/10 - BiochimicaCell Line TumorSurvivinmedicineHumansAnilidesViability assayCannabinoidsLiver NeoplasmsGeneral MedicineCell biologyBenzoxazinesPPAR gammaApoptosisCancer cellBenzamidesCannabinoidSignal transductionApoptosis Regulatory ProteinsProtein KinasesSignal TransductionBiochimie
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Aspidin PB, a phloroglucinol derivative, induces apoptosis in human hepatocarcinoma HepG2 cells by modulating PI3K/Akt/GSK3β pathway.

2012

Aspidin PB, a phloroglucinol derivative isolated from Dryopteris fragrans (L.) Schott, has been previously reported to exert high biological activities. In the present study, we analyzed the apoptotic mechanisms of aspidin PB on human hepatoma cell line, HepG2. Initially, aspidin PB was shown to inhibit the growth of HepG2 cells in a time and dose-dependent manner. After treatment with aspidin PB for 72 h, 48 h and 24 h using MTT assay, the IC(50) values were 10.59 μM, 20.86 μM and 46.59 μM, respectively. Aspidin PB was capable to induce apoptosis, as measured by mitochondrial membrane potential (ΔΨm), acridine orange (AO) staining and propidium iodide (PI)/annexin V-FITC double staining. T…

Carcinoma HepatocellularApoptosisBiologyPhloroglucinolToxicologyWortmanninchemistry.chemical_compoundGlycogen Synthase Kinase 3Phosphatidylinositol 3-KinasesAnnexinHumansMTT assayPropidium iodideProtein kinase BProtein Kinase InhibitorsPI3K/AKT/mTOR pathwayCell ProliferationPhosphoinositide-3 Kinase InhibitorsMembrane Potential MitochondrialGlycogen Synthase Kinase 3 betaMicroscopy ConfocalAcridine orangeLiver NeoplasmsGeneral MedicineHep G2 CellsFlow CytometryMolecular biologyAndrostadieneschemistryApoptosisWortmanninProto-Oncogene Proteins c-aktSignal TransductionChemico-biological interactions
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The Synthetic Cannabinoid WIN 55,212-2 Sensitizes Hepatocellular Carcinoma Cells to Tumor Necrosis Factor-Related Apoptosis-Inducing Ligand (TRAIL)-I…

2010

In this article, we demonstrate that the synthetic cannabinoid R-(+)-(2,3-dihydro-5-methyl-3-[(4-morpholinyl)methyl]pyrol[1,2,3-de]-1,4-benzoxazin-6-yl)-(1-naphthalenyl) methanone mesylate (WIN 55,212-2) sensitizes human hepatocellular carcinoma (HCC) cells to apoptosis mediated by tumor necrosis-related apoptosis inducing ligand (TRAIL). The apoptotic mechanism induced by treatment with WIN/TRAIL combination involved the loss of the mitochondrial transmembrane potential and led to the activation of caspases. In HCC cells, WIN treatment induced the up-regulation of TRAIL death receptor DR5, an effect that seemed to be related to the increase in the level of p8 and CHOP, two factors implicat…

Carcinoma HepatocellularDNA ComplementaryMorpholinesApoptosisNaphthalenesCHOPMembrane PotentialsTNF-Related Apoptosis-Inducing LigandCell Line TumorSurvivinmedicineHumansWIN 55212-2Protein kinase BTranscription factorCaspaseDNA PrimersPharmacologybiologyCannabinoidsReverse Transcriptase Polymerase Chain ReactionLiver NeoplasmsGene AmplificationDNA NeoplasmFlow CytometryBenzoxazinesReceptors TNF-Related Apoptosis-Inducing LigandApoptosisMitochondrial MembranesImmunologybiology.proteinCancer researchMolecular MedicineTumor necrosis factor alphaTranscription Factor CHOPmedicine.drugMolecular Pharmacology
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Stimulation of peroxisomal palmitoyl-CoA oxidase activity by ciprofibrate in hepatic cell lines: comparative studies in Fao, MH1C1 and HepG2 cells.

1993

The response of two rat cell lines, Fao and MH1C1, and one human cell line, HepG2, to the peroxisome proliferator ciprofibrate, was studied. Using a fluorometric assay for palmitoyl-CoA oxidase, the dose- and time-dependent increase of this enzymatic activity was determined. From the lowest concentration (100 microM) stimulation is evident in the two rat cell lines. In the Fao line, the activity was stimulated reaching a seven-fold increase over the control level at 250 microM after 72 h of treatment. In the MH1C1 line, the maximum stimulation, four- to five-fold, was obtained at 250 and 500 microM after 72 h. In the HepG2 cell line, activity increased two-fold at 250 microM after 72 h reac…

Carcinoma HepatocellularStimulationBiologyMicrobodiesClofibric AcidLiver Neoplasms ExperimentalmedicineTumor Cells CulturedAcyl-CoA oxidaseAnimalsHumansHypolipidemic AgentsOxidase testLiver NeoplasmsFibric AcidsCell BiologyGeneral MedicinePeroxisomePalmitoyl-CoA oxidase activityBiochemistryLiverCell cultureHepatic stellate cellCiprofibrateOxidoreductasesmedicine.drugBiology of the cell
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Loss of response of carnitine palmitoyltransferase I to okadaic acid in transformed hepatic cells

1998

The specific activity of carnitine palmitoyltransferase I (CPT-I) was similar in mitochondria isolated from rat Fao and human HepG2 hepatoma cells and from rat hepatocytes, but almost twofold higher in permeabilized hepatoma cells than in permeabilized hepatocytes. Short-term exposure to okadaic acid induced a ca. 80% stimulation of CPT-I in hepatocytes, whereas no significant response of the enzyme from hepatoma cells was evident. Thus, the high CPT-I activity displayed by hepatoma cells may be reached by hepatocytes upon challenge to okadaic acid. Reconstitution experiments with purified mitochondrial and cytoskeletal fractions showed that the cytoskeleton of hepatocytes produced a more r…

