Search results for " shock"

showing 10 items of 691 documents

Molecular chaperones in the brain endothelial barrier: neurotoxicity or neuroprotection?

2019

Brain microvascular endothelial cells (BMECs) interact with astrocytes and pericytes to form the blood-brain barrier (BBB). Their compromised function alters the BBB integrity, which is associated with early events in the pathogenesis of cancer, neurodegenerative diseases, and epilepsy. Interestingly, these conditions also induce the expression of heat shock proteins (HSPs). Here we review the contribution of major HSP families to BMEC and BBB function. Although investigators mainly report protective effects of HSPs in brain, contrasted results were obtained in BMEC, which depend both on the HSP and on its location, intra- or extracellular. The therapeutic potential of HSPs must be scrupulo…

0301 basic medicineReviewBiochemistryNeuroprotectionPathogenesis03 medical and health sciencesEpilepsy0302 clinical medicineHeat shock proteinGeneticsExtracellularMedicineAnimalsHumansMolecular Biologybusiness.industryNeurotoxicityCancerBrainEndothelial CellsBiological TransportCell Differentiationmedicine.diseaseNeuroprotectionCell biology030104 developmental biologyBlood-Brain Barriercardiovascular systembusiness030217 neurology & neurosurgeryFunction (biology)BiotechnologyMolecular ChaperonesFASEB journal : official publication of the Federation of American Societies for Experimental Biology
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Heat shock protein 70 dampens the inflammatory response of human PDL cells to mechanical loading in vitro

2019

BACKGROUND AND OBJECTIVE Previously, we demonstrated an inflammatory response of human PDL (hPDL) cells to mechanical loading. The cellular reaction was dampened by heat pre-treatment suggesting a protective role for heat shock proteins (HSP) during stress-induced ischemia. Here we explored if HSP70, which has already been documented in the pressure zone of tooth movement, might be regulatorily involved in the attenuation of the inflammatory response. MATERIALS AND METHODS Fifth passage hPDL cells were mechanically loaded in the presence of the HSP70 inhibitor VER155008. Cell morphology, HSP70 expression, viability, IL-6 and IL-8 expression were determined by means of microscopy, realtime-P…

0301 basic medicineTooth Movement TechniquesPeriodontal LigamentInflammatory responseIschemiaOsteoclastsCell morphology03 medical and health sciences0302 clinical medicineHeat shock proteinmedicineHumansHSP70 Heat-Shock ProteinsCells CulturedInflammationChemistry030206 dentistryAdhesionmedicine.diseaseIn vitroHsp70Cell biologyCell stress030104 developmental biologyPeriodonticsStress MechanicalJournal of Periodontal Research
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Effects of muscular dystrophy, exercise and blocking activin receptor IIB ligands on the unfolded protein response and oxidative stress

2016

Protein homeostasis in cells, proteostasis, is maintained through several integrated processes and pathways and its dysregulation may mediate pathology in many diseases including Duchenne muscular dystrophy (DMD). Oxidative stress, heat shock proteins, endoplasmic reticulum (ER) stress and its response, i.e. unfolded protein response (UPR), play key roles in proteostasis but their involvement in the pathology of DMD are largely unknown. Moreover, exercise and activin receptor IIB blocking are two strategies that may be beneficial to DMD muscle, but studies to examine their effects on these proteostasis pathways are lacking. Therefore, these pathways were examined in the muscle of mdx mice, …

0301 basic medicineX-Box Binding Protein 1Activin Receptors Type IIEukaryotic Initiation Factor-2MyostatinUPRBiochemistryMiceeIF-2 KinaseThioredoxinsSirtuin 1ENDOPLASMIC-RETICULUM STRESSDISULFIDE-ISOMERASEPhosphorylationta315Endoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsIN-VIVOta3141Activin receptorMOUSE MODELER STRESSEndoplasmic Reticulum Stress3. Good healthmedicine.anatomical_structuremyostatinPRESERVES MUSCLE FUNCTIONER-stressSKELETAL-MUSCLEmdxSignal TransductionEXPRESSIONmedicine.medical_specialtyXBP1MDX MICEBiologyProtein Serine-Threonine Kinases03 medical and health sciencesPhysiology (medical)Internal medicineHeat shock proteinPhysical Conditioning AnimalEndoribonucleasesmedicineAnimalsHumansRNA MessengerMuscle SkeletalSkeletal muscleMyostatinGENEActivating Transcription Factor 6Immunoglobulin Fc FragmentsMuscular Dystrophy DuchenneDisease Models Animal030104 developmental biologyProteostasisEndocrinologyGene Expression RegulationUnfolded protein responsebiology.proteinMice Inbred mdxProteostasisUnfolded Protein Response3111 BiomedicineCarrier ProteinsACVR2B
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Impact of polymer-modified gold nanoparticles on brain endothelial cells: exclusion of endoplasmic reticulum stress as a potential risk factor

