Search results for "Hsp"

showing 10 items of 557 documents

Heat shock protein-90 toward theranostics: a breath of fresh air in idiopathic pulmonary fibrosis.

2017

Heat shock proteins are potential biomarkers and therapeutic targets in idiopathic pulmonary fibrosis http://ow.ly/fHVP30hJUOl

0301 basic medicinePulmonary and Respiratory MedicinePathologymedicine.medical_specialtyTheranostic NanomedicinePulmonary FibrosisRespiratory SystemHSP90 Heat-Shock ProteinsTheranostic Nanomedicine03 medical and health sciencesIdiopathic pulmonary fibrosisFresh airHeat shock proteinPulmonary fibrosisMedicineHumansHSP90 Heat-Shock ProteinsRespiratory systemMyofibroblastsHeat-Shock Proteinsbusiness.industrymedicine.diseaseIdiopathic Pulmonary Fibrosis030104 developmental biologyPotential biomarkersbusinessThe European respiratory journal
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Molecular chaperones in tumors of salivary glands.

2020

The salivary glands are key components of the mouth and play a central role in its physiology. Their importance may be appreciated considering their number, occurrence in pairs, and distribution in the mouth: two parotids, two submandibular, two sublingual, and many other small ones scattered throughout the mouth. They produce saliva, without which ingestion of non-liquid nutrients and speech would be practically impossible. Nevertheless, the physiology and pathology of salivary glands are poorly understood. For instance, tumors of salivary glands occur, and their incidence is on the rise, but their etiology and pathogenesis are virtually unknown, although some risk factors have been identi…

0301 basic medicineSalivaHistologyPhysiologyDifferential diagnosiBiologyBioinformaticsmedicine.disease_causePathogenesis03 medical and health sciencesstomatognathic systemmedicineHSPAnimalsHumansEndoplasmic Reticulum Chaperone BiPTumorsSalivary glandTumorigenesiChaperoning system030102 biochemistry & molecular biologySalivary glandCell BiologyGeneral MedicineSalivary Gland Neoplasms030104 developmental biologymedicine.anatomical_structureCell Transformation NeoplasticChaperone (protein)Etiologybiology.proteinMolecular chaperoneBiomarker (medicine)Disease SusceptibilityDifferential diagnosisCarcinogenesisMolecular ChaperonesJournal of molecular histology
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Hsp60 quantification in human gastric mucosa shows differences between pathologies with various degrees of proliferation and malignancy grade

2021

Background: Stomach diseases are an important sector of gastroenterology, including proliferative benign

0301 basic medicineTechnologyPathologymedicine.medical_specialtyQH301-705.5QC1-999intestinal metaplasia03 medical and health sciences0302 clinical medicinechaperone systemMetaplasiamedicineGastric mucosaGeneral Materials ScienceBiology (General)QD1-999Instrumentationhealth care economics and organizationsFluid Flow and Transfer Processesbusiness.industryChaperone system Gastric carcinogenesis Gastric dysplasia Gastritis Hsp60 Intestinal metaplasiaSettore BIO/16 - Anatomia UmanaTPhysicsProcess Chemistry and TechnologyStomachdigestive oral and skin physiologygastritisGeneral EngineeringIntestinal metaplasiagastric dysplasiaEngineering (General). Civil engineering (General)Hsp60medicine.diseasedigestive system diseasesComputer Science ApplicationsChemistryGastric Dysplasia030104 developmental biologymedicine.anatomical_structureHyperplastic PolypDysplasia030220 oncology & carcinogenesisgastric carcinogenesisTA1-2040medicine.symptomGastritisbusiness
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BAG2 Interferes with CHIP-Mediated Ubiquitination of HSP72

2016

The maintenance of cellular proteostasis is dependent on molecular chaperones and protein degradation pathways. Chaperones facilitate protein folding, maturation, and degradation, and the particular fate of a misfolded protein is determined by the interaction of chaperones with co-chaperones. The co-factor CHIP (C-terminus of HSP70-inteacting protein, STUB1) ubiquitinates chaperone substrates and directs proteins to the cellular degradation systems. The activity of CHIP is regulated by two co-chaperones, BAG2 and HSPBP1, which are potent inhibitors of the E3 ubiquitin ligase activity. Here, we examined the functional correlation of HSP72, CHIP, and BAG2, employing human primary fibroblasts.…

