Search results for "chaperone"

showing 10 items of 249 documents

Rot1 plays an antagonistic role to Clb2 in actin cytoskeleton dynamics throughout the cell cycle.

2007

ROT1 is an essential gene whose inactivation causes defects in cell cycle progression and morphogenesis in budding yeast. Rot1 affects the actin cytoskeleton during the cell cycle at two levels. First, it is required for the maintenance of apical growth during bud growth. Second, Rot1 is necessary to polarize actin cytoskeleton to the neck region at the end of mitosis; because of this defect, rot1 cells do not properly form a septum to complete cell division. The inability to polarize the actin cytoskeleton at the end of mitosis is not due to a defect in the recruitment of the polarisome scaffold protein Spa2 or the actin cytoskeleton regulators Cdc42 and Cdc24 in the neck region. Previous …

Saccharomyces cerevisiae ProteinsGenes FungalArp2/3 complexmacromolecular substancesSaccharomyces cerevisiaeCyclin BActin remodeling of neuronsGene Expression Regulation FungalCDC2-CDC28 KinasesCytoskeletonCytoskeletonPolarisomebiologyCell CycleActin remodelingCell PolarityMembrane ProteinsCell BiologyActin cytoskeletonActinsCell biologyProfilinParacytophagyMutationbiology.proteinMolecular ChaperonesJournal of cell science
researchProduct

Unveiling novel interactions of histone chaperone Asf1 linked to TREX-2 factors Sus1 and Thp1

2014

13 páginas, 7 figuras, 2 yablas

Saccharomyces cerevisiae ProteinsTranscription Genetic(5-10) yAsf1Histone H2B ubiquitinationCell Cycle ProteinsSAGASaccharomyces cerevisiaeBiologyyeastMethylationTREX-2RNA TransportHistonesSus1Histone H3Histone H1Gene Expression Regulation FungalhistonesHistone H2ANucleosomeHistone codeTAP-MS strategyHistone ChaperonesRNA MessengerHistone octamerGeneticsNuclear ProteinsRNA-Binding ProteinsAcetylationCell BiologyYeastCell biologyRibonucleoproteinsHistone methyltransferaseProtein Processing Post-TranslationalMolecular ChaperonesResearch Paper
researchProduct

Hsp60 and human aging: Les liaisons dangereuses 

2013

Stressors can cause abnormal intracellular accumulation of Hsp60 and its localization in extramitochondrial sites, secretion, and circulation, with immune system activation. Dysfunction of chaperones associated with their quantitative and qualitative decline with aging (chaperonopathies of aging) characterizes senescence and is a potential causal factor in the physiological deterioration that occurs with it. The role of Hsp60 in aging is not easy to elucidate, because aging is accompanied by pathologies (e.g., cardiovascular and neurodegenerative disorders, osteoporosis, diabetes, cancer, etc.) in which Hsp60 has been implicated but, although those disorders are more frequent in the elderly…

SenescenceAginganimal structuresOsteoporosischemical and pharmacologic phenomenaInflammationDiseaseBiologycomplex mixturesMitochondrial ProteinsPathogenesisImmune systemDiabetes mellitusmedicineHumansCellular SenescenceAutoantibodiesHeart FailurefungiHSP 60 AGING CHAPERONES.Neurodegenerative DiseasesChaperonin 60Atherosclerosismedicine.diseaseMitochondriaImmune SystemImmunologyHSP60Arthropathy Neurogenicmedicine.symptomFrontiers in Bioscience
researchProduct

Overexpression of apolipoprotein J in human fibroblasts protects against cytotoxicity and premature senescence induced by ethanol and tert-butylhydro…

2008

Human diploid fibroblasts (HDFs) exposed to subcytotoxic stresses under H2O2, tert-butylhydroperoxide (t-BHP), and ethanol (EtOH) undergo stress-induced premature senescence (SIPS) characterized by many biomarkers of HDFs replicative senescence. Among these biomarkers are a growth arrest, an increase in the senescence-associated β-galactosidase activity, a senescent morphology, an overexpression of p21waf-1 and the subsequent inability to phosphorylate pRb, the presence of the common 4977-bp mitochondrial deletion, and an increase in the steady-state level of several senescence-associated genes such as apolipoprotein J (apo J). Apo J has been described as a survival gene against cytotoxic s…

SenescenceCell SurvivalGene ExpressionSimian virus 40Biologymedicine.disease_causeTritiumBiochemistrytert-ButylhydroperoxideGene expressionmedicineHumansOsteonectinRNA MessengerCytotoxicityCells CulturedCellular SenescenceCell Line TransformedGlycoproteinsClusterinEthanolCentral Nervous System DepressantsCell BiologyTransfectionOriginal ArticlesFibroblastsbeta-GalactosidaseMolecular biologyRecombinant ProteinsFibronectinsOxidative StressClusterinbiology.proteinPhosphorylationMitogensCell agingOxidative stressMolecular ChaperonesThymidineCell Stress and Chaperones
researchProduct

Chaperonopathies of senescence and the scrambling of interactions between the chaperoning and the immune systems

2010

Aging entails progressive deterioration of molecules and supramolecular structures, including Hsp chaperones and their complexes, paralleled by functional decline. Recent research has changed our views on Hsp chaperones. They work inside and outside cells in many locations, alone or forming teams, interacting with cells, receptors, and molecules that are not chaperones, in roles that are not typically attributed to chaperones, such as protein folding. Hsp chaperones form a physiological system with a variety of functions and interactions with other systems, for example, the immune system. We propose that chaperone malfunctioning due to structural damage or gene dysregulation during aging ha…

