Search results for "Calpain"

showing 10 items of 29 documents

PPAR gamma agonist leriglitazone improves frataxin-loss impairments in cellular and animal models of Friedreich Ataxia

2020

Friedreich ataxia (FRDA), the most common autosomal recessive ataxia, is characterized by degeneration of the large sensory neurons and spinocerebellar tracts, cardiomyopathy, and increased incidence in diabetes. The underlying pathophysiological mechanism of FRDA, driven by a significantly decreased expression of frataxin (FXN), involves increased oxidative stress, reduced activity of enzymes containing iron‑sulfur clus-ters (ISC), defective energy production, calcium dyshomeostasis, and impaired mitochondrial biogenesis, leading to mitochondrial dysfunction. The peroxisome proliferator-activated receptor gamma (PPARγ) is a ligand-activated transcriptional factor playing a key role in mito…

0301 basic medicineAtaxiaCell SurvivalCaspase 3PPAR agonistlcsh:RC321-57103 medical and health sciencesMice0302 clinical medicineIron-Binding ProteinsmedicineNeuritesAnimalsHumansMyocytes CardiacNeurodegenerationDorsal root ganglia neuronslcsh:Neurosciences. Biological psychiatry. NeuropsychiatryMembrane Potential MitochondrialNeuronsCardiomyocytesbiologyChemistryFrataxinNeurodegenerationCalpainLipid DropletsPeroxisomemedicine.diseaseCell biologyMitochondriaRatsPPAR gamma030104 developmental biologyNeurologyMitochondrial biogenesisFriedreich AtaxiaFrataxinbiology.proteinThiazolidinedionesmedicine.symptomMitochondrial function030217 neurology & neurosurgery
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Cardiac Glycoside Glucoevatromonoside Induces Cancer Type-Specific Cell Death.

2018

Cardiac glycosides (CGs) are natural compounds used traditionally to treat congestive heart diseases. Recent investigations repositioned CGs as potential anticancer agents. To discover novel cytotoxic CG scaffolds, we selected the cardenolide glucoevatromonoside (GEV) out of 46 CGs for its low nanomolar anti-lung cancer activity. GEV presented reduced toxicity toward non-cancerous cell types (lung MRC-5 and PBMC) and high-affinity binding to the Na+/K+-ATPase α subunit, assessed by computational docking. GEV-induced cell death was caspase-independent, as investigated by a multiparametric approach, and culminates in severe morphological alterations in A549 cells, monitored by transmission el…

0301 basic medicineCell typeProgrammed cell deathNecroptosis03 medical and health sciences0302 clinical medicineglucoevatromonosideCytotoxic T cellPharmacology (medical)non-canonical cell deathOriginal ResearchA549 cellPharmacologyU937 cellbiologyChemistrylcsh:RM1-950apoptosisCalpaincardiac glycoside3. Good healthlung cancer030104 developmental biologylcsh:Therapeutics. PharmacologyApoptosis030220 oncology & carcinogenesisCancer researchbiology.proteinFrontiers in pharmacology
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Isoform-specific function of calpains in cell adhesion disruption: studies in postlactational mammary gland and breast cancer.

2016

Cleavage of adhesion proteins is the first step for physiological clearance of undesired cells during postlactational regression of the mammary gland, but also for cell migration in pathological states such as breast cancer. The intracellular Ca2+-dependent proteases, calpains (CAPNs), are known to cleave adhesion proteins. The isoform-specific function of CAPN1 and CAPN2 was explored and compared in two models of cell adhesion disruption: mice mammary gland during weaning-induced involution and breast cancer cell lines according to tumor subtype classification. In both models, E-cadherin, β-catenin, p-120, and talin-1 were cleaved as assessed by western blot analysis. Both CAPNs were able …

0301 basic medicineMammary glandBreast NeoplasmsProximity ligation assayBiochemistry03 medical and health sciencesMiceWestern blotmedicineCell AdhesionAnimalsHumansLactationInvolution (medicine)BreastCell adhesionMolecular Biologybiologymedicine.diagnostic_testCalpainCalpainCell migrationCell BiologyCytosol030104 developmental biologymedicine.anatomical_structurebiology.proteinCancer researchFemaleThe Biochemical journal
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Host Cell Calpains Can Cleave Structural Proteins from the Enterovirus Polyprotein

2019

Enteroviruses are small RNA viruses that cause diseases with various symptoms ranging from mild to severe. Enterovirus proteins are translated as a single polyprotein, which is cleaved by viral proteases to release capsid and nonstructural proteins. Here, we show that also cellular calpains have a potential role in the processing of the enteroviral polyprotein. Using purified calpains 1 and 2 in an in vitro assay, we show that addition of calpains leads to an increase in the release of VP1 and VP3 capsid proteins from P1 of enterovirus B species, detected by western blotting. This was prevented with a calpain inhibitor and was dependent on optimal calcium concentration, especially for calpa…

