Search results for "DASE"

showing 10 items of 1891 documents

Acid hydrolase activity in red and white skeletal muscle of mice during a two-week period following exhausting exercise

1978

The activities of beta-glucuronidase, beta-N-acetylglucosaminidase, arylsulphatase, ribonuclease, p-nitrophenylphosphatase, and malate dehydrogenase together with protein content were assayed from representative mixed (m. rectus femoris), predominantly red (proximal heads of m. vastus lateralis, m.v. medius and m. v. intermedius), and predominantly white (distal head of m. vastus lateralis) muscle homogenates of mice during a two-week period following one single exposure to exhausting intermittent running on a treadmill. The activities of cathepsin D and beta-glycerophosphatase were assayed from mixed muscle only. In all three muscle types, particularly in red muscle, the activities of beta…

Malemedicine.medical_specialtyTime FactorsHydrolasesPhysiologyAcid PhosphatasePhysical ExertionClinical BiochemistryPhosphataseCathepsin DBiologyMalate dehydrogenaseMiceRibonucleasesMalate DehydrogenasePhysiology (medical)Internal medicineAcetylglucosaminidasemedicineAnimalsTreadmillReceptorArylsulfatasesGlucuronidase4-NitrophenylphosphataseMusclesSkeletal musclebiology.organism_classificationCathepsinsMediusEndocrinologymedicine.anatomical_structurebiology.proteinAcid hydrolasePfl�gers Archiv European Journal of Physiology
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Acid hydrolase activities in mouse cardiac and skeletal muscle following exhaustive exercise

1981

Acid hydrolase activities in skeletal and cardiac muscle were studied 5, 10 and 20 days after exhaustive intermittent running by untrained and endurance-trained mice. Exhaustion increased the activities of cathepsin D, beta-glucuronidase and ribonuclease, but not that of p-nitrophenylphosphatase in skeletal muscle of untrained mice. Activities were highest on the fifth day after exhaustion and decreased during the following two weeks. More intensive loading produced no changes in acid hydrolytic capacity in skeletal muscle of endurance-trained mice. Acid hydrolase activities in cardiac muscle of both untrained and trained mice were unaffected by exhaustive running. It is suggested that exha…

Malemedicine.medical_specialtyTime FactorsHydrolasesPhysiologyPhysical ExertionCathepsin DMicePhysiology (medical)Internal medicinemedicineAnimalsOrthopedics and Sports MedicineExertionGlucuronidasebiologyMusclesMyocardiumFiber necrosisPublic Health Environmental and Occupational HealthCardiac muscleSkeletal muscleGeneral MedicineHuman physiologyCathepsinsEndocrinologymedicine.anatomical_structureBiochemistrybiology.proteinLysosomesAcid hydrolaseEuropean Journal of Applied Physiology and Occupational Physiology
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Lysosomal changes related to exercise injuries and training-induced protection in mouse skeletal muscle

1984

Three experiments were designed to study the lysosomal changes associated with the development and maintenance of the endurance training induced resistance against exercise injuries in mouse skeletal muscles. The activities of arylsulphatase, cathepsin C, cathepsin D, and beta-glucuronidase were assayed from the red part of mouse quadriceps femoris muscle 4 days after prolonged strenuous running of 4-9 h duration. Exercise injuries were characterized by necrotic fibers and focal inflammation. Strenuous running of untrained mice induced necrotic lesions and a 4-5 fold increase in the activities of lysosomal enzymes. This lysosomal response was considerably reduced already by daily training b…

Malemedicine.medical_specialtyTime FactorsNecrosisHydrolasesPhysiologyPhysical ExertionCathepsin DCitrate (si)-SynthaseCathepsin CMiceNecrosisPhysical medicine and rehabilitationEndurance trainingInternal medicinemedicineAnimalsExertionArylsulfatasesGlucuronidasebusiness.industryMusclesSkeletal muscleCathepsinsQuadriceps femoris muscleEndocrinologymedicine.anatomical_structuremedicine.symptomLysosomesbusinesshuman activitiesMuscle ContractionMuscle contractionActa Physiologica Scandinavica
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Exercise-induced necrotic muscle damage and enzyme release in the four days following prolonged submaximal running in rats.