SenescencebiologyGeneral NeuroscienceGeneral Biochemistry Genetics and Molecular BiologyCell biologyCo-chaperoneImmune systemHistory and Philosophy of ScienceChaperone (protein)biology.proteinProtein foldingHSP60Functional declineReceptorAnnals of the New York Academy of Sciences
researchProduct

Hsp60 and Hsp10 in Ageing

2009

HSP and molecular chaperones, both referred to in this chapter as chaperones, are key players in development and senescence. With regard to senescence, several issues are critical: the role of normal chaperones in the process of ageing itself and in preventing and controlling age-associated diseases, the role of defective chaperones (chaperonopathies) in the onset and progression of senescence and in the etiology of old-age diseases, the interaction of chaperones with the immune system, and the potential of chaperones as therapeutic agents for counteracting the deleterious effects of ageing on molecules and cells and for treating proteinopathies of the elderly (chaperonotherapy). All these …

Senescencebiologybusiness.industryDiseaseBioinformaticsChaperoninPathogenesisImmune systemAgeingChaperone (protein)biology.proteinMedicinebusinessPathological
researchProduct

THE ROLE OF HSP60 IN AMYLOID BETA PATHWAY: RELEVANCE TO ALZHEIMER’S DISEASE

Alzheimer’s disease (AD) is a devastating neurodegenerative disorder affecting more than 40 million individuals worldwide. The high number of factors triggering the onset of AD justifies the current absence of disease-modifying therapies. The involved pathological mechanisms are still elusive and, therefore, the finding of effective therapies requires further elucidation of biomolecular mechanisms controlling AD pathogenesis. Particularly, the aberrant amyloidogenic cleavage of amyloid precursor protein (APP), amyloid beta (Aβ) peptide misfolding and oligomerization, and the impairment of the protein quality control machinery are key hallmarks characterizing the onset of the disease. Furthe…

Settore BIO/16 - Anatomia UmanaAmyloid beta peptideaggregationchaperoneAlzheimer's diseaseHsp60misfolding7PA2
researchProduct

The Chaperone System in Breast Cancer: Roles and Therapeutic Prospects of the Molecular Chaperones Hsp27, Hsp60, Hsp70, and Hsp90

2022

Breast cancer (BC) is a major public health problem, with key pieces of information needed for developing preventive and curative measures still missing. For example, the participation of the chaperone system (CS) in carcinogenesis and anti-cancer responses is poorly understood, although it can be predicted to be a crucial factor in these mechanisms. The chief components of the CS are the molecular chaperones, and here we discuss four of them, Hsp27, Hsp60, Hsp70, and Hsp90, focusing on their pro-carcinogenic roles in BC and potential for developing anti-BC therapies. These chaperones can be targets of negative chaperonotherapy, namely the elimination/blocking/inhibition of the chaperone(s)…

Settore BIO/16 - Anatomia UmanaCarcinogenesisOrganic ChemistryHSP27 Heat-Shock ProteinsBreast NeoplasmsChaperonin 60General MedicineCatalysisComputer Science ApplicationsInorganic ChemistryHumansbreast cancer chaperone system Hsp inhibitors Hsp27Hsp60Hsp70Hsp90 molecular chaperones immunotherapy negative chaperonotherapyCarcinogenesisFemaleHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsPhysical and Theoretical ChemistryMolecular BiologySpectroscopyInternational Journal of Molecular Sciences
researchProduct

EXPRESSION AND LOCALIZATION OF “CHAPEROKINE” HSP60 IN BRONCHIAL CULTURE MODELS MIMING COPD

Settore BIO/16 - Anatomia UmanaMolecular chaperones inflammatory chronic disease exosomes three-dimensional cultures
researchProduct

The Chaperone System in Salivary Glands: Hsp90 Prospects for Differential Diagnosis and Treatment of Malignant Tumors

2022

Salivary gland tumors represent a serious medical problem and new tools for differential diagnosis and patient monitoring are needed. Here, we present data and discuss the potential of molecular chaperones as biomarkers and therapeutic targets, focusing on Hsp10 and Hsp90. The salivary glands are key physiological elements but, unfortunately, the information and the means available for the management of their pathologies, including cancer, are scarce. Progress in the study of carcinogenesis has occurred on various fronts lately, one of which has been the identification of the chaperone system (CS) as a physiological system with presence in all cells and tissues (including the salivary gland…

Settore BIO/16 - Anatomia UmanaOrganic ChemistryAntineoplastic AgentsGeneral MedicineSettore MED/08 - Anatomia PatologicaSalivary Gland NeoplasmsSalivary GlandsCatalysisComputer Science ApplicationsDiagnosis DifferentialInorganic ChemistryHumanschaperone system differential diagnosis Ganetespib Hsp90 Hsp90 biomarker Hsp90 pathogenic negative chaperonotherapysalivary gland tumors Diagnosis Differential Humans Molecular Chaperones Salivary Glands Antineoplastic Agents Salivary Gland NeoplasmsHSP90 Heat-Shock ProteinsPhysical and Theoretical Chemistrysalivary gland tumors; chaperone system; Hsp90; Hsp90 pathogenic; negative chaperonotherapy; Ganetespib; Hsp90 biomarker; differential diagnosisMolecular BiologySpectroscopyMolecular Chaperones
researchProduct