Search results for "protein"

showing 10 items of 21431 documents

Mutant p53 induces Golgi tubulo-vesiculation driving a prometastatic secretome

2020

TP53 missense mutations leading to the expression of mutant p53 oncoproteins are frequent driver events during tumorigenesis. p53 mutants promote tumor growth, metastasis and chemoresistance by affecting fundamental cellular pathways and functions. Here, we demonstrate that p53 mutants modify structure and function of the Golgi apparatus, culminating in the increased release of a pro-malignant secretome by tumor cells and primary fibroblasts from patients with Li-Fraumeni cancer predisposition syndrome. Mechanistically, interacting with the hypoxia responsive factor HIF1α, mutant p53 induces the expression of miR-30d, which in turn causes tubulo-vesiculation of the Golgi apparatus, leading …

0301 basic medicineBiopsyGeneral Physics and AstronomyGolgi ApparatusAnimals Biopsy Breast Neoplasms Cell Line Tumor Cell Transformation Neoplastic Female Fibroblasts Gene Expression Regulation Neoplastic Golgi Apparatus Humans Hypoxia-Inducible Factor 1 alpha Subunit Li-Fraumeni Syndrome Mice MicroRNAs Microtubules Mutation Primary Cell Culture Secretory Vesicles Signal TransductionSkin Tumor Microenvironment Tumor Suppressor Protein p53 Xenograft Model Antitumor Assays02 engineering and technologymedicine.disease_causeCell TransformationMicrotubulesSettore BIO/09 - FisiologiaMetastasisLi-Fraumeni SyndromeMiceTumor MicroenvironmentGolgisecretory machinerySuper-resolution microscopyAnimals; Biopsy; Breast Neoplasms; Cell Line Tumor; Cell Transformation Neoplastic; Female; Fibroblasts; Gene Expression Regulation Neoplastic; Golgi Apparatus; Humans; Hypoxia-Inducible Factor 1 alpha Subunit; Li-Fraumeni Syndrome; Mice; MicroRNAs; Microtubules; Mutation; Primary Cell Culture; Secretory Vesicles; Signal Transduction; Skin; Tumor Microenvironment; Tumor Suppressor Protein p53; Xenograft Model Antitumor Assayslcsh:ScienceSkinMultidisciplinaryTumorChemistrymutant p53QCell migrationMicroRNASecretomics021001 nanoscience & nanotechnologyCell biologyGene Expression Regulation NeoplasticCell Transformation NeoplasticsymbolsFibroblastmiR-30dFemaleHypoxia-Inducible Factor 10210 nano-technologyBreast NeoplasmHumanSignal TransductionCancer microenvironmentStromal cellSecretory VesicleSciencePrimary Cell CultureBreast NeoplasmsMicrotubuleGolgi ApparatuSettore MED/08 - Anatomia Patologicaalpha SubunitGeneral Biochemistry Genetics and Molecular BiologyArticleCell Line03 medical and health sciencessymbols.namesakeCell Line TumormedicineAnimalsHumansSettore MED/05 - Patologia ClinicaSecretionTumor microenvironmentNeoplasticAnimalSecretory VesiclesGeneral ChemistryOncogenesGolgi apparatusHDAC6FibroblastsMicroreviewHypoxia-Inducible Factor 1 alpha SubunitmicroenvironmentXenograft Model Antitumor AssaysMicroRNAs030104 developmental biologyGene Expression RegulationMutationlcsh:QTumor Suppressor Protein p53Carcinogenesis
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H-ferritin and proinflammatory cytokines are increased in the bone marrow of patients affected by macrophage activation syndrome

2017

Summary Macrophage activation syndrome (MAS) is hyperinflammatory life-threatening syndrome, associated typically with high levels of serum ferritin. This is an iron storage protein including heavy (H) and light (L) subunits, categorized on their molecular weight. The H-/L subunits ratio may be different in tissues, depending on the specific tissue and pathophysiological status. In this study, we analysed the bone marrow (BM) biopsies of adult MAS patients to assess the presence of: (i) H-ferritin and L-ferritin; (ii) CD68+/H-ferritin+ and CD68+/L-ferritin+; and (iii) interleukin (IL)-1β, tumour necrosis factor (TNF) and interferon (IFN)-γ. We also explored possible correlations of these re…

