Search results for "TOC"

showing 10 items of 14693 documents

The dissociation of the Hsp60/pro-Caspase-3 complex by bis(pyridyl)oxadiazole copper complex (CubipyOXA) leads to cell death in NCI-H292 cancer cells

2017

Abstract Cell survival and proliferation are central to carcinogenesis, involving various mechanisms among which those that impede apoptosis are important. In this, the role of the molecular chaperone Hsp60 is unclear since it has been reported that it can be both, pro- or anti-apoptotic. A solution to this riddle is crucial to the development of anti-cancer therapies targeting Hsp60. We addressed this question using a tumor cell line, NCI-H292, and [Cu(3,5-bis(2′-pyridyl)-1,2,4-oxadiazole) 2 (H 2 O) 2 ](ClO 4 ) 2 , CubipyOXA , a copper-containing compound with cytotoxic properties. We treated cells with various doses of the compound and measured cell viability; apoptosis indicators; and le…

0301 basic medicineProgrammed cell deathanimal structuresApoptosischemical and pharmacologic phenomenaCaspase 3medicine.disease_causecomplex mixturesBiochemistryMitochondrial ProteinsHsp60/pC3 complexInorganic Chemistry03 medical and health sciences0302 clinical medicineCoordination ComplexesCell Line TumorNeoplasmsCubipyOXAmedicineHumansCytotoxic T cellViability assayCancerOxadiazolesCaspase 3ChemistryfungiApoptosiChaperonin 60Hsp60Neoplasm ProteinsCell biology030104 developmental biologyApoptosisPro-caspase-3 (pC3)Multiprotein Complexes030220 oncology & carcinogenesisCancer cellHSP60Apoptosis; Cancer; CubipyOXA; Hsp60; Hsp60/pC3 complex; Pro-caspase-3 (pC3); Biochemistry; Inorganic ChemistryCarcinogenesisCopper
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Extracellular histones disarrange vasoactive mediators reléase through COX-NOS interaction in human endothelial cells

2017

Abstract Extracellular histones are mediators of inflammation, tissue injury and organ dysfunction. Interactions between circulating histones and vascular endothelial cells are key events in histone‐mediated pathologies. Our aim was to investigate the implication of extracellular histones in the production of the major vasoactive compounds released by human endothelial cells (HUVECs), prostanoids and nitric oxide (NO). HUVEC exposed to increasing concentrations of histones (0.001 to 100 μg/ml) for 4 hrs induced prostacyclin (PGI2) production in a dose‐dependent manner and decreased thromboxane A2 (TXA2) release at 100 μg/ml. Extracellular histones raised cyclooxygenase‐2 (COX‐2) and prostac…

0301 basic medicineProstacyclinHistoneschemistry.chemical_compoundThromboxane A2Cytochrome P-450 Enzyme SystemSuperoxidesEnosvascular mediatorsGenètica humanabiologySuperoxideendothelial cellsIntramolecular OxidoreductasesEndothelial stem cellMolecular MedicineOriginal ArticleThromboxane-A SynthaseSignal Transductionmedicine.drugmedicine.medical_specialtyNitric Oxide Synthase Type IIIPrimary Cell CultureNitric OxideProstacyclin synthaseNitric oxideCyclic N-OxidesThromboxane A203 medical and health sciencesInternal medicineHuman Umbilical Vein Endothelial CellsmedicineExtracellularHumansRNA MessengerprostanoidsDose-Response Relationship DrugOriginal ArticlesCell Biologybiology.organism_classificationEpoprostenolÒxid nítric030104 developmental biologyEndocrinologyGene Expression RegulationchemistryCelecoxibCyclooxygenase 2Cyclooxygenase 1biology.proteinSpin LabelsProteïnesextracellular histones
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Pro- and Antitumorigenic Capacity of Immunoproteasomes in Shaping the Tumor Microenvironment

2021

Abstract Apart from the constitutive proteasome, the immunoproteasome that comprises the three proteolytic subunits LMP2, MECL-1, and LMP7 is expressed in most immune cells. In this study, we describe opposing roles for immunoproteasomes in regulating the tumor microenvironment (TME). During chronic inflammation, immunoproteasomes modulated the expression of protumorigenic cytokines and chemokines and enhanced infiltration of innate immune cells, thus triggering the onset of colitis-associated carcinogenesis (CAC) in wild-type mice. Consequently, immunoproteasome-deficient animals (LMP2/MECL-1/LMP7–null mice) were almost completely resistant to CAC development. In patients with ulcerative c…

