Search results for "P[9]"

showing 10 items of 142 documents

Identification of the plant compound geraniin as a novel Hsp90 inhibitor

2013

Besides its function in normal cellular growth, the molecular chaperone heat shock protein 90 (Hsp90) binds to a large number of client proteins required for promoting cancer cell growth and/or survival. In an effort to discover new small molecules able to inhibit the Hsp90 ATPase and chaperoning activities, we screened, by a surface plasmon resonance assay, a small library including different plant polyphenols. The ellagitannin geraniin, was identified as the most promising molecule, showing a binding affinity to Hsp90α similar to that of 17-(allylamino)-17-demethoxygeldanamycin (17AGG). Geraniin was able to inhibit in vitro the Hsp90α ATPase activity in a dose−dependent manner, with an in…

Geraniinlcsh:MedicineHsp90 inhibitorHeLachemistry.chemical_compoundJurkat CellsGlucosidesHeat shock proteinHumansMTT assayHSP90 Heat-Shock ProteinsCytotoxicitylcsh:ScienceMultidisciplinarybiologyChemistryCell growthlcsh:RCell Cyclebiology.organism_classificationHsp90Hydrolyzable TanninsBiochemistrybiology.proteinlcsh:QHeLa CellsResearch Article
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HSP90 in ageing progression and ageing related diseases

2014

HSP90 activities decline during ageing. Noteworthy, HSP90 mediated retrotransposon silencing seems to have a key role in the maintenance of genome integrity. Furthermore, inhibition of HSP90 activities lead to cell senescence and apoptosis. Original bioinformatics analyses and literature data will be discussed in the light of the potential involvement of HSP90 in ageing progression and ageing related diseases.

HSP90 AgeingSettore BIO/11 - Biologia Molecolare
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Nuovi derivati 3,5-diaril-4,5-diidropirazolici come inibitori di HSP90

2008

HSP90 derivati 35-diaril-45-diidropirazoliciSettore CHIM/08 - Chimica Farmaceutica
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Principal Component Analysis on molecular descriptors as alternative point of view in the search of new Hsp90 inhibitors

2008

HSP90 molecular descriptorSettore CHIM/08 - Chimica Farmaceutica
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PROGETTAZIONE, SINTESI E VALUTAZIONE BIOLOGICA DI NUOVI INIBITORI DI HSP90

2009

HSP90Settore CHIM/08 - Chimica Farmaceutica
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Protective role of heat shock proteins in Parkinson's disease.

2010

Parkinson’s disease (PD) is the second most common neurodegenerative disease after Alzheimer’s disease. Despite a large amount of research, the pathogenetic mechanism of these diseases has not yet been clarified. Abnormal protein folding, oxidative stress, mitochondrial dysfunction, and apoptotic mechanisms have all been reported as causes of neurodegenerative diseases in association with neuroinflammatory mechanisms which, by generating deleterious molecules, could promote the cascade of events leading to neurodegeneration. Heat shock proteins (HSPs) play a central role in preventing protein misfolding and inhibiting apoptotic activity, and represent a class of proteins potentially involve…

Heat shock proteins Parkinson disease neuroprotective roleParkinson's diseasebiologyNeurodegenerationParkinson DiseaseDiseasemedicine.diseasemedicine.disease_causeHsp90Hsp70PathogenesisNeurologyHeat shock proteinImmunologymedicinebiology.proteinAnimalsHumansHSP70 Heat-Shock ProteinsNeurology (clinical)HSP90 Heat-Shock ProteinsNeuroscienceOxidative stressHeat-Shock ProteinsNeuro-degenerative diseases
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Role of heme oxygenase-1 (HSP32) and HSP90 in glioblastoma

2017

Glioblastoma (GBM) is the most common and malignant primary brain tumor in adults. The current treatment regimes for glioblastoma demonstrated a low efficiency and offer a poor prognosis. Advancements in conventional treatment strategies have only yielded modest improvements in overall survival. The heat shockproteins, heme oxygenase-1 (HO-1) and Hsp90, serve these pivotal roles in tumor cells and have been identified as effective targets for developing therapeutics. This topic review summarizes the current preclinical and clinical evidences and rationale to define the potential of HO-1 and Hsp90 in GBM progression and chemoresistance.

