2012
Characterization of Lipid Droplet and Its Regulation by Caveolin‐1 in Endothelial Cells
Kuo A, Zhang X, Harrison K, Sessa W. Characterization of Lipid Droplet and Its Regulation by Caveolin‐1 in Endothelial Cells. The FASEB Journal 2012, 26: 597.1-597.1. DOI: 10.1096/fasebj.26.1_supplement.597.1.Peer-Reviewed Original ResearchDeficient endothelial cellsCav-1Lipid dropletsFatty acid uptakeLD formationCaveolin-1Putative hairpin structureSurface of LDsCav-1 null miceIntegral membrane proteinsCellular energy homeostasisPotential physiological functionsAcid uptakeEndothelial cellsLD homeostasisUnique organellesCaveolae microdomainsMembrane proteinsKey cell typesDiacylglycerol acyltransferasesNovel functionPlasma membraneBiological processesIntracellular regulationPhysiological functions
2007
Regulation of Caveolin‐2 Phosphorylation at Serines 23 and 36
Sowa G, Sessa W. Regulation of Caveolin‐2 Phosphorylation at Serines 23 and 36. The FASEB Journal 2007, 21: a1424-a1424. DOI: 10.1096/fasebj.21.6.a1424-b.Peer-Reviewed Original ResearchLipid rafts/caveolaeSerine 36 phosphorylationRafts/caveolaeSerine 23Cav-2Serine phosphorylationCav-1Phospho-specific antibodiesSubcellular fractionation dataSubcellular fractionation techniquesN-terminal serineEndothelial cellsCaveolar compartmentCaveolae assemblyLipid raftsSubcellular locationRegulated processSerine 36Caveolin-2Human endothelial cellsAdenoviral expressionIntracellular compartmentsPhosphorylationCaveolaeResidues 23
2001
Distinction between signaling mechanisms in lipid rafts vs. caveolae
Sowa G, Pypaert M, Sessa W. Distinction between signaling mechanisms in lipid rafts vs. caveolae. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 14072-14077. PMID: 11707586, PMCID: PMC61169, DOI: 10.1073/pnas.241409998.Peer-Reviewed Original ResearchConceptsCav-1Raft domainsLipid raftsCholesterol-rich lipid raft domainsLipid raft domainsCaveolae assemblyEndothelial nitric oxide synthaseCaveolae biogenesisAcylated proteinsSignal transductionSpatial regulationPlasma membraneNegative regulationCaveolin-1CaveolaeFirst clear exampleRaftsPhysical interactionProteinCellsRegulationENOS functionBiogenesisDomainClear example
2000
Reconstitution of an Endothelial Nitric-oxide Synthase (eNOS), hsp90, and Caveolin-1 Complex in Vitro EVIDENCE THAT hsp90 FACILITATES CALMODULIN STIMULATED DISPLACEMENT OF eNOS FROM CAVEOLIN-1*
Gratton J, Fontana J, O'Connor D, Garcı́a-Cardeña G, McCabe T, Sessa W. Reconstitution of an Endothelial Nitric-oxide Synthase (eNOS), hsp90, and Caveolin-1 Complex in Vitro EVIDENCE THAT hsp90 FACILITATES CALMODULIN STIMULATED DISPLACEMENT OF eNOS FROM CAVEOLIN-1*. Journal Of Biological Chemistry 2000, 275: 22268-22272. PMID: 10781589, DOI: 10.1074/jbc.m001644200.Peer-Reviewed Original ResearchConceptsEndothelial nitric oxide synthaseAssociation of eNOSNitric oxide synthaseLung microvascular endothelial cellsCaveolin-1Microvascular endothelial cellsENOS enzymatic activityAction of CaMBovine lung microvascular endothelial cellsENOS functionCalcium-activated calmodulinConcentration of CaMShock protein 90Addition of CaMEndothelial cellsVitro EvidenceCav-1Protein 90AssociationPresence of Hsp90