2013
Antigen-specific, antibody-coated, exosome-like nanovesicles deliver suppressor T-cell microRNA-150 to effector T cells to inhibit contact sensitivity
Bryniarski K, Ptak W, Jayakumar A, Püllmann K, Caplan MJ, Chairoungdua A, Lu J, Adams BD, Sikora E, Nazimek K, Marquez S, Kleinstein SH, Sangwung P, Iwakiri Y, Delgato E, Redegeld F, Blokhuis BR, Wojcikowski J, Daniel AW, Kormelink T, Askenase PW. Antigen-specific, antibody-coated, exosome-like nanovesicles deliver suppressor T-cell microRNA-150 to effector T cells to inhibit contact sensitivity. Journal Of Allergy And Clinical Immunology 2013, 132: 170-181.e9. PMID: 23727037, PMCID: PMC4176620, DOI: 10.1016/j.jaci.2013.04.048.Peer-Reviewed Original ResearchConceptsCutaneous contact sensitivityEffector T cellsT cell toleranceT cellsExosome-like nanovesiclesContact sensitivityCS-effector T cellsMiRNA-150Regulatory T cellsAntigen-specific mannerSuppressor T cellsRole of antibodiesAdoptive cell transfer modelCell transfer modelT cell regulationLight chainSuppressor cellsLymph nodesReactive haptenImmune suppressionMicroRNA-150Systemic injectionAntibody light chainIntravenous injectionSpleen cells
2011
Protein Phosphatase 2A Interacts with the Na+,K+-ATPase and Modulates Its Trafficking by Inhibition of Its Association with Arrestin
Kimura T, Han W, Pagel P, Nairn AC, Caplan MJ. Protein Phosphatase 2A Interacts with the Na+,K+-ATPase and Modulates Its Trafficking by Inhibition of Its Association with Arrestin. PLOS ONE 2011, 6: e29269. PMID: 22242112, PMCID: PMC3248462, DOI: 10.1371/journal.pone.0029269.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsArrestinBinding, CompetitiveChlorocebus aethiopsCOS CellsG-Protein-Coupled Receptor KinasesGene DeletionHumansImmunoprecipitationKidneyMicePhosphorylationProtein BindingProtein BiosynthesisProtein Phosphatase 2Protein Structure, SecondaryProtein SubunitsProtein TransportRatsSodium-Potassium-Exchanging ATPaseConceptsC subunitATPase traffickingCatalytic subunitP-type ATPase familyG proteinsCatalytic C subunitTwo-hybrid systemIon transport proteinsEffect of arrestinNative rat kidneyATPase interactsProtein phosphataseATPase familyReceptor kinaseHomologous sequencesTransport proteinsFunctional domainsTrafficking propertiesImportant regulatorArrestinReceptor signalingIon pumpsTraffickingDirect interactionPP2A
2003
Polycystin-1 Distribution Is Modulated by Polycystin-2 Expression in Mammalian Cells*
Grimm DH, Cai Y, Chauvet V, Rajendran V, Zeltner R, Geng L, Avner ED, Sweeney W, Somlo S, Caplan MJ. Polycystin-1 Distribution Is Modulated by Polycystin-2 Expression in Mammalian Cells*. Journal Of Biological Chemistry 2003, 278: 36786-36793. PMID: 12840011, DOI: 10.1074/jbc.m306536200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlotting, WesternCell LineCell MembraneCells, CulturedCOS CellsDNA, ComplementaryEndoplasmic ReticulumGene Expression RegulationMembrane ProteinsMiceMice, TransgenicMicroscopy, FluorescenceModels, BiologicalMutationPrecipitin TestsProtein BindingProtein BiosynthesisProteinsRecombinant Fusion ProteinsRNA, MessengerTransfectionTRPP Cation ChannelsConceptsPolycystin-1Polycystin-2Mammalian cellsLevel of expressionPolycystin-2 expressionEndoplasmic reticulumCell surfaceCOS-7 cellsNull cell lineRelative expression levelsSubcellular localizationFusion proteinGradient of expressionExpression levelsProteinCell linesPolycystinsAutosomal dominant polycystic kidney diseaseDominant polycystic kidney diseaseDivergent patternsExpressionPolycystic kidney diseaseReticulumCellsLocalization