Heme oxygenaseMolecular chaperonesHeat shock proteinHsp90GlioblastomaCancer
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HSP10,HSP70 AND HSP90 IMMUNOHISTOCHEMICAL LEVELS CHANGE IN ULCERATIVE COLITIS AFTER THERAPY

2011

Ulcerative colitis (UC) is a form of inflammatory bowel disease (IBD) characterized by damage of large bowel mucosa and frequent extra-intestinal autoimmune comorbidities. The role played in IBD pathogenesis by molecular chaperones known to interact with components of the immune system involved in inflammation is unclear. We previously demonstrated that mucosal Hsp60 decreases in UC patients treated with conventional therapies (mesalazine, probiotics), suggesting that this chaperonin could be a reliable biomarker useful for monitoring response to treatment, and that it might play a role in pathogenesis. In the present work we investigated three other heat shock protein/molecular chaperones:…

HistologyBiophysicsDown-RegulationInflammationcomorbidity.Inflammatory bowel diseaseulcerative colitis heat shock proteins Hsp molecular chaperones inflammation comorbidity.Pathogenesischemistry.chemical_compoundMesalazineulcerative colitis heat shock proteins Hsp molecular chaperones inflammation comorbidityHeat shock proteinChaperonin 10MedicineHspHumansHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsColitisMesalaminelcsh:QH301-705.5ulcerative colitisbusiness.industryBrief Reportmolecular chaperonesAnti-Inflammatory Agents Non-SteroidalCell Biologymedicine.diseaseUlcerative colitisImmunohistochemistrydigestive system diseaseschemistrylcsh:Biology (General)inflammationImmunologyheat shock proteinsBiomarker (medicine)Colitis Ulcerativemedicine.symptombusiness
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The chaperone system in cancer therapies: Hsp90

2023

AbstractThe chaperone system (CS) of an organism is composed of molecular chaperones, chaperone co-factors, co-chaperones, and chaperone receptors and interactors. It is present throughout the body but with distinctive features for each cell and tissue type. Previous studies pertaining to the CS of the salivary glands have determined the quantitative and distribution patterns for several members, the chaperones, in normal and diseased glands, focusing on tumors. Chaperones are cytoprotective, but can also be etiopathogenic agents causing diseases, the chaperonopathies. Some chaperones such as Hsp90 potentiate tumor growth, proliferation, and metastasization. Quantitative data available on t…

HistologyPhysiologyAktChaperonopathieMolecular chaperoneChaperone systemHsp90Cell BiologyGeneral MedicineNF-kBNegative chaperonotherapy
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Cellular responses and HSP70 expression during wound healing in Holothuria tubulosa (Gmelin, 1788).

2014

Wound repair is a key event in the regeneration mechanisms of echinoderms. We studied, at the behavioural, cellular and molecular levels, the wound healing processes in Holothuria tubulosa after injuries to the body wall. The experiments were performed for periods of up to 72 h, and various coelomocyte counts, as well as the expression of heat shock proteins (HS27, HSP70 and HSP90), were recorded. Dermal wound healing was nearly complete within 72 h. In the early stages, we observed the injured animals twisting their bodies to keep their injuries on the surface of the water for the extrusion of the buccal pedicles. At the cellular level, we found time-dependent variations in the circulating…

HolothurianStreImmunoblottingSettore BIO/05 - ZoologiaHSP27 Heat-Shock ProteinsAquatic ScienceAndrologyWestern blotHeat shock proteinmedicineHSPEnvironmental ChemistryAnimalsHolothuriaHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsSettore BIO/06 - Anatomia Comparata E CitologiaCoelomocyteWound Healingmedicine.diagnostic_testbiologyRegeneration (biology)Holothuria tubulosaGeneral Medicinebiology.organism_classificationHsp70Organ SpecificityImmunologyCoelomocyteWound healingHolothuriaFishshellfish immunology
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