Search results for "Shock proteins"

showing 10 items of 347 documents

Effects of intrinsic aerobic capacity, aging and voluntary running on skeletal muscle sirtuins and heat shock proteins

2016

Aim Sirtuins are proteins that connect energy metabolism, oxidative stress and aging. Expression of heat shock proteins (Hsps) is regulated by heat shock factors (HSFs) in response to various environmental and physiological stresses, such as oxidative stress. Oxidative stress accumulates during aging which makes cells more prone to DNA damage. Although many experimental animal models have been designed to study the effects of knockdown or overexpression of sirtuins, HSFs and Hsps, little is known about how aging per se affects their expression. Here we study the impact of intrinsic aerobic capacity, aging and voluntary exercise on the levels of sirtuins, HSFs and Hsps in skeletal muscle. Me…

0301 basic medicineAgingmedicine.medical_specialtyphysical activityCitrate (si)-SynthaseOxidative phosphorylationta3111medicine.disease_causeBiochemistryRunning03 medical and health sciences0302 clinical medicineEndocrinologyPhysical Conditioning AnimalHeat shock proteinInternal medicineGeneticsmedicineAnimalsSirtuinsAerobic exerciseta318skeletal muscleta315Muscle Skeletaloksidatiivinen stressiMolecular BiologyHeat-Shock ProteinsAerobic capacitybiologyagingBody WeightSkeletal muscleRats Inbred StrainsCell BiologyHsp70sirtuinOxidative Stress030104 developmental biologymedicine.anatomical_structureEndocrinologySirtuinbiology.proteinFemaleEnergy Intake030217 neurology & neurosurgeryOxidative stressExperimental Gerontology
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Heat shock protein (Hsp) regulation by muscarinic acetylcholine receptor (mAChR) activation in the rat hippocampus.

2018

The cholinergic system plays a crucial role in modulating in the central nervous system physiological responses such as neurogenesis, neuronal differentiation, synaptic plasticity, and neuroprotection. In a recent study, we showed that Oxotremorine-M, a non-selective muscarinic acetylcholine receptor agonist, is able to transactivate the fibroblast growth factor receptor and to produce a significant increase in the hippocampal primary neurite outgrowth. In the present study we aimed to explore in the rat hippocampus the possible effect of acute or chronic treatment with Oxotremorine-M on some heat shock proteins (Hsp60, Hsp70, Hsp90) and on activation of related transcription factor heat sh…

0301 basic medicineAgonistMalemedicine.medical_specialtymedicine.drug_classPhysiologyClinical BiochemistryNeuronal OutgrowthScopolamineheat shock proteinHsp90NeuroprotectionHippocampusHsp7003 medical and health sciencesmuscarinic receptor0302 clinical medicineHeat Shock Transcription FactorsHeat shock proteinInternal medicineMuscarinic acetylcholine receptormedicineOxotremorineAnimalsRats WistarHSF1Heat-Shock ProteinsNeuronsNeuronal PlasticityChemistryOxotremorineNeurodegenerative DiseasesCell BiologyReceptors Fibroblast Growth FactorReceptors MuscarinicHsp70Rats030104 developmental biologyEndocrinologyheat shock factor 1HSP60030217 neurology & neurosurgerymedicine.drugSignal TransductionJournal of cellular physiology
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The cytoprotective protein MANF promotes neuronal survival independently from its role as a GRP78 cofactor

2021

Mesencephalic astrocyte-derived neurotrophic factor (MANF) is an endoplasmic reticulum (ER)-stress-regulated protein exhibiting cytoprotective properties through a poorly understood mechanism in various in vitro and in vivo models of neuronal and non-neuronal damage. Although initially characterized as a secreted neurotrophic factor for midbrain dopamine neurons, MANF has recently gained more interest for its intracellular role in regulating the ER homeostasis, including serving as a cofactor of the chaperone glucose-regulated protein 78 (GRP78). We aimed for a better understanding of the neuroprotective mechanisms of MANF. Here we show for the first time that MANF promotes the survival of …