0301 basic medicineProteasome Endopeptidase ComplexCancer ResearchChemokineImmunologyMelanoma ExperimentalAntineoplastic AgentsInflammationmedicine.disease_causeArticleMice03 medical and health sciences0302 clinical medicineImmune systemCell Line TumorTumor MicroenvironmentmedicineAnimalsHumansMice KnockoutTumor microenvironmentInnate immune systembiologyChemistryMelanomaHistocompatibility Antigens Class IColitismedicine.diseaseMice Inbred C57BLCysteine Endopeptidases030104 developmental biology030220 oncology & carcinogenesisCancer researchbiology.proteinCytokinesFemalemedicine.symptomCarcinogenesisCD8T-Lymphocytes CytotoxicCancer Immunology Research
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The C-terminal Domains of Apoptotic BH3-only Proteins Mediate Their Insertion into Distinct Biological Membranes

2016

Changes in the equilibrium of pro- and anti-apoptotic members of the B-cell lymphoma-2 (Bcl-2) protein family in the mitochondrial outer membrane (MOM) induce structural changes that commit cells to apoptosis. Bcl-2 homology-3 (BH3)-only proteins participate in this process by either activating pro-apoptotic effectors or inhibiting anti-apoptotic components and by promoting MOM permeabilization. The association of BH3-only proteins with MOMs is necessary for the activation and amplification of death signals; however, the nature of this association remains controversial, as these proteins lack a canonical transmembrane sequence. Here we used an in vitro expression system to study the inserti…

0301 basic medicineProtein familyCèl·lulesBiologyBiochemistryMitochondrial Proteins03 medical and health sciencesProtein DomainsMembranes (Biologia)Protein-fragment complementation assayMembrane BiologyMicrosomesProto-Oncogene ProteinsHumansMolecular BiologyAdaptor Proteins Signal TransducingGeneticsBcl-2-Like Protein 11030102 biochemistry & molecular biologyCell MembraneBcl-2 familyProteïnes de membranaMembrane ProteinsBiological membraneCell BiologyFusion proteinTransmembrane proteinCell biology030104 developmental biologyMembraneProto-Oncogene Proteins c-bcl-2Membrane proteinB-cell lymphoma 2 (Bcl-2) family BH3-only apoptosis membrane insertion membrane protein mitochondrial apoptosis transmembrane domainApoptosis Regulatory ProteinsHydrophobic and Hydrophilic InteractionsHeLa CellsJournal of Biological Chemistry
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Mcl-1 and Bok transmembrane domains : Unexpected players in the modulation of apoptosis

2020

The Bcl-2 protein family comprises both proand antiapoptotic members that control the permeabilization of the mitochondrial outer membrane, a crucial step in the modulation of apoptosis. Recent research has demonstrated that the carboxyl-terminal transmembrane domain (TMD) of some Bcl-2 protein family mem-bers can modulate apoptosis; however, the transmembrane interactome of the antiapoptotic protein Mcl-1 remains largely unexplored. Here, we demonstrate that the Mcl-1 TMD forms homooligomers in the mitochondrial membrane, competes with full-length Mcl-1 protein with regards to its antiapoptotic function, and induces cell death in a Bok-dependent manner. While the Bok TMD oligomers locate p…

0301 basic medicineProtein familyMitochondrionBCL-X(L)Endoplasmic ReticulumInteractome114 Physical sciences03 medical and health sciencesBok0302 clinical medicineProtein DomainsMITOCHONDRIAhemic and lymphatic diseasesAnimalsHumansBcl-2Inner mitochondrial membraneMultidisciplinaryCell DeathChemistryEndoplasmic reticulumapoptosisMcl-1PATHWAYSLOCALIZATIONBiological SciencesTransmembrane protein3. Good healthCell biologytransmembraneTransmembrane domainstomatognathic diseasesGLYCOPHORIN-A DIMERIZATION030104 developmental biologyHELIX PACKINGProto-Oncogene Proteins c-bcl-2BAX030220 oncology & carcinogenesisMitochondrial MembranesPROSURVIVAL BCL-2 PROTEINSMOTIFSURVIVALMyeloid Cell Leukemia Sequence 1 Protein1182 Biochemistry cell and molecular biologyBacterial outer membraneHeLa Cells
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Lack of NFATc1 SUMOylation prevents autoimmunity and alloreactivity

