2014
Markers of Epithelial to Mesenchymal Transition in Association with Survival in Head and Neck Squamous Cell Carcinoma (HNSCC)
Pectasides E, Rampias T, Sasaki C, Perisanidis C, Kouloulias V, Burtness B, Zaramboukas T, Rimm D, Fountzilas G, Psyrri A. Markers of Epithelial to Mesenchymal Transition in Association with Survival in Head and Neck Squamous Cell Carcinoma (HNSCC). PLOS ONE 2014, 9: e94273. PMID: 24722213, PMCID: PMC3983114, DOI: 10.1371/journal.pone.0094273.Peer-Reviewed Original ResearchMeSH KeywordsAutomationBiomarkers, TumorCarcinoma, Squamous CellCohort StudiesEpithelial-Mesenchymal TransitionFemaleGene Expression ProfilingGene Expression Regulation, NeoplasticHead and Neck NeoplasmsHumansImage Processing, Computer-AssistedImmunohistochemistryKaplan-Meier EstimateMaleMultivariate AnalysisNeoplasm MetastasisPhenotypePrognosisProportional Hazards ModelsSquamous Cell Carcinoma of Head and NeckTreatment OutcomeConceptsProgression-free survivalSquamous cell carcinomaOverall survivalCell carcinomaE-cadherinPrimary squamous cell carcinomaNeck squamous cell carcinomaHigh-risk HNSCCKaplan-Meier analysisNovel therapeutic approachesMesenchymal transition phenotypeHigh metastatic potentialLow E-cadherinImproved OSInferior OSIndependent predictorsPoor prognosisCarcinoma prognosisClinicopathological parametersInclusion criteriaTherapeutic approachesTransition phenotypeMetastatic potentialMesenchymal transitionProtein expression analysis
2011
A Pathway for the Control of Anoikis Sensitivity by E-Cadherin and Epithelial-to-Mesenchymal Transition
Kumar S, Park SH, Cieply B, Schupp J, Killiam E, Zhang F, Rimm DL, Frisch SM. A Pathway for the Control of Anoikis Sensitivity by E-Cadherin and Epithelial-to-Mesenchymal Transition. Molecular And Cellular Biology 2011, 31: 4036-4051. PMID: 21746881, PMCID: PMC3187352, DOI: 10.1128/mcb.01342-10.Peer-Reviewed Original ResearchConceptsRegulation of anoikisE-cadherin complexMesenchymal transitionE-cadherinAnoikis sensitivityNuclear localizationInappropriate matrixAnoikis resistanceApoptotic responseOncogenic EMTAnoikisNRAGECellular sensitivityNovel pathwayUnknown mechanismAnkyrinEpithelial cellsEMTPathwayP14ARFCellsTbx2ComplexesGenesCytoplasm
2008
Prognostic Significance of Cadherin-Based Adhesion Molecules in Cutaneous Malignant Melanoma
Kreizenbeck GM, Berger AJ, Subtil A, Rimm DL, Rothberg BE. Prognostic Significance of Cadherin-Based Adhesion Molecules in Cutaneous Malignant Melanoma. Cancer Epidemiology Biomarkers & Prevention 2008, 17: 949-958. PMID: 18398036, PMCID: PMC3312613, DOI: 10.1158/1055-9965.epi-07-2729.Peer-Reviewed Original Research
2007
Definition of a direct extracellular interaction between Met and E‐cadherin
Reshetnikova G, Troyanovsky S, Rimm DL. Definition of a direct extracellular interaction between Met and E‐cadherin. Cell Biology International 2007, 31: 366-373. PMID: 17336101, DOI: 10.1016/j.cellbi.2007.01.022.Peer-Reviewed Original ResearchConceptsBT-549 cellsE-cadherinCadherin-dependent cell-cell contactsHT-29 cellsE-cadherin interactsHepatocyte growth factorCell-cell adhesionCell-cell contactCross-linking studiesDirect extracellular interactionTyrosine kinase receptor expressionExtracellular interactionsMolecular mechanismsExtracellular domainIntracellular compartmentsPhysical interactionCellular presentationFirst evidenceGrowth factorCellsBT-549HT-29ExpressionReceptor expressionMetS
2006
Reciprocal regulation of RhoA and RhoC characterizes the EMT and identifies RhoC as a prognostic marker of colon carcinoma
Bellovin DI, Simpson KJ, Danilov T, Maynard E, Rimm DL, Oettgen P, Mercurio AM. Reciprocal regulation of RhoA and RhoC characterizes the EMT and identifies RhoC as a prognostic marker of colon carcinoma. Oncogene 2006, 25: 6959-6967. PMID: 16715134, DOI: 10.1038/sj.onc.1209682.Peer-Reviewed Original ResearchMeSH KeywordsBiomarkers, TumorCadherinsCell Line, TumorColonic NeoplasmsEnzyme ActivationEpithelial CellsHumansImmunohistochemistryImmunoprecipitationNeoplasm InvasivenessPrognosisPromoter Regions, GeneticProto-Oncogene Protein c-ets-1Reverse Transcriptase Polymerase Chain ReactionRho GTP-Binding ProteinsRhoA GTP-Binding ProteinRhoC GTP-Binding ProteinRNA, Small InterferingTranscription, GeneticConceptsColon carcinomaRhoC expressionPrognostic markerRhoC protein expressionE-cadherinET-1 binding sitesClinical outcomesPoor outcomeColon cancer cellsColorectal tumorsET-1Colon cancerUse of shRNAMesenchymal transitionExpression correlatesCarcinomaAberrant expressionHigh expressionProtein expressionCancer cellsMesenchymal characteristicsEMTSubsequent activationReciprocal regulationCell migration