2016

A library of polymer-coated gold nanoparticles (AuNPs) differing in size and surface modifications was examined for uptake and induction of cellular stress responses in the endoplasmic reticulum (ER stress) in human brain endothelial cells (hCMEC/D3). ER stress is known to affect the physiology of endothelial cells (ECs) and may lead to inflammation or apoptosis. Thus, even if applied at non-cytotoxic concentrations ER stress caused by nanoparticles should be prevented to reduce the risk of vascular diseases and negative effects on the integrity of barriers (e.g. blood-brain barrier). We exposed hCMEC/D3 to twelve different AuNPs (three sizes: 18, 35, and 65 nm, each with four surface-modif…

0301 basic medicineXBP1BiPCell SurvivalPolymersBiomedical EngineeringMetal NanoparticlesApoptosis02 engineering and technologyBiologyEndoplasmic ReticulumToxicologyArticleCell LineProinflammatory cytokine03 medical and health sciencescell stressDownregulation and upregulationRisk FactorsHeat shock proteinAnimalsHumansHSP70 Heat-Shock ProteinsParticle SizeHeat-Shock ProteinsATF6Endoplasmic reticulumInterleukin-8ATF4Endothelial CellsMembrane Proteinsunfolded protein responseEndoplasmic Reticulum Stress021001 nanoscience & nanotechnologyQPActivating Transcription Factor 4Cell biology030104 developmental biologyBlood-Brain Barriertight junction proteinsImmunologyUnfolded protein responseGold0210 nano-technologyTranscription Factor CHOPNanotoxicology
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Viable But Not Culturable (VBNC) state of Brettanomyces bruxellensis in wine: New insights on molecular basis of VBNC behaviour using a transcriptomi…

2016

International audience; The spoilage potential of Brettanomyces bruxellensis in wine is strongly connected with the aptitude of this yeast to enter in a Viable But Non Culturable (VBNC) state when exposed to the harsh wine conditions. In this work, we characterized the VBNC behaviour of seven strains of B. bruxellensis representing a regional intraspecific biodiversity, reporting conclusive evidence for the assessment of VBNC as a strain-dependent character. The VBNC behaviour was monitored by fluorescein diacetate staining/flow cytometry for eleven days after addition of 0.4, 0.6, 0.8, 1 and 1.2 mg/L of molecular SO2 (entrance in the VBNC state) and after SO2 removal (exit from the VBNC st…

0301 basic medicine[ SDV.AEN ] Life Sciences [q-bio]/Food and NutritionColony Count MicrobialExpressionSaccharomyces-cerevisiaeTranscriptometranscriptomicsHomeostasisSulfur DioxideHeat-Shock Proteinsmedicine.diagnostic_testViabilityCarbohydrate MetabolismOxidation-ReductionVolatile phenol production030106 microbiologyBrettanomyces bruxellensisBrettanomycesBiologyFlow cytometryMicrobiology03 medical and health sciencesPhenolsHeat shock proteinsulphitemedicineSulfiteswineGeneRna-seqBrettanomyces; spoilage; sulphite; transcriptomics; Viable But Not Culturable (VBNC); wine; food science; microbiologyWineMicrobial ViabilityGene Expression ProfilingspoilagemicrobiologyDNA replicationNonculturable bacteriabiology.organism_classificationCampylobacter-jejuniSulfur-dioxideYeastYeastCulture MediaOxidative StressFood MicrobiologyViable But Not Culturable (VBNC)food science[SDV.AEN]Life Sciences [q-bio]/Food and NutritionSettore AGR/16 - Microbiologia Agraria
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The Antisense RNA Approach: a New Application for In Vivo Investigation of the Stress Response of Oenococcus oeni, a Wine-Associated Lactic Acid Bact…

