2023
Genetic Variants in ARHGEF6 Cause Congenital Anomalies of the Kidneys and Urinary Tract in Humans, Mice, and Frogs
Klämbt V, Buerger F, Wang C, Naert T, Richter K, Nauth T, Weiss A, Sieckmann T, Lai E, Connaughton D, Seltzsam S, Mann N, Majmundar A, Wu C, Onuchic-Whitford A, Shril S, Schneider S, Schierbaum L, Dai R, Bekheirnia M, Joosten M, Shlomovitz O, Vivante A, Banne E, Mane S, Lifton R, Kirschner K, Kispert A, Rosenberger G, Fischer K, Lienkamp S, Zegers M, Hildebrandt F. Genetic Variants in ARHGEF6 Cause Congenital Anomalies of the Kidneys and Urinary Tract in Humans, Mice, and Frogs. Journal Of The American Society Of Nephrology 2023, 34: 273-290. PMID: 36414417, PMCID: PMC10103091, DOI: 10.1681/asn.2022010050.Peer-Reviewed Original ResearchConceptsIntegrin-linked kinaseFocal adhesion proteinsThree-dimensional (3D) MadinCdc42/Rac1Genetic variantsRac1/Cdc42Loss of interactionFrog modelPolarity defectsExchange factorNovel genesFocal adhesionsLamellipodia formationARHGEF6Adhesion proteinsDisease genesDeleterious variantsCell spreadingLumen formationCell migrationGenesProteinHemizygous variantKidney cellsExome sequencing
2018
GAPVD1 and ANKFY1 Mutations Implicate RAB5 Regulation in Nephrotic Syndrome
Hermle T, Schneider R, Schapiro D, Braun DA, van der Ven AT, Warejko JK, Daga A, Widmeier E, Nakayama M, Jobst-Schwan T, Majmundar AJ, Ashraf S, Rao J, Finn LS, Tasic V, Hernandez JD, Bagga A, Jalalah SM, El Desoky S, Kari JA, Laricchia KM, Lek M, Rehm HL, MacArthur DG, Mane S, Lifton RP, Shril S, Hildebrandt F. GAPVD1 and ANKFY1 Mutations Implicate RAB5 Regulation in Nephrotic Syndrome. Journal Of The American Society Of Nephrology 2018, 29: 2123-2138. PMID: 29959197, PMCID: PMC6065084, DOI: 10.1681/asn.2017121312.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell MovementCells, CulturedCohort StudiesDisease ProgressionDrosophila melanogasterExome SequencingFemaleGene Expression RegulationGenetic Predisposition to DiseaseHumansMaleMass ScreeningMembrane ProteinsMutation, MissenseNephrotic SyndromePedigreePhosphate-Binding ProteinsPodocytesRab5 GTP-Binding ProteinsReal-Time Polymerase Chain ReactionRenal Insufficiency, ChronicRNA, Small InterferingConceptsSteroid-resistant nephrotic syndromeNovel monogenic causesCoimmunoprecipitation assaysHomozygous missense mutationPatient-derived mutationsMissense mutationsMonogenic causesHEK293T cellsActive Rab5GAPVD1Nephrotic syndromePodocyte migration rateEctopic expressionCases of SRNSPartial colocalizationSpecific pathogenetic pathwaysWhole-exome sequencingEarly-onset NSHuman NFunctional significancePodocyte migrationProteinMutationsPhysical interactionRab5A homozygous missense variant in VWA2, encoding an interactor of the Fraser-complex, in a patient with vesicoureteral reflux
van der Ven AT, Kobbe B, Kohl S, Shril S, Pogoda HM, Imhof T, Ityel H, Vivante A, Chen J, Hwang DY, Connaughton DM, Mann N, Widmeier E, Taglienti M, Schmidt JM, Nakayama M, Senguttuvan P, Kumar S, Tasic V, Kehinde EO, Mane SM, Lifton RP, Soliman N, Lu W, Bauer SB, Hammerschmidt M, Wagener R, Hildebrandt F. A homozygous missense variant in VWA2, encoding an interactor of the Fraser-complex, in a patient with vesicoureteral reflux. PLOS ONE 2018, 13: e0191224. PMID: 29351342, PMCID: PMC5774751, DOI: 10.1371/journal.pone.0191224.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino Acid SubstitutionAnimalsAnimals, NewbornBiomarkers, TumorCalcium-Binding ProteinsChildConsanguinityConserved SequenceExonsExtracellular Matrix ProteinsFraser SyndromeGene Expression Regulation, DevelopmentalHomozygoteHumansMaleMiceModels, AnimalModels, MolecularMutation, MissensePedigreeSequence Homology, Amino AcidUrogenital AbnormalitiesUrogenital SystemVesico-Ureteral RefluxConceptsMetanephric mesenchymeUreteric budWhole-exome sequencingHomozygosity mappingIntermolecular disulfide bond formationDisulfide bond formationDirect interactorsNeomorphic effectMonogenic causesCysteine residuesHomozygous missense mutationComplex subunit 1Unpaired cysteine residueNovel CAKUTSubunit 1Homozygous missense variantFraser ComplexMissense mutationsGenesProteinInteractorsMissense variantsMutationsExome sequencingNephrogenic zone
1990
Quantitation of the ras gene product in leukemic blast cells using enzymatic staining.
Gutheil J, Mane S, Bass K, Lee E, Needleman S. Quantitation of the ras gene product in leukemic blast cells using enzymatic staining. BioTechniques 1990, 9: 212-7. PMID: 2205250.Peer-Reviewed Original ResearchConceptsRas gene productGene productsRas speciesRas protein levelsProtein of interestGene product levelsQuantitation of proteinsSpecific ras mutationsUse of electrophoresisProtein levelsRas mutationsProteinP21 expressionHuman malignanciesSpeciesCellsLeukemic cellsMutationsEnzymatic stainingHigh specificityRadioactive reagentsExpressionElectrophoresisAssaysVivo
1989
Immunoprecipitation of cell lysates with RAP-5 does not specifically detect ras oncogene product p21
Gutheil J, Mane S, Kapil V, Needleman S. Immunoprecipitation of cell lysates with RAP-5 does not specifically detect ras oncogene product p21. Human Pathology 1989, 20: 1176-1180. PMID: 2687155, DOI: 10.1016/s0046-8177(89)80008-5.Peer-Reviewed Original ResearchPurification and characterization of human lysosomal membrane glycoproteins
Mane S, Marzella L, Bainton D, Holt V, Cha Y, Hildreth J, August J. Purification and characterization of human lysosomal membrane glycoproteins. Archives Of Biochemistry And Biophysics 1989, 268: 360-378. PMID: 2912382, DOI: 10.1016/0003-9861(89)90597-3.Peer-Reviewed Original ResearchConceptsLysosomal membrane glycoproteinsCell surface expressionHL-60 cellsPlasma membraneU937 myelomonocytic leukemia cellsMembrane glycoproteinsHuman lysosomal membrane glycoproteinsU937 cellsAddition of AsnDetergent-extractable proteinTissue culture cellsNH2-terminal sequence analysisHLAMP-2Mouse cellsMembrane flowSequence analysisMyelomonocytic leukemia cellsAntibody affinity chromatographyCell typesCulture cellsPeroxidase-positive granulesProteinHLAMP-1Lysosomal structuresAffinity chromatography