2022
Multi-Scalar Data Integration Links Glomerular Angiopoietin-Tie Signaling Pathway Activation With Progression of Diabetic Kidney Disease
Liu J, Nair V, Zhao Y, Chang D, Limonte C, Bansal N, Fermin D, Eichinger F, Tanner E, Bellovich K, Steigerwalt S, Bhat Z, Hawkins J, Subramanian L, Rosas S, Sedor J, Vasquez M, Waikar S, Bitzer M, Pennathur S, Brosius F, De Boer I, Chen M, Kretzler M, Ju W, Group F, Knight R, Lecker S, Stillman I, Bogen S, Amodu A, Ilori T, Maikhor S, Schmidt I, Beck L, Henderson J, Onul I, Verma A, Waikar S, McMahon G, Valerius M, Waikar S, Weins A, Colona M, Greka A, Hacohen N, Hoover P, Marshall J, Aulisio M, Chen Y, Janowczyk A, Jayapandian C, Viswanathan V, Bush W, Crawford D, Madabhushi A, Bush L, Cooperman L, Gonzalez-Vicente A, Herlitz L, Jolly S, Nguyen J, O’toole J, Palmer E, Poggio E, Sedor J, Sendrey D, Spates-Harden K, Taliercio J, Bjornstad P, Pyle L, Vinovskis C, Appelbaum P, Barasch J, Bomback A, Canetta P, D’Agati V, Kiryluk K, Kudose S, Mehl K, Shang N, Balderes O, Bansal S, Alexandrov T, Rennke H, El-Achkar T, Barwinska D, Bledsoe S, Borner K, Bueckle A, Cheng Y, Dagher P, Dunn K, Eadon M, Ferkowicz M, Herr B, Kelly K, Ferreira R, Quardokus E, Record E, Rivera M, Su J, Sutton T, Williams J, Winfree S, Menez S, Parikh C, Rosenberg A, Corona-Villalobos C, Wen Y, Johansen C, Rosas S, Roy N, Sun J, Williams M, Azeloglu E, Hansen J, He C, Iyengar R, Xiong Y, Prasad P, Srivastava A, Madhavan S, Parikh S, Rovin B, Shapiro J, Anderton C, Lukowski J, Pasa-Tolic L, Velickovic D, Oliver G, Ardayfio J, Bebiak J, Brown K, Campbell T, Campbell C, Hayashi L, Jefferson N, Roberts G, Saul J, Shpigel A, Stutzke C, Koewler R, Pinkeney R, Sealfon R, Troyanskaya O, Wong A, Tuttle K, Pollack A, Goltsev Y, Lucarelli N, Sarder P, Lake B, Zhang K, Boada P, Laszik Z, Nolan G, Anjani K, Sarwal M, Mukatash T, Sigdel T, Alloway R, Burg A, Lee P, Rike A, Shi T, Woodle E, Balis U, Blanc V, Conser N, Eddy S, Frey R, He Y, Hodgin J, Kretzler M, Lienczewski C, Luo J, Mariani L, Menon R, Otto E, Schaub J, Steck B, Elder M, Gilliam M, Hall D, Murugan R, Palevsky P, Randhawa P, Rosengart M, Tublin M, Vita T, Kellum J, Winters J, Alpers C, Berglund A, Blank K, Carson J, Daniel S, De Boer I, Dighe A, Dowd F, Grewenow S, Himmelfarb J, Hoofnagle A, Limonte C, McClelland R, Mooney S, Rezaei K, Shankland S, Snyder J, Wang R, Wilcox A, Williams K, Park C, Bansal S, Montellano R, Pamreddy A, Sharma K, Venkatachalam M, Ye H, Zhang G, Hedayati S, Kermani A, Lee S, Lu C, Miller R, Moe O, Patel J, Pillai A, Sambandam K, Torrealba J, Toto R, Vazquez M, Wang N, Wen N, Zhang D, Park H, Caprioli R, Patterson N, Sharman K, Spraggins J, Van de Plas R, Basta J, Diettman S, Gaut J, Jain S, Rauchman M, Vijayan A, Cantley L, Kakade V, Moledina D, Shaw M, Ugwuowo U, Wilson F, Arora T, Bitzer M, Brosius F, Gadegbeku C, Gipson D, Hawkins J, Kretzler M, Lienczewski C, Pennathur S, Troost J, Gadegbeku C, Bellovich K, Bhat Z, Massengill S, Perumal K. Multi-Scalar Data Integration Links Glomerular Angiopoietin-Tie Signaling Pathway Activation With Progression of Diabetic Kidney Disease. Diabetes 2022, 71: 2664-2676. PMID: 36331122, PMCID: PMC9750948, DOI: 10.2337/db22-0169.Peer-Reviewed Original ResearchConceptsEnd-stage kidney diseaseDiabetic kidney diseaseKidney diseaseAngiopoietin-2ANGPT2 levelsChinese cohort studyChronic kidney diseaseGlomerular filtration rateCardiovascular Health StudyPlasma angiopoietin-2High receptor expressionStandard clinical parametersSignaling Pathway ActivationPathway scoresThree-marker panelKidney outcomesCohort studyComposite outcomeClinical parametersEndothelial biomarkersFiltration rateReceptor expressionPrognostic biomarkerClinical phenotypingHealth Study
