2000
CD28 and LFA‐1 contribute to cyclosporin A‐resistant T cell growth by stabilizing the IL‐2 mRNA through distinct signaling pathways
Geginat J, Clissi B, Moro M, Dellabona P, Bender J, Pardi R. CD28 and LFA‐1 contribute to cyclosporin A‐resistant T cell growth by stabilizing the IL‐2 mRNA through distinct signaling pathways. European Journal Of Immunology 2000, 30: 1136-1144. PMID: 10760803, DOI: 10.1002/(sici)1521-4141(200004)30:4<1136::aid-immu1136>3.0.co;2-3.Peer-Reviewed Original ResearchMeSH KeywordsAntigens, CDB7-2 AntigenCalcineurinCD28 AntigensCells, CulturedCyclosporineCytoskeletonDendritic CellsDNA-Binding ProteinsDrug SynergismHumansIntercellular Adhesion Molecule-1Interleukin-2Lymphocyte ActivationLymphocyte Function-Associated Antigen-1Membrane GlycoproteinsMitogen-Activated Protein KinasesNFATC Transcription FactorsNF-kappa BNuclear ProteinsPromoter Regions, GeneticProtein BindingRNA StabilityRNA, MessengerSignal TransductionSuperantigensT-LymphocytesTranscription FactorsConceptsIL-2 mRNALFA-1ICAM-1IL-2 dependentT cell proliferationSubsequent T cell proliferationCostimulatory molecule CD28TCR-induced proliferationSignaling pathwaysT cell growthIL-2 transcriptsGraft rejectionDendritic cellsIL-2Clinical transplantationT lymphocytesMolecule CD28Primary T lymphocytesNF-kappaBCD28Distinct signaling pathwaysLower transcriptional rateDifferent signaling pathwaysProtein kinase activationCell proliferation
1997
Cytoskeletal rearrangement mediates human microvascular endothelial tight junction modulation by cytokines
Blum M, Toninelli E, Anderson J, Balda M, Zhou J, O'Donnell L, Pardi R, Bender J. Cytoskeletal rearrangement mediates human microvascular endothelial tight junction modulation by cytokines. American Journal Of Physiology 1997, 273: h286-h294. PMID: 9249502, DOI: 10.1152/ajpheart.1997.273.1.h286.Peer-Reviewed Original ResearchMeSH Keywords1-Methyl-3-isobutylxanthineActinsBucladesineCells, CulturedCytokinesCytoskeletonElectrophysiologyEndothelium, VascularHumansInfant, NewbornInterferon-gammaMaleMembrane PotentialsMembrane ProteinsMicrocirculationPhosphoproteinsSkinTight JunctionsTumor Necrosis Factor-alphaUmbilical VeinsZonula Occludens-1 ProteinConceptsTransmonolayer electrical resistanceSpecialized intercellular structuresTight junctionsF-actin cytoskeletonLarge vessel ECActin cytoskeletonEndothelial cell typesMicrovascular endothelial cellsCytoskeletal rearrangementsStriking fragmentationF-actinProtein distributionCytochalasin DCell typesIntercellular structuresBarrier regulationCytoskeletal alterationsConfocal microscopyMVEC monolayersZO-1Macromolecular fluxCentral roleEC permeabilityEndothelial cellsPrimary cultures
1996
Feedback modulation of ligand-engaged alpha L/beta 2 leukocyte integrin (LFA-1) by cyclic AMP-dependent protein kinase.
Rovere P, Inverardi L, Bender J, Pardi R. Feedback modulation of ligand-engaged alpha L/beta 2 leukocyte integrin (LFA-1) by cyclic AMP-dependent protein kinase. The Journal Of Immunology 1996, 156: 2273-9. PMID: 8690918, DOI: 10.4049/jimmunol.156.6.2273.Peer-Reviewed Original ResearchConceptsProtein kinase CAdhesion receptorsKinase CCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseCytoskeletal anchoring proteinsIntegrin-dependent activationCAMP-dependent kinase activationIntracellular cAMP elevationCAMP elevationHeterologous cell linesLeukocyte integrinsAnchoring proteinsRegulated processProtein kinaseAdenylyl cyclase isoformsMolecular basisKinase activationIntercellular adhesionF-actinCell deadhesionHuman intercellular adhesion molecule-1LFA-1 receptorsDependent adhesionShort-term regulation
1995
Conserved regions in the cytoplasmic domains of the leukocyte integrin alpha L beta 2 are involved in endoplasmic reticulum retention, dimerization, and cytoskeletal association.
Pardi R, Bossi G, Inverardi L, Rovida E, Bender J. Conserved regions in the cytoplasmic domains of the leukocyte integrin alpha L beta 2 are involved in endoplasmic reticulum retention, dimerization, and cytoskeletal association. The Journal Of Immunology 1995, 155: 1252-63. PMID: 7636193, DOI: 10.4049/jimmunol.155.3.1252.Peer-Reviewed Original ResearchMeSH KeywordsAllosteric RegulationAmino Acid SequenceAnimalsCell CompartmentationCell Line, TransformedChlorocebus aethiopsCytoskeletonEndoplasmic ReticulumLymphocyte Function-Associated Antigen-1Molecular Sequence DataProtein ConformationProtein MultimerizationProtein Structure, TertiaryRecombinant Fusion ProteinsSequence DeletionTetradecanoylphorbol AcetateT-LymphocytesTransfectionConceptsAlpha L beta 2Cytoplasmic domainEndoplasmic reticulum retentionCytoskeletal associationBeta subunitAlpha L subunitAlpha beta complexFunction of integrinsBeta 2GFFKR motifAdherent cellsDeletion mutantsSubstitution mutantsEctopic expressionIntegrin alphaPlasma membraneHeterodimer formationConserved regionsAdhesion receptorsBeta complexCytoplasmic truncationRegulated functionsL subunitsStructural determinantsAlpha L
1992
Antigen-receptor complex stimulation triggers protein kinase C-dependent CD11a/CD18-cytoskeleton association in T lymphocytes.
Pardi R, Inverardi L, Rugarli C, Bender J. Antigen-receptor complex stimulation triggers protein kinase C-dependent CD11a/CD18-cytoskeleton association in T lymphocytes. Journal Of Cell Biology 1992, 116: 1211-1220. PMID: 1346786, PMCID: PMC2289356, DOI: 10.1083/jcb.116.5.1211.Peer-Reviewed Original ResearchMeSH KeywordsActinsAdultAntigens, CDAntigens, Differentiation, T-LymphocyteCD18 AntigensCD3 ComplexChild, PreschoolCytoskeletal ProteinsCytoskeletonHumansLymphocyte ActivationLymphocyte Function-Associated Antigen-1PhosphorylationProtein Kinase CReceptors, Antigen, T-CellSignal TransductionT-LymphocytesConceptsProtein kinase C inhibitor staurosporineProtein kinase CT cell receptor complexCell receptor complexC inhibitor staurosporineHigh avidity stateSignal transductionCytoskeletal rearrangementsActin polymerizationIntercellular adhesionIntracellular signalsF-actinMolecular eventsInhibitor staurosporineKinase CAvidity stateLFA-1Membrane fractionCD11a/CD18 complexTCR complexTCR crosslinkingPKC desensitizationComplex activationReceptor complexFluorescence microscopy