Featured Publications
N-terminal syndecan-2 domain selectively enhances 6-O heparan sulfate chains sulfation and promotes VEGFA165-dependent neovascularization
Corti F, Wang Y, Rhodes JM, Atri D, Archer-Hartmann S, Zhang J, Zhuang ZW, Chen D, Wang T, Wang Z, Azadi P, Simons M. N-terminal syndecan-2 domain selectively enhances 6-O heparan sulfate chains sulfation and promotes VEGFA165-dependent neovascularization. Nature Communications 2019, 10: 1562. PMID: 30952866, PMCID: PMC6450910, DOI: 10.1038/s41467-019-09605-z.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsMiceNeovascularization, PhysiologicProtein DomainsRetinaSequence Analysis, ProteinSyndecan-2Syndecan-4Vascular Endothelial Growth Factor AVascular Endothelial Growth Factor Receptor-2Modulation of VEGF receptor 2 signaling by protein phosphatases
Corti F, Simons M. Modulation of VEGF receptor 2 signaling by protein phosphatases. Pharmacological Research 2016, 115: 107-123. PMID: 27888154, PMCID: PMC5205541, DOI: 10.1016/j.phrs.2016.11.022.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsHumansPhosphoprotein PhosphatasesPhosphorylationSignal TransductionVascular Endothelial Growth Factor AVascular Endothelial Growth Factor Receptor-2ConceptsProtein phosphatasePhosphorylation of serineVascular endothelial growth factor receptor 2 signalingSignal transduction cascadePrecise biological roleSpecific signaling pathwaysKinase biologyEukaryotic cellsSignal terminatorRegulatory subunitPositive regulatorTransduction cascadePhosphorylation stateBiological roleContext of cancerParticular proteinDifferent proteinsGenome sequencingSignaling pathwaysVEGF receptor 2Receptor 2 signalingVEGF signalsProteinPhosphataseGenetic modelsSyndecan 4 is required for endothelial alignment in flow and atheroprotective signaling
Baeyens N, Mulligan-Kehoe MJ, Corti F, Simon DD, Ross TD, Rhodes JM, Wang TZ, Mejean CO, Simons M, Humphrey J, Schwartz MA. Syndecan 4 is required for endothelial alignment in flow and atheroprotective signaling. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: 17308-17313. PMID: 25404299, PMCID: PMC4260558, DOI: 10.1073/pnas.1413725111.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAtherosclerosisBlotting, WesternCells, CulturedEndothelial CellsFemaleHuman Umbilical Vein Endothelial CellsHumansKruppel-Like Factor 4Kruppel-Like Transcription FactorsMaleMice, Inbred C57BLMice, KnockoutMicroscopy, ConfocalNF-kappa BReverse Transcriptase Polymerase Chain ReactionRNA InterferenceSignal TransductionStress, MechanicalSyndecan-4Vascular Endothelial Growth Factor Receptor-2ConceptsHuman umbilical vein endothelial cellsNF-κBProinflammatory NF-κBAtherosclerotic plaque burdenKruppel-like factor 2Umbilical vein endothelial cellsVEGF receptor 2Appearance of plaquesVein endothelial cellsHypercholesterolemic micePlaque burdenAntiinflammatory pathwayThoracic aortaReceptor 2Endothelial cellsEndothelial alignmentFlow correlatesCausal roleAtherosclerosisFactor 2MiceCyclic stretchLocalization correlatesActivationSyndecan-4
2018
Peptides derived from the histidine–proline rich glycoprotein bind copper ions and exhibit anti-angiogenic properties
Magrì A, Grasso G, Corti F, Finetti F, Greco V, Santoro AM, Sciuto S, La Mendola D, Morbidelli L, Rizzarelli E. Peptides derived from the histidine–proline rich glycoprotein bind copper ions and exhibit anti-angiogenic properties. Dalton Transactions 2018, 47: 9492-9503. PMID: 29963662, DOI: 10.1039/c8dt01560k.Peer-Reviewed Original ResearchMeSH KeywordsAngiogenesis InhibitorsAnimalsCell MovementCells, CulturedCopperEndothelial CellsExtracellular Signal-Regulated MAP KinasesHumansNeovascularization, PhysiologicPeptidesProteinsSwineVascular Endothelial Growth Factor Receptor-2ConceptsElectron paramagnetic resonanceCircular dichroismSpray ionization mass spectrometryPotential drug delivery systemElectron spray ionization mass spectrometryMeans of potentiometryIonization mass spectrometryDrug delivery systemsAmidic bondCopper ionsRole of copperParamagnetic resonanceMass spectrometryComplex speciesTrehalose derivativesProdrug systemEnzymatic degradationDelivery systemCopperPeptidesPotentiometryBondsUVSpectrometryDichroismThe Rab-effector protein RABEP2 regulates endosomal trafficking to mediate vascular endothelial growth factor receptor-2 (VEGFR2)-dependent signaling
Kofler N, Corti F, Rivera-Molina F, Deng Y, Toomre D, Simons M. The Rab-effector protein RABEP2 regulates endosomal trafficking to mediate vascular endothelial growth factor receptor-2 (VEGFR2)-dependent signaling. Journal Of Biological Chemistry 2018, 293: 4805-4817. PMID: 29425100, PMCID: PMC5880142, DOI: 10.1074/jbc.m117.812172.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsEndosomesEndothelial CellsMiceMice, Inbred BALB CProtein TransportProtein Tyrosine Phosphatase, Non-Receptor Type 1Rab GTP-Binding ProteinsRab4 GTP-Binding ProteinsRab7 GTP-Binding ProteinsSignal TransductionVascular Endothelial Growth Factor Receptor-2Vesicular Transport ProteinsConceptsEndosomal traffickingVascular endothelial growth factor receptor 2Phosphotyrosine phosphatase 1BVEGFR2 traffickingEndothelial growth factor receptor 2Small GTPase Rab4Rab effector proteinsEndothelial cell functionRab7-positive endosomesCell functionRab GTPaseSorting endosomesCell surface expressionMaster regulatorEndosomal compartmentsVEGFR2 degradationPhosphatase 1BRABEP2Dependent signalingVascular developmentVEGFR2 signalingHigh-resolution microscopyTraffickingEndosomesBiochemical assays