2014
GM-CSF Promotes Macrophage Alternative Activation after Renal Ischemia/Reperfusion Injury
Huen SC, Huynh L, Marlier A, Lee Y, Moeckel GW, Cantley LG. GM-CSF Promotes Macrophage Alternative Activation after Renal Ischemia/Reperfusion Injury. Journal Of The American Society Of Nephrology 2014, 26: 1334-1345. PMID: 25388222, PMCID: PMC4446881, DOI: 10.1681/asn.2014060612.Peer-Reviewed Original ResearchMeSH KeywordsAcute Kidney InjuryAnalysis of VarianceAnimalsBlotting, WesternCell ProliferationCells, CulturedDisease Models, AnimalGene Expression RegulationGranulocyte-Macrophage Colony-Stimulating FactorImmunohistochemistryKidney Tubules, ProximalMacrophage ActivationMaleMiceMice, Inbred C57BLMultivariate AnalysisPhenotypeRandom AllocationReal-Time Polymerase Chain ReactionReperfusion InjurySignal TransductionUp-RegulationConceptsIschemia/reperfusion injuryMacrophage alternative activationBone marrow-derived macrophagesAlternative activationMarrow-derived macrophagesTubular cellsGM-CSFReperfusion injuryReparative phenotypeTubular proliferationKidney ischemia/reperfusion injuryRenal ischemia/reperfusion injuryMouse proximal tubule cellsInitial kidney damageRepair phaseProximal tubule cellsTubular factorsIschemic injuryKidney damageProinflammatory macrophagesRenal repairMacrophage activationTubule cellsPharmacologic inhibitionMacrophages
2013
Met Activation Is Required for Early Cytoprotection after Ischemic Kidney Injury
Mason S, Hader C, Marlier A, Moeckel G, Cantley LG. Met Activation Is Required for Early Cytoprotection after Ischemic Kidney Injury. Journal Of The American Society Of Nephrology 2013, 25: 329-337. PMID: 24136921, PMCID: PMC3904569, DOI: 10.1681/asn.2013050473.Peer-Reviewed Original ResearchMeSH KeywordsAcute Kidney InjuryAnimalsApoptosisBcl-Associated Death ProteinGene Knockdown TechniquesKidneyKidney Tubules, ProximalMAP Kinase Signaling SystemMiceMice, Inbred C57BLMice, KnockoutOrgan SpecificityPhosphatidylinositol 3-KinasesPhosphorylationProtein Processing, Post-TranslationalProto-Oncogene Proteins c-aktReceptor Protein-Tyrosine KinasesReperfusion InjuryRibosomal Protein S6 Kinases, 70-kDaSignal TransductionConceptsIschemia/reperfusionKidney injuryIschemic injuryProximal tubulesInitial tubular injuryMET receptor expressionProximal tubule responseTubular cell survivalIschemic kidney injuryProximal tubule epithelial cellsRenal proximal tubule epithelial cellsTubular cell proliferationTubular cell apoptosisPI3K/Akt activationProapoptotic factor BadTubule epithelial cellsCell survivalTubule responseSerum creatinineTubular injuryKidney repairLiver abnormalitiesReceptor expressionInjuryMET activationChitinase-Like Protein Brp-39/YKL-40 Modulates the Renal Response to Ischemic Injury and Predicts Delayed Allograft Function
Schmidt IM, Hall IE, Kale S, Lee S, He CH, Lee Y, Chupp GL, Moeckel GW, Lee CG, Elias JA, Parikh CR, Cantley LG. Chitinase-Like Protein Brp-39/YKL-40 Modulates the Renal Response to Ischemic Injury and Predicts Delayed Allograft Function. Journal Of The American Society Of Nephrology 2013, 24: 309-319. PMID: 23291472, PMCID: PMC3559482, DOI: 10.1681/asn.2012060579.Peer-Reviewed Original ResearchMeSH KeywordsAdipokinesAnimalsApoptosisBiomarkersCells, CulturedChitinase-3-Like Protein 1Delayed Graft FunctionDisease Models, AnimalEpithelial CellsGlycoproteinsHumansKidneyKidney TransplantationLectinsMacrophagesMaleMiceMice, Inbred C57BLPhosphatidylinositol 3-KinasesPredictive Value of TestsProto-Oncogene Proteins c-aktReperfusion InjurySignal TransductionTransplantation, HomologousConceptsBRP-39/YKLGraft functionKidney injuryYKL-40Reparative responseDeceased donor kidney transplantationKidney ischemia/reperfusionHours of transplantImmediate graft functionDelayed graft functionTubular cell deathIschemia/reperfusionDegree of injuryAllograft functionCell apoptotic deathKidney hypoperfusionKidney transplantationSystemic hypotensionRenal failureIschemic injuryRenal ischemiaRenal responseUrinary levelsBRP-39Activation of Akt