0301 basic medicineTime FactorsUbiquitin-Protein LigasesImmunoblottingHSP72 Heat-Shock ProteinsUbiquitin-conjugating enzymeProtein degradationArticleCatalysisCell Linelcsh:ChemistryInorganic Chemistry03 medical and health sciencesUbiquitinddc:570Humansaging; BAG2; CHIP; HSP72; proteostasis; ubiquitinationPhysical and Theoretical ChemistryHSP72lcsh:QH301-705.5Molecular BiologyCellular SenescenceSpectroscopySTUB1proteostasisBAG2biologyCHIPagingOrganic ChemistryUbiquitinationGeneral MedicineComputer Science ApplicationsUbiquitin ligaseCell biology030104 developmental biologyProteostasislcsh:Biology (General)lcsh:QD1-999Chaperone (protein)biology.proteinRNA InterferenceProtein foldingMolecular ChaperonesInternational Journal of Molecular Sciences
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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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The HSP90 inhibitor, 17AAG, protects the intestinal stem cell niche and inhibits graft versus host disease development.

2016

IF 7.932; International audience; Graft versus host disease (GvHD), which is the primary complication of allogeneic bone marrow transplantation, can alter the intestinal barrier targeted by activated donor T-cells. Chemical inhibition of the stress protein HSP90 was demonstrated in vitro to inhibit T-cell activation and to modulate endoplasmic reticulum (ER) stress to which intestinal cells are highly susceptible. Since the HSP90 inhibitor 17-allylamino-demethoxygeldanamycin (17AAG) is developed in clinics, we explored here its ability to control intestinal acute GvHD in vivo in two mouse GvHD models (C57BL/6 -> BALB/c and FVB/N -> Lgr5-eGFP), ex vivo in intestine organoids and in vitro in …

0301 basic medicineX-Box Binding Protein 1Cancer ResearchLactams MacrocyclicRNA SplicingT-CellsGraft vs Host Disease[SDV.CAN]Life Sciences [q-bio]/Cancer[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiology[ SDV.CAN ] Life Sciences [q-bio]/CancerHsp90 inhibitor03 medical and health sciencesMiceSensitivityInflammatory-Bowel-diseaseGeneticsmedicineBenzoquinonesAnimals[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyNeural progenitor cellsHSP90 Heat-Shock ProteinsIntestinal MucosaStem Cell Niche[ SDV.GEN.GH ] Life Sciences [q-bio]/Genetics/Human genetics[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyMolecular BiologyLeukemia[ SDV.BC ] Life Sciences [q-bio]/Cellular BiologyBone-Marrow-TransplantationMoleculesmedicine.diseaseStem cell niche3. Good healthIre1-AlphaIntestinesMice Inbred C57BL030104 developmental biologyGraft-versus-host diseaseEr Stress[SDV.GEN.GH]Life Sciences [q-bio]/Genetics/Human geneticsCytoprotectionImmunologyMultiple-MyelomaFemaleOncogene
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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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Functions and Therapeutic Potential of Extracellular Hsp60, Hsp70, and Hsp90 in Neuroinflammatory Disorders

2021

Neuroinflammation is implicated in central nervous system (CNS) diseases, but the molecular mechanisms involved are poorly understood. Progress may be accelerated by developing a comprehensive view of the pathogenesis of CNS disorders, including the immune and the chaperone systems (IS and CS). The latter consists of the molecular chaperones; cochaperones; and chaperone cofactors, interactors, and receptors of an organism and its main collaborators in maintaining protein homeostasis (canonical function) are the ubiquitin–proteasome system and chaperone-mediated autophagy. The CS has also noncanonical functions, for instance, modulation of the IS with induction of proinflammatory cytokines. …

