Search results for "Phosphorylation"

showing 10 items of 975 documents

Multiple Myeloma-Derived Extracellular Vesicles Induce Osteoclastogenesis through the Activation of the XBP1/IRE1α Axis

2020

Bone disease severely affects the quality of life of over 70% of multiple myeloma (MM) patients, which daily experience pain, pathological fractures, mobility issues and an increased mortality. Recent data have highlighted the crucial role of the endoplasmic reticulum-associated unfolded protein response (UPR) in malignant transformation and tumor progression

0301 basic medicineCancer ResearchCell signalingXBP1Cellular differentiationlcsh:RC254-282Article03 medical and health sciences0302 clinical medicineSettore BIO/13 - Biologia ApplicataTranscription factorChemistryEndoplasmic reticulumextracellular-vesiclesExtracellular vesiclelcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogensCell biologymultiple myelomaUPR-related molecules030104 developmental biologyosteoclastsOncology030220 oncology & carcinogenesisUnfolded protein responsePhosphorylationbone diseaseCancers
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Dual Constant Domain-Fab: A novel strategy to improve half-life and potency of a Met therapeutic antibody

2016

The kinase receptor encoded by the Met oncogene is a sensible target for cancer therapy. The chimeric monovalent Fab fragment of the DN30 monoclonal antibody (MvDN30) has an odd mechanism of action, based on cell surface removal of Met via activation of specific plasma membrane proteases. However, the short half-life of the Fab, due to its low molecular weight, is a severe limitation for the deployment in therapy. This issue was addressed by increasing the Fab molecular weight above the glomerular filtration threshold through the duplication of the constant domains, in tandem (DCD-1) or reciprocally swapped (DCD-2). The two newly engineered molecules showed biochemical properties comparable…

0301 basic medicineCancer ResearchMice SCIDCancer targeted therapy0302 clinical medicineMice Inbred NODEpidermal growth factor receptorPhosphorylationbiologyChemistryImmunoglobulin Fab FragmentsAntibodies MonoclonalGeneral MedicineArticlesProto-Oncogene Proteins c-metHalf-lifeCell biologyOncology030220 oncology & carcinogenesisColonic NeoplasmsMetMolecular MedicineFemalemedicine.symptomSignal transductionAntibodySignal Transductionmedicine.drug_classColonAntibody; Cancer targeted therapy; Fab; Half-life; Met; Protein engineering; Cancer Research; Genetics; Molecular MedicineAntineoplastic AgentsMonoclonal antibody03 medical and health sciencesImmunoglobulin Fab FragmentsProtein DomainsCell Line TumormedicineGeneticsAnimalsHumansFabAntibodyCell growthMolecular biology030104 developmental biologyHEK293 CellsMechanism of actionHepatocyte Growth Factor ReceptorA549 Cellsbiology.proteinProtein engineering
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Phosphoproteome Profiling Reveals Multifunctional Protein NPM1 as part of the Irradiation Response of Tumor Cells

2019

To fight resistances to radiotherapy, the understanding of escape mechanisms of tumor cells is crucial. The aim of this study was to identify phosphoproteins that are regulated upon irradiation. The comparative analysis of the phosphoproteome before and after irradiation brought nucleophosmin (NPM1) into focus as a versatile phosphoprotein that has already been associated with tumorigenesis. We could show that knockdown of NPM1 significantly reduces tumor cell survival after irradiation. NPM1 is dephosphorylated stepwise within 1 hour after irradiation at two of its major phosphorylation sites: threonine-199 and threonine-234/237. This dephosphorylation is not the result of a fast cell cycl…

0301 basic medicineCancer ResearchProgrammed cell deathOriginal articleNucleoplasmCell cycle checkpointChemistryNucleolusmedicine.disease_causelcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogenslcsh:RC254-282Cell biologyDephosphorylation03 medical and health sciences030104 developmental biology0302 clinical medicineOncologyCytoplasm030220 oncology & carcinogenesismedicineCarcinogenesisIntracellularTranslational Oncology
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Chronic Sulforaphane Application Does Not Induce Resistance in Renal Cell Carcinoma Cells.

