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Aquaporin 1Aquaporin 5Aquaporin 3Aquaporin 4AquaporinsAquaporin 2Aquaporin 6WaterMercuric ChlorideOsmosisAquaglyceroporinsBlood Group AntigensWater-Electrolyte BalanceGlycerolPermeabilityCell Membrane PermeabilityPlant TranspirationKidney Tubules, CollectingKidney Concentrating AbilityDiabetes Insipidus, NephrogenicPlant ProteinsIon ChannelsNeuromyelitis OpticaPolyuriaBiological TransportXenopus laevisOsmotic PressureOocytesAntidiuretic AgentsMolecular Sequence DataTulipaVapor PressureAmino Acid SequenceCistaceaePlant RootsBrain EdemaMercury CompoundsCell MembraneMembrane ProteinsLens, CrystallineGene Expression Regulation, PlantEye ProteinsBody WaterRenal AgentsAnguillaOsmolar ConcentrationVasopressinsImmunohistochemistryDehydrationRNA, MessengerGlomeromycotaMicroscopy, Electron, Scanning TransmissionSalivary GlandsMyceliumDeamino Arginine VasopressinPropylene GlycolMesophyll CellsMesembryanthemumKidney MedullaKidneySubmandibular GlandReceptors, VasopressinDroughtsAstrocytesReverse Transcriptase Polymerase Chain ReactionXenopusMercuryGene ExpressionNobel PrizeRats, Sprague-DawleySpinacia oleraceaGlycerol KinaseProtein TransportPichiaFragariaRats, BrattleboroPlant StomataProteolipidsBlotting, WesternSaline Solution, HypertonicAntimony Potassium TartratePlant LeavesBase SequenceMalpighian TubulesGlial Fibrillary Acidic ProteinSequence Homology, Amino AcidRNA, ComplementaryImmunoblottingPhloretinMicroscopy, ImmunoelectronModels, MolecularFreezingSolute Carrier Family 12, Member 14-ChloromercuribenzenesulfonateMice, KnockoutDNA PrimersUreaHypertonic SolutionsArabidopsisGene Expression RegulationCell SizeMorulaSodium-Potassium-Chloride SymportersDNA, ComplementaryEpithelial CellsQuercusCloning, MolecularProtein ConformationZea maysMolecular Dynamics SimulationAcclimatizationPhylogenyHydroxyethyl Starch DerivativesSodium Chloride
Aquaporin 1: Aquaporin 1 forms a water-specific channel that is constitutively expressed at the PLASMA MEMBRANE of ERYTHROCYTES and KIDNEY TUBULES, PROXIMAL. It provides these cells with a high permeability to WATER. In humans polymorphisms of this protein result in the Colton blood group antigen.Aquaporin 5: Aquaporin 5 is a water-specific channel protein that is expressed primarily in alveolar, tracheal, and upper bronchial EPITHELIUM. It plays an important role in maintaining water HOMEOSTASIS in the LUNGS and may also regulate release of SALIVA and TEARS in the SALIVARY GLANDS and the LACRIMAL GLAND.Aquaporin 3: Aquaporin 3 is an aquaglyceroporin that is expressed in the KIDNEY COLLECTING DUCTS and is constitutively localized at the basolateral MEMBRANE.Aquaporin 4: Aquaporin 4 is the major water-selective channel in the CENTRAL NERVOUS SYSTEM of mammals.Aquaporins: A class of porins that allow the passage of WATER and other small molecules across CELL MEMBRANES.Aquaporin 2: Aquaporin 2 is a water-specific channel protein that is expressed in KIDNEY COLLECTING DUCTS. The translocation of aquaporin 2 to the apical PLASMA MEMBRANE is regulated by VASOPRESSIN, and MUTATIONS in AQP2 have been implicated in a variety of kidney disorders including DIABETES INSIPIDUS.Aquaporin 6: Aquaporin 6 is an aquaglyceroporin that is found primarily in KIDNEY COLLECTING DUCTS. AQP6 protein functions as an anion-selective channel.Water: A clear, odorless, tasteless liquid that is essential for most animal and plant life and is an excellent solvent for many substances. The chemical formula is hydrogen oxide (H2O). (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Mercuric Chloride: Mercury chloride (HgCl2). A highly toxic compound that volatizes slightly at ordinary temperature and appreciably at 100 degrees C. It is corrosive to mucous membranes and used as a topical antiseptic and disinfectant.Osmosis: Tendency of fluids (e.g., water) to move from the less concentrated to the more concentrated side of a semipermeable membrane.Aquaglyceroporins: A subgroup of aquaporins that transport WATER; GLYCEROL; and other small solutes across CELL MEMBRANES.Blood Group Antigens: Sets of cell surface antigens located on BLOOD CELLS. They are usually membrane GLYCOPROTEINS or GLYCOLIPIDS that are antigenically distinguished by their carbohydrate moieties.Water-Electrolyte Balance: The balance of fluid in the BODY FLUID COMPARTMENTS; total BODY WATER; BLOOD VOLUME; EXTRACELLULAR SPACE; INTRACELLULAR SPACE, maintained by processes in the body that regulate the intake and excretion of WATER and ELECTROLYTES, particularly SODIUM and POTASSIUM.Glycerol: A trihydroxy sugar alcohol that is an intermediate in carbohydrate and lipid metabolism. It is used as a solvent, emollient, pharmaceutical agent, and sweetening agent.Permeability: Property of membranes and other structures to permit passage of light, heat, gases, liquids, metabolites, and mineral ions.Cell Membrane Permeability: A quality of cell membranes which permits the passage of solvents and solutes into and out of cells.Plant Transpiration: The loss of water vapor by plants to the atmosphere. It occurs mainly from the leaves through pores (stomata) whose primary function is gas exchange. The water is replaced by a continuous column of water moving upwards from the roots within the xylem vessels. (Concise Dictionary of Biology, 1990)Kidney Tubules, Collecting: Straight tubes commencing in the radiate part of the kidney cortex where they receive the curved ends of the distal convoluted tubules. In the medulla the collecting tubules of each pyramid converge to join a central tube (duct of Bellini) which opens on the summit of the papilla.Kidney Concentrating Ability: The ability of the kidney to excrete in the urine high concentrations of solutes from the blood plasma.Diabetes Insipidus, Nephrogenic: A genetic or acquired polyuric disorder characterized by persistent hypotonic urine and HYPOKALEMIA. This condition is due to renal tubular insensitivity to VASOPRESSIN and failure to reduce urine volume. It may be the result of mutations of genes encoding VASOPRESSIN RECEPTORS or AQUAPORIN-2; KIDNEY DISEASES; adverse drug effects; or complications from PREGNANCY.Plant Proteins: Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.Ion Channels: Gated, ion-selective glycoproteins that traverse membranes. The stimulus for ION CHANNEL GATING can be due to a variety of stimuli such as LIGANDS, a TRANSMEMBRANE POTENTIAL DIFFERENCE, mechanical deformation or through INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS.Neuromyelitis Optica: A syndrome characterized by acute OPTIC NEURITIS; MYELITIS, TRANSVERSE; demyelinating and/or necrotizing lesions in the OPTIC NERVES and SPINAL CORD; and presence of specific autoantibodies to AQUAPORIN 4.Polyuria: Urination of a large volume of urine with an increase in urinary frequency, commonly seen in diabetes (DIABETES MELLITUS; DIABETES INSIPIDUS).Biological Transport: The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.Xenopus laevis: The commonest and widest ranging species of the clawed "frog" (Xenopus) in Africa. This species is used extensively in research. There is now a significant population in California derived from escaped laboratory animals.Osmotic Pressure: The pressure required to prevent the passage of solvent through a semipermeable membrane that separates a pure solvent from a solution of the solvent and solute or that separates different concentrations of a solution. It is proportional to the osmolality of the solution.Oocytes: Female germ cells derived from OOGONIA and termed OOCYTES when they enter MEIOSIS. The primary oocytes begin meiosis but are arrested at the diplotene state until OVULATION at PUBERTY to give rise to haploid secondary oocytes or ova (OVUM).Antidiuretic Agents: Agents that reduce the excretion of URINE, most notably the octapeptide VASOPRESSINS.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Tulipa: A plant genus of the family LILIACEAE. Members contain tuliposides and tulipalins and have been associated with allergic contact dermatitis in florists.Vapor Pressure: The contribution to barometric PRESSURE of gaseous substance in equilibrium with its solid or liquid phase.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Cistaceae: A plant family of the order Violales, subclass Dilleniidae, class Magnoliopsida. The common name of rock rose is used with several plants of this family.Plant Roots: The usually underground portions of a plant that serve as support, store food, and through which water and mineral nutrients enter the plant. (From American Heritage Dictionary, 1982; Concise Dictionary of Biology, 1990)Brain Edema: Increased intracellular or extracellular fluid in brain tissue. Cytotoxic brain edema (swelling due to increased intracellular fluid) is indicative of a disturbance in cell metabolism, and is commonly associated with hypoxic or ischemic injuries (see HYPOXIA, BRAIN). An increase in extracellular fluid may be caused by increased brain capillary permeability (vasogenic edema), an osmotic gradient, local blockages in interstitial fluid pathways, or by obstruction of CSF flow (e.g., obstructive HYDROCEPHALUS). (From Childs Nerv Syst 1992 Sep; 8(6):301-6)Mercury Compounds: Inorganic compounds that contain mercury as an integral part of the molecule.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Membrane Proteins: Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.Lens, Crystalline: A transparent, biconvex structure of the EYE, enclosed in a capsule and situated behind the IRIS and in front of the vitreous humor (VITREOUS BODY). It is slightly overlapped at its margin by the ciliary processes. Adaptation by the CILIARY BODY is crucial for OCULAR ACCOMMODATION.Gene Expression Regulation, Plant: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in plants.Eye ProteinsBody Water: Fluids composed mainly of water found within the body.Renal Agents: Drugs used for their effects on the kidneys' regulation of body fluid composition and volume. The most commonly used are the diuretics. Also included are drugs used for their antidiuretic and uricosuric actions, for their effects on the kidneys' clearance of other drugs, and for diagnosis of renal function.AnguillaOsmolar Concentration: The concentration of osmotically active particles in solution expressed in terms of osmoles of solute per liter of solution. Osmolality is expressed in terms of osmoles of solute per kilogram of solvent.Vasopressins: Antidiuretic hormones released by the NEUROHYPOPHYSIS of all vertebrates (structure varies with species) to regulate water balance and OSMOLARITY. In general, vasopressin is a nonapeptide consisting of a six-amino-acid ring with a cysteine 1 to cysteine 6 disulfide bridge or an octapeptide containing a CYSTINE. All mammals have arginine vasopressin except the pig with a lysine at position 8. Vasopressin, a vasoconstrictor, acts on the KIDNEY COLLECTING DUCTS to increase water reabsorption, increase blood volume and blood pressure.Immunohistochemistry: Histochemical localization of immunoreactive substances using labeled antibodies as reagents.Dehydration: The condition that results from excessive loss of water from a living organism.RNA, Messenger: RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.Glomeromycota: A phylum of fungi that are mutualistic symbionts and form ARBUSCULAR