Search results for " shock"

showing 10 items of 691 documents

Targeting heat shock proteins in cancer

2010

Heat shock proteins (HSPs) HSP27, HSP70 and HSP90 are powerful chaperones. Their expression is induced in response to a wide variety of physiological and environmental insults including anti-cancer chemotherapy, thus allowing the cell to survive to lethal conditions. Different functions of HSPs have been described to account for their cytoprotective function, including their role as molecular chaperones as they play a central role in the correct folding of misfolded proteins, but also their anti-apoptotic properties. HSPs are often overexpressed in cancer cells and this constitutive expression is necessary for cancer cells' survival. HSPs may have oncogene-like functions and likewise mediat…

Protein Foldingendocrine systemCancer ResearchCell SurvivalProtein ConformationCellAntineoplastic AgentsApoptosisBreast NeoplasmsHsp27NeoplasmsHeat shock proteinmedicineAnimalsHumansHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHeat-Shock ProteinsCell ProliferationbiologyCell growthCancermedicine.diseaseHsp90Hsp70Cell biologymedicine.anatomical_structureOncologyDrug Resistance NeoplasmCancer cellbiology.proteinMolecular ChaperonesCancer Letters
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Heat shock protein 27 is involved in SUMO-2/3 modification of heat shock factor 1 and thereby modulates the transcription factor activity

2009

Heat shock protein 27 (HSP27) accumulates in stressed cells and helps them to survive adverse conditions. We have already shown that HSP27 has a function in the ubiquitination process that is modulated by its oligomerization/phosphorylation status. Here, we show that HSP27 is also involved in protein sumoylation, a ubiquitination-related process. HSP27 increases the number of cell proteins modified by small ubiquitin-like modifier (SUMO)-2/3 but this effect shows some selectivity as it neither affects all proteins nor concerns SUMO-1. Moreover, no such alteration in SUMO-2/3 conjugation is achievable by another HSP, such as HSP70. Heat shock factor 1 (HSF1), a transcription factor responsib…

Protein sumoylationTranscriptional ActivationCancer Researchendocrine systemanimal structuresSUMO proteinHSP27 Heat-Shock ProteinsBiologyurologic and male genital diseasesenvironment and public healthSubstrate Specificity03 medical and health sciencesTransactivation0302 clinical medicineHeat Shock Transcription FactorsHeat shock proteinGeneticsAnimalsHumansAnimals Cell Nucleus/metabolism DNA-Binding Proteins/*metabolism HSP27 Heat-Shock Proteins/chemistry/*metabolism Hela Cells Humans Protein Multimerization Protein Structure[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyHSF1Protein Structure QuaternaryMolecular BiologyTranscription factorUbiquitinsHeat-Shock Proteins030304 developmental biologyCell Nucleus0303 health sciencesMolecular biologyHsp70Cell biologyHeat shock factorDNA-Binding ProteinsProtein TransportQuaternary Protein Transport Small Ubiquitin-Related Modifier Proteins/*metabolism Substrate Specificity Transcription Factors/*metabolism Transcriptional Activation Ubiquitins/*metabolism030220 oncology & carcinogenesisembryonic structuresSmall Ubiquitin-Related Modifier ProteinsProtein MultimerizationHeLa CellsMolecular ChaperonesTranscription Factors
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Protein modulation in mouse heart under acute and chronic hypoxia

2011

Exploring cellular mechanisms underlying beneficial and detrimental responses to hypoxia represents the object of the present study. Signaling molecules controlling adaptation to hypoxia (HIF-1α), energy balance (AMPK), mitochondrial biogenesis (PGC-1α), autophagic/apoptotic processes regulation and proteomic dysregulation were assessed. Responses to acute hypoxia (AH) and chronic hypoxia (CH) in mouse heart proteome were detected by 2-D DIGE, mass spectrometry and antigen-antibody reactions. Both in AH and CH, the results indicated a deregulation of proteins related to sarcomere stabilization and muscle contraction. Neither in AH nor in CH the HIF-1α stabilization was observed. In AH, the …

ProteomicsCell signalingProteomeImmunoblottingApoptosisBiologyProtein degradationBiochemistryTwo-Dimensional Difference Gel ElectrophoresisMiceContractile ProteinsHeat shock proteinmedicineAnimalsHypoxiaMolecular BiologyHeat-Shock ProteinsAnimalMyocardiumAutophagyAMPK / Animal proteomics / Apoptosis / Autophagy / Heart / HypoxiaApoptosiProteomicAMPKHeat-Shock ProteinHypoxia (medical)Hypoxia-Inducible Factor 1 alpha SubunitCell biologyGene Expression RegulationMitochondrial biogenesisBiochemistrySpectrometry Mass Matrix-Assisted Laser Desorption-IonizationAdenosylhomocysteinaseContractile Proteinmedicine.symptomEnergy MetabolismPROTEOMICS
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Effect of collagen substrates on proteomic modulation of breast cancer cells