2020

A novel transgenic mouse, in which the transcription factor NFATc1 bears lysine-to-arginine mutations that prevent modification by SUMO, develops normally and is healthy. However, SUMO-insensitive NFATc1 transmits strong tolerogenic signals, thus preventing autoimmune and alloimmune T cell responses.

0301 basic medicineProtein sumoylationEncephalomyelitis Autoimmune ExperimentalT cellStem Cells & RegenerationImmunologySUMO proteinAutoimmunityBiologyenvironment and public healthT-Lymphocytes RegulatoryArticleMinor Histocompatibility AntigensMice03 medical and health sciences0302 clinical medicineImmune systemNeuroinflammationAldesleukinSTAT5 Transcription FactormedicineAnimalsImmunology and AllergyTranscription factorMice Knockoutintegumentary systemNFATC Transcription FactorsExperimental autoimmune encephalomyelitisSumoylationNFATmedicine.diseaseCell biologyenzymes and coenzymes (carbohydrates)030104 developmental biologymedicine.anatomical_structureProto-Oncogene Proteins c-bcl-2030220 oncology & carcinogenesisCytokinesPositive Regulatory Domain I-Binding Factor 1Journal of Experimental Medicine
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Phosphoproteomics of the developing heart identifies PERM1 - An outer mitochondrial membrane protein.

2021

Heart development relies on PTMs that control cardiomyocyte proliferation, differentiation and cardiac morphogenesis. We generated a map of phosphorylation sites during the early stages of cardiac postnatal development in mice; we quantified over 10,000 phosphorylation sites and 5000 proteins that were assigned to different pathways. Analysis of mitochondrial proteins led to the identification of PGC-1- and ERR-induced regulator in muscle 1 (PERM1), which is specifically expressed in skeletal muscle and heart tissue and associates with the outer mitochondrial membrane. We demonstrate PERM1 is subject to rapid changes mediated by the UPS through phosphorylation of its PEST motif by casein ki…

0301 basic medicineProteomicsOrganogenesisMFN2Muscle ProteinsP70-S6 Kinase 1030204 cardiovascular system & hematologyMitochondrionMitochondria Heart03 medical and health sciencesMice0302 clinical medicineCa2+/calmodulin-dependent protein kinaseAnimalsMolecular BiologyMitochondrial transportMice KnockoutChemistryMyocardiumPhosphoproteomicsMembrane ProteinsHeartLipid MetabolismPhosphoproteinsSolute carrier familyCell biology030104 developmental biologyMitochondrial MembranesPhosphorylationCardiology and Cardiovascular MedicineJournal of molecular and cellular cardiology
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MHC class I loaded ligands from breast cancer cell lines: A potential HLA-I-typed antigen collection.

2018

Abstract To build a catalog of peptides presented by breast cancer cells, we undertook systematic MHC class I immunoprecipitation followed by elution of MHC class I-loaded peptides in breast cancer cells. We determined the sequence of 3196 MHC class I ligands representing 1921 proteins from a panel of 20 breast cancer cell lines. After removing duplicate peptides, i.e., the same peptide eluted from more than one cell line, the total number of unique peptides was 2740. Of the unique peptides eluted, more than 1750 had been previously identified, and of these, sixteen have been shown to be immunogenic. Importantly, half of these immunogenic peptides were shared between different breast cancer…