2005
Altered Localization of p120 Catenin During Epithelial to Mesenchymal Transition of Colon Carcinoma Is Prognostic for Aggressive Disease
Bellovin DI, Bates RC, Muzikansky A, Rimm DL, Mercurio AM. Altered Localization of p120 Catenin During Epithelial to Mesenchymal Transition of Colon Carcinoma Is Prognostic for Aggressive Disease. Cancer Research 2005, 65: 10938-10945. PMID: 16322241, DOI: 10.1158/0008-5472.can-05-1947.Peer-Reviewed Original ResearchConceptsSurvival timeMesenchymal transitionLymph node metastasisColorectal cancer progressionPoor patient outcomesE-cadherinLate-stage tumorsPatient survival timePost-EMT cellsP120ctn expressionAltered localizationLymph nodesNode metastasisAggressive diseaseTumor stagePrimary tumorTumor necrosisColorectal carcinomaPatient outcomesColon carcinoma cellsE-cadherin lossCytoplasmic stainingColon carcinomaCancer progressionCarcinoma cells
2000
α-Catenin Binds Directly to Spectrin and Facilitates Spectrin-Membrane Assembly in Vivo *
Pradhan D, Lombardo C, Roe S, Rimm D, Morrow J. α-Catenin Binds Directly to Spectrin and Facilitates Spectrin-Membrane Assembly in Vivo *. Journal Of Biological Chemistry 2000, 276: 4175-4181. PMID: 11069925, DOI: 10.1074/jbc.m009259200.Peer-Reviewed Original ResearchConceptsInteraction of spectrinClone A cellsΑ-catenin bindsAmino-terminal domainAmino acid regionSpectrin-actin skeletonCell-cell contactCell adhesion processesMadin-Darby canine kidneyAdhesion complexesConfluent Madin Darby canine kidneyCytoskeletal assemblyPlasma membraneDetergent solubilityMembrane assemblyAcid regionSpectrin skeletonMembrane regionsA cellsVivo roleSpectrinPhospholipid interactionsBiological membranesE-cadherinMolecular interactions
1998
Loss of p120ctn in human colorectal cancer predicts metastasis and poor survival
Gold J, Reynolds A, Rimm D. Loss of p120ctn in human colorectal cancer predicts metastasis and poor survival. Cancer Letters 1998, 132: 193-201. PMID: 10397474, DOI: 10.1016/s0304-3835(98)00190-6.Peer-Reviewed Original ResearchConceptsColorectal cancerPrimary human colorectal adenocarcinomasHigher stage diseasePoor clinical outcomeHuman colorectal cancerHuman colorectal adenocarcinomaStage diseaseClinical outcomesNodal metastasisColorectal adenocarcinomaPoor survivalColorectal tumorsColon cancerImmunohistochemical methodsMetastasisReduced expressionCancerE-cadherinP120ctn expressionLoss of p120ctnFamily membersSurvivalPreliminary studyExpressionComplete lossDynamic Interaction of PTPμ with Multiple Cadherins In Vivo
Brady-Kalnay S, Mourton T, Nixon J, Pietz G, Kinch M, Chen H, Brackenbury R, Rimm D, Del Vecchio R, Tonks N. Dynamic Interaction of PTPμ with Multiple Cadherins In Vivo. Journal Of Cell Biology 1998, 141: 287-296. PMID: 9531566, PMCID: PMC2132733, DOI: 10.1083/jcb.141.1.287.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, MonoclonalCadherinsCell LineCell Line, TransformedCerebellumCross ReactionsElectrophoresis, Polyacrylamide GelHumansImmunoblottingMiceProtein Tyrosine PhosphatasesRatsReceptor-Like Protein Tyrosine Phosphatases, Class 2Receptor-Like Protein Tyrosine Phosphatases, Class 8Recombinant Fusion ProteinsRecombinant ProteinsSpodopteraTransfectionConceptsReversible tyrosine phosphorylationCadherin-catenin complexTyrosine phosphorylationE-cadherinWC5 cellsTemperature-sensitive mutant formPresence of cadherinCadherin functionV-SrcCytoplasmic segmentMultiple cadherinsCadherin-4PTPmuSf9 cellsMutant formsRegulatory mechanismsAdhesive functionCadherinN-cadherinPhosphorylationDirect interactionThe expression of p120ctn protein in breast cancer is independent of alpha- and beta-catenin and E-cadherin.