2004

We have previously described the occurrence, in breast and colon cancer extra-cellular matrix, of an oncofoetal form of collagen, OF/LB, able to induce an increase in cell proliferation and motility in the breast cancer cell line 8701-BC. It also caused an increased amount of type V collagen which appears to exert an anti-proliferative effect on the same cells. The aim of the present study was to investigate, at the proteomic level, the effect of OF/LB and type V collagens used as substrates for neoplastic cell growth. Due to the complexity of a whole proteomic profile, a subset of significant protein classes was used to assess variations in protein expression levels. For this study we adop…

ProteomicsGene isoformmedicine.medical_specialtyHot TemperatureProteomeMotilityBreast NeoplasmsBiologyMatrix (biology)ProteomicsBiochemistryproteomic breast cancer cells collagenBreast cancerSettore BIO/13 - Biologia ApplicataCell Line TumorInternal medicineHeat shock protein[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyImage Processing Computer-AssistedmedicineHumansElectrophoresis Gel Two-DimensionalMolecular BiologyHeat-Shock ProteinsProteomic ProfileProteinsmedicine.diseaseCell biologyEndocrinologySpectrometry Mass Matrix-Assisted Laser Desorption-IonizationMultivariate AnalysisNeoplastic cellCollagenCell DivisionPROTEOMICS
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Changes in the proteome of sea urchin Paracentrotus lividus coelomocytes in response to LPS injection into the body cavity.

2020

Background The immune system of echinoderm sea urchins is characterised by a high degree of complexity that is not completely understood. The Mediterranean sea urchin Paracentrotus lividus coelomocytes mediate immune responses through phagocytosis, encapsulation of non-self particles, and production of diffusible factors including antimicrobial molecules. Details of these processes, and molecular pathways driving these mechanisms, are still to be fully elucidated. Principal findings In the present study we treated the sea urchin P. lividus with the bacterial lipopolysaccharide (LPS) and collected coelomocytes at different time-points (1, 3, 6 and 24 hours). We have shown, using label-free q…

ProteomicsLipopolysaccharidesProteomeHydrolasesBiochemistry0302 clinical medicineParacentrotusMedicine and Health SciencesSea urchinCoelomocyteImmune ResponseCytoskeleton0303 health sciencesPhagocytesMultidisciplinarybiologyChemistryQREukaryotaAnimal ModelsCell biologyEnzymesEchinodermExperimental Organism Systems030220 oncology & carcinogenesisProteomeParacentrotusMedicineProtein Interaction NetworksCellular Structures and OrganellesNetwork AnalysisResearch ArticleEchinodermsComputer and Information Sciencesfood.ingredientScienceImmunologyLipopolysaccharideEndocytosisResearch and Analysis MethodsParacentrotus lividusLymphatic System03 medical and health sciencesfoodPhagocytosisbiology.animalHeat shock proteinDNA-binding proteinsAnimalsProtein Interactions030304 developmental biologyPhagocytosiAnimalOrganismsBiology and Life SciencesProteinsCell Biologybiology.organism_classificationInvertebratesCytoskeletal ProteinsGuanosine TriphosphataseProtein-Protein InteractionsPhagocyteImmune SystemSea UrchinsAnimal StudiesEnzymologyParacentrotuPLoS ONE
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Identification of proteins in excretory/secretory extracts of Echinostoma friedi (Trematoda) from chronic and acute infections.

2006

In the present study, we describe the investigation of Echinostoma friedi excretory/secretory products using a proteomic approach combined with the use of heterologous antibodies. We have identified 18 protein spots corresponding to ten proteins, including cytoskeletal proteins like actin, tropomyosin, and paramyosin; glycolytic enzymes like enolase, glyceraldehyde 3P dehydrogenase, and aldolase; detoxifying enzymes like GSTs; and stress proteins like heat shock protein (Hsp) 70. Among these proteins, both actin and, to a lesser extent, Hsp70, exhibited differential expression patterns between chronic and acute infections in the Echinostoma-rodent model, suggesting that these proteins may p…

ProteomicsMolecular Sequence DataBiologyProteomicsBiochemistrySpecies SpecificityHeat shock proteinCricetinaeEchinostomaAnimalsAmino Acid SequenceRats WistarCytoskeletonMolecular BiologyPeptide sequenceEchinostomiasisMesocricetusAldolase AProteinsTropomyosinHsp70RatsDisease Models AnimalSecretory proteinBiochemistryAcute DiseaseChronic Diseasebiology.proteinProteomics
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Reproducible and Consistent Quantification of the Saccharomyces cerevisiae Proteome by SWATH-mass spectrometry *