2015

ABSTRACT Oenococcus oeni is a wine-associated lactic acid bacterium mostly responsible for malolactic fermentation in wine. In wine, O. oeni grows in an environment hostile to bacterial growth (low pH, low temperature, and ethanol) that induces stress response mechanisms. To survive, O. oeni is known to set up transitional stress response mechanisms through the synthesis of heat stress proteins (HSPs) encoded by the hsp genes, notably a unique small HSP named Lo18. Despite the availability of the genome sequence, characterization of O. oeni genes is limited, and little is known about the in vivo role of Lo18. Due to the lack of genetic tools for O. oeni , an efficient expression vector in O…

0301 basic medicine[SDV.BIO]Life Sciences [q-bio]/Biotechnology[ SDV.AEN ] Life Sciences [q-bio]/Food and Nutrition030106 microbiologyLactobacillus-plantarumWineEscherichia-coliApplied Microbiology and Biotechnologymolecular characterization03 medical and health sciencesGrowth-phaseBacterial ProteinsMembrane stabilizationHeat shock protein[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]Antisense TechnologyGene expression[SDV.IDA]Life Sciences [q-bio]/Food engineeringMalolactic fermentationEnvironmental MicrobiologyRNA AntisenseGene-expressionLactic AcidHeat-Shock ProteinsOenococcusOenococcus oeniLeuconostoc-oenosEcologybiologyEthanolLactococcus lactisMalolactic fermentation[ SDV.BIO ] Life Sciences [q-bio]/BiotechnologyGene Expression Regulation Bacterialbiology.organism_classification[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/BacteriologyAntisense RNABiochemistryLactococcus-lactisHeat-shock-proteinFermentationOenococcusFood ScienceBiotechnology
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Heat Shock Protein 60 in Cardiovascular Physiology and Diseases.

2020

Heat shock protein 60 (HSP60) is a highly conserved protein abundantly expressed in both prokaryotic and eukaryotic cells. In mammals, HSP60 has been primarily considered to reside in the mitochondria, where HSP60 and HSP10 form a complex and facilitate mitochondrial protein folding. However, HSP60 is also observed in the cytoplasm, the plasma membrane, and the extracellular space. HSP60 regulates a broad spectrum of cellular events including protein trafficking, peptide hormone signaling, cell survival, cell proliferation, inflammation, and immunization. In the cardiovascular system, growing evidence indicates that HSP60 could not only play an important role under physiological conditions,…

0301 basic medicineanimal structuresMini Reviewheat shock proteinheart failureInflammationchemical and pharmacologic phenomenacardiomyocyteBiologyMitochondrionBiochemistry Genetics and Molecular Biology (miscellaneous)Biochemistrycomplex mixtures03 medical and health sciences0302 clinical medicineHeat shock proteinmedicineMolecular Bioscienceslcsh:QH301-705.5Molecular BiologyCell growthfungiCardiovascular physiologyCell biology030104 developmental biologylcsh:Biology (General)Cytoplasm030220 oncology & carcinogenesisHSP60medicine.symptomSignal transductionatherosclerosisHSP60Frontiers in molecular biosciences
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Complex Destabilization in the Mitochondrial Chaperonin Hsp60 Leads to Disease.

2020

Several neurological disorders have been linked to mutations in chaperonin genes and more specifically to the HSPD1 gene. In humans, HSPD1 encodes for the mitochondrial Heat Shock Protein 60 (mtHsp60) chaperonin, which carries out essential protein refolding reactions that help maintain mitochondrial and cellular homeostasis. It functions as a macromolecular complex that provides client proteins an environment that favors proper folding in an ATP dependent manner. It has been established that mtHsp60 plays a crucial role in the proper folding of mitochondrial proteins involved in ATP producing pathways. Recently, various single-point mutations in the mtHsp60 encoding gene have been directly…

