Search results for "HSP90"

showing 10 items of 88 documents

HSP90 and HSP70: Implication in Inflammation Processes and Therapeutic Approaches for Myeloproliferative Neoplasms.

2015

Myeloproliferative neoplasms (MPN) are clonal stem cell disorders that lead to the excessive production of one or more blood cell lineages. It has been reported that, in most MPN, inflammatory cytokines are frequently increased, indicating that inflammation plays a crucial role in these disorders. Heat shock proteins (HSP) are induced in response to many stressful conditions from heat shock to hypoxia and inflammation. Besides their chaperone and cytoprotective functions, HSPs are key players during inflammation, hence the term “chaperokine.” Through their chaperone activity, HSP90, a stabilizer of many oncogenes (e.g., JAK2), and HSP70, a powerful antiapoptotic chaperone, tightly regulate …

ImmunologyInflammationReview ArticleBiologyModels BiologicalProinflammatory cytokineMyeloproliferative DisordersHeat shock proteinlcsh:PathologymedicineHumansHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsMolecular Targeted TherapyMyeloproliferative DisordersCell BiologyHsp90Chaperone (protein)ImmunologyCancer researchbiology.proteinmedicine.symptomSignal transductionStem cellInflammation Mediatorslcsh:RB1-214Signal TransductionMediators of inflammation
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Geldanamycin and its derivatives as Hsp90 inhibitors

2012

The Hsp90 molecule, one of the most abundant heat shock proteins in mammalian cells, maintains homeostasis and prevents stress-induced cellular damage. Hsp90 is expressed under normal conditions at a level of about 1-2 Percent of total proteins, while its expression increases 2-10 fold in cancer cells. The two main constitutively expressed isoforms of Hsp90 are known as Hsp90-alpha and Hsp90-beta, and their upregulation is associated with tumor progression, invasion and formation of metastases, as well as development of drug resistance. The Hsp90 is a key target for many newly established, potent anticancer agents containing Hsp90 N-terminal ATP binding inhibitors, such as geldanamycin, and…

IndolesLactams MacrocyclicCyclin-Dependent KinaseAntineoplastic AgentsTanespimycinBenzoquinoneModels BiologicalAntineoplastic Agentchemistry.chemical_compoundDownregulation and upregulationTransforming Growth Factor betaCyclin-dependent kinaseHeat shock proteinBenzoquinonespolycyclic compoundsAnimalsHumansHSP90 Heat-Shock ProteinsbiologyAnimalTriazolesGeldanamycinHsp90Cyclin-Dependent KinasesProto-Oncogene Proteins c-rafHSP90 Heat-Shock Proteinsrc-Family KinaseschemistryTumor progressionMutationCancer cellbiology.proteinCancer researchMacrolidesMacrolideTriazoleTumor Suppressor Protein p53Animals; Antineoplastic Agents; Benzoquinones; Cyclin-Dependent Kinases; HSP90 Heat-Shock Proteins; Humans; Lactams Macrocyclic; Macrolides; Models Biological; Mutation; Novobiocin; Proto-Oncogene Proteins c-raf; Transforming Growth Factor beta; Triazoles; Tumor Suppressor Protein p53; src-Family KinasesNovobiocinHumanFrontiers in Bioscience
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Heat Shock Proteins Alterations in Rheumatoid Arthritis

2022

Rheumatoid arthritis (RA) is a chronic inflammatory and autoimmune disease characterized by the attack of the immune system on the body’s healthy joint lining and degeneration of articular structures. This disease involves an increased release of inflammatory mediators in the affected joint that sensitize sensory neurons and create a positive feedback loop to further enhance their release. Among these mediators, the cytokines and neuropeptides are responsible for the crippling pain and the persistent neurogenic inflammation associated with RA. More importantly, specific proteins released either centrally or peripherally have been shown to play opposing roles in the pathogenesis of this dise…

InflammationHeat shock proteins Hsp therapy Inflammation Neurogenic inflammation Rheumatoid arthritis VaccineOrganic ChemistryGeneral MedicineChaperonin 60CatalysisComputer Science ApplicationsInorganic ChemistryArthritis RheumatoidHumansHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsPhysical and Theoretical ChemistryMolecular BiologySpectroscopyHeat-Shock Proteins
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Identification of HSP90 as a new GABARAPL1 (GEC1)-interacting protein