0301 basic medicineProteasesentsyymitRNA virusviruksetvirusesPeptideCleavage (embryo)infektiotMass SpectrometryArticle03 medical and health sciencesViral ProteinsCapsidVirologyCleaveEnterovirus InfectionsAnimalsHumansCells CulturedGlycoproteinsPolyproteinschemistry.chemical_classification030102 biochemistry & molecular biologybiologyChemistryCalpainenterovirusvirus diseasesRNA virusCalpainbiochemical phenomena metabolism and nutritionbiology.organism_classificationAmino acidRatspolyproteinenterovirukset030104 developmental biologyInfectious DiseasesBiochemistryCapsidproteolytic processingProteolysisbiology.proteinCapsid ProteinsproteiinitPeptidescalpain
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Ca2+ signalling plays a role in celastrol‐mediated suppression of synovial fibroblasts of rheumatoid arthritis patients and experimental arthritis in…

2019

Background and purpose Celastrol exhibits anti-arthritic effects in rheumatoid arthritis (RA), but the role of celastrol-mediated Ca2+ mobilization in treatment of RA remains undefined. Here, we describe a regulatory role for celastrol-induced Ca2+ signalling in synovial fibroblasts of RA patients and adjuvant-induced arthritis (AIA) in rats. Experimental approach We used computational docking, Ca2+ dynamics and functional assays to study the sarcoplasmic/endoplasmic reticulum Ca2+ ATPase pump (SERCA). In rheumatoid arthritis synovial fibroblasts (RASFs)/rheumatoid arthritis fibroblast-like synoviocytes (RAFLS), mechanisms of Ca2+ -mediated autophagy were analysed by histological, immunohis…

0301 basic medicinemusculoskeletal diseasesMaleProgrammed cell deathSERCAArthritisSarcoplasmic Reticulum Calcium-Transporting ATPasesArthritis RheumatoidRats Sprague-Dawley03 medical and health scienceschemistry.chemical_compound0302 clinical medicineBAPTAmedicineAutophagyAnimalsHumansCalcium SignalingCells CulturedPharmacologyMice KnockoutGene knockdownbiologyChemistrySynovial MembraneCalpainFibroblastsmedicine.diseaseResearch PapersArthritis ExperimentalTriterpenesCalcineurin030104 developmental biologyGene Expression RegulationCelastrolbiology.proteinCancer researchPentacyclic Triterpenes030217 neurology & neurosurgeryResearch PaperBritish Journal of Pharmacology
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Effects of fatiguing jumping exercise on mRNA expression of titin-complex proteins and calpains.

2009

Eccentric exercise induced by electrostimulation increases mRNA expression of titin-complex proteins in rodent skeletal muscle. In this study, mRNA expression of titin, muscle LIM protein (MLP), cardiac ankyrin repeat protein (CARP), ankyrin repeat domain protein 2 (Ankrd2), diabetes-related ankyrin repeat protein (DARP), and calcium-activated proteinases, calpains, were investigated in human skeletal muscle after fatiguing jumping exercise. Fatiguing jumping exercise did not change mRNA expression of titin, DARP, calpain 1, or calpain 3. MLP, Ankrd2 and calpain 2 mRNA levels were increased 2 days postexercise. CARP mRNA level was already elevated 30 min and remained elevated 2 days postexe…

ANKRD2AdultMalemedicine.medical_specialtyPhysiologyMuscle ProteinsYoung AdultPhysiology (medical)Internal medicinemedicineMyocyteAnkyrinHumansConnectinRNA MessengerCarpMuscle SkeletalExercisechemistry.chemical_classificationbiologyCalpainSkeletal muscleCalpainbiology.organism_classificationAnkyrin RepeatBiomechanical Phenomenamedicine.anatomical_structureEndocrinologychemistryThighMuscle Fatiguebiology.proteinAnkyrin repeatTitinElectrophoresis Polyacrylamide Gelsense organsStress MechanicalProtein KinasesMuscle ContractionJournal of applied physiology (Bethesda, Md. : 1985)
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Acute change of titin at mid-sarcomere remains despite 8 wk of plyometric training

2014

Purpose: The purpose of this study was to investigate skeletal muscle changes induced by an acute bout of plyometric exercise (PlyEx) both before and after PlyEx training, to understand if titin is affected differently after PlyEx training. Methods: Healthy untrained individuals (N=11) completed the 1stPlyEx (10x10 squat-jumps, 1min rest). Thereafter, 6 subjects completed 8 weeks of PlyEx, while 5 controls abstained from any jumping activity. Seven days after the last training session all subjects completed the 2ndPlyEx. Blood samples were collected before, 6 hours and 1, 2, 3 and 4 days after each acute bout of PlyEx, and muscle biopsies 4 days before and 3 days after each acute bout of Pl…