2018

Background/aim Since the natural compound sulforaphane (SFN) has been shown to stop tumor growth, renal cell carcinoma (RCC) patients often use this drug in addition to their prescribed oncotherapy. The aim of this study was to examine whether resistance to SFN may develop after long-term application. Materials and methods Several RCC cell lines were incubated with SFN for short periods of time (24-72 h) or long periods of time (8 weeks) and cell growth, proliferation, and cell-cycle proteins were analyzed. Results Both short- and long-term application of SFN distinctly reduced RCC cell growth and proliferation. However, differences in the distribution of cells in each phase of the cell cyc…

0301 basic medicineCancer ResearchTime FactorsCell SurvivalCell Cycle Proteins03 medical and health scienceschemistry.chemical_compoundIsothiocyanatesCell Line TumorAnticarcinogenic AgentsHumansPhosphorylationProtein kinase BCarcinoma Renal CellCell ProliferationCyclin-dependent kinase 1biologyCell growthCyclin-dependent kinase 2General MedicineCell cycleKidney NeoplasmsGene Expression Regulation Neoplastic030104 developmental biologyOncologychemistryCell cultureA549 CellsDrug Resistance NeoplasmSulfoxidesCancer researchbiology.proteinSignal transductionDrug Screening Assays AntitumorSulforaphaneSignal TransductionAnticancer research
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Induction of cancer cell stemness by depletion of macrohistone H2A1 in hepatocellular carcinoma.

2017

Hepatocellular carcinomas (HCC) contain a subpopulation of cancer stem cells (CSCs), which exhibit stem cell–like features and are responsible for tumor relapse, metastasis, and chemoresistance. The development of effective treatments for HCC will depend on a molecular-level understanding of the specific pathways driving CSC emergence and stemness. MacroH2A1 is a variant of the histone H2A and an epigenetic regulator of stem-cell function, where it promotes differentiation and, conversely, acts as a barrier to somatic-cell reprogramming. Here, we focused on the role played by the histone variant macroH2A1 as a potential epigenetic factor promoting CSC differentiation. In human HCC section…

0301 basic medicineCarcinoma HepatocellularBiologyMetastasisHistones03 medical and health sciencesCancer stem cellHistone H2AmedicineHumansEpigeneticsPhosphorylationCell ProliferationHepatologyCell growthGene Expression ProfilingLiver NeoplasmsTranscription Factor RelAHep G2 Cellsmedicine.disease030104 developmental biologyHistoneCancer cellCancer researchbiology.proteinNeoplastic Stem CellsReprogrammingHepatology (Baltimore, Md.)
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Magnesium and Other Biometals in Oxidative Medicine and Redox Biology

2017

No abstract available.

0301 basic medicineCell Biology magnesiumAgingSettore MED/09 - Medicina InternaArticle Subjectchemistry.chemical_elementOxidative phosphorylationBiologyBiochemistryRedox03 medical and health sciencesAnimalsHumansMagnesiumBiochemistry; Aging; Cell Biology magnesiumlcsh:QH573-671Magnesiumlcsh:CytologyCell BiologyGeneral MedicineTrace ElementsOxidative Stress030104 developmental biologyEditorialchemistryBiochemistryOxidation-ReductionOxidative Medicine and Cellular Longevity
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The Double-Edged Sword Profile of Redox Signaling: Oxidative Events As Molecular Switches in the Balance between Cell Physiology and Cancer.

2018

The intracellular redox state in the cell depends on the balance between the level of reactive oxygen species (ROS) and the activity of defensive systems including antioxidant enzymes. This balance is a dynamic process that can change in relation to many factors and/or stimuli induced within the cell. ROS production is derived from physiological metabolic events. For instance, mitochondria represent the major ROS sources during oxidative phosphorylation, but other systems, such as NADPH oxidase or specific enzymes in certain metabolisms, may account for ROS production as well. Whereas high levels of ROS perturb the cell environment, causing oxidative damage to biological macromolecules, low…

0301 basic medicineCell physiologyOxidative phosphorylationMitochondrionToxicologymedicine.disease_cause03 medical and health sciencesOxidative Stress ROS antioxidant systems0302 clinical medicineNeoplasmsmedicineAnimalsHumanschemistry.chemical_classificationReactive oxygen speciesNADPH oxidasebiologyChemistryNADPH OxidasesGeneral MedicineCell biology030104 developmental biology030220 oncology & carcinogenesisbiology.proteinSignal transductionReactive Oxygen SpeciesOxidation-ReductionIntracellularOxidative stressSignal TransductionChemical research in toxicology
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Defining Human Tyrosine Kinase Phosphorylation Networks Using Yeast as an In Vivo Model Substrate.

