Search results for "calpain"

showing 10 items of 29 documents

CALPAIN ACTIVITY MAINTAINS GOOD HEALTH OF CENTENARIAN T CELLS; SUMMARY OF THE CALPACENT PROJECT

2017

Causes of aging-associated deterioration of human immunity, and the reasons why the immune system of the oldest old individuals (centenarians) is relatively robust, remain moot. Intracellular proteolysis system of two proteases – µ- and m-calpain – and their inhibitor – calpastatin (the calpain-calpastatin system (CCS)) - is active in resting human peripheral blood T cells, participating in maintenance of their readiness to proliferate and secrete cytokines in response to stimulation. The amounts of the CCS proteins decrease in resting T lymphocytes of healthy elderly, only to return in the centenarians to those levels seen in the young individuals. We compared the calpain activities and th…

GerontologyAbstractsHealth (social science)business.industryMedicineCentenarianLife-span and Life-course StudiesbusinessHealth Professions (miscellaneous)Calpain activityInnovation in Aging
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Selective uptake and degradation of c-Fos and v-Fos by rat liver lysosomes

1996

AbstractThe transcription factor c-Fos is a short-lived protein and calpains and ubiquitin-dependent systems have been proposed to be involved in its degradation. In this report, we consider a lysosomal degradation pathway for c-Fos. Using a cell-free assay, we have found that freshly isolated lysosomes can take up and degrade c-Fos with high efficiency. v-Fos, the oncogenic counterpart of c-Fos, can also be taken up by lysosomes, yet the amount of incorporated protein is much lower. c-Fos uptake is independent of its phosphorylation state but it appears to be regulated by dimerization with differentially phosphorylated forms of c-Jun, while v-Fos escapes this regulation. Moreover, we show …

LeupeptinsProto-Oncogene Proteins c-junBiophysicsProtein degradationProtein degradationTransfectionBiochemistryc-FosCell Linechemistry.chemical_compoundStructural BiologyLysosomeGeneticsmedicineAnimalsHumansProtease InhibitorsTrypsinPhosphorylationMolecular BiologyTranscription factorc-FosCell-Free Systembiologyc-junLeupeptinc-Junv-FosCalpainCell BiologyLysosomeRecombinant ProteinsRatsKineticsOncogene Proteins v-fosmedicine.anatomical_structureLiverchemistryBiochemistrybiology.proteinPhosphorylationElectrophoresis Polyacrylamide GelLysosomesProto-Oncogene Proteins c-fosHeLa CellsFEBS Letters
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Differential functions of calpain 1 during epithelial cell death and adipocyte differentiation in mammary gland involution

2014

Calpains become activated in the mammary gland early during weaning, cleaving several proteins located mainly in the cell membrane, but also in other organelles such as lysosomes, mitochondria and nuclei. By immunofluorescence and Western blot analysis, we have demonstrated the nuclear translocation of calpain-1 and calpain-2, together with the cleavage of several cytoplasmic nucleoporins in epithelial cells of the lobulo-alveolar compartment. In vivo and in vitro calpain inhibition prevented this nucleoporin degradation. In addition, calpain-1 was also present in the nucleus of non-epithelial mammary tissue cells, concomitant with adipocyte re-differentiation. Calpain-1 was internalized wi…

MaleCellular differentiationBiochemistryHistonesMicechemistry.chemical_compoundHistone H3Mammary Glands AnimalAdipocyteAdipocytesAnimalsLactationMolecular BiologyMammary gland involutionbiologyCalpainCell DifferentiationEpithelial CellsCalpainCell BiologyMolecular biologyNuclear Pore Complex ProteinsProtein TransportHistoneGene Expression Regulationchemistrybiology.proteinH3K4me3FemaleNucleoporinBiochemical Journal
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Involvement of cyclin-dependent kinase-5 in the kainic acid-mediated degeneration of glutamatergic synapses in the rat hippocampus.

