Search results for "Hsp"

showing 10 items of 557 documents

Similarities and singularities of three DnaK proteins from the cyanobacterium Synechocystis sp. PCC 6803.

2010

In the genome of completely sequenced mesophilic cyanobacterium Synechocystis sp. PCC 6803 three DnaK proteins are encoded, which share a high degree of sequence identity in their N-terminal ATPase region as well as in the adjacent peptide-binding domain. However, as typical for DnaK proteins, the C-termini of the three Synechocystis proteins are highly diverse. To study the functions of the three Synechocystis DnaK proteins in more detail, we have analyzed the abundance of the individual proteins in Synechocystis cells as well as dnaK expression under various stress conditions. The presented results show that all three Synechocystis DnaK proteins interact with the same GrpE nucleotide exch…

Physiologygenetic processesAmino Acid MotifsMolecular Sequence DataSequence alignmentPlant SciencePlasma protein bindingBiologymedicine.disease_causeMicrobiologyConserved sequenceNucleotide exchange factorBacterial ProteinsStress PhysiologicalmedicineHSP70 Heat-Shock ProteinsAmino Acid SequencePeptide sequenceConserved SequenceHeat-Shock ProteinsMutationSynechocystisSynechocystisCell BiologyGeneral MedicineGene Expression Regulation Bacterialbiology.organism_classificationBiochemistrybiological sciencesMutationbacteriaSequence AlignmentFunction (biology)Protein BindingPlantcell physiology
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Effects of Pleurotus eryngii var. eryngii in "in vitro" and "in vivo" cancerogenetic models

2018

Heat shock proteins (Hsps) are highly expressed in a variety of cancer types contributing to tumor cell propagation and protection against apoptosis [1]. The current anti-cancer therapy is not always target specific and often is associated with complications for patients, Therefore new effective, specific and less toxic therapeutic approaches are needed. Medicinal mushrooms have emerged as wonderful source of nutraceuticals, anti-oxidants, anticancer, prebiotic, anti-inflammatory, cardiovascular, anti-microbial, and anti-diabetic. The ongoing research projects are aimed to promote mushrooms as new generation ‘‘biotherapeutics’’[2]. The aim of this study was to evaluate whether the cold-wate…

Pleurotus eryngii Hsp60 cancer progression C26 cells
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Shipping noise affecting immune responses of European spiny lobster (Palinuruselephas)

2015

Marine crustaceans are influenced by numerous environmental factors. Environmental stress from pollutants seems to affect their metabolism, growth, moulting, survival, and immune defence. Recently, it has become clear that there is an impact of the global increase in sea noise levels due to shipping traffic on crustacean welfare. Considering the ecological and commercial importance of the European spiny lobster (Palinurus elephas (Fabricius, 1787)) in most parts of the Mediterranean coastal area, in the present study we investigated whether shipping noise pollution contribute to changing the immune parameters of stress in the European spiny lobster. The animals were exposed to a mix of nois…

Pollutantanimal structuresbiologyEcologyPalinurus elephafungiPalinurus elephasSettore BIO/05 - ZoologiaAquatic animalbiology.organism_classificationCrustaceanEuropean spiny lobsterImmune systemNoise pollutionPO activityAnimal Science and ZoologyHsp27Immune responseSpiny lobsterMoultingEcology Evolution Behavior and SystematicsShellfishCanadian Journal of Zoology
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Combinatory effects of temperature stress and nonionic organic pollutants on stress protein (hsp70) gene expression in the freshwater spongeEphydatia…

1995

This is the first documentation of a heat shock protein (hsp) response in sponges. Subjecting the freshwater sponge Ephydatia fluviatilis to temperature stress (18 to 33 C; 2 h) resulted in an increased expression (>10 times) of the M{sub r}70,000 (hsp70). The induction of hsp70 could be demonstrated on the level of gene expression and by quantification of the hsp70 protein. Temperature stress also resulted in a 25% reduction of sponge cell proliferation. A mixture of nonionic organic compound was extracted from water from the polluted Schwarzbach River (S. Hesse, Germany) by adsorption onto XAD-7 resin. Concentrations of this Schwarzbach River water extract at two and four items ambient le…

PollutantbiologyCell growthEcologyHealth Toxicology and Mutagenesisbiology.organism_classificationHsp70chemistry.chemical_compoundSpongechemistryHeat shock proteinGene expressionEnvironmental ChemistryFood scienceWater pollutionXenobioticEnvironmental Toxicology and Chemistry
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Heat shock proteins: essential proteins for apoptosis regulation

2008

Abstract Many different external and intrinsic apoptotic stimuli induce the accumulation in the cells of a set of proteins known as stress or heat shock proteins (HSPs). HSPs are conserved proteins present in both prokaryotes and eukaryotes. These proteins play an essential role as molecular chaperones by assisting the correct folding of nascent and stress-accumulated misfolded proteins, and by preventing their aggregation. HSPs have a protective function, that is they allow the cells to survive to otherwise lethal conditions. Various mechanisms have been proposed to account for the cytoprotective functions of HSPs. Several of these proteins have demonstrated to directly interact with compo…

Programmed cell deathCell signalingReviewsMitochondrionBiologyModels BiologicallysosomesLysosomeHeat shock proteindeath receptorsmedicineAnimalsHumansemerging chemotherapeutic treatmentsHeat-Shock ProteinsCell Deathhaematopoietic malignanciesapoptosiscell signallingCell BiologyMitochondriaNeoplasm ProteinsCell biologymedicine.anatomical_structurecaspasesHematologic Neoplasmsheat shock proteinsMolecular MedicineProtein foldingHSP60Signal transductionMolecular ChaperonesSignal TransductionJournal of Cellular and Molecular Medicine
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L'hsp60 e l'hsp10 sono iperespresse durante la cancerogenesi prostatica