Carcinoma Hepatocellularendocrine system diseasesMitochondria LiverMitochondrionBiologyBiochemistrychemistry.chemical_compoundLiver Neoplasms ExperimentalOkadaic AcidTumor Cells CulturedmedicineAnimalsHumansheterocyclic compoundsCarnitine O-palmitoyltransferaseCytoskeletonneoplasmsCell Line TransformedPharmacologyCarnitine O-PalmitoyltransferaseLiver NeoplasmsOkadaic aciddigestive system diseasesMitochondriaRatsCell biologyKineticsmedicine.anatomical_structureBiochemistrychemistryCell cultureHepatocyteHepatic stellate cellCarnitine palmitoyltransferase IBiochemical Pharmacology
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Improving the preclinical models for the study of chemotherapy-induced cardiotoxicity: a Position Paper of the Italian Working Group on Drug Cardioto…

2015

Although treatment for heart failure induced by cancer therapy has improved in recent years, the prevalence of cardiomyopathy due to antineoplastic therapy remains significant worldwide. In addition to traditional mediators of myocardial damage, such as reactive oxygen species, new pathways and target cells should be considered responsible for the impairment of cardiac function during anticancer treatment. Accordingly, there is a need to develop novel therapeutic strategies to protect the heart from pharmacologic injury, and improve clinical outcomes in cancer patients. The development of novel protective therapies requires testing putative therapeutic strategies in appropriate animal model…

Cardiac function curveACE inhibitorsCardiotonic AgentsNeuregulin-1CardiomyopathyAntineoplastic AgentsPreclinical modelsCardioprotectionCardiotonic AgentsPharmacologyBioinformaticsmedicine.disease_causeCancer therapy-induced cardiac injury ;Preclinical modelsMitochondria HeartBeta-blockersNeoplasmsCancer therapy-induced cardiac injuryMedicineAnimalsHumansCardiac stem cellsCardioprotectionCardiotoxicityACE inhibitors; Beta-blockers; Cancer therapy-induced cardiac injury; Cardiac stem cells; Cardioprotection; Mitochondria; Neuregulin-1; Oxidative stress; Preclinical models; Statinsbusiness.industryStatinsCancermedicine.diseaseCardiotoxicityMitochondriaCancer therapy-induced cardiac injury Preclinical models Cardioprotection Mitochondria Neuregulin-1 Oxidative stress Statins Beta-blockers ACE inhibitors Cardiac stem cellsDisease Models AnimalOxidative StressHeart failureCardiology and Cardiovascular MedicinebusinessOxidative stress
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Down-regulation of OPA1 alters mouse mitochondrial morphology, PTP function, and cardiac adaptation to pressure overload

2012

AIMS: The optic atrophy 1 (OPA1) protein is an essential protein involved in the fusion of the mitochondrial inner membrane. Despite its high level of expression, the role of OPA1 in the heart is largely unknown. We investigated the role of this protein in Opa1(+/-) mice, having a 50% reduction in OPA1 protein expression in cardiac tissue. METHODS AND RESULTS: In mutant mice, cardiac function assessed by echocardiography was not significantly different from that of the Opa1(+/+). Electron and fluorescence microscopy revealed altered morphology of the Opa1(+/-) mice mitochondrial network; unexpectedly, mitochondria were larger with the presence of clusters of fused mitochondria and altered c…

Cardiac function curveendocrine systemPhysiologyAdaptation BiologicalDown-RegulationBiologyMitochondrionMitochondrial Membrane Transport ProteinsPermeabilityGTP PhosphohydrolasesMitochondrial ProteinsMice03 medical and health sciencesMitochondrial membrane transport protein0302 clinical medicinePhysiology (medical)Optic Atrophy Autosomal DominantPressuremedicineAnimalsMyocyteMyocytes CardiacInner mitochondrial membrane030304 developmental biologyMice KnockoutPressure overload0303 health sciencesMitochondrial Permeability Transition Poremedicine.diseaseeye diseasesMitochondriaCell biologyBiochemistryMitochondrial permeability transition poreMitochondrial Membranesbiology.proteinOptic Atrophy 1Cardiology and Cardiovascular Medicine030217 neurology & neurosurgeryCardiovascular Research
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Cardiotoxicity of mitoxantrone treatment in a german cohort of 639 multiple sclerosis patients

2014

Background and PurposezzThe aim of this study was to elucidate the role of therapy-related cardiotoxicity in multiple sclerosis (MS) patients treated with mitoxantrone and to identify potential predictors for individual risk assessment. MethodszzWithin a multicenter retrospective cohort design, cardiac side effects attributed to mitoxantrone were analyzed in 639 MS patients at 2 MS centers in Germany. Demographic, disease, treatment, and follow-up data were collected from hospital records. Patients regularly received cardiac monitoring during the treatment phase. ResultszzNone of the patients developed symptomatic congestive heart failure. However, the frequency of patients experiencing car…

Cardiac function curvemedicine.medical_specialtyCardiotoxicityMitoxantronedose dependencybusiness.industryCumulative doseMultiple sclerosiscardiotoxicityRetrospective cohort studymultiple sclerosismedicine.diseasemitoxantroneNeurologyInternal medicineCohortmedicineOriginal ArticleNeurology (clinical)Risk factorbusinessIntensive care medicineFunction and Dysfunction of the Nervous Systemmedicine.drug
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