Search results for "Hsp"

showing 10 items of 557 documents

In vivoanalysis of the lumenal binding protein (BiP) reveals multiple functions of its ATPase domain

2007

International audience; The endoplasmic reticulum (ER) chaperone binding protein (BiP) binds exposed hydrophobic regions of misfolded proteins. Cycles of ATP hydrolysis and nucleotide exchange on the ATPase domain were shown to regulate the function of the ligand-binding domain in vitro. Here we show that ATPase mutants of BiP with defective ATP-hydrolysis (T46G) or ATP-binding (G235D) caused permanent association with a model ligand, but also interfered with the production of secretory, but not cytosolic, proteins in vivo. Furthermore, the negative effect of BiP(T46G) on secretory protein synthesis was rescued by increased levels of wild-type BiP, whereas the G235D mutation was dominant. U…

0106 biological sciencesgenetic structuresRecombinant Fusion ProteinsATPaseBlotting WesternGreen Fluorescent ProteinsPlant ScienceBINDING PROTEINEndoplasmic ReticulumModels Biological01 natural sciencesChromatography Affinity[SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants genetics03 medical and health sciencesAdenosine TriphosphateTobaccoPROTEIN FOLDINGGeneticsImmunoprecipitationEndoplasmic Reticulum Chaperone BiPHSP70Heat-Shock Proteins030304 developmental biologyCHAPERONEAdenosine Triphosphatases0303 health sciencesbiologyHydrolysisProtoplastsEndoplasmic reticulumBinding proteinCell BiologyPlants Genetically ModifiedLigand (biochemistry)Secretory proteinBiochemistryChaperone (protein)MutationChaperone bindingbiology.proteinATPASEElectrophoresis Polyacrylamide GelProtein foldingMolecular ChaperonesProtein BindingSignal Transduction010606 plant biology & botanyThe Plant Journal
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Human skeletal muscle type 1 fibre distribution and response of stress-sensing proteins along the titin molecule after submaximal exhaustive exercise.

2017

Early responses of stress-sensing proteins, muscle LIM protein (MLP), ankyrin repeat proteins (Ankrd1/CARP and Ankrd2/Arpp) and muscle-specific RING finger proteins (MuRF1 and MuRF2), along the titin molecule were investigated in the present experiment after submaximal exhaustive exercise. Ten healthy men performed continuous drop jumping unilaterally on a sledge apparatus with a submaximal height until complete exhaustion. Five stress-sensing proteins were analysed by mRNA measurements from biopsies obtained immediately and 3 h after the exercise from exercised vastus lateralis muscle while control biopsies were obtained from non-exercised legs before the exercise. Decreased maximal jump h…

0301 basic medicineANKRD2AdultMalemedicine.medical_specialtyANKRD1HistologyAdolescentVastus lateralis musclePhysical ExertionMuscle Proteinslihaksetmedicine.disease_causetuki- ja liikuntaelimet03 medical and health sciencesYoung Adult0302 clinical medicineJumpingHsp27Internal medicinemedicinestress-sensing proteinsHumanstitinConnectinMolecular BiologyExerciseurheiluvammatbiologySkeletal muscleCell BiologyAnatomyhuman skeletal muscleMedical Laboratory Technology030104 developmental biologymedicine.anatomical_structureEndocrinologyMuscle Fibers Slow-Twitchbiology.proteinexercise induced muscle damageTitinAnkyrin repeat030217 neurology & neurosurgeryHistochemistry and cell biology
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Quantitative patterns of Hsps in tubular adenoma compared with normal and tumor tissues reveal the value of Hsp10 and Hsp60 in early diagnosis of lar…

2016

Large bowel carcinogenesis involves accumulation of genetic alterations leading to transformation of normal mucosa into dysplasia and, lastly, adenocarcinoma. It is pertinent to elucidate the molecular changes occurring in the pre-neoplastic lesions to facilitate early diagnosis and treatment. Heat shock proteins (Hsps), many of which are molecular chaperones, are implicated in carcinogenesis, and their variations with tumor progression encourage their study as biomarkers. There are many reports on Hsps and cancer but none to our knowledge on their systematic quantification in pre-neoplastic lesions of the large bowel. We performed immunohistochemical determinations of Hsp10, Hsp60, Hsp70, …