2011

Increased levels of glutamate causing excitotoxic damage accompany neurological disorders such as ischemia/stroke, epilepsy and some neurodegenerative diseases. Cyclin-dependent kinase-5 (Cdk5) is important for synaptic plasticity and is deregulated in neurodegenerative diseases. However, the mechanisms by which kainic acid (KA)-induced excitotoxic damage involves Cdk5 in neuronal injury are not fully understood. In this work, we have thus studied involvement of Cdk5 in the KA-mediated degeneration of glutamatergic synapses in the rat hippocampus. KA induced degeneration of mossy fiber synapses and decreased glutamate receptor (GluR)6/7 and post-synaptic density protein 95 (PSD95) levels in…

MaleNeuronsKainic Acidhippocampuynaptic degenerationCalpainIntracellular Signaling Peptides and ProteinsMembrane ProteinsCyclin-Dependent Kinase 5Settore BIO/09 - FisiologiaHippocampusRatsReceptors Kainic AcidNerve DegenerationSynapsescyclin-dependent kinase-5Excitatory Amino Acid AgonistsAnimalsHumansCalciumRats WistarDisks Large Homolog 4 ProteinCells CulturedThe European journal of neuroscience
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Androglobin: a chimeric globin in metazoans that is preferentially expressed in mammalian testes

2012

Abstract: Comparative genomic studies have led to the recent identification of several novel globin types in the Metazoa. They have revealed a surprising evolutionary diversity of functions beyond the familiar O2 supply roles of hemoglobin and myoglobin. Here we report the discovery of a hitherto unrecognized family of proteins with a unique modular architecture, possessing an N-terminal calpain-like domain, an internal, circular permuted globin domain, and an IQ calmodulin-binding motif. Putative orthologs are present in the genomes of many metazoan taxa, including vertebrates. The calpain-like region is homologous to the catalytic domain II of the large subunit of human calpain-7. The glo…

MaleProtein subunitAmino Acid MotifsMolecular Sequence DataProtein domain610 Medicine & healthBiologyGenome10052 Institute of PhysiologyEvolution MolecularMice03 medical and health scienceschemistry.chemical_compound0302 clinical medicine1311 GeneticsTestisGene expressionGenetics1312 Molecular BiologyAnimalsHumansGene familyAmino Acid SequenceGlobinBiologyMolecular BiologyGenePhylogenyEcology Evolution Behavior and Systematics030304 developmental biologyGenetics0303 health sciencesCalpainRecombinant ProteinsGlobinsProtein Structure TertiaryChemistry1105 Ecology Evolution Behavior and SystematicsMyoglobinchemistryMultigene Family10076 Center for Integrative Human Physiology570 Life sciences; biologyCalmodulin-Binding ProteinsHuman medicineSequence Alignment030217 neurology & neurosurgeryResearch Article
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The molecular basis of filamin binding to integrins and competition with talin.

2006

The ability of adhesion receptors to transmit biochemical signals and mechanical force across cell membranes depends on interactions with the actin cytoskeleton. Filamins are large, actin-crosslinking proteins that connect multiple transmembrane and signaling proteins to the cytoskeleton. Here, we describe the high-resolution structure of an interface between filamin A and an integrin adhesion receptor. When bound, the integrin beta cytoplasmic tail forms an extended beta strand that interacts with beta strands C and D of the filamin immunoglobulin-like domain (IgFLN) 21. This interface is common to many integrins, and we suggest it is a prototype for other IgFLN domain interactions. Notabl…

Models MolecularTalinanimal structuresIntegrin beta ChainsProtein ConformationFilaminsRecombinant Fusion ProteinsIntegrinMolecular Sequence Datamacromolecular substancesPlasma protein bindingFilaminCrystallography X-RayFilamin bindingMiceContractile ProteinsFLNAAnimalsAmino Acid SequenceMolecular BiologyNuclear Magnetic Resonance BiomolecularBinding SitesbiologySequence Homology Amino AcidCalpainMicrofilament ProteinsReproducibility of ResultsCell BiologyActin cytoskeletonCell biologyProtein Structure Tertiarybody regionsIntegrin alpha Mbiology.proteinNIH 3T3 CellsIntegrin beta 6Protein BindingMolecular cell
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Calpains mediate epithelial-cell death during mammary gland involution: mitochondria and lysosomal destabilization.

2012

Our aim was to elucidate the physiological role of calpains (CAPN) in mammary gland involution. Both CAPN-1 and -2 were induced after weaning and its activity increased in isolated mitochondria and lysosomes. CAPN activation within the mitochondria could trigger the release of cytochrome c and other pro-apoptotic factors, whereas in lysosomes it might be essential for tissue remodeling by releasing cathepsins into the cytosol. Immunohistochemical analysis localized CAPNs mainly at the luminal side of alveoli. During weaning, CAPNs translocate to the lysosomes processing membrane proteins. To identify these substrates, lysosomal fractions were treated with recombinant CAPN and cleaved produc…