0301 basic medicineBiFC bimolecular fluorescence complementationMST microscale thermophoresisPDIA1 protein disulfide isomerase family A member 1ApoptosisNEUROTROPHIC FACTOR MANFEndoplasmic ReticulumBiochemistryprotein-protein interactionMiceBimolecular fluorescence complementationUPR unfolded protein responseENDOPLASMIC-RETICULUM STRESSMesencephalonNeurotrophic factorsInsulin-Secreting CellsProtein Interaction MappingBINDINGCOMPREHENSIVE RESOURCEATF6unfolded protein response (UPR)PDIA6 protein disulfide isomerase family A member 6PPIs protein-protein interactionsEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsNPTN neuroplastinbiologyChemistryapoptosisunfolded protein responsedopamine neurons3. Good healthCell biologyGDNF glial cell line–derived neurotrophic factorIRE1-ALPHASBD substrate-binding domainendoplasmic reticulum stressMANF mesencephalic astrocyte-derived neurotrophic factorTm tunicamycinneuroprotectionResearch ArticleProtein BindingSignal TransductionGRP78Protein Disulfide-Isomerase FamilyCell SurvivalTH tyrosine hydroxylasePrimary Cell CultureSCG superior cervical ganglionProtein Disulfide-IsomerasesIRE1 inositol-requiring enzyme 1ER-STRESSER endoplasmic reticulum03 medical and health sciencesohjelmoitunut solukuolemaC-MANF C-terminal domain of MANFCSPs chemical shift perturbationsAnimalsHumansHSP70 Heat-Shock ProteinsNerve Growth FactorsNBD nucleotide-binding domainNMR nuclear magnetic resonanceMolecular Biology030102 biochemistry & molecular biologyBIPATF6Dopaminergic NeuronsGene Expression ProfilingBinding proteinneuronal cell deathDISSOCIATIONCell BiologyNEI nucleotide exchange inhibitorEmbryo MammalianadenosiinitrifosfaattiATPhermosolutmesencephalic astrocyte-derived neurotrophic factorprotein–protein interactionPERK protein kinase RNA-like ER kinaseHEK293 Cells030104 developmental biologyGene Expression RegulationChaperone (protein)Tg thapsigarginbiology.proteinUnfolded protein responseAP-MS affinity purification mass spectrometry1182 Biochemistry cell and molecular biologyGFP-SH SH-tagged GFPendoplasmic reticulum stress (ER stress)DA dopaminemesencephalic astrocyte-derived neurotrophic factor (MANF)proteiinitNeuroplastin
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Membrane-anchored heat-shock protein 70 (Hsp70) in cancer.

2020

International audience; Hsp70 is a highly conserved and inducible heat shock protein that belongs to the HSP70 family of molecular chaperones and plays a central role in protein homeostasis. The main function of Hsp70 is to protect cells from physiological, pathological and environmental insults, as it assists an ATP-dependent manner the process of protein folding. Since Hsp70 provides critical cell survival functions, cancer cells are assumed to rely on this chaperone. Strong evidence suggests that Hsp70 is upregulated in different type of cancers and is involved in tumor growth, invasion, migration and resistance to anti-cancer therapy. Interestingly, this Hsp70 upregulation induces Hsp70…

0301 basic medicineCancer ResearchCarcinogenesisCell SurvivalHsp70 translocation[SDV]Life Sciences [q-bio]Antineoplastic AgentsExosomesTargeting Hsp7003 medical and health sciences0302 clinical medicineDownregulation and upregulationHeat shock proteinNeoplasmsExtracellularHumansHSP70 Heat-Shock ProteinsExosomal Hsp70biologyChemistryCell MembraneHsp70Cell biologyUp-Regulation[SDV] Life Sciences [q-bio]030104 developmental biologyMembraneMembrane Hsp70Oncology030220 oncology & carcinogenesisChaperone (protein)Cancer cellbiology.proteinDisease ProgressionProtein foldingCancer letters
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The Binding Mechanism of Epolactaene to Hsp60 Unveiled by in Silico Modelling

