2020
Endothelial cell–glucocorticoid receptor interactions and regulation of Wnt signaling
Zhou H, Mehta S, Srivastava SP, Grabinska K, Zhang X, Wong C, Hedayat A, Perrotta P, Fernández-Hernando C, Sessa WC, Goodwin JE. Endothelial cell–glucocorticoid receptor interactions and regulation of Wnt signaling. JCI Insight 2020, 5: e131384. PMID: 32051336, PMCID: PMC7098785, DOI: 10.1172/jci.insight.131384.Peer-Reviewed Original ResearchConceptsEndothelial glucocorticoid receptorVascular inflammationGlucocorticoid receptorGlucocorticoid receptor regulationGlucocorticoid receptor resultsUpregulation of WntEndogenous glucocorticoidsExogenous glucocorticoidsGlucocorticoid response elementCardiovascular diseaseMouse endothelial cellsMouse modelEndothelial WNTInflammationReceptor regulationEndothelial cellsReceptors resultsNext-generation sequencingReceptor interactionReceptorsRegulation of WntWnt pathwayGlucocorticoidsRecent dataWnt
2016
NgBR is essential for endothelial cell glycosylation and vascular development
Park EJ, Grabińska K, Guan Z, Sessa WC. NgBR is essential for endothelial cell glycosylation and vascular development. EMBO Reports 2016, 17: 167-177. PMID: 26755743, PMCID: PMC5290814, DOI: 10.15252/embr.201540789.Peer-Reviewed Original ResearchConceptsVascular developmentCis-prenyltransferase activityEmbryonic lethalityKnockout embryosProtein glycosylationTransmembrane proteinDefective glycosylationCell glycosylationEndothelial cellsDevelopment defectsKnockout resultsNgBRDolichol phosphateVE-cadherinGlycosylationYolk sacProteinEndothelial proteinsCellsIntegrated roleEmbryogenesisSubunitsEmbryosApoptosisEnd products
2014
Mutation of Nogo-B Receptor, a Subunit of cis-Prenyltransferase, Causes a Congenital Disorder of Glycosylation
Park EJ, Grabińska K, Guan Z, Stránecký V, Hartmannová H, Hodaňová K, Barešová V, Sovová J, Jozsef L, Ondrušková N, Hansíková H, Honzík T, Zeman J, Hůlková H, Wen R, Kmoch S, Sessa WC. Mutation of Nogo-B Receptor, a Subunit of cis-Prenyltransferase, Causes a Congenital Disorder of Glycosylation. Cell Metabolism 2014, 20: 448-457. PMID: 25066056, PMCID: PMC4161961, DOI: 10.1016/j.cmet.2014.06.016.Peer-Reviewed Original ResearchConceptsProtein glycosylationCis-prenyltransferaseGPI anchor biosynthesisDolichol synthesisSynthesis of dolicholO-mannosylationAnchor biosynthesisFirst enzymeGenetic basisC-terminusCongenital disorderFunction mutationsGlycosylationEssential roleEnhanced accumulationMutationsYeastNgBRSubunitsDolicholFibroblastsBiosynthesisTerminusFree cholesterolProtein