Search results for "cathepsin D"

showing 10 items of 34 documents

Cathepsin D Content in Colorectal Cancer

1995

Cathepsin D content and activity were determined in matched paired sets of colorectal tumor tissue and normal mucosa and correlated with a number of biological and clinical parameters. Significantly higher cathepsin D activity was measured in tumor cytosol compared to paired normal mucosa (p < 0.02), in Dukes’ stage A tumors compared to Dukes’ B and C (p < 0.05), in tumors < 5 cm compared to those > 5 cm, or in tumors with a low proliferation rate compared to those with a high proliferation rate (p < 0.05). Moreover, significant differences in enzyme activity between tumor tissue and paired normal mucosa were observed in node-positive and G2 tumors (p < 0.05). No significa…

Tumor progression.chemistry.chemical_classificationCathepsin D activityCancer ResearchPathologymedicine.medical_specialtyColorectal cancerbusiness.industryCathepsin DGeneral MedicineLysosomal proteinasemedicine.diseaseCathepsin D activityColorectal cancerMolecular biologyMetastasisCorrelationEnzymeOncologychemistryTumor progressionPreliminary reportmedicinebusinessOncology
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Kinetics of in vivo inhibition of tissue cathepsin d by pepstatin A

1988

1. 1. We have investigated the kinetics of inhibition of cathepsin D in heart, liver and skeletal muscle of CD-1 mice following administration of 25, 50, 100 and 200 mg/kg i.p. of pepstatin A, a specific inhibitor of this protease. 2. 2. In the liver, a significant inhibition of cathepsin D occurred up to at least 15 days, whereas, in heart and skeletal muscle, this inhibition lasted for a much shorter period of time. 3. 3. These results show that the recovery of enzyme activity to normal values is dose-dependent and that, at the same dose level, marked differences occur in the recovery of enzyme activity in these organ tissues, the liver being the most sensitive one. © 1988.

Pepstatin Amedicine.medical_treatmentPeriod (gene)KineticsCathepsin DBiochemistryCathepsin DMicechemistry.chemical_compoundIn vivoPepstatinsmedicineAnimalsProteasebiologyMusclesMyocardiumSkeletal muscleEnzyme assayKineticsmedicine.anatomical_structureLiverchemistryBiochemistrybiology.proteinFemaleProteinase InhibitorsOligopeptidesPepstatin
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Effects of age and prolonged running on proteolytic capacity in mouse cardiac and skeletal muscles.

1981

Male NMRI-mice, aged 3, 6, 9, and 12 months, were made to run for a period of 4 4 at a speed of 13.5 m/min on a motor-driven treadmill, 5 days after exertion, selected enzymatic estimates of acid and alkaline proteolytic as well as energy metabolic capacities were analyzed from the cardiac muscle and from the red and white parts of m. quadriceps femoris (MQF). The activities of alkaline and myofibrillar proteases increased most considerably in skeletal muscles with age. Cathepsin D and beta-glucuronidase activities were less affected in both muscles. Prolonged running increased the activities of cathepsin D, dipeptidyl aminopeptidase I and beta-glucuronidase in the white and, especially in …

Malemedicine.medical_specialtyAgingNecrosisPhysiologyPhysical ExertionCathepsin DStimulationBiologyExcretionMiceInternal medicinemedicineAnimalsExertionMusclesMyocardiumCardiac muscleSkeletal muscleProteinsEndocrinologymedicine.anatomical_structureBiochemistrymedicine.symptomMyofibrilPeptide HydrolasesActa physiologica Scandinavica
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Cathepsin D in the malignant progression of neoplastic diseases

1992

Recent studies suggest that aspartic proteinase Cathepsin D may be implicated in the process of tumor invasion and metastasis. In fact several in vitro observations showed that this proteinase may facilitate the spread of neoplastic cells through different mechanisms related to its proteolytic activity by acting at different levels of the metastatic cascade. Cathepsin D may promote tumor cell proliferation by acting as an autocrine mitogen through the activation of latent forms of growth factors or by interacting with growth factor receptors. The enzyme was also shown to be able to degrade in vitro extracellular matrix and to activate latent precursors forms of other proteinases involved in…

InvasionMetastasiCathepsin DPepstatin
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Cathepsin D, B and L circulating levels as prognostic markers of malignant progression

1996

Growing evidence indicates that lysosomal Cathepsins D (CD), B (CB) and L (CL) may promote carcinogenesis and tumor progression. Therefore, we evaluated their potential value as biochemical parameters of malignant progression in patients with benign diseases which may undergo malignant transformation, such as liver cirrhosis (LC) and chronic pancreatitis (CHP) as well as in hepatocellular carcinoma (HCC) and pancreatic cancer (DPC). CD, CB and CL serum levels were determined by immunoenzymatic assays in LC, CHP, HCC or DPC patients and correlated with a number of biochemical and clinical parameters of these diseases. CD serum levels were increased in LC, CHP and HCC, but not in the DPC grou…