MYCORRHIZAE with PLANT ROOTS.Microscopy, Electron, Scanning Transmission: A type of TRANSMISSION ELECTRON MICROSCOPY in which the object is examined directly by an extremely narrow electron beam scanning the specimen point-by-point and using the reactions of the electrons that are transmitted through the specimen to create the image. It should not be confused with SCANNING ELECTRON MICROSCOPY.Salivary Glands: Glands that secrete SALIVA in the MOUTH. There are three pairs of salivary glands (PAROTID GLAND; SUBLINGUAL GLAND; SUBMANDIBULAR GLAND).Mycelium: The body of a fungus which is made up of HYPHAE.Deamino Arginine Vasopressin: A synthetic analog of the pituitary hormone, ARGININE VASOPRESSIN. Its action is mediated by the VASOPRESSIN receptor V2. It has prolonged antidiuretic activity, but little pressor effects. It also modulates levels of circulating FACTOR VIII and VON WILLEBRAND FACTOR.Propylene Glycol: A clear, colorless, viscous organic solvent and diluent used in pharmaceutical preparations.Mesophyll Cells: Large and highly vacuolated cells possessing many chloroplasts occuring in the interior cross-section of leaves, juxtaposed between the epidermal layers.Mesembryanthemum: A plant genus of the family AIZOACEAE. It is a native of Africa and widely planted for erosion control to stabilize soil along roadsides and beaches.Kidney Medulla: The internal portion of the kidney, consisting of striated conical masses, the renal pyramids, whose bases are adjacent to the cortex and whose apices form prominent papillae projecting into the lumen of the minor calyces.Kidney: Body organ that filters blood for the secretion of URINE and that regulates ion concentrations.Submandibular Gland: One of two salivary glands in the neck, located in the space bound by the two bellies of the digastric muscle and the angle of the mandible. It discharges through the submandibular duct. The secretory units are predominantly serous although a few mucous alveoli, some with serous demilunes, occur. (Stedman, 25th ed)Receptors, Vasopressin: Specific molecular sites or proteins on or in cells to which VASOPRESSINS bind or interact in order to modify the function of the cells. Two types of vasopressin receptor exist, the V1 receptor in the vascular smooth muscle and the V2 receptor in the kidneys. The V1 receptor can be subdivided into V1a and V1b (formerly V3) receptors.Droughts: Prolonged dry periods in natural climate cycle. They are slow-onset phenomena caused by rainfall deficit combined with other predisposing factors.Astrocytes: A class of large neuroglial (macroglial) cells in the central nervous system - the largest and most numerous neuroglial cells in the brain and spinal cord. Astrocytes (from "star" cells) are irregularly shaped with many long processes, including those with "end feet" which form the glial (limiting) membrane and directly and indirectly contribute to the BLOOD-BRAIN BARRIER. They regulate the extracellular ionic and chemical environment, and "reactive astrocytes" (along with MICROGLIA) respond to injury.Reverse Transcriptase Polymerase Chain Reaction: A variation of the PCR technique in which cDNA is made from RNA via reverse transcription. The resultant cDNA is then amplified using standard PCR protocols.Xenopus: An aquatic genus of the family, Pipidae, occurring in Africa and distinguished by having black horny claws on three inner hind toes.Mercury: A silver metallic element that exists as a liquid at room temperature. It has the atomic symbol Hg (from hydrargyrum, liquid silver), atomic number 80, and atomic weight 200.59. Mercury is used in many industrial applications and its salts have been employed therapeutically as purgatives, antisyphilitics, disinfectants, and astringents. It can be absorbed through the skin and mucous membranes which leads to MERCURY POISONING. Because of its toxicity, the clinical use of mercury and mercurials is diminishing.Gene Expression: The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.Nobel PrizeRats, Sprague-Dawley: A strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company.Spinacia oleracea: A widely cultivated plant, native to Asia, having succulent, edible leaves eaten as a vegetable. (From American Heritage Dictionary, 1982)Glycerol Kinase: An enzyme that catalyzes the formation of glycerol 3-phosphate from ATP and glycerol. Dihydroxyacetone and L-glyceraldehyde can also act as acceptors; UTP and, in the case of the yeast enzyme, ITP and GTP can act as donors. It provides a way for glycerol derived from fats or glycerides to enter the glycolytic pathway. EC 2.7.1.30.Protein Transport: The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.Pichia: Yeast-like ascomycetous fungi of the family Saccharomycetaceae, order SACCHAROMYCETALES isolated from exuded tree sap.Fragaria: A plant genus of the family ROSACEAE known for the edible fruit.Rats, Brattleboro: A mutant strain of Rattus norvegicus used in research on renal function and hypertension and as a disease model for diabetes insipidus.Plant Stomata: Closable openings in the epidermis of plants on the underside of leaves. They allow the exchange of gases between the internal tissues of the plant and the outside atmosphere.Proteolipids: Protein-lipid combinations abundant in brain tissue, but also present in a wide variety of animal and plant tissues. In contrast to lipoproteins, they are insoluble in water, but soluble in a chloroform-methanol mixture. The protein moiety has a high content of hydrophobic amino acids. The associated lipids consist of a mixture of GLYCEROPHOSPHATES; CEREBROSIDES; and SULFOGLYCOSPHINGOLIPIDS; while lipoproteins contain PHOSPHOLIPIDS; CHOLESTEROL; and TRIGLYCERIDES.Blotting, Western: Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.Saline Solution, Hypertonic: Hypertonic sodium chloride solution. A solution having an osmotic pressure greater than that of physiologic salt solution (0.9 g NaCl in 100 ml purified water).Antimony Potassium Tartrate: A schistosomicide possibly useful against other parasites. It has irritant emetic properties and may cause lethal cardiac toxicity among other adverse effects.Plant Leaves: Expanded structures, usually green, of vascular plants, characteristically consisting of a bladelike expansion attached to a stem, and functioning as the principal organ of photosynthesis and transpiration. (American Heritage Dictionary, 2d ed)Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Malpighian Tubules: Slender tubular or hairlike excretory structures found in insects. They emerge from the alimentary canal between the mesenteron (midgut) and the proctodeum (hindgut).Glial Fibrillary Acidic Protein: An intermediate filament protein found only in glial cells or cells of glial origin. MW 51,000.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.RNA, Complementary: Synthetic transcripts of a specific DNA molecule or fragment, made by an in vitro transcription system. This cRNA can be labeled with radioactive uracil and then used as a probe. (King & Stansfield, A Dictionary of Genetics, 4th ed)Immunoblotting: Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies.PhloretinMicroscopy, Immunoelectron: Microscopy in which the samples are first stained immunocytochemically and then examined using an electron microscope. Immunoelectron microscopy is used extensively in diagnostic virology as part of very sensitive immunoassays.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Freezing: Liquids transforming into solids by the removal of heat.Solute Carrier Family 12, Member 1: Na-K-Cl transporter in the ASCENDING LIMB OF LOOP OF HENLE. It mediates active reabsorption of sodium chloride and is inhibited by LOOP DIURETICS such as FUROSEMIDE; and BUMETANIDE. Mutations in the gene encoding SLC12A1 are associated with a BARTTER SYNDROME.4-Chloromercuribenzenesulfonate: A cytotoxic sulfhydryl reagent that inhibits several subcellular metabolic systems and is used as a tool in cellular physiology.Mice, Knockout: Strains of mice in which certain GENES of their GENOMES have been disrupted, or "knocked-out". To produce knockouts, using RECOMBINANT DNA technology, the normal DNA sequence of the gene being studied is altered to prevent synthesis of a normal gene product. Cloned cells in which this DNA alteration is successful are then injected into mouse EMBRYOS to produce chimeric mice. The chimeric mice are then bred to yield a strain in which all the cells of the mouse contain the disrupted gene. Knockout mice are used as EXPERIMENTAL ANIMAL MODELS for diseases (DISEASE MODELS, ANIMAL) and to clarify the functions of the genes.DNA Primers: Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.Urea: A compound formed in the liver from ammonia produced by the deamination of amino acids. It is the principal end product of protein catabolism and constitutes about one half of the total urinary solids.Hypertonic Solutions: Solutions that have a greater osmotic pressure than a reference solution such as blood, plasma, or interstitial fluid.Arabidopsis: A plant genus of the family BRASSICACEAE that contains ARABIDOPSIS PROTEINS and MADS DOMAIN PROTEINS. The species A. thaliana is used for experiments in classical plant genetics as well as molecular genetic studies in plant physiology, biochemistry, and development.Gene Expression Regulation: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.Cell Size: The quantity of volume or surface area of CELLS.Morula: An early embryo that is a compact mass of about 16 BLASTOMERES. It resembles a cluster of mulberries with two types of cells, outer cells and inner cells. Morula is the stage before BLASTULA in non-mammalian animals or a BLASTOCYST in mammals.Sodium-Potassium-Chloride Symporters: A subclass of symporters that specifically transport SODIUM CHLORIDE and/or POTASSIUM CHLORIDE across cellular membranes in a tightly coupled process.DNA, Complementary: Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.Epithelial Cells: Cells that line the inner and outer surfaces of the body by forming cellular layers (EPITHELIUM) or masses. Epithelial cells lining the SKIN; the MOUTH; the NOSE; and the ANAL CANAL derive from ectoderm; those lining the RESPIRATORY SYSTEM and the DIGESTIVE SYSTEM derive from endoderm; others (CARDIOVASCULAR SYSTEM and LYMPHATIC SYSTEM) derive from mesoderm. Epithelial cells can be classified mainly by cell shape and function into squamous, glandular and transitional epithelial cells.Quercus: A plant genus of the family FAGACEAE that is a source of TANNINS. Do not confuse with Holly (ILEX).Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.Protein Conformation: The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).Zea mays: A plant species of the family POACEAE. It is a tall grass grown for its EDIBLE GRAIN, corn, used as food and animal FODDER.Molecular Dynamics Simulation: A computer simulation developed to study the motion of molecules over a period of time.Acclimatization: Adaptation to a new environment or to a change in the old.Phylogeny: The relationships of groups of organisms as reflected by their genetic makeup.Hydroxyethyl Starch Derivatives: Starches that have been chemically modified so that a percentage of OH groups are substituted with 2-hydroxyethyl ether groups.Sodium Chloride: A ubiquitous sodium salt that is commonly used to season food.