0301 basic medicinechaperoninMini ReviewCellular homeostasisBiologyBiochemistry Genetics and Molecular Biology (miscellaneous)BiochemistryGroELChaperonin03 medical and health sciences0302 clinical medicineHeat shock proteinprotein foldingmtHsp60Molecular BiosciencesMolecular Biologylcsh:QH301-705.5Point mutationGroELFKBP5 GeneCell biology030104 developmental biologylcsh:Biology (General)030220 oncology & carcinogenesisHSP60Protein foldingchaperonopathyFrontiers in molecular biosciences
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Heat Shock Proteins in Alzheimer’s Disease: Role and Targeting

2018

Among diseases whose cure is still far from being discovered, Alzheimer’s disease (AD) has been recognized as a crucial medical and social problem. A major issue in AD research is represented by the complexity of involved biochemical pathways, including the nature of protein misfolding, which results in the production of toxic species. Considering the involvement of (mis)folding processes in AD aetiology, targeting molecular chaperones represents a promising therapeutic perspective. This review analyses the connection between AD and molecular chaperones, with particular attention toward the most important heat shock proteins (HSPs) as representative components of the human chaperome: Hsp60,…

0301 basic medicineheat shock proteinDiseaseReviewprotein TauHsp70lcsh:ChemistrychaperoneEnzyme Inhibitorslcsh:QH301-705.5SpectroscopybiologyGeneral MedicineHsp60Hsp90Computer Science Applicationsamyloid peptideModels AnimalHSP60Protein foldingAlzheimer’s diseaseheat shock proteins; chaperones; Alzheimer’s disease; amyloid peptide; protein Tau; Hsp60; Hsp70; Hsp90Tau proteintau ProteinsHsp90Computational biologyCatalysisInorganic ChemistryMitochondrial Proteins03 medical and health sciencesAlzheimer DiseaseHeat shock proteinAnimalsHumanschaperonesHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsPhysical and Theoretical ChemistryMolecular BiologyAmyloid beta-PeptidesSettore BIO/16 - Anatomia UmanaOrganic ChemistryChaperonin 60Settore CHIM/06 - Chimica OrganicaHsp70030104 developmental biologylcsh:Biology (General)lcsh:QD1-999heat shock proteinsbiology.protein
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Elevated sodium leads to the increased expression of HSP60 and induces apoptosis in HUVECs

2017

Atherosclerosis is the leading cause of death in the world. We have previously shown that expression of heat shock protein 60 (HSP60) on the surface of endothelial cells is the main cause of initiating the disease as it acts as a T cell auto-antigen and can be triggered by classical atherosclerosis risk factors, such as infection (e.g. Chlamydia pneumoniae), chemical stress (smoking, oxygen radicals, drugs), physical insult (heat, shear blood flow) and inflammation (inflammatory cytokines, lipopolysaccharide, oxidized low density lipoprotein, advanced glycation end products). In the present study, we show that increasing levels of sodium chloride can also induce an increase in intracellular…

0301 basic medicinelcsh:MedicineApoptosisBlood PressureSodium Chloride030204 cardiovascular system & hematologyVascular MedicineHeat Shock ResponseEpitheliumUmbilical veinWhite Blood CellsSpectrum Analysis Techniques0302 clinical medicineAnimal CellsGlycationMedicine and Health Scienceslcsh:ScienceCellular Stress ResponsesMultidisciplinaryCell DeathT CellsFlow CytometryProtein TransportChemistryCell ProcessesSpectrophotometryPhysical SciencesHypertensionCytophotometryCellular TypesAnatomymedicine.symptomIntracellularResearch Articlemedicine.medical_specialtyImmune CellsSodiumImmunologychemistry.chemical_elementInflammationBiologyResearch and Analysis MethodsImmunophenotypingProinflammatory cytokine03 medical and health sciencesInternal medicineHeat shock proteinHuman Umbilical Vein Endothelial CellsmedicineHumansHeat shockBlood CellsSodiumlcsh:RChemical CompoundsBiology and Life SciencesEndothelial CellsEpithelial CellsChaperonin 60Cell BiologyAtherosclerosisBiological Tissue030104 developmental biologyEndocrinologyGene Expression RegulationchemistryImmunologySaltslcsh:QBiomarkersPLOS ONE
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