2011

GABARAPL1 belongs to the small family of GABARAP proteins (including GABARAP, GABARAPL1 and GABARAPL2/GATE-16), one of the two subfamilies of the yeast Atg8 orthologue. GABARAPL1 is involved in the intracellular transport of receptors, via an interaction with tubulin and GABA(A) or kappa opioid receptors, and also participates in autophagy and cell proliferation. In the present study, we identify the HSP90 protein as a novel interaction partner for GABARAPL1 using GST pull-down, mass spectrometry and coimmunoprecipitation experiments. GABARAPL1 and HSP90 partially colocalize in MCF-7 breast cancer cells overexpressed Dsred-GABARAPL1 and in rat brain. Moreover, treatment of MCF-7 cells overe…

LeupeptinsLactams MacrocyclicGABARAPATG8Blotting WesternLactacystinCysteine Proteinase InhibitorsBiologyBiochemistryMass SpectrometryCell Linechemistry.chemical_compoundCell Line TumorMG132BenzoquinonesAnimalsHumansImmunoprecipitationHSP90 Heat-Shock ProteinsReceptorAdaptor Proteins Signal TransducingMicroscopy ConfocalHEK 293 cellsGeneral MedicineHsp90RatsBiochemistrychemistryProteasomebiology.proteinMicrotubule-Associated ProteinsBiochimie
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Heat shock proteins in fibrosis and wound healing: Good or evil?

2014

Heat shock proteins (HSPs) are key regulators of cell homeostasis, and their cytoprotective role has been largely investigated in the last few decades. However, an increasing amount of evidence highlights their deleterious effects on several human pathologies, including cancer, in which they promote tumor cell survival, proliferation and drug resistance. Therefore, HSPs have recently been suggested as therapeutic targets for improving human disease outcomes. Fibrotic diseases and cancer share several properties; both pathologies are characterized by genetic alterations, uncontrolled cell proliferation, altered cell interactions and communication and tissue invasion. The discovery of new HSP…

MAPK/ERK pathwayPulmonary FibrosisCellApoptosisBiologyCell Physiological PhenomenaTransforming Growth Factor beta1PathogenesisFibrosisNeoplasmsHeat shock proteinmedicineHumansHSP70 Heat-Shock ProteinsPharmacology (medical)HSP90 Heat-Shock ProteinsHSP110 Heat-Shock ProteinsHSP47 Heat-Shock ProteinsHeat-Shock ProteinsPharmacologyWound HealingCell growthCancerEndomyocardial Fibrosismedicine.diseaseFibrosisHeat-Shock Proteins Smallmedicine.anatomical_structureImmunologyCancer researchCollagenWound healingPharmacology & Therapeutics
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Stress proteins HSP90 and Gp96 in graft-versus-host disease : pathophysiological, diagnostic and therapeutic implication

2015

Allogeneic hematopoietic cell transplantation is a treatment for certain disorders including hematologic malignancies. Graft-versus-host-disease (GvHD) is a major, life-threatening complication. It is due to the recognition of recipient antigens by donor T cells, which activate and damage tissues. Intestinal barrier alteration plays a critical role in GvHD. Heat shock proteins (HSP)90 include five members, three cytosolic members named HSP90, and one member localized in endoplasmic reticulum (ER) called Gp96 and able to gain extracellular level in case of stress. We show in our thesis that 17AAG, a HSP90 inhibitor, reduces GvHD mortality in a mouse model. This effect is associated with an i…

Maladie du greffon contre l’hôte intestinale17AAG[SDV.MHEP] Life Sciences [q-bio]/Human health and pathologyIntestinal graft-versus-host disease[SDV.IMM] Life Sciences [q-bio]/ImmunologyMaladie du greffon contre l’hôteHSP90Complement C3Complément C3Gp96Graft-versus-host disease
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X-linked primary ciliary dyskinesia due to mutations in the cytoplasmic axonemal dynein assembly factor PIH1D3

2017

By moving essential body fluids and molecules, motile cilia and flagella govern respiratory mucociliary clearance, laterality determination and the transport of gametes and cerebrospinal fluid. Primary ciliary dyskinesia (PCD) is an autosomal recessive disorder frequently caused by non-assembly of dynein arm motors into cilia and flagella axonemes. Before their import into cilia and flagella, multi-subunit axonemal dynein arms are thought to be stabilized and pre-assembled in the cytoplasm through a DNAAF2–DNAAF4–HSP90 complex akin to the HSP90 co-chaperone R2TP complex. Here, we demonstrate that large genomic deletions as well as point mutations involving PIH1D3 are responsible for an X-li…

