Search results for "CELL-ACTIVATION"

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eNOS S-nitrosylates β-actin on Cys374 and regulates PKC-θ at the immune synapse by impairing actin binding to profilin-1.

2017

The actin cytoskeleton coordinates the organization of signaling microclusters at the immune synapse (IS); however, the mechanisms involved remain poorly understood. We show here that nitric oxide (NO) generated by endothelial nitric oxide synthase (eNOS) controls the coalescence of protein kinase C-¿ (PKC-¿) at the central supramolecular activation cluster (c-SMAC) of the IS. eNOS translocated with the Golgi to the IS and partially colocalized with F-actin around the c-SMAC. This resulted in reduced actin polymerization and centripetal retrograde flow of ß-actin and PKC-¿ from the lamellipodium-like distal (d)-SMAC, promoting PKC-¿ activation. Furthermore, eNOS-derived NO S-nitrosylated ß-…

Life Sciences & Biomedicine - Other Topics0301 basic medicinePOLARIZATIONIMMUNOLOGICAL SYNAPSEImmunological SynapsesT-LymphocytesPROTEINGolgi ApparatusCYTOSKELETONRetrograde FlowBiochemistryARP2/3 COMPLEXT-CELL-ACTIVATIONProfilinsWhite Blood CellsContractile ProteinsFluorescence MicroscopyAnimal CellsMedicine and Health SciencesPseudopodiaBiology (General)Post-Translational ModificationCells CulturedProtein Kinase CMicroscopyT CellsGeneral NeuroscienceLight MicroscopyNeurochemistryRecombinant Proteins3. Good healthIsoenzymesPOLYMERIZATIONProtein TransportCell ProcessesRNA InterferenceCellular TypesNeurochemicalsGeneral Agricultural and Biological SciencesLife Sciences & BiomedicineResearch ArticleBiochemistry & Molecular BiologyNitric Oxide Synthase Type IIIQH301-705.5Imaging TechniquesRecombinant Fusion ProteinsImmune CellsImmunologyLibrary scienceAntigen-Presenting Cellsmacromolecular substancesBiologyNitric OxideResearch and Analysis MethodsGeneral Biochemistry Genetics and Molecular BiologyCell Line03 medical and health sciencesFluorescence ImagingHumansCysteineNITRIC-OXIDE SYNTHASEBiologyScience & TechnologyBlood CellsRECEPTORGeneral Immunology and MicrobiologyBiology and Life SciencesProteinsCell BiologyActinsS-NitrosylationEnzyme ActivationLuminescent ProteinsCytoskeletal Proteins030104 developmental biologyAmino Acid SubstitutionRETROGRADE FLOWProtein Kinase C-thetaMutationProtein Processing Post-TranslationalNeuroscienceActin PolymerizationPLoS biology
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Arginine deficiency leads to impaired cofilin dephosphorylation in activated human T lymphocytes

2012

The amino acid arginine is fundamentally involved in the regulation of the immune response during infection, inflammatory diseases and tumor growth. Arginine deficiency (e.g. due to the myeloid cell enzyme arginase) inhibits proliferation and effector functions of activated T lymphocytes. Here, we studied intracellular mechanisms mediating this suppression of human T lymphocytes. Our proteomic analysis revealed an impaired dephosphorylation of the actin-binding protein cofilin upon T-cell activation in the absence of arginine. We show that this correlates with alteration of actin polymerization and impaired accumulation of CD2 and CD3 in the evolving immunological synapse in T cell-antigen …

STIMULATIONEXPRESSIONHYPORESPONSIVENESSArginineCell SurvivalT-Lymphocytesmedicine.medical_treatmentCD3ImmunologyT cellsmacromolecular substancesMETABOLISMBiologyArginineLymphocyte ActivationDephosphorylationmedicineHumansImmunology and AllergyPhosphorylationCell ProliferationHUMAN GRANULOCYTE ARGINASEScience & TechnologySYNAPSE FORMATIONimmune regulationACTIN CYTOSKELETONGeneral MedicineT lymphocyteCofilincell activationTRANSLOCATIONCell biologyArginaseCytokineActin Depolymerizing Factors1107 ImmunologyCELL-ACTIVATIONLeukocytes Mononuclearbiology.proteinPhosphorylationIMMUNE-SYSTEMLife Sciences & BiomedicineInternational Immunology
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