1994

Male Wistar rats were made to run uphill on a treadmill 5.5° incline at 17 m min−1 for 4 h, and killed for muscle and serum sampling 2, 4, 12, 24, 48 or 96 h after the exertion. To estimate the degree of muscle damage,β-glucuronidase activity, total protein concentration, water content and morphology were examined in the red parts of quadriceps femoris (MQF) and soleus (MS) muscles, the distal white part of the rectus femoris muscle (MRF) and the superficial part of triceps brachii muscle (MTB). Simultaneous serum samples were assayed for creatine kinase (CK) activity and carbonic anhydrase III (CA III) concentration. Fibre swelling and interstitial oedema were detected in MS at 4 h and in …

Malemedicine.medical_specialtyTime FactorsPhysiologyClinical BiochemistryInflammationPhysical exerciseRectus femoris muscleMotor ActivityNecrosisBody WaterPhysiology (medical)Internal medicinemedicineAnimalsExertionRats WistarCreatine KinaseCarbonic AnhydrasesGlucuronidaseSoleus musclebiologyMusclesTriceps brachii muscleSkeletal muscleAnatomyRatsMicroscopy ElectronEndocrinologymedicine.anatomical_structurebiology.proteinPhysical EnduranceCreatine kinasemedicine.symptomPflugers Archiv : European journal of physiology
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Effect of endurance training on the capacity of red and white skeletal muscle of mouse to oxidize carboxyl-14C-labelled palmitate.

1977

Three groups of mice were trained for 1, 4 and 5 months according to different running programs on a motor driven treadmill and the fatty acid oxidation capacity (FAO) and the activities of some enzymes of energy metabolism (cytochrome c oxidase, malate dehydrogenase, triosephosphate dehydrogenase, and lactate dehydrogenase) were determined from m. quadriceps femoris (MQF). Endurance training increased the FAO [5-month training 4 days/week, 30 min/day 22% (p less than 0.05); 1-month training, 7 days/week, 150 min/day 37% (p less than 0.001); 4-month training, 5 days/week, 60 min/day 24% (p less than 0.05)]. The activities of cytochrome c oxidase and malate dehydrogenase increased approx. 30…

Malemedicine.medical_specialtyTime FactorsPhysiologyPhysical ExertionPalmitatesPalmitic AcidsBiologyMalate dehydrogenaseElectron Transport Complex IVchemistry.chemical_compoundMiceEndurance trainingMalate DehydrogenaseLactate dehydrogenaseInternal medicineOxidative enzymemedicineCytochrome c oxidaseAnimalsCarbon RadioisotopesBeta oxidationchemistry.chemical_classificationL-Lactate DehydrogenaseMusclesSkeletal muscleGlyceraldehyde-3-Phosphate DehydrogenasesEnzymeEndocrinologymedicine.anatomical_structurechemistrybiology.proteinOxidation-ReductionActa physiologica Scandinavica
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Collagen metabolism of mouse skeletal muscle during the repair of exercise injuries.

1986

The activities of prolyl 4-hydroxylase and beta-glucuronidase, the concentration of hydroxyproline as well as reticulin and collagen type III, IV and V stainings were followed in skeletal muscle during a 20-day period after a 9-h treadmill running in untrained and trained male mice, aged 4-6 months. The prolonged 9-h running of untrained mice temporarily increased prolyl 4-hydroxylase activity 2, 5 and 10 days after exercise, more prominently in the red than in the white part of quadriceps femoris-muscle, and in analogical manner as beta-glucuronidase activity in tibialis anterior-muscle. Twenty days after exercise these enzymatic activities were back to the control level. The hydroxyprolin…

Malemedicine.medical_specialtyTime FactorsPhysiologyRatónClinical BiochemistryPhysical ExertionProcollagen-Proline DioxygenasePhysical exerciseBiologyCollagen Type IIIHydroxyprolinechemistry.chemical_compoundMicePhysiology (medical)Internal medicinemedicineAnimalsRegenerationExertionGlucuronidaseReticulin stainHistocytochemistryMusclesSkeletal muscleStainingHydroxyprolineReticulinEndocrinologymedicine.anatomical_structurechemistryCollagenPflugers Archiv : European journal of physiology
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Delayed effects of ciprofibrate on rat liver peroxisomal properties and proto-oncogene expression.

1995

Peroxisome proliferators (PPs) are non-genotoxic carcinogens in rodents. Their reversible effects on rat liver have been studied with ciprofibrate and fenofibrate. We found that with the hypolipemic drug fenofibrate a pause of 28 days is sufficient for a return to normal status, whereas with the highly potent PP ciprofibrate, the stimulation of ACO mRNA levels remains after its withdrawal. We investigated the effects of the renewal of the treatment with PPs on other peroxisomal parameters and proto-oncogene expression using Wistar rats. Interestingly, c-myc expression was enhanced even upon drug withdrawal, and was more stimulated by the second exposure to ciprofibrate, while c-fos expressi…

Malemedicine.medical_specialtyTime FactorseducationStimulationMitochondria LiverBiologyBiochemistryMicrobodiesDrug withdrawalClofibric AcidFenofibrateInternal medicineProto-Oncogene ProteinsGene expressionmedicineAnimalsRats WistarCarcinogenPharmacologyFenofibrateOncogeneFibric AcidsPeroxisomemedicine.diseaseRatsEndocrinologyLiverMicrosomes LiverCiprofibrateAcyl-CoA OxidaseOxidoreductasesmedicine.drugBiochemical pharmacology
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Dexamethasone upregulates Nox1 expression in vascular smooth muscle cells.