0301 basic medicineBiopsymedicine.medical_treatment0302 clinical medicineBone MarrowcytokineImmunology and AllergyInterleukinBlood ProteinsSyndromeMiddle AgedC-Reactive ProteinCytokinemedicine.anatomical_structureCytokinesTumor necrosis factor alphaInflammation Mediatorsmedicine.symptommacrophage activation syndromeAdultImmunologyAntigens Differentiation MyelomonocyticInflammationmacrophageBiologyProinflammatory cytokine03 medical and health sciencesAntigens CDmedicineHumansAgedRetrospective StudiesInflammation030203 arthritis & rheumatologyMacrophagesferritinOriginal ArticlesMacrophage Activationmedicine.diseaseFerritinSettore MED/16 - Reumatologia030104 developmental biologyMacrophage activation syndromeApoferritinsImmunologybiology.proteinBone marrowCytokine; Ferritin; Hyperferritinaemic syndrome; Macrophage; Macrophage activation syndrome; Immunology and Allergy; Immunologycytokine; ferritin; hyperferritinaemic syndrome; macrophage; macrophage activation syndromehyperferritinaemic syndrome
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Exploration of Fas S-Nitrosylation by the Biotin Switch Assay

2017

International audience; S-nitrosylation is the covalent attachment of nitric oxide radical to the thiol side chain of cysteine. The death receptor Fas/CD95 can be S-nitrosylated in cancer cell lines by NO donors or iNOS activation. This posttranslational modification (PTM) induces Fas aggregation into lipid rafts and enhances FasL-mediated signaling and apoptosis. In this report, we describe the detection of Fas S-nitrosylation by the most commonly used method, the biotin switch assay (BSA) technique, that allows the detection of this very labile covalent modification in cells or tissues. Briefly, this technique relies on the ability of ascorbate to reduce the covalent bond between the NO r…

0301 basic medicineBiotin switch assaybiologyChemistryNitrosylationNeutrAvidinNitric oxideS-NitrosylationFas receptorGlyceryl trinitrate3. Good health03 medical and health sciences030104 developmental biology0302 clinical medicineBiochemistryApoptosisCovalent bondFas S030220 oncology & carcinogenesisBiotinylationbiology.protein[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyLipid raft[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyCysteine
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New 1,4-Dihydropyridines Down-regulate Nitric Oxide in Animals with Streptozotocin-induced Diabetes Mellitus and Protect Deoxyribonucleic Acid agains…

2015

Diabetes mellitus (DM) and its complications cause numerous health and social problems throughout the world. Pathogenic actions of nitric oxide (NO) are responsible to a large extent for development of complications of DM. Search for compounds regulating NO production in patients with DM is thus important for the development of pharmacological drugs. Dihydropyridines (1,4-DHPs) are prospective compounds from this point of view. The goals of this study were to study the in vivo effects of new DHPs on NO and reactive nitrogen and oxygen species production in a streptozotocin (STZ)-induced model of DM in rats and to study their ability to protect DNA against nocive action of peroxynitrite. STZ…

0301 basic medicineBlood GlucoseMaleDihydropyridinesNitric Oxide Synthase Type IIIXanthine DehydrogenaseDown-RegulationNitric Oxide Synthase Type IIDHPS030204 cardiovascular system & hematologyPharmacologyToxicologyEndothelial NOSKidneyNitric OxideProtective AgentsNitric oxideDiabetes Mellitus Experimental03 medical and health scienceschemistry.chemical_compound0302 clinical medicinePeroxynitrous AcidmedicineAnimalsRats WistarReactive nitrogen speciesPharmacologybiologyGeneral MedicineDNAStreptozotocinReactive Nitrogen SpeciesRatsNitric oxide synthasePeroxynitrous acid030104 developmental biologyBiochemistrychemistryLiverbiology.proteinReactive Oxygen SpeciesPeroxynitritemedicine.drugBasicclinical pharmacologytoxicology
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Unsaturated Oral Fat Load Test Improves Glycemia, Insulinemia and Oxidative Stress Status in Nondiabetic Subjects with Abdominal Obesity.

2016

Aims To evaluate the changes in glycemia, insulinemia, and oxidative stress markers during an oral fat load test in nondiabetic subjects with abdominal obesity and to analyze the association between postprandial oxidative stress markers and postprandial glucose and insulin responses. Methods We included 20 subjects with abdominal obesity (waist circumference > 102 cm for men and > 88 cm for women) and 20 healthy lean controls (waist circumference < 102 cm for men and < 88 cm for women). After 12 hours of fasting we performed a standardized fat load test (0–8 hours) with supracal® (50 g/m2). We determined metabolic parameters, oxidized and reduced glutathione, and malondialdehyde. Results In…