0301 basic medicineProteomicsPlant BiologyPeptideLigandsBiochemistryEpitopeAnalytical ChemistryEpitopesBreast cancerT cell-mediated immune responseHLA Antigens2.1 Biological and endogenous factorsAetiologyCancerchemistry.chemical_classificationAntigen PresentationTumorbiologyBiochemistry & Molecular BiologyBiophysicsBreast NeoplasmsArticleCell LineVaccine Related03 medical and health sciencesImmune systemBreast cancerAntigenAntigens NeoplasmCell Line TumorMHC class ImedicineGeneticsHumansAmino Acid SequenceAntigensMHC class I-restricted peptidesTumor associated antigensPreventionHistocompatibility Antigens Class ICancermedicine.diseaseHigh-Throughput Screening Assays030104 developmental biologychemistryCell cultureNeo-antigensMutationbiology.proteinCancer researchNeoplasmImmunizationBiochemistry and Cell Biology
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MycoKey Round Table Discussions of Future Directions in Research on Chemical Detection Methods, Genetics and Biodiversity of Mycotoxins

2018

MycoKey, an EU-funded Horizon 2020 project, includes a series of “Roundtable Discussions” to gather information on trending research areas in the field of mycotoxicology. This paper includes summaries of the Roundtable Discussions on Chemical Detection and Monitoring of mycotoxins and on the role of genetics and biodiversity in mycotoxin production. Discussions were managed by using the nominal group discussion technique, which generates numerous ideas and provides a ranking for those identified as the most important. Four questions were posed for each research area, as well as two questions that were common to both discussions. Test kits, usually antibody based, were one major focus of the…

0301 basic medicineProteomicsSettore CHIM/01 - CHIMICA ANALITICAComputer scienceHealth Toxicology and MutagenesisBiodiversitylcsh:Medicinebiological controlmicrobiomeToxicology//purl.org/becyt/ford/1 [https]transcriptomicscommunication with non-scientistsA better understanding of metabolomics from the cellular to the ecosystem level is needed to inform and control mycotoxin production control and remediation. Antibody-based diagnostics have become an acceptable standard in many practical applications but sophisticated multi-mycotoxin detection protocols are the future for many official regulatory controls especially as the number of toxins that are regulated increases and need more standardization and cross-laboratory validation.antibodies2. Zero hungerGeneticsbiologyNominal groupBiodiversitymetabolomicsGeneral partnershipBiological controlAntibodiesBiological controlCommunication with non-scientists Metabolomics Microbiome Multi-mycotoxin detection protocols Nominal group discussion technique ProteomicsTranscriptomicsmulti-mycotoxin detection protocolsSettore AGR/12 - PATOLOGIA VEGETALECommunication with non-scientistsEnvironmental MonitoringNominal group discussion techniqueOpinionAntibodies03 medical and health sciencesMycotoxicologyBiointeractions and Plant HealthproteomicsFood supplyAnimalsHumansMetabolomicsnominal group discussion technique//purl.org/becyt/ford/1.6 [https]Transcriptomicsbusiness.industryResearchlcsh:RUsabilityMycotoxinsbiology.organism_classification030104 developmental biologyMulti-mycotoxin detection protocolsRound tableRankingMicrobiomeEPSbusinesscommunication with non-scientistToxins
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Proteomics Standards Initiative: Fifteen Years of Progress and Future Work.

2017

Abstract: The Proteomics Standards Initiative (PSI) of the Human Proteome Organization (HUPO) has now been developing and promoting open community standards and software tools in the field of proteomics for 15 years. Under the guidance of the chair, co-chairs, and other leadership positions, the PSI working groups are tasked with the development and maintenance of community standards via special workshops and ongoing work. Among the existing, ratified standards, the PSI working groups continue to update PSI-MI XML, MITAB, mzML, mzIdentML, mzQuantML, mzTab, and the MIAPE (Minimum Information About a Proteomics Experiment) guidelines with the advance of new technologies and techniques. Furthe…

0301 basic medicineProteomicsprotein quantificationEmerging technologiesComputer sciencecomputer.internet_protocolGuidelines as Topiccomputer.software_genreBiochemistry03 medical and health sciencesprotein identificationHuman proteome projectHumansCommunity standardsquality controlDatabases ProteinBiologydatabasemass spectrometryComputer. Automation030102 biochemistry & molecular biologyApplication programming interfaceProteomics Standards InitiativeGeneral ChemistryReference StandardsData sciencemetabolomicsChemistry030104 developmental biologyPerspectivedata standardWeb servicebioinformatics softwareWorking groupcomputerXMLSoftwaremolecular interactionsJournal of proteome research
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