2017

Systematic assessment of tyrosine kinase-substrate relationships is fundamental to a better understanding of cellular signaling and its profound alterations in human diseases such as cancer. In human cells, such assessments are confounded by complex signaling networks, feedback loops, conditional activity, and intra-kinase redundancy. Here we address this challenge by exploiting the yeast proteome as an in vivo model substrate. We individually expressed 16 human non-receptor tyrosine kinases (NRTKs) in Saccharomyces cerevisiae and identified 3,279 kinase-substrate relationships involving 1,351 yeast phosphotyrosine (pY) sites. Based on the yeast data without prior information, we generated …

0301 basic medicineCell signalingHistologySaccharomyces cerevisiae ProteinsSaccharomyces cerevisiaeAmino Acid MotifsSaccharomyces cerevisiaeInteractomeReceptor tyrosine kinaseArticlePathology and Forensic Medicine03 medical and health scienceschemistry.chemical_compoundHumansProtein Interaction MapsPhosphorylationbiologyTyrosine phosphorylationCell BiologyProtein-Tyrosine Kinasesbiology.organism_classificationYeastCell biology030104 developmental biologychemistrybiology.proteinPhosphorylationTyrosine kinaseSequence AlignmentCell systems
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Identification of the integrin-binding site on coagulation factor VIIa required for proangiogenic PAR2 signaling.

2018

The tissue factor (TF) pathway serves both hemostasis and cell signaling, but how cells control these divergent functions of TF remains incompletely understood. TF is the receptor and scaffold of coagulation proteases cleaving protease-activated receptor 2 (PAR2) that plays pivotal roles in angiogenesis and tumor development. Here we demonstrate that coagulation factor VIIa (FVIIa) elicits TF cytoplasmic domain-dependent proangiogenic cell signaling independent of the alternative PAR2 activator matriptase. We identify a Lys-Gly-Glu (KGE) integrin-binding motif in the FVIIa protease domain that is required for association of the TF-FVIIa complex with the active conformer of integrin β1. A po…

0301 basic medicineCell signalingImmunologyIntegrinNeovascularization PhysiologicFactor VIIa030204 cardiovascular system & hematologyBiochemistryThromboplastinThrombosis and Hemostasis03 medical and health sciencesTissue factorMice0302 clinical medicineAnimalsHumansReceptor PAR-2Protein Interaction Domains and MotifsProtein Interaction MapsProtein kinase ACells CulturedIntegrin bindingBinding SitesbiologyChemistryIntegrin beta1Cell BiologyHematologyCell biologyCrosstalk (biology)030104 developmental biologyADP-Ribosylation Factor 6biology.proteinNIH 3T3 CellsPhosphorylationSignal transductionProtein BindingSignal TransductionBlood
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The Role of Nrf2 and PPARγ in the Improvement of Oxidative Stress in Hypertension and Cardiovascular Diseases

2020

Reactive oxygen species are an important element of redox regulation in cells and tissues. During physiological processes, molecules undergo chemical changes caused by reduction and oxidation reactions. Free radicals are involved in interactions with other molecules, leading to oxidative stress. Oxidative stress works two ways depending on the levels of oxidizing agents and products. Excessive action of oxidizing agents damages biomolecules, while a moderate physiological level of oxidative stress (oxidative eustress) is necessary to control life processes through redox signaling required for normal cellular operation. High levels of reactive oxygen species (ROS) mediate pathological change…

0301 basic medicineCell signalingNF-E2-Related Factor 2PhysiologyBlood PressureReviewOxidative phosphorylationmedicine.disease_cause03 medical and health sciences0302 clinical medicinemedicineAnimalsHumansProtein kinase BPI3K/AKT/mTOR pathwaychemistry.chemical_classificationReactive oxygen speciesKelch-Like ECH-Associated Protein 1ChemistryGeneral MedicineKEAP1Antioxidant Response ElementsNFE2L2Cell biologyPPAR gammaOxidative Stress030104 developmental biologyCardiovascular DiseasesHypertensionReactive Oxygen Species030217 neurology & neurosurgeryOxidative stressSignal TransductionPhysiological Research
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