0301 basic medicineBlood GlucoseMalePhysiologymedicine.medical_treatmentlcsh:MedicineBiochemistryFatschemistry.chemical_compound0302 clinical medicineEndocrinologyMalondialdehydeMedicine and Health SciencesInsulinlcsh:ScienceAbdominal obesityMultidisciplinaryOrganic CompoundsMonosaccharidesMiddle AgedMalondialdehydePostprandial PeriodGlutathioneLipidsChemistryPostprandialCholesterolPhysiological ParametersObesity AbdominalPhysical SciencesFemalemedicine.symptomResearch ArticleAdultmedicine.medical_specialtyWaistAdolescentLipoproteinsCarbohydrates030209 endocrinology & metabolism03 medical and health sciencesYoung AdultInsulin resistanceInternal medicinemedicineHumansObesityAgedDiabetic EndocrinologyEndocrine Physiologybusiness.industryInsulinUnsaturated fatlcsh:RBody WeightOrganic ChemistryChemical CompoundsBiology and Life SciencesProteinsCell Biologymedicine.diseaseObesityHormonesFats UnsaturatedOxidative Stress030104 developmental biologyEndocrinologyGlucosechemistryCase-Control Studieslcsh:QInsulin ResistancebusinessPloS one
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Low level activity thresholds for changes in NMR biomarkers and genes in high risk subjects for type 2 diabetes

2017

AbstractOur objectives were to determine if there are quantitative associations between amounts and intensities of physical activities (PA) on NMR biomarkers and changes in skeletal muscle gene expressions in subjects with high risk for type 2 diabetes (T2D) performing a 3-month PA intervention. We found that PA was associated with beneficial biomarker changes in a factor containing several VLDL and HDL subclasses and lipids in principal component analysis (P = &lt;0.01). Division of PA into quartiles demonstrated significant changes in NMR biomarkers in the 2nd - 4th quartiles compared to the 1st quartile representing PA of less than 2850 daily steps (P = 0.0036). Mediation analysis of PA-…

0301 basic medicineBlood GlucoseMaleVery low-density lipoprotein[SDV]Life Sciences [q-bio]prévention des maladieslcsh:MedicineAdipose tissueMuscle ProteinsType 2 diabetes030204 cardiovascular system & hematologyOverweight0302 clinical medicinemaladie cardiovasculairelcsh:ScienceComputingMilieux_MISCELLANEOUSBODY-WEIGHT CHANGEMultidisciplinaryMiddle AgedMagnetic Resonance Imaging[SDV] Life Sciences [q-bio]ADIPOSE-TISSUEBiomarker (medicine)SKELETAL-MUSCLEFemalemedicine.symptombiomarqueurINSULIN-RESISTANCE ATHEROSCLEROSISAutre (Sciences du Vivant)Adultmedicine.medical_specialtydiabète de type 2expression géniqueCarbohydrate metabolismALL-CAUSEArticle03 medical and health sciencesMedical researchLIPID-METABOLISMInternal medicineDiabetes mellitusmedicineAPOLIPOPROTEIN-D POLYMORPHISMHumansObesityNUCLEAR-MAGNETIC-RESONANCEMuscle SkeletalExercisebusiness.industryMORTALITYlcsh:RLipid metabolismsurpoidsLIPOPROTEIN PARTICLE-SIZEmedicine.disease030104 developmental biologyEndocrinologyPHYSICAL-ACTIVITYDiabetes Mellitus Type 2Gene Expression Regulationlcsh:QbusinessBiomarkers
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Decreased consumption of branched-chain amino acids improves metabolic health

2016

Protein-restricted (PR), high-carbohydrate diets improve metabolic health in rodents, yet the precise dietary components that are responsible for these effects have not been identified. Furthermore, the applicability of these studies to humans is unclear. Here, we demonstrate in a randomized controlled trial that a moderate PR diet also improves markers of metabolic health in humans. Intriguingly, we find that feeding mice a diet specifically reduced in branched-chain amino acids (BCAAs) is sufficient to improve glucose tolerance and body composition equivalently to a PR diet via metabolically distinct pathways. Our results highlight a critical role for dietary quality at the level of amino…

0301 basic medicineBlood GlucoseMalemedicine.medical_specialtyAdipose Tissue WhiteAdipose tissueBiologybranched-chain amino acids (BCAAs)General Biochemistry Genetics and Molecular BiologyArticle03 medical and health sciences0302 clinical medicineStress PhysiologicalInternal medicineInsulin-Secreting CellsGlucose IntolerancemedicineAnimalsHumansbiochemistryObesitylcsh:QH301-705.5Metabolic health2. Zero hungerchemistry.chemical_classificationgenetics and molecular biology (all)GluconeogenesisOrgan SizeMiddle Agedmedicine.diseaseObesityAmino acidFibroblast Growth FactorsMice Inbred C57BLProtein-restricted (PR)030104 developmental biologyEndocrinologyPharmacological interventionslcsh:Biology (General)BiochemistrychemistryGluconeogenesisDiet qualitybiochemistry; genetics and molecular biology (all)Dietary Proteins030217 neurology & neurosurgeryAmino Acids Branched-Chain
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The Involvement of Toll-like Receptor-2 in Arterial Thrombus Formation.