MaleCytoplasmProtein FoldingAxoneme[SDV]Life Sciences [q-bio][SDV.GEN] Life Sciences [q-bio]/Genetics[SDV.MHEP.PSR]Life Sciences [q-bio]/Human health and pathology/Pulmonology and respiratory tractouterGenes X-LinkedChilddefectsPhylogenyZebrafisharmsSequence DeletionvariantsIntracellular Signaling Peptides and ProteinsGenetic Diseases X-LinkedPedigreeMultidisciplinary Sciences[SDV] Life Sciences [q-bio]motilityChild PreschoolMicrotubule ProteinsSperm MotilityScience & Technology - Other TopicsFemaleAdultAdolescentinnerUK10K Rare Groupr2tp complexof-function mutationsArticleMicroscopy Electron TransmissionMD MultidisciplinaryExome SequencingAnimalsHumansPoint MutationCiliaHSP90 Heat-Shock Proteins[SDV.GEN]Life Sciences [q-bio]/GeneticsScience & TechnologyKartagener SyndromeInfant NewbornAxonemal DyneinsDisease Models AnimalHEK293 Cells[SDV.MHEP.PSR] Life Sciences [q-bio]/Human health and pathology/Pulmonology and respiratory tractidentifies mutationsproteinApoptosis Regulatory ProteinsSequence AlignmentMolecular ChaperonesNature Communications
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A randomized phase II study of ganetespib, a heat shock protein 90 inhibitor, in combination with docetaxel in second-line therapy of advanced non-sm…

2015

Background: This trial was designed to evaluate the activity and safety of ganetespib in combination with docetaxel in advanced non-small cell lung cancer (NSCLC) and to identify patient populations most likely to benefit from the combination. Patients and methods: Patients with one prior systemic therapy for advanced disease were eligible. Docetaxel (75 mg/m<sup>2</sup> on day 1) was administered alone or with ganetespib (150 mg/m<sup>2</sup> on days 1 and 15) every 3 weeks. The primary end points were progression-free survival (PFS) in two subgroups of the adenocarcinoma population: patients with elevated lactate dehydrogenase (eLDH) and mutated KRAS (mKRAS). Resul…

MaleOncologyHSP90 inhibitormedicine.medical_specialtyLung NeoplasmsPopulationGanetespibPhases of clinical researchDocetaxelAdenocarcinomaNeutropeniaDisease-Free SurvivalProto-Oncogene Proteins p21(ras)Carcinoma Non-Small-Cell LungInternal medicineAntineoplastic Combined Chemotherapy ProtocolsmedicineHumansHSP90 Heat-Shock ProteinsLung cancereducationAgedProportional Hazards Modelseducation.field_of_studyL-Lactate Dehydrogenasebusiness.industryHazard ratioHematologyMiddle AgedTriazolesmedicine.diseaseTreatment OutcomeAdvanced NSCLCOncologyDocetaxelGanetespibAdenocarcinomaFemaleTaxoidsbusinessmedicine.drugAnnals of Oncology
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Molecular Cloning and mRNA Expression of Heat Shock Protein Genes and Their Response to Cadmium Stress in the Grasshopper Oxya chinensis

2015

Heat shock proteins (Hsps) are highly conserved molecular chaperones that are synthesized in response to stress. In this study, we cloned the full-length sequences of the Grp78 (glucose-regulated protein 78), Hsp70, Hsp90, and Hsp40 genes from the Chinese rice grasshopper Oxya chinensis. The full-length cDNA sequences of OcGrp78, OcHsp70, OcHsp90, and OcHsp40 contain open reading frames of 1947, 1920, 2172, and 1042 bp that encode proteins of 649, 640, 724, and 347 amino acids, respectively. Fluorescent real-time quantitative PCR (RT-qPCR) was performed to quantify the relative transcript levels of these Hsp genes in different tissues and developmental stages. The mRNAs encoding these four …

MaleZygotelcsh:MedicineGrasshoppersOpen Reading FramesStress PhysiologicalComplementary DNAHeat shock proteinGene expressionAnimalsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsRNA MessengerCloning Molecularlcsh:ScienceEndoplasmic Reticulum Chaperone BiPGeneHeat-Shock ProteinsRegulation of gene expressionMultidisciplinarybiologylcsh:RHSP40 Heat-Shock ProteinsHsp90Molecular biologyHsp70Real-time polymerase chain reactionGene Expression RegulationLarvabiology.proteinInsect ProteinsFemalelcsh:QResearch ArticleCadmiumSignal TransductionPLOS ONE
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Heat shock proteins and ulcerative colitis: The start of a new era?

2015

Malemedicine.medical_specialtybusiness.industryGastroenterologyMEDLINEmedicine.diseaseUlcerative colitisGastroenterologySurgeryHeat shock proteinInternal medicineHumansMedicineColitis UlcerativeFemaleHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsIntestinal MucosaColitisbusinessPrecancerous ConditionsArab Journal of Gastroenterology
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