2023
Inactivation of Minar2 in mice hyperactivates mTOR signaling and results in obesity
Lotfollahzadeh S, Xia C, Amraei R, Hua N, Kandror K, Farmer S, Wei W, Costello C, Chitalia V, Rahimi N. Inactivation of Minar2 in mice hyperactivates mTOR signaling and results in obesity. Molecular Metabolism 2023, 73: 101744. PMID: 37245847, PMCID: PMC10267597, DOI: 10.1016/j.molmet.2023.101744.Peer-Reviewed Original ResearchConceptsMTOR activationHigh-fat dietObesity-associated diseasesGlucose toleranceKO miceChronic diseasesPathophysiological roleBody fatMetabolic disordersHypertrophic adipocytesKnockout miceObesityAdipose tissuePhysiological negative regulatorType 2HEK-293 cellsImpaired expressionComplex disorderCell culture studiesAdipocytesDiseaseMiceDisordersMTORUnknown role
2022
Central Gαi2 Protein Mediated Neuro-Hormonal Control of Blood Pressure and Salt Sensitivity
Amraei R, Moreira J, Wainford R. Central Gαi2 Protein Mediated Neuro-Hormonal Control of Blood Pressure and Salt Sensitivity. Frontiers In Endocrinology 2022, 13: 895466. PMID: 35837296, PMCID: PMC9275552, DOI: 10.3389/fendo.2022.895466.Peer-Reviewed Original ResearchConceptsDietary sodium intakeG protein-coupled receptorsParaventricular nucleusBlood pressureSodium intakeElectrolyte homeostasisCentral angiotensin II type 1 receptorsAcute isotonic volume expansionAngiotensin II type 1 receptorII type 1 receptorSalt sensitivityMajor public health issueAcute pharmacological activationAfferent renal nervesNeuro-hormonal responseSalt-sensitive animalsDevelopment of hypertensionSalt-resistant ratsIsotonic volume expansionHypothalamic paraventricular nucleusMultiple G protein-coupled receptorsType 1 receptorNeuro-hormonal controlGαi/oPublic health issue
2021
The cell adhesion molecule TMIGD1 binds to moesin and regulates tubulin acetylation and cell migration
Rahimi N, Ho R, Chandler K, De La Cena K, Amraei R, Mitchel A, Engblom N, Costello C. The cell adhesion molecule TMIGD1 binds to moesin and regulates tubulin acetylation and cell migration. Journal Of Biomedical Science 2021, 28: 61. PMID: 34503512, PMCID: PMC8427838, DOI: 10.1186/s12929-021-00757-z.Peer-Reviewed Original ResearchConceptsMitotic spindle organizationERM familyΑ-tubulinSpindle organizationCell migrationApical localizationN-terminal ERM domainCRISPR/Cas9-mediated knockoutMitotic spindle assemblyCell-cell adhesionCas9-mediated knockoutFilopodia-like protrusionsNovel tumor suppressorComplex functional interplayActin organizationERM domainLysine acetylationTMIGD1Spindle assemblyCarboxyl terminusFunctional interplayMoesinCell cycleTumor suppressorEzrin
2020
Transmembrane and Immunoglobulin Domain Containing 1, a Putative Tumor Suppressor, Induces G2/M Cell Cycle Checkpoint Arrest in Colon Cancer Cells
De La Cena K, Ho R, Amraei R, Woolf N, Tashjian J, Zhao Q, Richards S, Walker J, Huang J, Chitalia V, Rahimi N. Transmembrane and Immunoglobulin Domain Containing 1, a Putative Tumor Suppressor, Induces G2/M Cell Cycle Checkpoint Arrest in Colon Cancer Cells. American Journal Of Pathology 2020, 191: 157-167. PMID: 33129760, PMCID: PMC7788663, DOI: 10.1016/j.ajpath.2020.09.015.Peer-Reviewed Original ResearchConceptsCell cycleColorectal cancerCell cycle checkpoint arrestCell cycle inhibitor proteinsNovel tumor suppressor geneFull molecular mechanismsPutative tumor suppressorColon cancer cellsTumor suppressor geneG2/M phaseSporadic human colorectal cancerNormal intestinal epithelial cellsEpigenetic mechanismsCheckpoint arrestTMIGD1Inhibitor proteinNovel potential therapeutic targetIntestinal epithelial cellsMolecular mechanismsTumor suppressorPoor overall survivalSuppressor geneDevelopment of adenomasImmunoglobulin domainHuman colorectal cancerCell adhesion molecule IGPR-1 activates AMPK connecting cell adhesion to autophagy
Amraei R, Alwani T, Ho R, Aryan Z, Wang S, Rahimi N. Cell adhesion molecule IGPR-1 activates AMPK connecting cell adhesion to autophagy. Journal Of Biological Chemistry 2020, 295: 16691-16699. PMID: 32978258, PMCID: PMC7864065, DOI: 10.1074/jbc.ra120.014790.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAMP-Activated Protein KinasesAnimalsAutophagyAutophagy-Related Protein-1 HomologBeclin-1CD28 AntigensCell AdhesionHEK293 CellsHumansI-kappa B KinaseIntracellular Signaling Peptides and ProteinsLipopolysaccharidesMicroscopy, FluorescenceMicrotubule-Associated ProteinsPhosphorylationPrimatesRNA, Guide, KinetoplastidaSirolimusSubstrate SpecificityConceptsIGPR-1Cell adhesionCell adhesion molecule IGPR-1Proline-rich receptor-1Serine/threonine kinaseKey serine/threonine kinaseAmino acid starvationBeclin-1Phosphorylation of AMPThreonine kinaseAutophagy stimuliKinase assaysLC3-II levelsCellular stressNutrient deprivationProtein kinaseCell adhesion moleculeProtein ULK1IκB kinase βEndothelial barrier functionKinase βCellular assaysPhosphorylationSubsequent activationCell detachment
2019
c-Cbl targets PD-1 in immune cells for proteasomal degradation and modulates colorectal tumor growth
Lyle C, Richards S, Yasuda K, Napoleon M, Walker J, Arinze N, Belghasem M, Vellard I, Yin W, Ravid J, Zavaro E, Amraei R, Francis J, Phatak U, Rifkin I, Rahimi N, Chitalia V. c-Cbl targets PD-1 in immune cells for proteasomal degradation and modulates colorectal tumor growth. Scientific Reports 2019, 9: 20257. PMID: 31882749, PMCID: PMC6934810, DOI: 10.1038/s41598-019-56208-1.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCD8-Positive T-LymphocytesColorectal NeoplasmsGene Expression Regulation, NeoplasticHumansMacrophagesMice, KnockoutPhosphorylationProgrammed Cell Death 1 ReceptorProteasome Endopeptidase ComplexProto-Oncogene Proteins c-cblTumor BurdenTumor MicroenvironmentUbiquitinationUbiquitin-Protein LigasesConceptsPD-1Immune cellsTumor microenvironmentColorectal cancerCell death 1 proteinPD-1 regulationDeath 1 proteinImmune checkpoint receptorsColorectal tumor growthC-CblCasitas B lymphomaCRC xenograftsImmune checkpointsCheckpoint receptorsAutoimmune diseasesT lymphocytesTumor suppressive activitySuppressive activityTumor phagocytosisTumor growthFinger functionB lymphomaHigh expressionMiceXenografts