Search results for "Arylsulfatases"

showing 8 items of 8 documents

Oxidative and lysosomal capacity in skeletal muscle of mice after endurance training of different intensities

1978

The activity of certain enzymes of energy metabolism (cytochrome c oxidase, citrate synthase, malate dehydrogenase, and lactate dehydrogenase) and of lysosomes (beta-glucuronidase, beta-N-acetylglucosamindase, arylsuphatase, ribonuclease, deoxyribonuclease, acid phosphatase, and cathepsin D) was assayed from m. rectus femoris of mice trained 5 days per week, 1 hr per day for 4 weeks according to 4 different programmes: I. running speed 20 m/min, horizontal track, II. 25 m/min, horizontal track, III. 20 m/min 8 degrees uphill inclination, and IV. 25 m/min 8 degrees uphill inclination. Oxidative capacity increased and anaerobic capacity decreased without distinction between the different tran…

Malemedicine.medical_specialtyPhysiologyAcid PhosphataseCathepsin DCitrate (si)-SynthaseMalate dehydrogenaseElectron Transport Complex IVMicechemistry.chemical_compoundRibonucleasesMalate DehydrogenaseEndurance trainingLactate dehydrogenaseInternal medicineAcetylglucosaminidasemedicineAnimalsCitrate synthaseCytochrome c oxidaseArylsulfatasesGlucuronidaseDeoxyribonucleasesPhysical Education and TrainingL-Lactate DehydrogenasebiologyHistocytochemistryMusclesAcid phosphataseSkeletal muscleCathepsinsEndocrinologymedicine.anatomical_structurechemistryBiochemistrybiology.proteinEnergy MetabolismLysosomesActa Physiologica Scandinavica
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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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Sulfatide excreting heterozygous carrier of juvenile metachromatic leukodystrophy or asymptomatic patient of adult metachromatic leukodystrophy.

1975

In a family with juvenile metachromatic leukodystrophy (sulfatide lipidosis) 2 patients showed residual arysulfatase A activities of 5--6%. The patients' healthy father was characterized biochemically by a 39% normal activity of leukocyte plus plasma arylsulfatase A. The father was further characterized by a high sulfatide excretion (0.2--0.5 mg/I urine) and, paradoxically, by a normal sulfatide degrading enzyme activity in vitro. This special carrier is suspected to be heterozygous for a) arylsulfatase A deficiency and b) arylsulfatase A (sulfatidase) lability. This presumed additional genetic defect could be the cause of the sulfatide excretion which, in turn, would be a sign of the precl…

AdultMalemedicine.medical_specialtyArylsulfatase AHeterozygoteUrineBiologyAsymptomaticExcretionDrug StabilityInternal medicineGeneticsmedicineHumansChildGenetics (clinical)ArylsulfatasesSulfoglycosphingolipidsLeukodystrophy Metachromaticmedicine.diseaseEnzyme assayIn vitroMetachromatic leukodystrophyEnzyme ActivationEndocrinologybiology.proteinFemalemedicine.symptomSulfatasesArylsulfataseHumangenetik
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Food deprivation decreases the exertion-induced acid hydrolase response in mouse skeletal muscle

1988

Strenuous prolonged running causes muscle fibre necrosis in skeletal muscles. The muscle injury is associated with inflammation and a strong increase in the total activities of certain acid hydrolases a few days after exertion. The activity changes of acid hydrolases quantitatively well reflect the severity of histopathological changes during the myopathy (for review see Salminen, Acta Physiol Scand [Suppl 539] 1985). In this study male NMRI-mice were exposed to a protocol of fasting and refeeding together with or without a 6 h run on a treadmill at 13.5 m.min-1. The animals were killed 4 days after the exercise and samples from the red part of quadriceps femoris were analyzed for arylsulfa…

Malemedicine.medical_specialtyPhysiologyPhysical ExertionPhysical exerciseMiceEndurance trainingPhysiology (medical)Internal medicineAnimalsMedicineOrthopedics and Sports MedicineFemurExertionTreadmillMyopathyArylsulfatasesGlucuronidaseStarvationbiologybusiness.industryMusclesPublic Health Environmental and Occupational HealthSkeletal muscleGeneral MedicineEndocrinologymedicine.anatomical_structurebiology.proteinSulfatasesmedicine.symptomFood DeprivationbusinessAcid hydrolaseEuropean Journal of Applied Physiology and Occupational Physiology
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Lysosomal changes related to ageing and physical exercise in mouse cardiac and skeletal muscles.