Dillon DA, D'Aquila T, Reynolds AB, Fearon ER, Rimm DL. The expression of p120ctn protein in breast cancer is independent of alpha- and beta-catenin and E-cadherin. American Journal Of Pathology 1998, 152: 75-82. PMID: 9422525, PMCID: PMC1858125.Peer-Reviewed Original Research
1997
Vinculin Is Associated with the E-cadherin Adhesion Complex*
Hazan R, Kang L, Roe S, Borgen P, Rimm D. Vinculin Is Associated with the E-cadherin Adhesion Complex*. Journal Of Biological Chemistry 1997, 272: 32448-32453. PMID: 9405455, DOI: 10.1074/jbc.272.51.32448.Peer-Reviewed Original ResearchConceptsE-cadherin complexAdhesion complexesMDA-MB-468 cellsCalcium-dependent cell-cell adhesionE-cadherin adhesion complexAlpha-catenin geneCadherin-dependent adhesionCell-cell adhesionCell adhesion complexesE-cadherinCell linesAlpha-catenin expressionAlpha cateninReciprocal immunoprecipitationCytoplasmic interactionsCoprecipitation analysisAnti-vinculin antibodiesVinculinCadherinCytoplasmic connectionsFusion proteinE-cadherin expressionSame binding siteMDA-MB-468 breast cancer cell lineCell lysatesTranscriptional defects underlie loss of E-cadherin expression in breast cancer.
Ji X, Woodard AS, Rimm DL, Fearon ER. Transcriptional defects underlie loss of E-cadherin expression in breast cancer. Molecular Cancer Research 1997, 8: 773-8. PMID: 9218871.Peer-Reviewed Original ResearchMeSH KeywordsAntimetabolites, AntineoplasticAzacitidineBreast NeoplasmsCadherinsCloning, MolecularDecitabineDNA MethylationDNA-Binding ProteinsGene Expression Regulation, NeoplasticHumansPromoter Regions, GeneticTrans-ActivatorsTranscription Factor AP-2Transcription FactorsTranscription, GeneticTumor Cells, CulturedConceptsE-cad expressionBreast cancerEpithelial cancersHuman breast cancer cell linesMost breast cancersDifferent epithelial cancersBreast cancer cell linesMajority of cancersE-cadherin expressionCancer cell linesCell adhesion moleculeProgression eventsCancerAdhesion moleculesTumor heterogeneityE-cadherinFunctional assaysCell linesSomatic mutationsE-cad geneGene expression differencesExpressionPromoter activityGene expressionReporter gene constructs
1996
Expression of a candidate cadherin in T lymphocytes.
Cepek KL, Rimm DL, Brenner MB. Expression of a candidate cadherin in T lymphocytes. Proceedings Of The National Academy Of Sciences Of The United States Of America 1996, 93: 6567-6571. PMID: 8692857, PMCID: PMC39065, DOI: 10.1073/pnas.93.13.6567.Peer-Reviewed Original ResearchConceptsCell adhesion eventsV8 protease digestionHuman T-cell leukemic cell lineT-cell leukemic cell lineCytoplasmic domainHomotypic adhesion moleculeCadherinLeukemic cell linesAdhesion eventsMolecular massProtease digestionHomotypic adhesionHeterotypic adhesionE-cadherinPeptide mapsSpeciesCell linesEpithelial cellsWider roleMucosal epithelial cellsAdhesion moleculesIntestinal intraepithelial T lymphocytesPan-cadherinCellsSolid tissues
1995
Frequent alterations in E-cadherin and alpha- and beta-catenin expression in human breast cancer cell lines.