AdultMaleSarcomeresmedicine.medical_specialtyPhysiologyZ-disk streaming acute bouts calpain eccentric exerciseMuscle ProteinsPlyometric ExerciseSarcomerePhysiology (medical)HumansMedicinePlyometricsConnectinTissue DistributionMuscle SkeletalExercisebiologySettore BIO/16 - Anatomia UmanaCalpainbusiness.industrySkeletal musclemusculoskeletal systemAdaptation Physiologicalmedicine.anatomical_structurebiology.proteinPhysical therapyFemaleTitinPlyometric trainingAutolysisbusinessMuscle ContractionJournal of Applied Physiology
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Impaired calcium homeostasis in aged hippocampal neurons

2009

Abstract Development of neurodegenerative diseases such as Alzheimer's and Parkinson's disease is strongly age-associated. The impairment of calcium homeostasis is considered to be a key pathological event leading to neuronal dysfunction and cell death. However, the exact impact of aging on calcium homeostasis in neurons remains largely unknown. In the present work we have investigated intracellular calcium levels in cultured primary hippocampal neurons from young (2 months) and aged (24 months) rat brains. Upon stimulation with glutamate or hydrogen peroxide aged neurons in comparison to young neurons demonstrated an increased vulnerability to these disease-related toxins. Measurement of c…

Agingmedicine.medical_specialtyNeurotoxinsGlutamic Acidchemistry.chemical_elementHippocampusBiologyCalciumHippocampusCalcium in biologyRats Sprague-DawleyInternal medicinemedicineAnimalsCalcium SignalingOrganic ChemicalsCells CulturedCellular SenescenceNeuronsCalcium metabolismCalpainGeneral NeuroscienceNeurodegenerationGlutamate receptorCalpainHydrogen PeroxideOxidantsmedicine.diseaseRatsOxidative Stressmedicine.anatomical_structureEndocrinologynervous systemchemistryNerve Degenerationbiology.proteinCalciumNeuronNeuroscienceNeuroscience Letters
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Bortezomib induces in HepG2 cells IkappaBalpha degradation mediated by caspase-8.

2006

The present paper demonstrates that the proteasome inhibitor bortezomib, which behaves as an apoptotic agent in hepatoma HepG2 cells, caused in these cells a decrease in IkappaBalpha level and a consequent increase in NF- kappaB activity. The effect already appeared at 4 h of treatment and preceded the onset of apoptosis which was observed at 24 h. Our results demonstrate that bortezomib-induced IkappaBalpha degradation occurred in conjunction with the activation of caspase-8; moreover, the decrease in IkappaBalpha level was prevented in a dose-dependent manner by the addition of z-IETD, a specific inhibitor of caspase-8. Bortezomib caused the same effects in non-tumor Chang liver cells, wh…

Clinical BiochemistryBiologyCaspase 8Cell LineBortezomibchemistry.chemical_compoundNF-KappaB Inhibitor alphaCell Line Tumormedicinehepatoblastoma proteasome inhibitors NF-kB apoptosisHumansMolecular BiologyCaspase 8BortezomibLiver NeoplasmsNF-kappa BNF-κBCalpainCell BiologyGeneral MedicineMolecular biologyBoronic AcidsIκBαchemistryLiverApoptosisCell culturePyrazinesCancer researchProteasome inhibitorbiology.proteinI-kappa B Proteinsmedicine.drug
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Calpains promote α2β1 integrin turnover in nonrecycling integrin pathway

2012

A novel virus- and integrin clustering–specific pathway diverts integrin from its normal endo/exocytic traffic to a nonrecycling degradative endosomal route. Clustering of α2β1 integrin causes redistribution of the integrin to perinuclear endosomes, leading to enhanced integrin turnover promoted by calpains.

EndosomeIntegrinCD18Medical and Health SciencesCD49cCell LineCollagen receptorFocal adhesion03 medical and health sciencesCell Line TumorHumansMolecular Biology030304 developmental biology0303 health sciencesFocal AdhesionsTumorbiologyCalpain030302 biochemistry & molecular biologyCell MembraneCell BiologyArticlesBiological Sciences3. Good healthCell biologyEnterovirus B HumanProtein TransportIntegrin alpha MMembrane Traffickingbiology.proteinIntegrin beta 6Enterovirus BIntegrin alpha2beta1HumanDevelopmental BiologySignal TransductionMolecular Biology of the Cell
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