2018

There is emerging evidence for the participation of toll-like receptor-2 (TLR2) expressed on platelets and endothelial cells in the setting of arterial thrombosis. In isolated human platelets, TLR2/1 activation was demonstrated to induce platelet activation, secretion, aggregation, adhesion to collagen coatings and the formation of platelet-leukocyte conjugates, whereas murine platelets were less sensitive to TLR2/1 stimulation. Also, endothelial cells can be activated by stimulation with TLR2 agonists, resulting in increased expression of adhesion molecules, synthesis of inflammatory mediators and Weibel-Palade body exocytosis. Endothelial TLR2 signalling promotes atherosclerotic lesion de…

0301 basic medicineBlood Platelets030204 cardiovascular system & hematology03 medical and health sciences0302 clinical medicineVon Willebrand factormedicineAnimalsHumansPlateletPlatelet activationInflammationToll-like receptorbiologyCell adhesion moleculeChemistryEndothelial CellsCarotid Artery ThrombosisThrombosisHematologyArteriesmedicine.diseasePlatelet ActivationThrombosisPlaque AtheroscleroticToll-Like Receptor 2TLR2030104 developmental biologyCancer researchbiology.proteinHamostaseologie
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CD36-fibrin interaction propagates FXI-dependent thrombin generation of human platelets.

2019

Thrombin converts fibrinogen to fibrin and activates blood and vascular cells in thrombo-inflammatory diseases. Platelets are amplifiers of thrombin formation when activated by leukocyte- and vascular cell-derived thrombin. CD36 on platelets acts as sensitizer for molecules with damage-associated molecular patterns, thereby increasing platelet reactivity. Here, we investigated the role of CD36 in thrombin-generation on human platelets, including selected patients with advanced chronic kidney disease (CKD). Platelets deficient in CD36 or blocked by anti-CD36 antibody FA6.152 showed impaired thrombin generation triggered by thrombin in calibrated automated thrombography. Using platelets with …

0301 basic medicineBlood PlateletsCD36 AntigensCD36InflammationFibrinogenBiochemistryFibrin03 medical and health sciences0302 clinical medicineThrombinBlocking antibodyGeneticsmedicineHumansPlateletRenal Insufficiency ChronicMolecular BiologyFactor XIFibrinbiologyChemistryCell adhesion moleculeThrombinPlatelet ActivationBlood Coagulation FactorsCell biology030104 developmental biologybiology.proteinmedicine.symptom030217 neurology & neurosurgerycirculatory and respiratory physiologyBiotechnologymedicine.drugFASEB journal : official publication of the Federation of American Societies for Experimental BiologyREFERENCES
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Impaired Platelet Function in Sept8-Deficient Mice In Vitro.

2020

AbstractSeptins (Septs) are a widely expressed protein family of 13 mammalian members, recognized as a unique component of the cytoskeleton. In human platelets, we previously described that SEPT4 and SEPT8 are localized surrounding α-granules and move to the platelet surface after activation, indicating a possible role in platelet physiology. In this study, we investigated the impact of Sept8 on platelet function in vitro using Sept8-deficient mouse platelets. Deletion of Sept8 in mouse platelets caused a pronounced defect in activation of the fibrinogen receptor integrin αIIbβ3, α-granule exocytosis, and aggregation, especially in response to the glycoprotein VI agonist convulxin. In contr…

0301 basic medicineBlood PlateletsGenotypePlatelet AggregationFibrinogen receptorIntegrinPlatelet Glycoprotein GPIIb-IIIa Complex030204 cardiovascular system & hematologyFibrinogenCytoplasmic GranulesExocytosisExocytosis03 medical and health sciences0302 clinical medicineLysosomeCrotalid VenomsmedicineAnimalsPlateletLectins C-TypeLactadherinMice KnockoutbiologyChemistryThrombinFibrinogenConvulxinHematologyPlatelet ActivationCell biologyMice Inbred C57BL030104 developmental biologymedicine.anatomical_structurePhenotypebiology.proteinFemaleLysosomesSeptinsmedicine.drugThrombosis and haemostasis
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