2006
Pathophysiology of leukocyte–tissue interactions
Molteni R, Fabbri M, Bender JR, Pardi R. Pathophysiology of leukocyte–tissue interactions. Current Opinion In Cell Biology 2006, 18: 491-498. PMID: 16904306, DOI: 10.1016/j.ceb.2006.08.001.Peer-Reviewed Original Research
2005
Dynamic Partitioning into Lipid Rafts Controls the Endo-Exocytic Cycle of the αL/β2 Integrin, LFA-1, during Leukocyte Chemotaxis
Fabbri M, Di Meglio S, Gagliani MC, Consonni E, Molteni R, Bender JR, Tacchetti C, Pardi R. Dynamic Partitioning into Lipid Rafts Controls the Endo-Exocytic Cycle of the αL/β2 Integrin, LFA-1, during Leukocyte Chemotaxis. Molecular Biology Of The Cell 2005, 16: 5793-5803. PMID: 16207819, PMCID: PMC1289422, DOI: 10.1091/mbc.e05-05-0413.Peer-Reviewed Original ResearchConceptsDetergent-resistant membranesInternalized receptorsLate endosomal pathwayCholesterol-sequestering agentRab11 mutantDRM associationPolarized recyclingCell rearCell frontPlasma membraneChemoattractant stimulationEndocytic compartmentsEndosomal pathwayAdhesion receptorsCell migrationNew protrusionsIntegrinsLFA-1Dynamic redistributionMutantsLamellipodiaAdhesive interactionsPrimary neutrophilsIntracellular accumulationΒ2 integrins
1999
A tyrosine‐based sorting signal in the β2 integrin cytoplasmic domain mediates its recycling to the plasma membrane and is required for ligand‐supported migration
Fabbri M, Fumagalli L, Bossi G, Bianchi E, Bender J, Pardi R. A tyrosine‐based sorting signal in the β2 integrin cytoplasmic domain mediates its recycling to the plasma membrane and is required for ligand‐supported migration. The EMBO Journal 1999, 18: 4915-4925. PMID: 10487744, PMCID: PMC1171563, DOI: 10.1093/emboj/18.18.4915.Peer-Reviewed Original ResearchConceptsIntegrin cytoplasmic domainCytoplasmic domainBeta-subunit cytoplasmic domainAdhesive functionTyrosine-based endocytic signalsSubunit cytoplasmic domainClathrin-dependent endocytosisSite-directed mutagenesisNon-conservative substitutionsChinese hamster ovary cellsEndocytic signalsRegulated internalizationMembrane rufflesUnrelated functionsRecycling compartmentHamster ovary cellsEctopic expressionPlasma membraneReceptor recyclingDegradative pathwayIntegrin dynamicsCell adhesionCell migrationCell surfaceOvary cells
1996
Integrin-dependent induction of functional urokinase receptors in primary T lymphocytes.
Bianchi E, Ferrero E, Fazioli F, Mangili F, Wang J, Bender J, Blasi F, Pardi R. Integrin-dependent induction of functional urokinase receptors in primary T lymphocytes. Journal Of Clinical Investigation 1996, 98: 1133-1141. PMID: 8787676, PMCID: PMC507535, DOI: 10.1172/jci118896.Peer-Reviewed Original ResearchMeSH KeywordsAdenylyl CyclasesBreast NeoplasmsCD18 AntigensCell MovementCyclic AMPFemaleFlow CytometryHumansImmunologic CappingIntegrin beta1Lymphocyte ActivationLymphocytes, Tumor-InfiltratingPancreatic NeoplasmsProtein Kinase CReceptors, Cell SurfaceReceptors, Urokinase Plasminogen ActivatorRNA, MessengerSecond Messenger SystemsT-LymphocytesUrokinase-Type Plasminogen ActivatorConceptsUrokinase plasminogen activatorAntigen receptor complexProtein kinase C activationAnti-uPAR antibodiesPlasminogen activator/plasmin systemKinase C activationPrimary human tumor specimensRegulated processPrimary T lymphocytesHuman tumor specimensT lymphocytesT cellsUrokinase receptorCell migrationExtracellular matrixReceptor complexC activationProtein levelsSites of inflammationT cell migrationPlasminogen activationCatalytic activationIntracellular cyclic AMPPlasmin systemCyclic AMP