Pierceall W, Woodard A, Morrow J, Rimm D, Fearon E. Frequent alterations in E-cadherin and alpha- and beta-catenin expression in human breast cancer cell lines. Oncogene 1995, 11: 1319-26. PMID: 7478552.Peer-Reviewed Original ResearchMeSH KeywordsAlpha CateninBase SequenceBeta CateninBlotting, SouthernBlotting, WesternBreast NeoplasmsCadherinsCytoskeletal ProteinsFemaleGene DeletionGene ExpressionHumansMolecular Sequence DataMutationOligodeoxyribonucleotidesPolymerase Chain ReactionPolymorphism, Single-Stranded ConformationalReceptor, ErbB-2RibonucleasesTrans-ActivatorsTumor Cells, CulturedConceptsAlpha-catenin proteinE-cadherin transcriptE-cadherinE-cadherin expressionBeta-catenin expressionCell linesBreast cancer cell linesEpithelial cell-cell interactionsCancer cell linesBeta-catenin proteinCancer-derived cell linesMembrane cytoskeletal proteinsCell-cell interactionsBreast cancer-derived cell linesE-cadherin geneHuman breast cancer-derived cell linesLoss of functionTransmembrane proteinAdherens junctionsCytoskeletal matrixCadherin proteinCytoskeletal proteinsTranscript levelsFrequent alterationsSequence alterationsAlpha 1(E)-catenin is an actin-binding and -bundling protein mediating the attachment of F-actin to the membrane adhesion complex.
Rimm DL, Koslov ER, Kebriaei P, Cianci CD, Morrow JS. Alpha 1(E)-catenin is an actin-binding and -bundling protein mediating the attachment of F-actin to the membrane adhesion complex. Proceedings Of The National Academy Of Sciences Of The United States Of America 1995, 92: 8813-8817. PMID: 7568023, PMCID: PMC41057, DOI: 10.1073/pnas.92.19.8813.Peer-Reviewed Original ResearchConceptsF-actinBundling proteinE-cadherin-mediated cell-cell contactsHomotypic cell-cell adhesionBundles F-actinEpithelial cell polarityCortical actin cytoskeletonCell-cell adhesionActin-binding proteinsFull-length proteinE-cadherinCell-cell contactMembrane adhesion complexesBundles actinCell polarityHierarchy of interactionsActin cytoskeletonAdhesion complexesCytoplasmic domainCosedimentation assaysSedimentation assaysAdditional proteinsMolecular basisActin filamentsActin complexReduced alpha-catenin and E-cadherin expression in breast cancer.
Rimm DL, Sinard JH, Morrow JS. Reduced alpha-catenin and E-cadherin expression in breast cancer. Laboratory Investigation 1995, 72: 506-12. PMID: 7745946.Peer-Reviewed Original ResearchConceptsE-cadherinSteady-state levelsE-cadherin expressionHomotypic cell adhesion proteinMetastatic diseaseCell adhesion proteinsHuman E-cadherinCell-cell interactionsCytoplasmic proteinsTime of biopsyAdhesion proteinsAggressive tumor behaviorAdhesive functionEffector elementsAdhesion cascadeAbsent E-cadherin expressionTypes of cancerJunctional complexesProteinBreast cancerEpithelial tumorsSensitive markerTumor behaviorExpressionCancer
1994
Adhesion between epithelial cells and T lymphocytes mediated by E-cadherin and the αEβ7 integrin
Cepek K, Shaw S, Parker C, Russell G, Morrow J, Rimm D, Brenner M. Adhesion between epithelial cells and T lymphocytes mediated by E-cadherin and the αEβ7 integrin. Nature 1994, 372: 190-193. PMID: 7969453, DOI: 10.1038/372190a0.Peer-Reviewed Original ResearchConceptsIntraepithelial lymphocytesAdhesion moleculesT cellsIntestinal intra-epithelial lymphocytesEpithelial cellsIntestinal intraepithelial lymphocytesIntra-epithelial lymphocytesMucosal immune systemE-cadherinTissue-specific retentionTissue-specific compartmentalizationLymphoid structuresT lymphocytesImmune systemLymphocyte homingLymphocytesΑEβ7Molecular Cloning of Human E-Cadherin Suggests a Novel Subdivision of the Cadherin Superfamily
Rimm DL, Morrow JS. Molecular Cloning of Human E-Cadherin Suggests a Novel Subdivision of the Cadherin Superfamily. Biochemical And Biophysical Research Communications 1994, 200: 1754-1761. PMID: 8185635, DOI: 10.1006/bbrc.1994.1656.Peer-Reviewed Original ResearchConceptsHuman E-cadherinClassical cadherinsE-cadherinDown-stream signaling cascadesCadherin functionRelated cadherinsHomology domainCytoplasmic domainSequence motifsDomain homologyUnprocessed proteinMolecular cloningCytoplasmic interactionsHuman proteinsCDNA libraryDesmosomal cadherinsSignaling cascadesCadherinMolecular massT-cadherinNovel subdivisionProteinRET oncogeneCloningHomology