2003
Distribution and regulation of expression of serum‐ and glucocorticoid‐induced kinase‐1 in the rat kidney
de la Rosa D, Coric T, Todorovic N, Shao D, Wang T, Canessa C. Distribution and regulation of expression of serum‐ and glucocorticoid‐induced kinase‐1 in the rat kidney. The Journal Of Physiology 2003, 551: 455-466. PMID: 12816971, PMCID: PMC2343216, DOI: 10.1113/jphysiol.2003.042903.Peer-Reviewed Original ResearchMeSH KeywordsAdrenalectomyAldosteroneAnimalsAntibodiesAntibody SpecificityBlotting, NorthernBlotting, WesternCells, CulturedDNA, ComplementaryElectrophoresis, Polyacrylamide GelEpithelial CellsGene Expression Regulation, EnzymologicGlucocorticoidsImmediate-Early ProteinsImmunoblottingIn Vitro TechniquesIsoenzymesKidneyKidney TubulesMicroscopy, FluorescenceNuclear ProteinsProtein Serine-Threonine KinasesRatsRats, Sprague-DawleyRNASubcellular FractionsTransfectionConceptsGlucocorticoid-induced kinase 1Kinase 1Ion channelsRegulation of expressionConstitutive high expressionBasolateral membraneRenal epithelial cellsSubcellular localizationLevel of expressionRegulation of levelsEpithelial ion channelsSGK1 proteinMammalian kidneyApical membraneDirect interactionSGK1Epithelial cellsWestern blottingHigh expressionExpressionExpression of SGK1ProteinRat kidneyTransportersPhysiological changes
1994
An SH3 binding region in the epithelial Na+ channel (alpha rENaC) mediates its localization at the apical membrane.
Rotin D, Bar‐Sagi D, O'Brodovich H, Merilainen J, Lehto V, Canessa C, Rossier B, Downey G. An SH3 binding region in the epithelial Na+ channel (alpha rENaC) mediates its localization at the apical membrane. The EMBO Journal 1994, 13: 4440-4450. PMID: 7925286, PMCID: PMC395375, DOI: 10.1002/j.1460-2075.1994.tb06766.x.Peer-Reviewed Original ResearchConceptsC-terminal regionAlpha-spectrinSH3 domainCytoskeletal interactionsFusion proteinTerminal proline-rich regionAlpha-rENaCApical membranePolarized epithelial cellsProline-rich sequenceN-terminal proteinProline-rich regionEpithelial cellsApical membrane localizationCytoskeletal protein ankyrinProper channel functionPrimary rat alveolar epithelial cellsEpithelial cell lysatesMembrane localizationRat alveolar epithelial cellsProtein ankyrinApical localizationPlasma membraneRecombinant fusion proteinMolecular mechanismsAmiloride-sensitive epithelial Na+ channel is made of three homologous subunits
Canessa C, Schild L, Buell G, Thorens B, Gautschi I, Horisberger J, Rossier B. Amiloride-sensitive epithelial Na+ channel is made of three homologous subunits. Nature 1994, 367: 463-467. PMID: 8107805, DOI: 10.1038/367463a0.Peer-Reviewed Original ResearchConceptsEpithelial sodium channelRat epithelial sodium channelSodium channelsSodium reabsorptionSodium balanceDistal colonAmiloride-sensitive epithelial sodium channelPharmacological profileBlood volumeRenal tubulesRat epithelialExocrine glandsEpithelial cellsΑ-subunitDistal partNative channelsExpression cloningAldosteroneLungColon