2016

Molecular Dynamics (MD) simulations and DFT/MM calculations were performed in order to rationalize available experimental results and to provide structural details on the binding mechanism of Epolactaene (EPO) to the 60 KDa Heat Shock Protein (Hsp60). The available crystal structure of Hsp60 represents the last step of the chaperone folding cycle, while the Hsp60-EPO complex was obtained by using a homology model of Hsp60, in order to simulate a state related to the beginning of the folding cycle (Rs1). The results of MD simulations point out that EPO shows the highest binding affinity for the empty ATP binding site. The presence of ATP opens a channel that allows the entrance of both EPO d…

0301 basic medicineConformational changeanimal structuresStereochemistryProteins · Molecular Dynamics · Density Functional Theory · Heat Shock Proteins · Epolactaene010402 general chemistry01 natural sciences03 medical and health sciencesMolecular dynamicschemistry.chemical_compoundHeat shock proteinHomology modelingBinding siteEpolactaenebiologyChemistrySettore BIO/16 - Anatomia UmanafungiGeneral ChemistrySettore CHIM/06 - Chimica Organica0104 chemical sciencesCrystallography030104 developmental biologyCovalent bondSettore CHIM/03 - Chimica Generale E InorganicaChaperone (protein)biology.protein
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Exosome secretion by Leishmania infantum modulate the chemotactic behavior and cytokinic expression creating an environment permissive for early infe…

2019

Abstract In recent years, several studies demonstrated the role of exosomes in intercellular communications, several Leishmania species belonging to subgenera Leishmania and Viannia have been demonstrated to release exosomes, and their role in parasite-macrophage interactions and in leishmaniasis development has been investigated. However, the release of exosomes by Leishmania infantum has not been studied so far. The aim of this study was to isolate and characterize L. infantum exosomes, and to investigate the biological activity of these exosomes in macrophage cultures. To this end, exosomes were collected from both amastigote and promastigote L. infantum conditioned medium by ultracentri…

0301 basic medicineCytokines production; Exosomes; Leishmania infantum030231 tropical medicineImmunologyGene ExpressionBiologyExosomesExosomeMicrobiology03 medical and health sciences0302 clinical medicineImmune systemparasitic diseasesMacrophageHumansHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsLeishmania infantumAmastigoteCytokineHSP70 Heat-Shock ProteinCytokines productionChemotaxisInterleukin-18InterleukinChemotaxiGeneral MedicineU937 Cells030108 mycology & parasitologybiology.organism_classificationLeishmaniaMicrovesiclesInterleukin-10ExosomeHSP90 Heat-Shock ProteinInfectious DiseasesCytokinesParasitologyLeishmania infantumHumanExperimental parasitology
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Hsp40 Is Involved in Cilia Regeneration in Sea Urchin Embryos

2003

In a previous paper we demonstrated that, in Paracentrotus lividus embryos, deciliation represents a specific kind of stress that induces an increase in the levels of an acidic protein of about 40 kD (p40). Here we report that deciliation also induces an increase in Hsp40 chaperone levels and enhancement of its ectodermal localization. We suggest that Hsp40 might play a chaperoning role in cilia regeneration.

0301 basic medicineEmbryo NonmammalianHistologyParacentrotus lividus03 medical and health sciences0302 clinical medicineStress PhysiologicalCulture Techniquesbiology.animalEctodermBotanyAnimalsRegenerationElectrophoresis Gel Two-DimensionalCiliaSettore BIO/06 - Anatomia Comparata E CitologiaSea urchinHeat-Shock ProteinsCentrosomebiologyCiliumEmbryoHSP40 Heat-Shock ProteinsSea urchin embryobiology.organism_classificationHsp40 deciliation sea urchinCell biology030104 developmental biologySea UrchinsAnatomy030217 neurology & neurosurgeryMolecular Chaperones
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Exosomes in cancer theranostic: Diamonds in the rough

2017

IF 3.306; International audience; During the last 10 years, exosomes, which are small vesicles of 50-200 nm diameter of endosomal origin, have aroused a great interest in the scientific and clinical community for their roles in intercellular communication in almost all physiological and pathological processes. Most cells can potentially release these nanovesicles that share with the parent cell a similar lipid bilayer with transmembrane proteins and a panel of enclosed soluble proteins such as heat shock proteins and genetic material, thus acting as potential nanoshuttles of biomarkers. Exosomes surface proteins allow their targeting and capture by recipient cells, while the exosomes' conte…