The cystic fibrosis transmembrane conductance regulator activates aquaporin 3 in airway epithelial cells. (1/184)

Enhanced osmotic water permeability has been observed in Xenopus oocytes expressing cystic fibrosis transmembrane conductance regulator (CFTR) protein. Subsequent studies have shown that CFTR activates an endogenous water permeability in oocytes, but that CFTR itself is not the water channel. Here, we show CFTR-dependent activation of endogenous water permeability in normal but not in cystic fibrosis human airway epithelial cells. Cell volume was measured by novel confocal x-z laser scanning microscopy. Glycerol uptake and antisense studies suggest CFTR-dependent regulation of aquaporin 3 (AQP3) water channels in airway epithelial cells. Regulatory interaction was confirmed by coexpression of CFTR and AQP3 cloned from human airways in Xenopus oocytes and of CFTR and rat AQP3 in Chinese hamster ovary cells. These findings indicate that CFTR is a regulator of AQP3 in airway epithelial cells.  (+info)

Transport of water and glycerol in aquaporin 3 is gated by H(+). (2/184)

Aquaporins (AQPs) were expressed in Xenopus laevis oocytes in order to study the effects of external pH and solute structure on permeabilities. For AQP3 the osmotic water permeability, L(p), was abolished at acid pH values with a pK of 6.4 and a Hill coefficient of 3. The L(p) values of AQP0, AQP1, AQP2, AQP4, and AQP5 were independent of pH. For AQP3 the glycerol permeability P(Gl), obtained from [(14)C]glycerol uptake, was abolished at acid pH values with a pK of 6.1 and a Hill coefficient of 6. Consequently, AQP3 acts as a glycerol and water channel at physiological pH, but predominantly as a glycerol channel at pH values around 6.1. The pH effects were reversible. The interactions between fluxes of water and straight chain polyols were inferred from reflection coefficients (sigma). For AQP3, water and glycerol interacted by competing for titratable site(s): sigma(Gl) was 0.15 at neutral pH but doubled at pH 6.4. The sigma values were smaller for polyols in which the -OH groups were free to form hydrogen bonds. The activation energy for the transport processes was around 5 kcal mol(-1). We suggest that water and polyols permeate AQP3 by forming successive hydrogen bonds with titratable sites.  (+info)

Renal expression of aquaporins in liver cirrhosis induced by chronic common bile duct ligation in rats. (3/184)

Semiquantitative immunoblotting was used to investigate the expression levels of the four major renal aquaporins, the Na-K-2Cl cotransporter of the thick ascending limb, the type 3 Na-H exchanger, and the Na-K-ATPase in kidneys from rats with cirrhosis secondary to common bile duct ligation (CBDL). These rats had significant water retention and hyponatremia. In contrast to models of cirrhosis induced by carbon tetrachloride, aquaporin-2 expression in CBDL-induced cirrhosis was decreased. Thus, these results show that in the setting of extracellular fluid volume expansion, excessive water retention with hyponatremia can occur in the absence of increases in aquaporin-2 abundance. In addition, the expression levels of the two basolateral collecting duct aquaporins (aquaporin-3 and -4) were decreased in CBDL rats relative to sham-operated control rats. Similarly, the Na-K-2Cl cotransporter of the thick ascending limb and the type 3 Na-H exchanger showed decreases in expression. In contrast, the expression levels of aquaporin-1 and the all subunit of the Na-K-ATPase were not decreased. Thus, dysregulation of multiple water channels and ion transporters may play a role in water balance abnormalities associated with CBDL-induced cirrhosis in rats.  (+info)