Programmed cell deathBiologyMitochondrionMitochondrial ProteinsMiceMammary Glands AnimalLysosomal-Associated Membrane Protein 2AnimalsInvolution (medicine)Molecular BiologyMammary gland involutionCathepsinOriginal PaperCalpainCalpainEpithelial CellsCell BiologyCathepsinsCell biologyMitochondriaEnzyme ActivationCytosolMembrane proteinProteolysisbiology.proteinFemaleLysosomesCell death and differentiation
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Targeting the mitochondrial pathway to induce apoptosis/necrosis through ROS by a newly developed Schiff’s base to overcome MDR in cancer

2011

Abstract Multidrug resistance (MDR) in cancer, a major obstacle to successful application of cancer chemotherapy, is often characterized by over-expression of multidrug resistance-related proteins such as MRP1, P-gp or elevated glutathione (GSH) level. Efflux of drugs by functional P-gp, MRP1 and elevated GSH level can confer resistance to apoptosis induced by a range of different stimuli. Therefore, it is necessary to develop new cell death inducers with relatively lower toxicity toward non-malignant cells that can overcome MDR by induction of apoptotic or non-apoptotic cell death pathways. Herein we report the synthesis and spectroscopic characterization of a GSH depleting, redox active S…

Programmed cell deathMagnetic Resonance SpectroscopyNecrosisApoptosisMitochondrionBiologymedicine.disease_causeBiochemistryEhrlich ascites carcinomaMiceNecrosisCell Line TumorNeoplasmsSpectroscopy Fourier Transform InfraredmedicineAnimalsCytotoxic T cellCytotoxicitySchiff BasesCalpainCaspase 3General MedicineFlow CytometryGlutathioneMitochondriaBiochemistryDrug Resistance NeoplasmApoptosisCancer researchCalciumSpectrophotometry Ultravioletmedicine.symptomReactive Oxygen SpeciesOxidative stressBiochimie
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µ-Calpain conversion of antiapoptotic Bfl-1 (BCL2A1) into a prodeath factor reveals two distinct alpha-helices inducing mitochondria-mediated apoptos…

2011

Anti-apoptotic Bfl-1 and pro-apoptotic Bax, two members of the Bcl-2 family sharing a similar structural fold, are classically viewed as antagonist regulators of apoptosis. However, both proteins were reported to be death inducers following cleavage by the cysteine protease µ-calpain. Here we demonstrate that calpain-mediated cleavage of full-length Bfl-1 induces the release of C-terminal membrane active α-helices that are responsible for its conversion into a pro-apoptotic factor. A careful comparison of the different membrane-active regions present in the Bfl-1 truncated fragments with homologous domains of Bax show that helix α5, but not α6, of Bfl-1 induces cell death and cytochrome c r…

Programmed cell deathProtein StructureCancer Treatmentlcsh:MedicineApoptosisMitochondrionCleavage (embryo)BiochemistryProtein Structure SecondaryMinor Histocompatibility AntigensMiceCell Line TumorMolecular Cell BiologyAnimalsHumanslcsh:ScienceProtein InteractionsBiologyMultidisciplinaryMicroscopy ConfocalbiologyCell DeathCalpainCytochrome clcsh:RCytochromes cProteinsCalpainCysteine proteaseCell biologyMitochondriaProto-Oncogene Proteins c-bcl-2OncologyApoptosisbiology.proteinMedicinelcsh:QElectrophoresis Polyacrylamide GelGlobular ProteinsBCL2-related protein A1Research ArticlePloS one
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Calpain 1 and 2 Are Required for RNA Replication of Echovirus 1▿

2007

ABSTRACT Calpains are calcium-dependent cysteine proteases that degrade cytoskeletal and cytoplasmic proteins. We have studied the role of calpains in the life cycle of human echovirus 1 (EV1). The calpain inhibitors, including calpeptin, calpain inhibitor 1, and calpain inhibitor 2 as well as calpain 1 and calpain 2 short interfering RNAs, completely blocked EV1 infection in the host cells. The effect of the inhibitors was not specific for EV1, because they also inhibited infection by other picornaviruses, namely, human parechovirus 1 and coxsackievirus B3. The importance of the calpains in EV1 infection also was supported by the fact that EV1 increased calpain activity 3 h postinfection. …

ProteasesImmunoelectron microscopyImmunologyParechovirusVirus ReplicationMicrobiologyCell LineViral entryVirologyHumansGene SilencingEnzyme InhibitorsMicroscopy ImmunoelectronMicroscopy ConfocalbiologyCalpainCytoplasmic VesiclesRNACalpainMolecular biologyCell biologyVirus-Cell InteractionsEnterovirus B HumanViral replicationCell cultureInsect ScienceCalpain-2biology.proteinRNA Viral
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