2003

Prostata hsp60 hsp10
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Heat shock proteins in hematopoietic malignancies

2012

Inducible heat shock proteins are molecular chaperones whose expression is increased after many different types of stress. They have a protective function helping the cell to cope with lethal conditions. Their basal expression is low in nonstressed, normal and nontransformed cells. However, in cancer cells and particularly in hematological malignancies, they are surprisingly abundant. Malignant cells have to rewire their metabolic requirements and therefore have a higher need for chaperones. This cancer cell addiction for HSPs is the basis for the use of HSP inhibitors in cancer therapy. HSPs have been shown to interact with different key apoptotic proteins. As a result, HSPs can essentiall…

ProteasesCell SurvivalCellular differentiationCellHSP27 Heat-Shock ProteinsApoptosisModels Biological03 medical and health sciences0302 clinical medicineHeat shock proteinmedicineAnimalsHumansHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHeat-Shock ProteinsCaspaseCell Proliferation030304 developmental biology0303 health sciencesbiologyCell DifferentiationCell BiologyNeoplasm Proteins3. Good healthCell biologyHaematopoiesismedicine.anatomical_structureApoptosisHematologic NeoplasmsMyelodysplastic Syndromes030220 oncology & carcinogenesisCancer cellbiology.proteinProtein Processing Post-TranslationalMolecular ChaperonesSignal TransductionExperimental Cell Research
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Heat Shock Proteins: Cell Protection through Protein Triage

2010

Heat shock proteins (HSPs) are chaperones that catalyze the proper folding of nascent proteins and the refolding of denatured proteins. The ubiquitin-proteasome system is an error-checking system that directs improperly folded proteins for destruction. A coordinated interaction between the HSPs (renaturation) and the proteasome (degradation) must exist to assure protein quality control mechanisms. Although it still remains unknown how the decision of folding vs. degradation is taken, many pieces of evidence demonstrate that HSPs interact directly or indirectly with the proteasome, assuring quite selectively the proteasomal degradation of certain proteins under stress conditions. In this rev…

Proteasome Endopeptidase ComplexHSP27 Heat-Shock Proteinslcsh:MedicinePlasma protein bindingModels Biologicallcsh:TechnologyGeneral Biochemistry Genetics and Molecular Biologycell stressHsp27Heat shock proteinAnimalsHumansHSP70 Heat-Shock ProteinsHSP90 Heat-Shock Proteinslcsh:ScienceMini-Review ArticleGeneral Environmental Sciencebiologylcsh:Tubiquitination processlcsh:RGeneral MedicineCrystallinsHsp90Hsp70Cell biologyproteasomeBiochemistryProteasomeheat shock proteinsbiology.proteinlcsh:QSignal transductionProtein qualityProtein BindingSignal TransductionThe Scientific World Journal
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Chaperone action in the posttranslational topological reorientation of the hepatitis B virus large envelope protein: Implications for translocational…

2003

The large L envelope protein of the hepatitis B virus utilizes a new folding pathway to acquire a dual transmembrane topology in the endoplasmic reticulum (ER). The process involves cotranslational membrane integration and subsequent posttranslational translocation of its preS subdomain into the ER. Here, we demonstrate that the conformational and functional heterogeneity of L depends on the action of molecular chaperones. Using coimmunoprecipitation, we observed specific interactions between L and the cytosolic Hsc70, in conjunction with Hsp40, and between L and the ER-resident BiP in mammalian cells. Complex formation between L and Hsc70 was abolished when preS translocation was artifici…

Protein ConformationImmunoprecipitationHSC70 Heat-Shock Proteinsmacromolecular substancesTopologyProtein structureViral Envelope ProteinsAnimalsHSP70 Heat-Shock ProteinsEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsMultidisciplinarybiologyEndoplasmic reticulumHSC70 Heat-Shock ProteinsBiological SciencesPrecipitin TestsTransport proteinProtein TransportMembrane topologyChaperone (protein)COS Cellsbiology.proteinProtein topologyCarrier ProteinsProtein Processing Post-TranslationalMolecular ChaperonesProceedings of the National Academy of Sciences
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Curcumin Affects HSP60 Folding Activity and Levels in Neuroblastoma Cells.

2020

The fundamental challenge in fighting cancer is the development of protective agents able to interfere with the classical pathways of malignant transformation, such as extracellular matrix remodeling, epithelial−mesenchymal transition and, alteration of protein homeostasis. In the tumors of the brain, proteotoxic stress represents one of the main triggering agents for cell transformation. Curcumin is a natural compound with anti-inflammatory and anti-cancer properties with promising potential for the development of therapeutic drugs for the treatment of cancer as well as neurodegenerative diseases. Among the mediators of cancer development, HSP60 is a key factor for the maintenance of…

Protein FoldingCurcuminCell SurvivalCellCatalysisMalignant transformationCell Linelcsh:ChemistryInorganic ChemistryMitochondrial Proteinschemistry.chemical_compoundNeuroblastomaDownregulation and upregulationHeat shock proteinmedicinepost-translational modificationsHumansSecretionPhysical and Theoretical Chemistrylcsh:QH301-705.5Molecular BiologySpectroscopyCell ProliferationHeat shock proteinDose-Response Relationship DrugCommunicationOrganic Chemistrymolecular chaperonesUbiquitinationGeneral MedicineChaperonin 60Computer Science ApplicationsCell biologyUp-RegulationBrain tumorGene Expression Regulation Neoplasticmedicine.anatomical_structurelcsh:Biology (General)lcsh:QD1-999chemistryApoptosisheat shock proteinsMolecular chaperoneCurcuminbrain tumorsHSP60Post-translational modificationHSP60extracellular HSP60International journal of molecular sciences
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