1982

Physical exercise increased the activities of arylsulphatase, cathepsin D and β-glucuronidase in mouse skeletal muscle but not in cardiac muscle. Exercise-induced lysosomal response was more prominent in young adult than in senescent mice. The lipofuscin content of cardiac and skeletal muscles increased markedly during ageing and was also found to increase slightly after exertion in young mice, but not in senescent ones.

Malemedicine.medical_specialtyAgingPhysical ExertionCathepsin DPhysical exerciseCathepsin DLipofuscinLipofuscinCellular and Molecular NeuroscienceMiceInternal medicinemedicineAnimalsExertionYoung adultMolecular BiologyArylsulfatasesGlucuronidasePharmacologybusiness.industryMusclesMyocardiumCardiac muscleSkeletal muscleCell BiologyAnatomyCathepsinsmedicine.anatomical_structureEndocrinologyAgeingMolecular MedicinebusinessLysosomesExperientia
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Susceptibility of mouse skeletal muscles to exercise injuries.

1983

The susceptibility to exercise-induced myopathy was studied by histological and biochemical methods in various skeletal muscles of mice 3-4 days after a single bout of prolonged running. The degree of exercise injuries varied greatly in different muscles. Soleus and the red deep parts of quadriceps femoris were the most severely affected muscles. Extensive or scattered necrosis of muscle fibers was associated with focal inflammation and a five- to nine-fold increase in the activity of beta-glucuronidase in these muscles. Slight necrotic changes and a two- to three-fold increase in the activity of beta-glucuronidase were observed in tibialis anterior, plantaris, and the red deep parts of gas…

MaleNecrosisPhysiologyPhysical ExertionPhysical exerciseBiologyNecrotic ChangeBicepsRunningCellular and Molecular NeuroscienceMiceNecrosisPhysiology (medical)EdemamedicineAnimalsMyopathyArylsulfatasesGlucuronidaseFocal inflammationInflammationMusclesAnatomyOrgan SpecificityNeurology (clinical)medicine.symptomMusclenerve
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Prednisolone decreases exercise-induced acid hydrolase response in mouse skeletal muscle.

1984

Male NMRI-mice were subjected to exhaustive treadmill exercise. 3 and 6 days after the exertion, quadriceps femoris muscles were examined histologically and analyzed for acid hydrolases in order to follow the degree and progress of injuries. Prednisolone (PRED), an anti-inflammatory corticosteroid, was given to some of the animals in order to modify the exercise response. The PRED administration began 14 h before exercise and continued until the end of the experiment (6 days). The doses were 25 and 50 mg . kg-1 i.p. twice a day. The activities of both arylsulphatase and beta-glucuronidase increased significantly in the exercise control group after 3 and 6 days. The increase in activity corr…

Malemedicine.medical_specialtyNecrosisPhysiologymedicine.drug_classPrednisolonePhysical ExertionPhysical exerciseInflammationMice Inbred StrainsBiologyMiceMuscular DiseasesPhysiology (medical)Internal medicinemedicineAnimalsRegenerationOrthopedics and Sports MedicineExertionArylsulfatasesGlucuronidaseMyositisMusclesPublic Health Environmental and Occupational HealthSkeletal muscleGeneral Medicinemedicine.anatomical_structureEndocrinologyGlucoseDepression ChemicalPrednisolonebiology.proteinExercise TestCorticosteroidmedicine.symptomSulfatasesAcid hydrolasemedicine.drugEuropean 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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