Functional characterization and localization of AQP3 in the human colon. (4/184)

Water channels or aquaporins (AQPs) have been identified in a large variety of tissues. Nevertheless, their role in the human gastrointestinal tract, where their action is essential for the reabsorption and secretion of water and electrolytes, is still unclear. The purpose of the present study was to investigate the structure and function of water channels expressed in the human colon. A cDNA fragment of about 420 bp with a 98% identity to human AQP3 was amplified from human stomach, small intestine and colon by reverse transcription polymerase chain reaction (RT-PCR) and a transcript of 2.2 kb was expressed more abundantly in colon than in jejunum, ileum and stomach as indicated by Northern blots. Expression of mRNA from the colon of adults and children but not from other gastrointestinal regions in Xenopus oocytes enhanced the osmotic water permeability, and the urea and glycerol transport in a manner sensitive to an antisense AQP3 oligonucleotide, indicating the presence of functional AQP3. Immunocytochemistry and immunofluorescence studies in human colon revealed that the AQP3 protein is restricted to the villus epithelial cells. The immunostaining within these cells was more intense in the apical than in the basolateral membranes. The presence of AQP3 in villus epithelial cells suggests that AQP3 is implicated in water absorption across human colonic surface cells.  (+info)

The role of aquaporins in dendritic cell macropinocytosis. (5/184)

Immature dendritic cells (DCs) constitutively take up large volumes of fluid by macropinocytosis and concentrate the macrosolutes in the endocytic compartment. This concentration mechanism that is the basis of their high capacity to present soluble antigens requires that DCs be capable of rapidly exchanging water across their membranes. We report that two members of the aquaporin family, AQP3 and AQP7, are expressed in immature DCs and are downregulated after maturation. Treatment of DCs with p-chloromercuribenzenesulphonate (pCMBS), a mercuric drug that blocks aquaporins, inhibited uptake and concentration of macrosolutes taken up by fluid phase endocytosis and led to dramatic cell swelling. In contrast, pCMBS did not affect receptor-mediated endocytosis via the mannose receptor. These findings indicate that aquaporins represent essential elements of a volume control mechanism that allows DCs to concentrate macrosolutes taken up via macropinocytosis.  (+info)

Nephrogenic diabetes insipidus in mice lacking aquaporin-3 water channels. (6/184)

Aquaporin-3 (AQP3) is a water channel expressed at the basolateral plasma membrane of kidney collecting-duct epithelial cells. The mouse AQP3 cDNA was isolated and encodes a 292-amino acid water/glycerol-transporting glycoprotein expressed in kidney, large airways, eye, urinary bladder, skin, and gastrointestinal tract. The mouse AQP3 gene was analyzed, and AQP3 null mice were generated by targeted gene disruption. The growth and phenotype of AQP3 null mice were grossly normal except for polyuria. AQP3 deletion had little effect on AQP1 or AQP4 protein expression but decreased AQP2 protein expression particularly in renal cortex. Fluid consumption in AQP3 null mice was more than 10-fold greater than that in wild-type litter mates, and urine osmolality (<275 milliosmol) was much lower than in wild-type mice (>1,200 milliosmol). After 1-desamino-8-d-arginine-vasopressin administration or water deprivation, the AQP3 null mice were able to concentrate their urine partially to approximately 30% of that in wild-type mice. Osmotic water permeability of cortical collecting-duct basolateral membrane, measured by a spatial filtering optics method, was >3-fold reduced by AQP3 deletion. To test the hypothesis that the residual concentrating ability of AQP3 null mice was due to the inner medullary collecting-duct water channel AQP4, AQP3/AQP4 double-knockout mice were generated. The double-knockout mice had greater impairment of urinary-concentrating ability than did the AQP3 single-knockout mice. Our findings establish a form of nephrogenic diabetes insipidus produced by impaired water permeability in collecting-duct basolateral membrane. Basolateral membrane aquaporins may thus provide blood-accessible targets for drug discovery of aquaretic inhibitors.  (+info)

Aquaporin 3 cloned from Xenopus laevis is regulated by the cystic fibrosis transmembrane conductance regulator. (7/184)

The cystic fibrosis transmembrane conductance regulator (CFTR) is essential for epithelial electrolyte transport and has been shown to be a regulator of epithelial Na(+), K(+), and Cl(-) channels. CFTR also enhances osmotic water permeability when activated by cAMP. This was detected initially in Xenopus oocytes and is also present in human airway epithelial cells, however, the mechanisms remain obscure. Here, we show that CFTR activates aquaporin 3 expressed endogenously and exogenously in oocytes of Xenopus laevis. The interaction requires stimulation of wild type CFTR by cAMP and an intact first nucleotide binding domain as demonstrated for other CFTR-protein interactions.  (+info)

Dysregulation of renal aquaporins and Na-Cl cotransporter in CCl4-induced cirrhosis. (8/184)

BACKGROUND: Severe hepatic cirrhosis is associated with abnormal renal water retention. METHODS: Semiquantitative immunoblotting was employed to investigate the abundance of the major renal aquaporins (water channels) and sodium-dependent cotransporters in kidneys from control rats and rats with cirrhosis secondary to chronic CCl4 inhalation. RESULTS: The cirrhotic rats had ascites and manifested a water excretion defect detected by a standard water-loading test. The abundance of aquaporin-1 (the major aquaporin in the proximal tubule) was increased, an effect markedly accentuated in high-density membrane fractions prepared by differential centrifugation. Differential centrifugation studies demonstrated a redistribution of aquaporin-2 from high-density to low-density membranes, compatible with increased trafficking of aquaporin-2 to the plasma membrane. The abundance of aquaporin-3, but not aquaporin-2, was increased in collecting ducts of rats with CCl4-induced cirrhosis. The Na-K-2Cl cotransporter of the thick ascending limb showed no change in abundance. However, the abundance of the thiazide-sensitive Na-Cl cotransporter of the distal convoluted tubule was markedly suppressed in cirrhotic rats, possibly contributing to a defect in urinary dilution. CONCLUSIONS: In this model of cirrhosis, the development of a defect in urinary dilution may be multifactorial, with contributions from at least four abnormalities in transporter regulation: (1) an increase in the renal abundance of aquaporin-1, (2) a cellular redistribution of aquaporin-2 in the collecting duct compatible with trafficking to the plasma membrane without an increase in total cellular aquaporin-2, (3) an increase in the renal abundance of aquaporin-3, and (4) a decrease in the abundance of the thiazide-sensitive cotransporter of the distal convoluted tubule.  (+info)