2014

<b><i>Background/Aim:</i></b> It has been demonstrated that dexamethasone-induced hypertension can be prevented by the NADPH oxidase inhibitor apocynin. The effect of dexamethasone on NADPH oxidase, however, is unknown. The present study was conducted to investigate the effect of dexamethasone on the gene expression of Nox1, the major NADPH oxidase isoform in vascular smooth muscle cells. <b><i>Results:</i></b> Oral treatment of Wistar-Kyoto rats with dexamethasone (0.03 mg/kg/day) for 12 days led to an upregulation of Nox1 mRNA expression in the aorta. In cultured A7r5 rat aortic smooth muscle cells, dexamethasone increased Nox1 mRNA expressi…

Malemedicine.medical_specialtyVascular smooth muscleTime FactorsMyocytes Smooth Musclemedicine.disease_causeRats Inbred WKYDexamethasoneHistone DeacetylasesMuscle Smooth Vascularchemistry.chemical_compoundReceptors GlucocorticoidInternal medicinemedicineAnimalsNADH NADPH Oxidoreductasescardiovascular diseasesRNA MessengerGlucocorticoidsDexamethasoneAortaPharmacologychemistry.chemical_classificationReactive oxygen speciesNADPH oxidasebiologyDose-Response Relationship DrugChemistryfungifood and beveragesGeneral MedicineRatsUp-RegulationEndocrinologyNOX1Gene Knockdown TechniquesApocynincardiovascular systembiology.proteinNADPH Oxidase 1Oxidative stresscirculatory and respiratory physiologymedicine.drugPharmacology
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Differential effects of diabetes on the expression of the gp91phox homologues nox1 and nox4.

2004

The nox2-dependent NADPH oxidase was shown to be a major superoxide source in vascular disease, including diabetes. Smooth muscle cells of large arteries lack the phagocytic gp91phox subunit of the enzyme; however, two homologues have been identified in these cells, nox1 and nox4. It remained to be established whether also increases in protein levels of the nonphagocytic NADPH oxidase contribute to increased superoxide formation in diabetic vessels. To investigate changes in the expression of these homologues, we measured their expression in aortic vessels of type I diabetic rats. Eight weeks after streptozotocin treatment, we found a doubling in nox1 protein expression, while the expressio…

Malemedicine.medical_specialtyXanthine OxidaseVasodilator AgentsBlotting WesternFluorescent Antibody TechniqueNitric OxideBiochemistryNitric oxideDiabetes Mellitus Experimentalchemistry.chemical_compoundNitroglycerinSuperoxidesPhysiology (medical)Internal medicinemedicineAnimalsNADH NADPH OxidoreductasesRats WistarXanthine oxidaseAortaNADPH oxidasebiologySuperoxideMyocardiumMicrofilament ProteinsElectron Spin Resonance SpectroscopyNOX4NADPH Oxidase 1Endothelial CellsNADPH OxidasesPhosphoproteinsImmunohistochemistryAcetylcholineRatsNitric oxide synthaseEndocrinologychemistryNADPH Oxidase 4NOX1cardiovascular systembiology.proteinNADPH Oxidase 1Nitric Oxide SynthaseCell Adhesion MoleculesFree radical biologymedicine
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Microvascular effects of the inhibition of dipeptidylpeptidase IV by linagliptin in nondiabetic hypertensive patients

2015

Recent studies suggest vascular benefits of dipeptidylpeptidase IV (DPP-IV) inhibition in patients with diabetes mellitus. Only little is known about potential vascular effects of DPP-IV inhibitors in nondiabetic individuals. The aim of this study was to investigate the effect of DPP-IV inhibition in a nondiabetic hypertensive population.This was a double-blinded, randomized, placebo-controlled, mechanistic study, comparing microvascular effects of the DPP-IV inhibitor linagliptin with placebo in nondiabetic individuals with a history of arterial hypertension. Twenty-one patients received 5 mg linagliptin (5 women; age 67.6 ± 6.0 years; mean ± SD), whereas 22 patients were randomized to pla…

Malemedicine.medical_specialtyanimal structuresPhysiologyMEDLINELinagliptin030209 endocrinology & metabolism030204 cardiovascular system & hematologyArginineLinagliptinlaw.inventionTransforming Growth Factor beta103 medical and health sciences0302 clinical medicineDouble-Blind MethodRandomized controlled triallawDiabetes mellitusInternal medicineInternal MedicinemedicineHumansArterial PressureIn patientCystatin CCyclic GMPDipeptidylpeptidase ivAgedGlycated HemoglobinDipeptidyl-Peptidase IV Inhibitorsbusiness.industryRetinal VesselsMiddle Agedmedicine.diseaseC-Reactive ProteinEndocrinologyRegional Blood FlowHypertensionMicrovesselsFemaleCardiology and Cardiovascular Medicinebusinessmedicine.drugJournal of Hypertension
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