0301 basic medicineEndosomeReviewexosomes[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyModels BiologicalTheranostic NanomedicineMetastasis03 medical and health sciencesCellular and Molecular NeuroscienceDrug Delivery SystemsNeoplasmsHeat shock proteincancer diagnosisBiomarkers TumormedicineAnimalsHumansTumor microenvironment[ SDV.BC ] Life Sciences [q-bio]/Cellular BiologyCancerCell Biologymedicine.diseasePrimary tumorMicrovesicles3. Good healthCell biology030104 developmental biologyTumor progressionheat shock proteinscancer therapy
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HSP110 sustains chronic NF-κB signaling in activated B cell diffuse large B cell lymphoma through MyD88 stabilization

2018

International audience; Activated B cell diffuse large B cell lymphoma (ABC-DLBCL) is an aggressive lymphoproliferative disorder involving chronic NF-κB activation. Several mutations in the BCR and the MyD88 signaling pathway components, such as MyD88 L265P, are implicated in this aberrant activation. Among heat-shock proteins, HSP110 has recently been identified as a pro- survival and/or proliferation factor in many cancers but its role in ABC-DLBCL survival mechanisms remained to be established. We observed that shRNA-mediated HSP110 silencing decreased the survival of several ABC-DLBCL cell lines, decreased IgM-MyD88 co-localization and subsequent NF-κB signaling. Conversely, over-expres…

0301 basic medicineImmunology[SDV.CAN]Life Sciences [q-bio]/CancerBiochemistry[ SDV.CAN ] Life Sciences [q-bio]/CancerCohort Studies03 medical and health sciencesimmune system diseaseshemic and lymphatic diseasesmedicineTumor Cells CulturedGene silencingHumansHSP110 Heat-Shock ProteinsB cellChemistryProtein StabilityWild typebreakpoint cluster regionNF-kappa BCell BiologyHematologymedicine.disease3. Good healthLymphoma030104 developmental biologymedicine.anatomical_structureCell cultureMyeloid Differentiation Factor 88Cancer researchLymphoma Large B-Cell DiffuseSignal transductionDiffuse large B-cell lymphomaSignal Transduction
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Conformational dynamics of a single protein monitored for 24 hours at video rate

2018

We use plasmon rulers to follow the conformational dynamics of a single protein for up to 24 h at a video rate. The plasmon ruler consists of two gold nanospheres connected by a single protein linker. In our experiment, we follow the dynamics of the molecular chaperone heat shock protein 90 (Hsp90), which is known to show “open” and “closed” conformations. Our measurements confirm the previously known conformational dynamics with transition times in the second to minute time scale and reveals new dynamics on the time scale of minutes to hours. Plasmon rulers thus extend the observation bandwidth 3–4 orders of magnitude with respect to single-molecule fluorescence resonance energy transfer a…

0301 basic medicineLetterProtein ConformationMolecular ConformationFOS: Physical sciencesHsp90Bioengineeringsingle molecule02 engineering and technology7. Clean energyQuantitative Biology - Quantitative Methods03 medical and health sciencesMolecular dynamicsFluorescence Resonance Energy TransferNanotechnologyGeneral Materials ScienceHSP90 Heat-Shock ProteinsPhysics - Biological PhysicsQuantitative Methods (q-bio.QM)PlasmonPhysicsVideo rateMechanical EngineeringProtein dynamics92Biomolecules (q-bio.BM)General ChemistrySurface Plasmon Resonance021001 nanoscience & nanotechnologyCondensed Matter PhysicsGold nanospheres030104 developmental biologyFörster resonance energy transferQuantitative Biology - BiomoleculesBiological Physics (physics.bio-ph)Chemical physicsFOS: Biological sciencesprotein dynamicsPlasmon rulernonergodicityGold0210 nano-technologyLinker
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