AdultAged 80 and overMaleTumor progression.Carcinoma HepatocellularCirrhosiVHepatocellular carcinomaCathepsin LLiver NeoplasmsPancreatic cancerMiddle AgedPrognosisCathepsin DCathepsinsLCathepsin BPancreatic NeoplasmsCysteine EndopeptidasesChronic HepatiticEndopeptidasesBiomarkers TumorHumansFemaleAged
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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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Enhanced autophagic-lysosomal activity and increased BAG3-mediated selective macroautophagy as adaptive response of neuronal cells to chronic oxidati…

2019

Oxidative stress and a disturbed cellular protein homeostasis (proteostasis) belong to the most important hallmarks of aging and of neurodegenerative disorders. The proteasomal and autophagic-lysosomal degradation pathways are key measures to maintain proteostasis. Here, we report that hippocampal cells selected for full adaptation and resistance to oxidative stress induced by hydrogen peroxide (oxidative stress-resistant cells, OxSR cells) showed a massive increase in the expression of components of the cellular autophagic-lysosomal network and a significantly higher overall autophagic activity. A comparative expression analysis revealed that distinct key regulators of autophagy are upregu…

0301 basic medicineClinical BiochemistryLFQ Label-free quantificationLETM Leucine zipper and EF-hand containing transmembrane proteinmedicine.disease_causeBiochemistryCHX Cycloheximide0302 clinical medicineBNIP3 Bcl-2 interacting protein 3RAPA RapamycinPIK3C3 Class III PI3‐kinasePhosphorylationlcsh:QH301-705.5Neuronslcsh:R5-920PolyUB PolyubiquitinChemistryBAG3OPA1 Optic atrophy 1TOR Serine-Threonine KinasesWIPI1 WD repeat domain phosphoinositide-interacting protein 1ATG Autophagy relatedTFEB Transcription factor EBCell biologyMitochondriasiRNA Small interfering RNADLP1 Dynamin-like protein 1LAMP1 Lysosomal‐associated membrane protein 1PURO Puromycinlcsh:Medicine (General)Protein homeostasisResearch PaperBafA1 Bafilomycin A1LAMP2 Lysosomal‐associated membrane protein 2Proteasome Endopeptidase ComplexRAB18 Member RAS oncogeneTUB TubulinLC3 Light chain 3 proteinOxidative phosphorylationBAG3CTSD Cathepsin DModels BiologicalCell Line03 medical and health sciencesDownregulation and upregulationMacroautophagymedicineAutophagyHumansAdaptationBAG1 Bcl-2-associated athanogene 1BECN1 Beclin1PI3K/AKT/mTOR pathwayAdaptor Proteins Signal TransducingTEM Transmission electron microscopyHsp70 Heat shock protein 70Organic ChemistryAutophagyAutophagosomesmTOR Mammalian target of rapamycinHsp70Oxidative Stress030104 developmental biologyProteostasislcsh:Biology (General)CV CanavanineBAG3 Bcl-2-associated athanogene 3MTT (3-(45-Dimethylthiazol-2-yl)-25-Diphenyltetrazolium Bromide)Apoptosis Regulatory ProteinsLysosomes030217 neurology & neurosurgeryOxidative stressRedox Biology
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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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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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Lysosomal alterations in heart and liver of mice treated with doxorubicin.

1985

This study was carried out to evaluate the influence of long-term treatment with doxorubicin (DXR) (4mg/kg IV for 5 weeks) on heart and liver lysosomes of mice. We evaluated the variations in both total and "sedimentable" enzyme activity of cathepsin D, which is the major endopeptidase of myocites and probably involved in physiologic and pathologic degradation of actomyosin and mitochondria, and that of acid phosphatase, which is more prominent in interstitial cells. Our results show that marked changes occur in both total and sedimentable enzyme activity of cathepsin D in the heart of treated animals and to a lesser extent in the liver. In contrast, no modification of either total or sedim…

Cancer Researchmedicine.medical_specialtyAcid Phosphatasecardiotoxicity lisosomal enzymesCathepsin DMice Inbred StrainsToxicologyCathepsin DPathogenesisAdriamycinMiceLysosomeInternal medicinemedicineAnimalsPharmacology (medical)DoxorubicinPharmacologyCardiotoxicitybiologyMyocardiumAcid phosphataseHeartEnzyme assayEndocrinologymedicine.anatomical_structureOncologyLiverDoxorubicinToxicitybiology.proteinFemaleLysosomesmedicine.drugCancer chemotherapy and pharmacology
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