2023
Calreticulin Regulates SARS-CoV-2 Spike Protein Turnover and Modulates SARS-CoV-2 Infectivity
Rahimi N, White M, Amraei R, Lotfollahzadeh S, Xia C, Michalak M, Costello C, Mühlberger E. Calreticulin Regulates SARS-CoV-2 Spike Protein Turnover and Modulates SARS-CoV-2 Infectivity. Cells 2023, 12: 2694. PMID: 38067122, PMCID: PMC10705507, DOI: 10.3390/cells12232694.Peer-Reviewed Original ResearchMeSH KeywordsCalciumCalreticulinEndothelial CellsHumansPost-Acute COVID-19 SyndromeProlineSARS-CoV-2Spike Glycoprotein, CoronavirusConceptsSARS-CoV-2 infectivityCardiovascular complicationsS-RBDSARS-CoV-2 infectionEndothelial cellsMajor clinical hallmarksSpike proteinCOVID-19 patientsCoronavirus disease 2019SARS-CoV-2 spike proteinSARS-CoV-2S proteinProteasomal inhibitor bortezomibHuman endothelial cellsShRNA-mediated knockdownCalcium hemostasisClinical hallmarkDisease 2019Inhibitor bortezomibCalcium homeostasisAcidification of lysosomesRole of calreticulinTreatment of cellsProtein levelsComplications
2022
Extracellular vimentin is an attachment factor that facilitates SARS-CoV-2 entry into human endothelial cells
Amraei R, Xia C, Olejnik J, White M, Napoleon M, Lotfollahzadeh S, Hauser B, Schmidt A, Chitalia V, Mühlberger E, Costello C, Rahimi N. Extracellular vimentin is an attachment factor that facilitates SARS-CoV-2 entry into human endothelial cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2113874119. PMID: 35078919, PMCID: PMC8833221, DOI: 10.1073/pnas.2113874119.Peer-Reviewed Original ResearchConceptsSARS-CoV-2 infectionHuman endothelial cellsSARS-CoV-2 entrySARS-CoV-2S-protein interactionEndothelial cellsIdentification of vimentinShRNA-mediated knockdownIntermediate filament proteinsBinding of vimentinHEK-293 cellsAttachment factorsViral entrySARS-CoV-2 S proteinDevelopment of therapeuticsExtracellular vimentinS protein receptorInfectious SARS-CoV-2Host cellsCellular componentsCoexpression of vimentinFilament proteinsPrimary entry receptorSARS-CoV-2 spike proteinS protein
2019
The cell adhesion molecule IGPR-1 is activated by and regulates responses of endothelial cells to shear stress
Ho R, Tahboub R, Amraei R, Meyer R, Varongchayakul N, Grinstaff M, Rahimi N. The cell adhesion molecule IGPR-1 is activated by and regulates responses of endothelial cells to shear stress. Journal Of Biological Chemistry 2019, 294: 13671-13680. PMID: 31341021, PMCID: PMC6746441, DOI: 10.1074/jbc.ra119.008548.Peer-Reviewed Original ResearchConceptsIGPR-1Cell adhesion molecule IGPR-1Proline-rich receptor-1AKT Ser/ThrActin stress fiber assemblySer/ThrCell-cell junctionsStress fiber assemblyCell-cell contactEndothelial cellsActin fiber assemblyEndothelial cell remodelingFiber assemblyCell mechanosensingBlood flow-induced shear stressCell remodelingCellular responsesMechanical signalsVascular endothelial cellsImportant playersFlow-induced shear stressPhosphorylationCellsReceptor 1Cell borders