1999
Activated ERK2 Interacts with and Phosphorylates the Docking Protein GAB1*
Roshan B, Kjelsberg C, Spokes K, Eldred A, Crovello C, Cantley L. Activated ERK2 Interacts with and Phosphorylates the Docking Protein GAB1*. Journal Of Biological Chemistry 1999, 274: 36362-36368. PMID: 10593929, DOI: 10.1074/jbc.274.51.36362.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell LineDogsEnzyme ActivationMitogen-Activated Protein Kinase 1PhosphoproteinsPhosphorylationSignal TransductionSubstrate Specificity
1998
Phosphoinositide 3-Kinase Regulates Phospholipase Cγ-mediated Calcium Signaling*
Rameh L, Rhee S, Spokes K, Kazlauskas A, Cantley L, Cantley L. Phosphoinositide 3-Kinase Regulates Phospholipase Cγ-mediated Calcium Signaling*. Journal Of Biological Chemistry 1998, 273: 23750-23757. PMID: 9726983, DOI: 10.1074/jbc.273.37.23750.Peer-Reviewed Original ResearchMeSH KeywordsAndrostadienesBinding SitesCalciumChromonesEnzyme InhibitorsHumansIsoenzymesKineticsMorpholinesPhosphatidylinositol 3-KinasesPhosphatidylinositol PhosphatesPhospholipase C gammaPlatelet-Derived Growth FactorReceptors, Platelet-Derived Growth FactorRecombinant Fusion ProteinsSignal TransductionTransfectionTumor Cells, CulturedType C PhospholipasesWortmanninConceptsPlatelet-derived growth factor receptorIntracellular calcium releaseCalcium releasePI3KGrowth factor receptorIntracellular calciumIP3 generationInositol trisphosphate generationIP3 productionFactor receptorVivo relevanceCalcium signalingTrisphosphate generationHepG2 cellsSelective activationAddition of wortmanninPhospholipase CγActivation of Phospholipase C-γ by Phosphatidylinositol 3,4,5-Trisphosphate*
Bae Y, Cantley L, Chen C, Kim S, Kwon K, Rhee S. Activation of Phospholipase C-γ by Phosphatidylinositol 3,4,5-Trisphosphate*. Journal Of Biological Chemistry 1998, 273: 4465-4469. PMID: 9468499, DOI: 10.1074/jbc.273.8.4465.Peer-Reviewed Original ResearchConceptsPLC-gamma isozymesPhospholipase CSrc homology 2 domainNIH 3T3 cellsCOS-7 cellsSpecific phospholipase CPLC gamma tyrosine phosphorylationAction of PISignal transductionCatalytic subunitTyrosine phosphorylationSpecific PIInhibitor LY294002PLC activationCell membranePhosphatidylinositolInositol phosphate formationIsozymesActivationCellsTransductionPIPhosphorylationSubunitsBisphosphate
1997
The Lipid Products of Phosphoinositide 3-Kinase Increase Cell Motility through Protein Kinase C*
Derman M, Toker A, Hartwig J, Spokes K, Falck JR, Chen C, Cantley L, Cantley L. The Lipid Products of Phosphoinositide 3-Kinase Increase Cell Motility through Protein Kinase C*. Journal Of Biological Chemistry 1997, 272: 6465-6470. PMID: 9045671, DOI: 10.1074/jbc.272.10.6465.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAndrostadienesAnimalsCell MembraneCell MovementDown-RegulationEnzyme ActivationEnzyme InhibitorsMiceNaphthalenesPhosphatidylinositol 3-KinasesPhosphatidylinositol PhosphatesPhosphotransferases (Alcohol Group Acceptor)Platelet-Derived Growth FactorProtein Kinase CSignal TransductionWortmanninConceptsProtein kinase CCell motilityLipid productsKinase CPKC family membersNIH 3T3 cellsIndependent PKC isoformsMembrane rufflingActin reorganizationCellular motilityPKC isoformsPtdInsVivo rolePhosphoinositideMotilityFirst demonstrationRecent studiesFamily membersComplete inhibitionCellsRufflingPhosphatidylinositolPrevious observationsIsoformsTrisphosphate