IJMS | Free Full-Text | Lipopolysaccharide Modifies Glycerol Permeability and Metabolism in 3T3-L1 AdipocytesIJMS | Free Full-Text | Lipopolysaccharide Modifies Glycerol Permeability and Metabolism in 3T3-L1 Adipocytes
Aquaglyceroporins-aquaporin membrane channels (AQP) that conduct glycerol and other small neutral solutes in addition to water-play major roles in obesity. In adipocytes, aquaglyceroporins mediate glycerol uptake and release across the plasma membrane, which are two key steps for triacylglycerols (TAGs) synthesis (lipogenesis) and hydrolysis (lipolysis). The aim of this study was to assess both glycerol permeability and metabolism in undifferentiated 3T3-L1 cells (UDCs) as well as in untreated (CTL-DCs) versus lipopolysaccharide (LPS-DCs)-treated differentiated 3T3-L1 adipocytes. Glycerol release, TAGs content and whole membrane glycerol permeability were significantly increased in DCs as compared to UDCs. Moreover, in DCs, LPS treatment significantly increased TAGs content and decreased glycerol permeability. In addition, a significant reduction in whole membrane glycerol permeability was observed in LPS-DCs as compared to CTL-DCs. The relative contributions of AQP3, AQP7 and AQP9 (facilitated
Molecular Exchange through the Vesicle Membrane of Siloxane Surfactant in Water/Glycerol Mixed SolventsMolecular Exchange through the Vesicle Membrane of Siloxane Surfactant in Water/Glycerol Mixed Solvents
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AQP10 Polyclonal Antibody, Biotin Conjugated | EpiGentekAQP10 Polyclonal Antibody, Biotin Conjugated | EpiGentek
Background Water channel required to promote glycerol permeability and water transport across cell membranes. May contribute to water transport in the upper portion of small intestine. Isoform 2 is not permeable to urea and...
GFIT result for T02297GFIT result for T02297
Glycerol-3-phosphate ABC transporter, permease protein UgpA (TC 3.A.1.1.3; K17321 glycerol transport system substrate-binding ...
Aquaporin 2 - WikipediaAquaporin 2 - Wikipedia
AQP2 is found in the apical cell membranes of the kidneys collecting duct principal cells and in intracellular vesicles located throughout the cell. It is the only aquaporin regulated by vasopressin. The basic job of aquaporin 2 is to reabsorb water from the urine while its being removed from the blood by the kidney. Aquaporin 2 is in kidney epithelial cells and usually lies dormant in intracellular vesicle membranes. When it is needed, vasopressin binds to the cell surface vasopressin receptor thereby activating a signaling pathway that causes the aquaporin 2 containing vesicles to fuse with the plasma membrane, so the aquaporin 2 can be used by the cell. This aquaporin is regulated in two ways by the peptide hormone vasopressin: short-term regulation (minutes) through trafficking of AQP2 vesicles to the apical region where they fuse with the apical plasma membrane long-term regulation (days) through an increase in AQP2 gene expression. This aquaporin is also regulated by food intake. Fasting ...
Gentaur Molecular :FabGennix \ Aquaporin 4, FITC conjugates \ AQP4-FITCGentaur Molecular :FabGennix \ Aquaporin 4, FITC conjugates \ AQP4-FITC
Gentaur molecular products has all kinds of products like :search , FabGennix \ Aquaporin 4, FITC conjugates \ AQP4-FITC for more molecular products just contact us
Gentaur Molecular :FabGennix \ Aquaporin 8, Host species: Rabbit, Polyclonal antibody \ AQP-801APGentaur Molecular :FabGennix \ Aquaporin 8, Host species: Rabbit, Polyclonal antibody \ AQP-801AP
Gentaur molecular products has all kinds of products like :search , FabGennix \ Aquaporin 8, Host species: Rabbit, Polyclonal antibody \ AQP-801AP for more molecular products just contact us
Aquaporin 4 - wikidocAquaporin 4 - wikidoc
Aquaporin 4 is found in the basolateral cell membrane of principal collecting duct cells and provide a pathway for water to exit these cells. AQP4 is constitutively expressed. AQP4 is expressed in astrocytes and are upregulated by direct insult to the central nervous system. ...
Expression and subcellular localization of aquaporin water channels in the polarized hepatocyte cell line, WIF-B<...Expression and subcellular localization of aquaporin water channels in the polarized hepatocyte cell line, WIF-B<...
TY - JOUR. T1 - Expression and subcellular localization of aquaporin water channels in the polarized hepatocyte cell line, WIF-B. AU - Gradilone, Sergio A.. AU - Tietz, Pamela S.. AU - Splinter, Patrick L.. AU - Marinelli, Raúl A.. AU - LaRusso, Nicholas F.. PY - 2005/8/18. Y1 - 2005/8/18. N2 - Background: Recent data suggest that canalicular bile secretion involves selective expression and coordinated regulation of aquaporins (AQPs), a family of water channels proteins. In order to further characterize the role of AQPs in this process, an in vitro cell system with retained polarity and expression of AQPs and relevant solute transporters involved in bile formation is highly desirable. The WIF-B cell line is a highly differentiated and polarized rat hepatoma/human fibroblast hybrid, which forms abundant bile canalicular structures. This cell line has been reported to be a good in vitro model for studying hepatocyte polarity. Results: Using RT-PCR, immunoblotting and confocal immunofluorescence, ...
Aquaporin water channels in liver: their significance in bile formation. | Semantic ScholarAquaporin water channels in liver: their significance in bile formation. | Semantic Scholar
Semantic Scholar extracted view of Aquaporin water channels in liver: their significance in bile formation. by Raúl Alberto Marinelli et al.
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Aquaporin (AQP) 6 belongs to the aquaporin water channel family. Unlike other aquaporins, AQP6 functions not as a water channel but as an anion-selective channel. Single-channel analyses have shown AQP6 to flicker rapidly ...
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Aquaporin (AQP) 6 belongs to the aquaporin water channel family. Unlike other aquaporins, AQP6 functions not as a water channel but as an anion-selective channel. Single-channel analyses have shown AQP6 to flicker rapidly ...
PublicationsPublications
Resveratrol and gallic acid were co-loaded in phospholipid vesicles aiming at protecting the skin from external injuries, such as oxidative stress and microbial infections. Liposomes were prepared using biocompatible phospholipids dispersed in water. To improve vesicle stability and applicability, the phospholipids and the phenols were dispersed in water/propylene glycol or water/glycerol, thus obtaining PEVs and glycerosomes, respectively. The vesicles were characterized by size, morphology, physical stability, and their therapeutic efficacy was investigated in vitro. The vesicles were spherical, unilamellar and small in size: liposomes and glycerosomes were around 70 nm in diameter, while PEVs were larger (∼170 nm). The presence of propylene glycol or glycerol increased the viscosity of the vesicle systems, positively affecting their stability. The ability of the vesicles to promote the accumulation of the phenols (especially gallic acid) in the skin was demonstrated, as well as their ...
Aquaporin 1 Summary Report | CureHunterAquaporin 1 Summary Report | CureHunter
Aquaporin 1: Aquaporin 1 forms a water-specific channel that is constitutively expressed at the PLASMA MEMBRANE of ERYTHROCYTES and KIDNEY TUBULES, PROXIMAL. It provides these cells with a high permeability to WATER. In humans polymorphisms of this protein result in the Colton blood group antigen.
Aquaporin A/S ProfileAquaporin A/S Profile
Aquaporin A/S is a global cleantech company located in Kongens Lyngby, Denmark. Aquaporin is dedicated to revolutionizing water purification through the use of industrial biotechn
Aquaporin-8Aquaporin-8
Aquaporin 8 (AQP8) is a water channel protein. Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). Aquaporin 8 mRNA is found in pancreas and colon but not other tissues. [provided by RefSeq, Jul 2008 ...
Plasma Membrane Abundance of Human Aquaporin 5 Is Dynamically Regulated by Multiple Pathways - pdf descargarPlasma Membrane Abundance of Human Aquaporin 5 Is Dynamically Regulated by Multiple Pathways - pdf descargar
Plasma Membrane Abundance of Human Aquaporin 5 Is Dynamically Regulated by Multiple Pathways. . Biblioteca virtual para leer y descargar libros, documentos, trabajos y tesis universitarias en PDF. Material universiario, documentación y tareas realizadas por universitarios en nuestra biblioteca. Para descargar gratis y para leer online.
Visualizing gene expression with MRIVisualizing gene expression with MRI