0301 basic medicineAdenomaMaleDysplasiaPathologymedicine.medical_specialtyColorectal cancerColonLarge bowelChaperoneBiologyAdenocarcinomamedicine.disease_causeBiochemistryMitochondrial Proteins03 medical and health sciencesBiomarker; Chaperone; Dysplasia; Hsps; Large bowel; Tubular adenoma; Biochemistry; Cell Biology0302 clinical medicineTubular adenomaHeat shock proteinmedicineBiomarkers TumorChaperonin 10HspHumansIntestinal MucosaEarly Detection of CancerAgedTubular adenomaAged 80 and overLamina propriaOriginal PaperBiomarkerCell BiologyChaperonin 60Middle Agedmedicine.disease030104 developmental biologymedicine.anatomical_structureDysplasiaTumor progression030220 oncology & carcinogenesisCase-Control StudiesImmunologyAdenocarcinomaFemaleCarcinogenesisColorectal Neoplasms
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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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ALCOHOLIC LIVER DISEASE: A MOUSE MODEL REVEALS PROTECTION BY LACTOBACILLUS FERMENTUM

2016

Objectives Alcoholism is one of the most devastating diseases with high incidence, but knowledge of its pathology and treatment is still plagued with gaps mostly because of the inherent limitations of research with patients. We developed an animal model for studying liver histopathology, Hsp (heat-shock protein)-chaperones involvement, and response to treatment. Methods The system was standardized using mice to which ethanol was orally administered alone or in combination with Lactobacillus fermentum following a precise schedule over time and applying, at predetermined intervals, a battery of techniques (histology, immunohistochemistry, western blotting, real-time PCR, immunoprecipitation, …

0301 basic medicineAlcoholic liver diseasePathologymedicine.medical_specialtyLactobacillus fermentumOriginal ContributionsPharmacologylaw.invention03 medical and health sciencesProbioticLiver diseaselawFibrosismedicineSettore BIO/06 - Anatomia Comparata E Citologiaprobiotics lactobacillus fermentum alcoholic liver diesease HspSettore MED/12 - Gastroenterologiabiologybusiness.industryGastroenterologymedicine.diseasebiology.organism_classificationNitric oxide synthase030104 developmental biologybiology.proteinImmunohistochemistrySteatosisbusiness
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Hsp60, amateur chaperone in amyloid-beta fibrillogenesis

2016

BACKGROUND: Molecular chaperones are a very special class of proteins that play essential roles in many cellular processes like folding, targeting and transport of proteins. Moreover, recent evidence indicates that chaperones can act as potentially strong suppressor agents in Alzheimer's disease (AD). Indeed, in vitro experiments demonstrate that several chaperones are able to significantly slow down or suppress aggregation of Aβ peptide and in vivo studies reveal that treatment with specific chaperones or their overexpression can ameliorate some distinct pathological signs characterizing AD. METHODS: Here we investigate using a biophysical approach (fluorescence, circular dichroism (CD), t…

0301 basic medicineAmyloidMolecular chaperonesAmyloid betaBiophysicsPlasma protein bindingInhibition mechanismsBiochemistryChaperoninChaperonin03 medical and health sciences0302 clinical medicinemedicineHumansInhibition mechanismMolecular BiologyAmyloid aggregationAmyloid beta-PeptidesbiologyNeurodegenerationP3 peptideFibrillogenesisChaperonin 60medicine.diseaseAlzheimer's disease treatmentCell biology030104 developmental biologyChaperone (protein)biology.proteinHSP60030217 neurology & neurosurgeryProtein BindingBiochimica et Biophysica Acta (BBA) - General Subjects
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Effect of Jasonia glutinosa on immune and oxidative status of gilthead seabream (Sparus aurata L.).

2020

Jasonia glutinosa (rock-tea, RT) has numerous biological activities. In the present work, the beneficial effects of dietary RT on gilthead seabream (Sparus aurata L.) were studied. Fish fed experimental diets containing 0 (control), 10 or 30% of RT for 15 and 30 days. Samples from skin mucus, blood, head kidney, liver and gut were obtained at 15 and 30 days. The antioxidant properties from RT were analysed such as the antioxidant capacity and phenolic content. The heat shock protein 70 level (HSP70) and the total oxidized proteins were evaluated on skin mucus as stress markers. Immune parameters, both humoral (peroxidase activity, immunoglobulin M levels and complement activity) and cellula…

0301 basic medicineAntioxidantmedicine.drug_classmedicine.medical_treatmentImmunostimulantAquatic ScienceBiologyAsteraceaemedicine.disease_causeImmunostimulantTeleostsAntioxidantsAndrology03 medical and health sciencesImmune systemAdjuvants ImmunologicSettore AGR/20 - ZoocolturemedicineEnvironmental ChemistryAnimalsImmunity CellularPlant ExtractsImmunity04 agricultural and veterinary sciencesGeneral MedicineMucusAnimal FeedImmunity InnateSea BreamRespiratory burstHsp70DietImmunity HumoralOxidative Stress030104 developmental biologyRock tea (Jasonia glutinosa)Gilthead seabream (Sparus aurata L.)Dietary Supplements040102 fisheriesbiology.protein0401 agriculture forestry and fisheriesAntioxidantOxidative stressPeroxidaseFishshellfish immunology
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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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