2018
hMENA isoforms impact NSCLC patient outcome through fibronectin/β1 integrin axis
Di Modugno F, Spada S, Palermo B, Visca P, Iapicca P, Di Carlo A, Antoniani B, Sperduti I, Di Benedetto A, Terrenato I, Mottolese M, Gandolfi F, Facciolo F, Chen EI, Schwartz MA, Santoni A, Bissell MJ, Nisticò P. hMENA isoforms impact NSCLC patient outcome through fibronectin/β1 integrin axis. Oncogene 2018, 37: 5605-5617. PMID: 29907768, PMCID: PMC6193944, DOI: 10.1038/s41388-018-0364-3.Peer-Reviewed Original ResearchConceptsCell lung cancer patientsNSCLC patient outcomeFavorable clinical outcomeLung cancer patientsMechanism of actionClinical outcomesCancer patientsStromal fibronectinClinical managementTranscription factor 1Patient outcomesPatient riskΒ1 integrin expressionIntegrin axisNuclear expressionIntegrin expressionCell invasivenessCancer cellsFibronectin productionExtracellular matrix componentsFactor 1G-actin/F-actin ratioΒ1 integrin activationΒ1 integrin ligandsHMena
2012
p21-Activated kinase 4 promotes prostate cancer progression through CREB
Park M, Lee H, Lee C, You S, Kim D, Park B, Kang M, Heo W, Shin E, Schwartz M, Kim E. p21-Activated kinase 4 promotes prostate cancer progression through CREB. Oncogene 2012, 32: 2475-2482. PMID: 22710715, DOI: 10.1038/onc.2012.255.Peer-Reviewed Original ResearchConceptsP21-activated kinase 4Prostate cancer progressionProstate cancerCancer progressionLNCaP-FGC cellsPromising therapeutic targetKinase 4Prostate cancer cellsDU145 prostate cancer cellsSpecific protein kinase A (PKA) inhibitorProtein kinase A (PKA) inhibitorElevation of cAMPNeuroendocrine differentiationNude miceTherapeutic targetActive PAK4Downstream effector pathwaysTumor progressionDecreased expressionTumor formationCancerCancer cellsPC-3ProgressionEffector pathways
2009
RalA-Exocyst Complex Regulates Integrin-Dependent Membrane Raft Exocytosis and Growth Signaling
Balasubramanian N, Meier JA, Scott DW, Norambuena A, White MA, Schwartz MA. RalA-Exocyst Complex Regulates Integrin-Dependent Membrane Raft Exocytosis and Growth Signaling. Current Biology 2009, 20: 75-79. PMID: 20005108, PMCID: PMC2822103, DOI: 10.1016/j.cub.2009.11.016.Peer-Reviewed Original ResearchConceptsPlasma membraneRecycling endosomesGrowth signalingActivation of Arf6Small GTPase RalACaveolin-dependent internalizationLipid raft microdomainsAnchorage-independent growthEffects of integrinsExocyst complexActive RalARaft microdomainsMembrane raftsRaft markersIntegrin signalingPancreatic cancer cellsRalAAnchorage dependenceAnchorage independenceCell growthSignalingCell detachmentCancer cellsEndosomesExocytosis
2002
Integrins regulate the apoptotic response to DNA damage through modulation of p53
Lewis JM, Truong TN, Schwartz MA. Integrins regulate the apoptotic response to DNA damage through modulation of p53. Proceedings Of The National Academy Of Sciences Of The United States Of America 2002, 99: 3627-3632. PMID: 11904424, PMCID: PMC122574, DOI: 10.1073/pnas.062698499.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodiesApoptosisCaspase 3CaspasesCell AdhesionCell SurvivalChromosome AberrationsCyclin-Dependent Kinase Inhibitor p16DNA DamageFibroblastsHumansIntegrinsMelanomaMiceMutationNuclear ProteinsOrgan SpecificityProto-Oncogene ProteinsProto-Oncogene Proteins c-mdm2Radiation, IonizingSarcomaTumor Cells, CulturedTumor Suppressor Protein p14ARFTumor Suppressor Protein p53ConceptsTumor cellsTherapy-resistant tumorsModulation of p53Susceptible tumor cellsDNA damageLevels of p53Low p53 levelsApoptosis of cellsTherapy resistanceAntiintegrin antibodiesCancer cellsP53 levelsSurvival of cellsP53Nonadherent cellsCell typesSurvivalApoptotic responseCellsP19 ARFApoptosisChromosomal instabilityFibroblastic cell typesDamageChemotherapy