The researchers showed that this technique was successful in monitoring gene expression in a brain tumor in mice. After implanting the tumor, they gave the mice a drug to trigger the tumor cells to express the aquaporin reporter gene, which made the tumor look darker in MRI images.. "Overexpression of aquaporin has no negative impact on cells because it is exclusive to water and simply allows the molecules to go back and forth across the cell membrane," Shapiro says. Under normal physiological conditions the number of water molecules entering and exiting an aquaporin-expressing cell is the same, so that the total amount of water in each cell does not change. "Aquaporin is a very convenient way to genetically change the way that cells look under MRI.". Though the work was done in mice, it has the potential for clinical translation, according to Shapiro. Aquaporin is a naturally occurring gene and will not cause an immune reaction. Previously developed reporter genes for MRI have been much more ...
Portal - Browse - Keyword - A | aquaporinPortal - Browse - Keyword - A | aquaporin
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Publications | Max Planck Institute for Biophysical ChemistryPublications | Max Planck Institute for Biophysical Chemistry
Stahlberg, H.; Braun, T.; de Groot, B. L.; Philippsen, A.; Borgnia, M. J.; Agre, P.; Kuehlbrandt, W.; Engel, A.: The 6.9Å Structure of GlpF: A Basis for Homology Modeling of the Glycerol Channel from Escherichia coli. Journal of Structural Biology 132, pp. 133 - 141 (2000 ...
Aquaporin water channels in liver: Their significance in bile formation - Marinelli - 2003 - Hepatology - Wiley Online LibraryAquaporin water channels in liver: Their significance in bile formation - Marinelli - 2003 - Hepatology - Wiley Online Library
Marinelli RA, Pham L, Agre P, La Russo NF. Secretin promotes osmotic water transport in rat cholangiocytes by incresing aquaporin-1 water channels in plasma membrane. Evidence for a secretin-induced vesicular translocation of aquaporin-1. J Biol Chem 1997; 272: 12984-12988 ...
Structure of a Nobel-prize winning molecule: AquaporinStructure of a Nobel-prize winning molecule: Aquaporin
After producing a recombinant form of AqpZ in E. coli, the proteins were crystallized--capturing five water molecules inside--and then analyzed by state-of-the-art high-resolution X-ray diffraction techniques. The architecture of aquaporin Z is typical of aquaporins, with a spiral of eight oxygens providing water-binding sites inside the channel. The outer membrane and cytoplasmic ends of the channel are wider than the interior, which is long and narrow. This structure demonstrates that aquaporin selectivity arises in part from erecting a physical barrier: small molecules, like water, can easily pass, but larger ones simply cant fit. And the strategic positioning of amino acid residues with hydrophilic or hydrophobic properties along the channel helps police the influx of molecules based on their affinity for water. While it seems two amino acid chains located in the middle of the channel also provide a water-friendly surface, Stroud et al. say they play a more intriguing role. Noting that the ...
Aquaporin 11/12 (IPR016697) | InterPro | EMBL-EBIAquaporin 11/12 (IPR016697) | InterPro | EMBL-EBI
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
OriGene - Aqp4 (BC024526) cDNA CloneOriGene - Aqp4 (BC024526) cDNA Clone
Aqp4 - Aqp4 (untagged) - Mouse aquaporin 4 (cDNA clone MGC:37514 IMAGE:4985265), (10ug) available for purchase from OriGene - Your Gene Company.
AQP5 - WikipediaAQP5 - Wikipedia
Aquaporin-5 is a protein that in humans is encoded by the AQP5 gene. Aquaporin 5 (AQP5) is a water channel protein. Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). Aquaporin 5 plays a role in the generation of saliva, tears and pulmonary secretions. AQP0, AQP2, AQP5, and AQP6 are closely related and all map to 12q13. Aquaporin GRCh38: Ensembl release 89: ENSG00000161798 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000044217 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse PubMed Reference:". Lee MD, Bhakta KY, Raina S, Yonescu R, Griffin CA, Copeland NG, Gilbert DJ, Jenkins NA, Preston GM, Agre P (Jun 1996). "The human Aquaporin-5 gene. Molecular characterization and chromosomal localization". J Biol Chem. 271 (15): 8599-604. doi:10.1074/jbc.271.15.8599. PMID 8621489. "Entrez Gene: AQP5 aquaporin 5". Verkman AS (2003). "Role of aquaporin water channels in eye function". Exp. Eye Res. 76 (2): 137-43. ...
Aquaporin | DesalinationAquaporin | Desalination
With Aquaporin Inside™ Reverse Osmosis membranes, water treatment can be done with lower energy consumption compared to conventional membrane technology. The benefit comes from the aquaporin proteins which are very efficient in transporting water. This enables the water treatment plant to increase the capacity of treated wastewater without increasing the energy consumption, or remaining at the same capacity level while lowering the energy consumption. At the same time, Aquaporin membranes has the potential to remove also small, neutral compounds such as micro pollutants/trace organics, improving re-use water quality.. Aquaporin Inside™ Forward Osmosis ...
Aquaporin1 - What does Aquaporin1 stand for? The Free DictionaryAquaporin1 - What does Aquaporin1 stand for? The Free Dictionary
Looking for online definition of Aquaporin1 or what Aquaporin1 stands for? Aquaporin1 is listed in the Worlds largest and most authoritative dictionary database of abbreviations and acronyms
Estrogen prevents increased hepatic aquaporin-9 expression and glycerol uptake during starvation. | IRIS Univ. BariEstrogen prevents increased hepatic aquaporin-9 expression and glycerol uptake during starvation. | IRIS Univ. Bari
In starvation, glycerol is released from adipose tissue and serves as an important precursor for hepatic gluconeogenesis. By unknown gender-specific mechanisms, women suppress the endogenous glucose production better than men and respond to metabolic stress with higher plasma glycerol levels. Hepatic glycerol uptake is facilitated by aquaporin-9 (AQP9), a broad-selectivity neutral solute channel, and represents an insulin-regulated step in supplying gluconeogenesis with glycerol. In the current study, hepatic AQP9 abundance was increased 2.6-fold in starved male rats as assessed by immunoblotting and immunohistochemistry. By contrast, starvation had no significant effect on hepatic AQP9 expression in female rats. Coordinately, plasma glycerol levels remained unchanged upon starvation in male rats whereas it was increased in female rats. The different responses to starvation were paralleled by higher glycerol permeability in basolateral hepatocyte membranes from starved male rats as compared to ...
Aquaporin membrane protein, molecular model - Stock Image C035/5236 - Science Photo LibraryAquaporin membrane protein, molecular model - Stock Image C035/5236 - Science Photo Library
Aquaporin membrane protein, molecular model. Computer illustration showing the structure of a molecule of the human aquaporin 1 protein (blue, and white ribbon). Aquaporins are membrane proteins that form channels (centre) that help water molecules (red and white spheres) pass in and out of cells. Unlike ion channels, aquaporins help prevent ions and other dissolved substances carrying electrical charge from entering the cell, as they only allow lone water molecules or certain uncharged solutes to pass through. This helps maintain the electrochemical potential of the cell membrane. - Stock Image C035/5236
Aquaporin 11, a regulator of water efflux at retinal Müller glial cell surface decreases concomitant with immune-mediated...Aquaporin 11, a regulator of water efflux at retinal Müller glial cell surface decreases concomitant with immune-mediated...
Müller glial cells are important regulators of physiological function of retina. In a model disease of retinal inflammation and spontaneous recurrent uveitis in horses (ERU), we could show that retinal Müller glial cells significantly change potassium and water channel protein expression during autoimmune pathogenesis. The most significantly changed channel protein in neuroinflammatory ERU was aquaporin 11 (AQP11). Aquaporins (AQP, 13 members) are important regulators of water and small solute transport through membranes. AQP11 is an unorthodox member of this family and was assigned to a third group of AQPs because of its difference in amino acid sequence (conserved sequence is only 11 %) and especially its largely unknown function. In order to gain insight into the distribution, localization, and function of AQP11 in the retina, we first developed a novel monoclonal antibody for AQP11 enabling quantification, localization, and functional studies. In the horse retina, AQP11 was exclusively expressed
ALZFORUM | NETWORKING FOR A CUREALZFORUM | NETWORKING FOR A CURE