0301 basic medicineamyotrophic lateral sclerosislcsh:TechnologychaperonopathiesProinflammatory cytokinelcsh:Chemistrys disease03 medical and health sciences0302 clinical medicinechaperone systemmedicineamyotrophic lateral sclerosiGeneral Materials Sciencelcsh:QH301-705.5InstrumentationchaperonotherapyNeuroinflammationFluid Flow and Transfer Processesbiologylcsh:TMechanism (biology)Process Chemistry and Technologymolecular chaperonesNeurodegenerationAutophagyGeneral EngineeringParkinson’S diseasemolecular chaperonemedicine.diseaseHuntington’ s diseaseHsp90lcsh:QC1-999Computer Science Applications030104 developmental biologylcsh:Biology (General)lcsh:QD1-999lcsh:TA1-2040multiple sclerosiChaperone (protein)Alzheimerbiology.proteinHSP60lcsh:Engineering (General). Civil engineering (General)Alzheimer’s diseaseNeurosciencelcsh:Physics030217 neurology & neurosurgeryHuntington’s diseaseApplied Sciences
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The Challenging Riddle about the Janus-Type Role of Hsp60 and Related Extracellular Vesicles and miRNAs in Carcinogenesis and the Promises of Its Sol…

2021

Hsp60 is one of the most ancient and evolutionarily conserved members of the chaperoning system. It typically resides within mitochondria, in which it contributes to maintaining the organelle’s proteome integrity and homeostasis. In the last few years, it has been shown that Hsp60 also occurs in other locations, intracellularly and extracellularly, including cytosol, plasma-cell membrane, and extracellular vesicles (EVs). Consequently, non-canonical functions and interacting partners of Hsp60 have been identified and it has been realized that it is a hub molecule in diverse networks and pathways and that it is implicated, directly or indirectly, in the development of various pathological co…

0301 basic medicineanimal structuresBiologyMitochondrionmedicine.disease_causechaperonopathieslcsh:TechnologyChaperoninlcsh:Chemistry03 medical and health sciences0302 clinical medicinemicroRNAmedicineExtracellularGeneral Materials ScienceInstrumentationlcsh:QH301-705.5CarcinogenesichaperonotherapymiRNAFluid Flow and Transfer Processeslcsh:TProcess Chemistry and Technologyextracellular vesicle (EV)fungiGeneral EngineeringHsp60lcsh:QC1-999Computer Science ApplicationsCell biologyCytosol030104 developmental biologylcsh:Biology (General)lcsh:QD1-999lcsh:TA1-2040030220 oncology & carcinogenesisProteomeChaperonopathieHSP60Carcinogenesislcsh:Engineering (General). Civil engineering (General)carcinogenesislcsh:PhysicsApplied Sciences
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The histone deacetylase inhibitor SAHA induces HSP60 nitration and its extracellular release by exosomal vesicles in human lung-derived carcinoma cel…

2015

// Claudia Campanella 1, 2, * , Antonella D'Anneo 3, * , Antonella Marino Gammazza 1, 2, * , Celeste Caruso Bavisotto 1, 2 , Rosario Barone 1, 2 , Sonia Emanuele 4 , Filippa Lo Cascio 1 , Emanuele Mocciaro 1 , Stefano Fais 5 , Everly Conway De Macario 6 , Alberto J.L. Macario 2, 6 , Francesco Cappello 1, 2 , Marianna Lauricella 4 1 Department of Experimental Biomedicine and Clinical Neurosciences, Section of Human Anatomy “Emerico Luna”, University of Palermo, Palermo, Italy 2 Euro-Mediterranean Institute of Science and Technology, Palermo, Italy 3 Department of Biological, Chemical and Pharmaceutical Sciences and Technologies, Laboratory of Biochemistry, University of Palermo, Palermo, Ita…

0301 basic medicineanimal structuresLung Neoplasmsmedicine.drug_classCell SurvivalNitrosationExosomes; Histone deacetylase inhibitor; HSP60; Oxidative stress; SAHAchemical and pharmacologic phenomenaAntineoplastic AgentsApoptosisexosomesBiologyHydroxamic Acidscomplex mixturesMitochondrial Proteins03 medical and health sciencesCell Line TumorSettore BIO/10 - BiochimicamedicineHumansoxidative stressSecretionViability assayCell ProliferationVorinostatHistone deacetylase inhibitorCell growthSettore BIO/16 - Anatomia UmanaHistone deacetylase inhibitorfungiSAHAChaperonin 60MicrovesiclesHistone Deacetylase InhibitorsExosome030104 developmental biologyOncologyApoptosisImmunologyCancer researchOxidative streHSP60Histone deacetylaseProtein Processing Post-TranslationalHSP60Research Paper
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