2015

Targeted mass spectrometry by selected reaction monitoring (S/MRM) has proven to be a suitable technique for the consistent and reproducible quantification of proteins across multiple biological samples and a wide dynamic range. This performance profile is an important prerequisite for systems biology and biomedical research. However, the method is limited to the measurements of a few hundred peptides per LC-MS analysis. Recently, we introduced SWATH-MS, a combination of data independent acquisition and targeted data analysis that vastly extends the number of peptides/proteins quantified per sample, while maintaining the favorable performance profile of S/MRM. Here we applied the SWATH-MS t…

ProteomicsOsmosisSaccharomyces cerevisiae Proteins1303 BiochemistryOsmotic shockSaccharomyces cerevisiae610 Medicine & health10071 Functional Genomics Center ZurichSaccharomyces cerevisiaeOsmosisMass spectrometryBiochemistryMass SpectrometryAnalytical Chemistry1312 Molecular BiologyData-independent acquisitionMolecular Biology1602 Analytical ChemistryChromatographybiologySelected reaction monitoringTechnological Innovation and ResourcesReproducibility of Resultsbiology.organism_classificationTargeted mass spectrometryProteomeCarbohydrate Metabolism570 Life sciences; biologyPeptidesMolecular & Cellular Proteomics
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New protein clustering of breast cancer tissue proteomics using actin content as a cellularity indicator

2008

In the present study, we report the comparative proteome profiles of proteins solubilized from 37 breast cancer surgical tissues, normalized for the actin content. Blood-derived proteins were excluded from the analysis. Among the tumor-derived protein spots, a large proportion (39%) was found present in all patients. These included several glycolytic enzymes, detox and heat shock proteins, members of annexin and S100 protein families, cathepsin D, and two “rare” proteins, DDAH2 involved in the angiogenesis control, and the oncogene PARK7. Other proteins, such as psoriasin, galectin1, cofilin, peroredoxins, SH3L1, and others, showed sporadic presence and high expression level, which suggests…

ProteomicsProteomeBlotting WesternCathepsin DBreast NeoplasmsBiologyProteomicsBiochemistryS100 proteinPeptide Mappingbreast cancer tissueAnnexinHeat shock proteinCluster AnalysisHumansElectrophoresis Gel Two-DimensionalSettore BIO/06 - Anatomia Comparata E CitologiaOncogeneReproducibility of ResultsGeneral Chemistrybreast cancer tissues; proteomicsCofilinMolecular biologyActinsSettore MED/18 - Chirurgia GeneraleSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationProteomeFemale
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Fatal anaphylactic shock and Taenia solium infestation: a possible link?

2009

Pulmonary and Respiratory MedicineFatal outcomebusiness.industryImmunologyFatal anaphylactic shockTAENIA SOLIUManaphylactic shockmedicine.disease_causemedicine.diseaseTAENIA SOLIUM; anaphylactic shockmedicine.drug_formulation_ingredientSettore MED/43 - Medicina LegaleInfestationImmunologyTaenia soliummedicineAnaphylactic shockImmunology and AllergyHelminthsTaeniasisCestode infectionsbusinessAnaphylaxis
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Induction of stress proteins in human endothelial cells by heavy metal ions and heat shock.

1999

In the present study, we compared the induction of heat shock proteins (HSPs) by heat and heavy metal ions in three different endothelial cell types, namely, human umbilical vein endothelial cells, human pulmonary microvascular endothelial cells, and the cell line EA.hy 926. Our results show that especially Zn2+and Cd2+are inducers of 70-kDa (HSP70), 60-kDa (HSP60), 32-kDa (HSP32), and 27-kDa (HSP27) HSPs. The strength of inducibility is specific for each HSP. Ni2+and Co2+only show an inducible effect at very high concentrations, that is, in the clearly cytotoxic range. Furthermore, we investigated the time course of HSP expression and the involvement of heat shock factor-1. Our study demon…

Pulmonary and Respiratory MedicineUmbilical VeinsPhysiologyMetal ions in aqueous solutionBlotting WesternGene ExpressionBiologyUmbilical veinPhysiology (medical)Heat shock proteinMetals HeavyGene expressionmedicineHumansHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsRNA MessengerFluorescent Antibody Technique IndirectCells CulturedHeat-Shock ProteinsCell BiologyChaperonin 60Endothelial stem cellmedicine.anatomical_structureCell cultureShock (circulatory)ImmunologyBiophysicsEndothelium Vascularmedicine.symptomHeat-Shock ResponseBlood vesselThe American journal of physiology
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