I think it will be found that aquaporin 3 will be the item of interest (1).. Aquaporin 3 is found in normal skeletal myofibres (2).. I suspect it will be found that the problem is not a mutation, but something interfering with the normal proper function of the aqp3 channels.. Aquaporin 3 is, in addition to being a water channel, also an arsenic transporter.. Arsenic has been implicated in Alzheimers in at least a few instances. For example, this statement appears in Reference 3 below:. Arsenic can induce apoptosis in cortical neurons of rats. This process is based on the activation of JNK3 and p38 MAPK by arsenic...[which] can activate p38 MAPK and JNK3..... And the title of the last paper speaks for itself: "Arsenic exposure may be a risk factor for Alzheimers disease.". ...
Anti-Aquaporin 3 AntibodyAnti-Aquaporin 3 Antibody
Polyclonal antibody for AQUAPORIN 3/AQP3 detection. Host: Rabbit.Size: 100μg/vial. Tested applications: IHC-P. Reactive species: Human. AQUAPORIN 3/AQP3 information: Molecular Weight: 31544 MW; Subcellular Localization: Basolateral cell membrane; Multi-pa
anti-Aquaporin 10 antibody, C-term | GeneTexanti-Aquaporin 10 antibody, C-term | GeneTex
Aquaporin 10 antibody, C-term (aquaporin 10) for WB. Anti-Aquaporin 10 pAb (GTX45889) is tested in Human samples. 100% Ab-Assurance.
Aquaporin expression and function in human pluripotent stem cell -derived retinal pigment epithelial cells | IOVS | ARVO...Aquaporin expression and function in human pluripotent stem cell -derived retinal pigment epithelial cells | IOVS | ARVO...
Purpose: The expression of aquaporin water channel genes are shown to be affected in several pathological conditions of retina, such as in diabetic retinopathy, retinal ischemia and in autoimmune uveitis. Human native retinal pigment epithelial (RPE) cells and immortalized human RPEs are formerly shown to express aquaporins, still the expression of aquaporins in stem cell derived RPE have not been previously elucidated. The objective of this study was to determine the expression of several aquaporin genes (aquaporin1,- 3, -4, -5, -6, -7, -10, -11 and -12) and assess the localization of aquaporin 1 water channel protein in human embryonic (hESCs) and induced pluripotent stem cells (hiPSCs) derived RPE cells.. Methods: hESC- and hiPSC derived RPE cells were grown as monolayer in serum-free media. The expression of aquaporin genes was determined with qRT-PCR. The localization of AQP1-protein was studied with confocal microscopy. Finally, the functionality of aquaporins was assessed with dye ...
The Plasma Membrane of Arabidopsis thaliana Contains a Mercury-Insensitive Aquaporin That Is a Homolog of the Tonoplast Water...The Plasma Membrane of Arabidopsis thaliana Contains a Mercury-Insensitive Aquaporin That Is a Homolog of the Tonoplast Water...
Plant cells contain proteins that are members of the major intrinsic protein (MIP) family, an ancient family of membrane channel proteins characterized by six membrane-spanning domains and two asparagine-proline-alanine (NPA) amino acid motifs in the two halves of the protein. We recently demonstrated that [gamma]-TIP, one of the MIP homologs found in the vacuolar membrane of plant cells, is an aquaporin or water channel protein (C. Maurel, J. Reizer, J.I. Schroeder, M.J. Chrispeels [1993] EMBO J 12: 2241-2247). RD28, another MIP homolog in Arabidopsis thaliana, was first identified as being encoded by a turgor-responsive transcript. To find out if RD28 is a water channel protein, rd28 cRNA was injected into Xenopus laevis oocytes. Expression of RD28 caused a 10- to 15-fold increase in the osmotic water permeability of the oocytes, indicating that the protein creates water channels in the plasma membrane of the oocytes and is an aquaporin just like its homolog [gamma]-TIP. Although RD28 has ...
Aquaporin-3 facilitates epidermal cell migration and proliferation during wound healing<...Aquaporin-3 facilitates epidermal cell migration and proliferation during wound healing<...
TY - JOUR. T1 - Aquaporin-3 facilitates epidermal cell migration and proliferation during wound healing. AU - Hara-Chikuma, Mariko. AU - Verkman, A. S.. PY - 2008/2/1. Y1 - 2008/2/1. N2 - Healing of skin wounds is a multi-step process involving the migration and proliferation of basal keratinocytes in epidermis, which strongly express the water/glycerol-transporting protein aquaporin-3 (AQP3). In this study, we show impaired skin wound healing in AQP3-deficient mice, which results from distinct defects in epidermal cell migration and proliferation. In vivo wound healing was ∼80% complete in wild-type mice at 5 days vs ∼50% complete in AQP3 null mice, with remarkably fewer proliferating, BrdU-positive keratinocytes. After AQP3 knock-down in keratinocyte cell cultures, which reduced cell membrane water and glycerol permeabilities, cell migration was slowed by more than twofold, with reduced lamellipodia formation at the leading edge of migrating cells. Proliferation of AQP3 knock-down ...
Molecular Basis of pH and Ca2+ Regulation of Aquaporin Water Permeability | JGPMolecular Basis of pH and Ca2+ Regulation of Aquaporin Water Permeability | JGP
This paper strongly supports the conclusion that AQP0 has a high permeability mode and a low permeability mode. How do these two modes differ? Available structural data on the nature of the water-filled pore through AQP1 and the glycerol facilitator suggest a possible answer. For both, water and glycerol must move through the pore by single-file diffusion. The crystal structure and molecular dynamic simulations suggest that there are multiple water molecules in the pore. There are ∼6 waters seen in the narrow constriction of the pore in the X-ray structure (Sui et al., 2001), and molecular dynamic simulations suggest that there are ∼7 or 8 water molecules moving in concert in the single-file portion of the pore (Tajkhorshid et al., 2002; Zhu et al., 2004). The lack of passage of ionic current through AQP0 and AQP1 is explained by electrostatic considerations that strongly inhibit the movement of protons into the NPA region or hydroxyls into regions flanking either side of the NPA region (de ...
Evidence for the Expression of Aquaporin 5 in the Mammalian Conjunctival Epithelium | IOVS | ARVO JournalsEvidence for the Expression of Aquaporin 5 in the Mammalian Conjunctival Epithelium | IOVS | ARVO Journals
Purpose: : To demonstrate in the conjunctiva the presence of aquaporin type 5 (AQP5), a water channel homologue found in the apical membrane of several tissues including the cornea. Presently, there are no reports indicating as to which AQP might be expressed apically in the conjunctiva; only AQP3 has been identified in the lateral membranes of rat and human conjunctival epithelia. Because we had data from gene-expression microarray assays (Turner; ARVO 2004) indicating message for AQP5 in the human conjunctiva, tissue samples from human, as well as from rats and rabbits (given the ease of their procurement), were analyzed to confirm that the AQP5 protein was indeed expressed in mammalian conjunctivae. Methods: : Goat polyclonal IgG against AQP5 was purchased commercially and used in immunoblotting and immunohistochemical techniques to identify and localize the water channel in rat, rabbit and human epithelia. Results: : Immunoblot analysis of rabbit bulbar-plus-palpebral plasma membrane ...
Aquaporin-3 in Keratinocytes and Skin: Its Role and Interaction With Phospholipase D2Aquaporin-3 in Keratinocytes and Skin: Its Role and Interaction With Phospholipase D2
Aquaporin 3 (AQP3) is an aquaglyceroporin that transports water and glycerol and is expressed in the epidermis, among other epithelial tissues. We have recently shown that there is an association between this glycerol channel and phospholipase D2 (PLD2) in caveolin-rich membrane microdomains. While …
Nadia Skauli - Institutt for medisinske basalfagNadia Skauli - Institutt for medisinske basalfag
Stahl, Katja; Rahmani, Soulmaz; Prydz, Agnete; Skauli, Nadia; MacAulay, Nanna; Mylonakou, Maria-Niki; Torp, Reidun; Skare, Øivind; Berg, Torill; Leergaard, Trygve Brauns; Paulsen, Ragnhild Elisabeth; Ottersen, Ole Petter & Amiry-Moghaddam, Mahmood (2018). Targeted deletion of the aquaglyceroporin AQP9 is protective in a mouse model of Parkinsons disease. PLOS ONE. ISSN 1932-6203. 13(3) . doi: 10.1371/journal.pone.0194896 Fulltekst i vitenarkiv. Vis sammendrag More than 90% of the cases of Parkinsons disease have unknown etiology. Gradual loss of dopaminergic neurons of substantia nigra is the main cause of morbidity in this disease. External factors such as environmental toxins are believed to play a role in the cell loss, although the cause of the selective vulnerability of dopaminergic neurons remains unknown. We have previously shown that aquaglyceroporin AQP9 is expressed in dopaminergic neurons and astrocytes of rodent brain. AQP9 is permeable to a broad spectrum of substrates including ...
DataCite SearchDataCite Search
