2000
In vivo delivery of the caveolin-1 scaffolding domain inhibits nitric oxide synthesis and reduces inflammation
Bucci M, Gratton J, Rudic R, Acevedo L, Roviezzo F, Cirino G, Sessa W. In vivo delivery of the caveolin-1 scaffolding domain inhibits nitric oxide synthesis and reduces inflammation. Nature Medicine 2000, 6: 1362-1367. PMID: 11100121, DOI: 10.1038/82176.Peer-Reviewed Original ResearchConceptsCaveolin-1Signal transductionSmall-molecule mimicryCaveolae assemblyInternalization sequenceCoat proteinEndothelial cellsPhysiological importanceEndothelial nitric oxide synthase (eNOS) inhibitorTransductionCholesterol transportNitric oxide synthase inhibitorChimeric peptideInhibits nitric oxide synthesisOxide synthase inhibitorNitric oxide synthesisNew therapeutic approachesNitric oxide productionSelective inhibitionDomainPeptidesCaveolinAcute inflammationCellsSystemic administration
1999
Codistribution of NOS and caveolin throughout peripheral vasculature and skeletal muscle of hamsters
Segal S, Brett S, Sessa W. Codistribution of NOS and caveolin throughout peripheral vasculature and skeletal muscle of hamsters. American Journal Of Physiology 1999, 277: h1167-h1177. PMID: 10484439, DOI: 10.1152/ajpheart.1999.277.3.h1167.Peer-Reviewed Original ResearchConceptsCaveolin-3Caveolin-1Skeletal muscleCaveolin isoformsCoat proteinCaveolinFunctional interactionIntact organismEnzyme isoformsNitric oxide synthase activitySmooth muscle cellsMuscle fibersOxide synthase activityVascular smooth muscleSynthase activitySkeletal muscle fibersMuscle cellsIsoformsCell systemSystemic vasculatureVena cavaFemoral arteryAbdominal aortaPeripheral vasculatureEndothelial cells
1997
Dissecting the Interaction between Nitric Oxide Synthase (NOS) and Caveolin FUNCTIONAL SIGNIFICANCE OF THE NOS CAVEOLIN BINDING DOMAININ VIVO *
Garcı́a-Cardeña G, Martasek P, Masters B, Skidd P, Couet J, Li S, Lisanti M, Sessa W. Dissecting the Interaction between Nitric Oxide Synthase (NOS) and Caveolin FUNCTIONAL SIGNIFICANCE OF THE NOS CAVEOLIN BINDING DOMAININ VIVO *. Journal Of Biological Chemistry 1997, 272: 25437-25440. PMID: 9325253, DOI: 10.1074/jbc.272.41.25437.Peer-Reviewed Original ResearchConceptsCaveolin-1Peripheral membrane proteinsInteraction of eNOSC-terminal tailAmino acids 310Direct interactionCo-transfection experimentsSite-directed mutagenesisNovel functional roleEndothelial nitric oxide synthaseMolecular chaperonesCytoplasmic domainCaveolin isoformsDeletion mutantsMammalian cellsEndothelial cell lysatesGlutathione S-transferaseMembrane proteinsCaveolin-2Coat proteinNegative regulationCaveolin-3Endothelial cellsDirect bindingGolgi region
1996
Endothelial Nitric Oxide Synthase Is Regulated by Tyrosine Phosphorylation and Interacts with Caveolin-1*
García-Cardeña G, Fan R, Stern D, Liu J, Sessa W. Endothelial Nitric Oxide Synthase Is Regulated by Tyrosine Phosphorylation and Interacts with Caveolin-1*. Journal Of Biological Chemistry 1996, 271: 27237-27240. PMID: 8910295, DOI: 10.1074/jbc.271.44.27237.Peer-Reviewed Original ResearchConceptsNovel regulatory mechanismTyrosine phosphorylationCaveolin-1Bovine aortic endothelial cellsRegulatory mechanismsProtein tyrosine phosphatase inhibitorCaveolin-interacting proteinsPhosphoamino acid analysisTyrosine phosphatase inhibitorTreatment of BAECBovine lung microvascular endothelial cellsEndothelial nitric oxide synthaseSubcellular traffickingPhosphatase inhibitorCoat proteinEndothelial cellsMetabolic labelingSodium orthovanadatePhosphorylationCaveolaeAortic endothelial cellsLung microvascular endothelial cellsProteinAcid analysisImmunoprecipitation