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Aquaporin 1Aquaporin 5Aquaporin 3Aquaporin 4AquaporinsAquaporin 2Aquaporin 6WaterOsmosisAquaglyceroporinsBlood Group AntigensMercuric ChlorideWater-Electrolyte BalanceGlycerolAmino Acid SequenceKidney Tubules, CollectingPermeabilityKidney Concentrating AbilityDiabetes Insipidus, NephrogenicCell Membrane PermeabilityDNA, ComplementaryPolyuriaNeuromyelitis OpticaBase SequencePlant TranspirationPlant ProteinsIon ChannelsRNA, MessengerBiological TransportXenopus laevisOocytesAntidiuretic AgentsRenal AgentsOsmotic PressureMolecular Sequence DataCell MembraneBrain EdemaVasopressinsMembrane ProteinsDeamino Arginine VasopressinLens, CrystallineEye ProteinsImmunohistochemistryTulipaVapor PressurePlant RootsBody WaterGene ExpressionMercury CompoundsOsmolar ConcentrationGene Expression Regulation, PlantCistaceaeKidneyKidney MedullaReverse Transcriptase Polymerase Chain ReactionRats, BrattleboroSalivary GlandsAnguillaGene LibraryDehydrationReceptors, VasopressinBlotting, WesternSubmandibular GlandAstrocytesDNA PrimersProtein TransportXenopusRats, Sprague-DawleyGene Expression RegulationSequence AlignmentGlomeromycotaMyceliumMicroscopy, Electron, Scanning TransmissionMicroscopy, ImmunoelectronPropylene GlycolImmunoblottingMesophyll CellsMesembryanthemumBlotting, NorthernDNASolute Carrier Family 12, Member 1Mice, KnockoutGlycerol KinaseMercuryDroughtsSaline Solution, HypertonicCell LinePichiaProteolipidsSpinacia oleraceaRNA, ComplementaryPlant LeavesGlial Fibrillary Acidic ProteinNobel PrizeLLC-PK1 CellsUreaFragariaPhylogenyHypertonic SolutionsModels, Molecular
MalignantProteinGeneLevelsGlycerolMembraneSequenceHighly expressedWater channelSerialCellNormal
Malignant1
  • Given the strong link between the regulation of some of these genes and the growth and dissemination of gastrointestinal cancers, we believe their aberrant expression in UC may provide a mechanism for epithelial hyper-proliferation and, in the context of malignant transformation, for tumour growth. (bmj.com)
Protein3
  • Aquaporin-9 (AQP-9) is a protein that in humans is encoded by the AQP9 gene. (wikipedia.org)
  • The aquaporins/major intrinsic protein are a family of water-selective membrane channels. (wikipedia.org)
  • REG4, S100P, SERPINB5 and REG1A protein expression was confirmed by immunohistochemistry (n=23). (bmj.com)
Gene1
  • This study shows that GHR1 and GHR2 gene expression are differentially regulated by physiological levels of GH and insulin in tilapia primary hepatocytes. (bvsalud.org)
Levels1
  • Expression of inflammation-related genes such as REG1A and IL8 returned to control levels during remission. (bmj.com)
Glycerol1
  • Aquaporin 3 (AQP3) is a peroxiporin, a membrane protein that channels hydrogen peroxide in addition to water and glycerol. (bvsalud.org)
Membrane1
  • The aquaporins/major intrinsic protein are a family of water-selective membrane channels. (wikipedia.org)
Sequence2
  • Aquaporin-9 has greater sequence similarity with AQP3 and AQP7 and they may be a subfamily. (wikipedia.org)
  • The raw data of the sequence tags have been made publicly available (Gene Expression Omnibus, series accession number GSE6252). (biomedcentral.com)
Highly expressed2
  • We characterized the transcriptome of normal cervical tissue and evaluated the highly expressed genes in terms of tissue specificity, concordant expression among the normal libraries and their altered expression in CIN III lesions (Figure 1B ). (biomedcentral.com)
  • In skin photoaging samples, PVT1 and AQP3 were poorly expressed, while miR-551b-3p was highly expressed. (bvsalud.org)
Water channel1
  • Since E-cadherin and the water channel aquaporin-3 are important for both skin function and cell migration, and aquaporin-3 is furthermore involved in wound healing of the skin demonstrated by impaired wound healing in aquaporin-3-null mice, we hypothesized that E-cadherin and aquaporin-3 expression may be dysregulated in chronic wounds. (bvsalud.org)
Serial1
  • This was accomplished by immunohistochemical stainings of E-cadherin and aquaporin-3 on serial sections followed by qualitative evaluation of staining patterns, which revealed low expression of both E-cadherin and aquaporin-3 at the wound edge. (bvsalud.org)
Cell2
  • We evaluated H2O2 uptake, cell migratory capacity, and expression of PI3K, pAkt/Akt in three breast cancer cell lines, MCF7, SkBr3, and SUM159PT, and in the nontumorigenic breast epithelial cell line MCF10A. (bvsalud.org)
  • These results suggest that in breast cancer cell lines, AQP3 is not directly related to PI3K/Akt pathway but rather in a cell-line-dependent manner. (bvsalud.org)
Normal1
  • We demonstrate the utility of this baseline data by identifying genes with aberrant expression in CIN III when compared to normal tissue. (biomedcentral.com)