Objective: It is well known that VEGFR expression is correlated with peritumoral brain edema in meningiomas. Also Aquaporin4 seems to induce the perifocal edema. In our study we analyzed the correlation of VEGFR1, VEGFR2 and Aquaporin4 to the brain edema. Additionally a potential correlation between[for full text, please go to the a.m. URL ...
Are aquaporin 4 antibodies appear in any other context than Devics syndrom?Are aquaporin 4 antibodies appear in any other context than Devic's syndrom?
Hi, Bit more than a month ago my mom developed burning sensation on her back and stomach, she went to a doc but he said its nothing lifetreatening and she waited for for her turn for the tests, it was like this for a week or two. Few weeks ago the burning sensation became too much to bear and my mom went to a hospital. They took her in and the next day she had issues walking and day later she couldnt walk on her own at all. After a few days they put her on some steroid IV thing for
Are aquaporin 4 antibodies appear in any other context than Devics syndrom?Are aquaporin 4 antibodies appear in any other context than Devic's syndrom?
Hi, Bit more than a month ago my mom developed burning sensation on her back and stomach, she went to a doc but he said its nothing lifetreatening and she waited for for her turn for the tests, it was like this for a week or two. Few weeks ago the burning sensation became too much to bear and my mom went to a hospital. They took her in and the next day she had issues walking and day later she couldnt walk on her own at all. After a few days they put her on some steroid IV thing for
The Gonen Lab: Structure GalleryThe Gonen Lab: Structure Gallery
PDB 2B6O, EMDB 2973 - 1.9Å resolutuion electron crystallography structure of the water channel Aquaporin-0 in its closed state. ...
The zebrafish genome encodes the largest vertebrate repertoire of functional aquaporins with dual paralogy and substrate...The zebrafish genome encodes the largest vertebrate repertoire of functional aquaporins with dual paralogy and substrate...
Background: Aquaporins are integral membrane proteins that facilitate the transport of water and small solutes across cell membranes. These proteins are vital for maintaining water homeostasis in living organisms. In mammals, thirteen aquaporins (AQP0-12) have been characterized, but in lower vertebrates, such as fish, the diversity, structure and substrate specificity of these membrane channel proteins are largely unknown. Results: The screening and isolation of transcripts from the zebrafish (Danio rerio) genome revealed eighteen sequences structurally related to the four subfamilies of tetrapod aquaporins, i.e., aquaporins (AQP0, -1 and -4), water and glycerol transporters or aquaglyceroporins (Glps; AQP3 and AQP7-10), a water and urea transporter (AQP8), and two unorthodox aquaporins (AQP11 and -12). Phylogenetic analyses of nucleotide and deduced amino acid sequences demonstrated dual paralogy between teleost and human aquaporins. Three of the duplicated zebrafish isoforms have unlinked ...
Anti-PIP2-7 | plasma membrane aquaporin antibodiesAnti-PIP2-7 | plasma membrane aquaporin antibodies
plasma membrane intrinsic protein 2-7, PIP2;7, plasma membrane intrinsic protein 3, salt stress-induced major intrinsic protein, P93004, Q9ATM4 Plasma membrane aquaporin, PIP2;7 is water channel protein required for water transport across cell membrane
KAKEN - Researchers | KITAGAWA Motoji (80262898)KAKEN - Researchers | KITAGAWA Motoji (80262898)
Affiliation：Nagoya University of Arts and Sciences,栄養学部,教授, Research Field：Gastroenterology,Gastroenterology,General physiology, Keywords：CFTR,単離小葉間膵管,膵導管細胞,5-hydroxytriptamine,水チャネル,HCO_3^-分泌,aquaporin,Na^+-HCO_3^-共輸送体,pancreatic duct cell,細胞内Cl^-濃度, # of Research Projects：9, # of Research Products：0
Arsenic transport by zebrafish aquaglyceroporins | BMC Molecular Biology | Full TextArsenic transport by zebrafish aquaglyceroporins | BMC Molecular Biology | Full Text
Arsenic is one of the most ubiquitous toxins and endangers the health of tens of millions of humans worldwide. It is a mainly a water-borne contaminant. Inorganic trivalent arsenic (AsIII) is one of the major species that exists environmentally. The transport of AsIII has been studied in microbes, plants and mammals. Members of the aquaglyceroporin family have been shown to actively conduct AsIII and its organic metabolite, monomethylarsenite (MAsIII). However, the transport of AsIII and MAsIII in in any fish species has not been characterized. In this study, five members of the aquaglyceroporin family from zebrafish (Danio rerio) were cloned, and their ability to transport water, glycerol, and trivalent arsenicals (AsIII and MAsIII) and antimonite (SbIII) was investigated. Genes for at least seven aquaglyceroporins have been annotated in the zebrafish genome project. Here, five genes which are close homologues to human AQP3, AQP9 and AQP10 were cloned from a zebrafish cDNA preparation. These genes were
We investigated the in vivo ramifications of a book aquaporin 4We investigated the in vivo ramifications of a book aquaporin 4
... (AQP4) inhibitor 2-(nicotinamide)-1,3,4-thiadiazole, TGN-020, inside a mouse style of focal cerebral ischemia using 7. research convincingly exhibited that pretreatment using the AQP4 inhibitor TGN-020 considerably reduced the quantity of mind edema connected with ischemic damage. Ischemic edema is usually thought to be initiated by influx of Na+ connected with energy failing. Higher osmolarity circumstances create the generating force for drinking water influx into cells, leading to ionic edema [17]. This early edema stage, so-called cytotoxic edema, is certainly thought to last a long time before mass leakage of drinking water into the human brain ensues, making so-called vasogenic edema [18]. AQP4 is certainly thought to play a substantial function in the real drinking water flux in both procedures. Flux through AQP4 is certainly buy 154992-24-2 bidirectional and solely reliant on osmolarity distinctions between your two spaces ...
Involvement of aquaporin in thromboxane A<sub>2</sub> receptor-mediated, G<sub>12/13</sub>/RhoA/NHE-sensitive cell swelling in...Involvement of aquaporin in thromboxane A<sub>2</sub> receptor-mediated, G<sub>12/13</sub>/RhoA/NHE-sensitive cell swelling in...
TY - JOUR. T1 - Involvement of aquaporin in thromboxane A2 receptor-mediated, G12/13/RhoA/NHE-sensitive cell swelling in 1321N1 human astrocytoma cells. AU - Saito, Masaki. AU - Tanaka, Hiroyuki. AU - Sasaki, Masako. AU - Kurose, Hitoshi. AU - Nakahata, Norimichi. PY - 2010/1/1. Y1 - 2010/1/1. N2 - The physiological role of the thromboxane A2 (TXA2) receptor expressed on glial cells remains unclear. We previously reported that 1321N1 human astrocytoma cells pretreated with dibutyryl cyclic AMP (dbcAMP) became swollen in response to U46619, a TXA2 analogue. In the present study, we examined the detailed mechanisms of TXA2 receptor-mediated cell swelling in 1321N1 cells. The cell swelling caused by U46619 was suppressed by expression of p115-RGS, an inhibitory peptide of Gα12/13 pathway and C3 toxin, an inhibitory protein for RhoA. The swelling was also inhibited by treatment with Y27632, a Rho kinase inhibitor and 5-(ethyl-N-isopropyl)amiloride (EIPA), a Na+/H+-exchanger inhibitor. Furthermore, ...
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EGFR-mediated expression of aquaporin-3 is involved in human s...EGFR-mediated expression of aquaporin-3 is involved in human s...
EGFR-mediated expression of aquaporin-3 is involved in human skin fibroblast migration: AQP3 (aquaporin-3), known as an integral membrane channel in epidermal k
Anti-Aquaporin 3/AQP3 Antibody | KO Validated | Alomone LabsAnti-Aquaporin 3/AQP3 Antibody | KO Validated | Alomone Labs
Anti-Aquaporin 3 Antibody (#AQP-003) from Alomone Labs is a highly specific rabbit polyclonal Ab directed against an epitope of rat AQP3. Applications: IFC, IHC, IP, WB. Free samples available. Control antigen included. Lyophilized. Global shipping at room temperature. Your top supplier for aquaporin research!
KAKEN - Researchers | SATO Shinya (50468047)KAKEN - Researchers | SATO Shinya (50468047)
Affiliation：University of Miyazaki,Faculty of Medicine,Assistant, Research Field：Otorhinolaryngology, Keywords：Aquaporin,生体分子,Dexamethasone,lippopolysaccaride,Immunohistocemistru,免疫染色法,嗅覚,パッチクランプ,難聴,モータ蛋白, # of Research Projects：3, # of Research Products：39
IJMS | Free Full-Text | Fragment Screening of Human Aquaporin 1IJMS | Free Full-Text | Fragment Screening of Human Aquaporin 1
Aquaporins (AQPs) are membrane proteins that enable water transport across cellular plasma membranes in response to osmotic gradients. Phenotypic analyses have revealed important physiological roles for AQPs, and the potential for AQP water channel modulators in various disease states has been proposed. For example, AQP1 is overexpressed in tumor microvessels, and this correlates with higher metastatic potential and aggressiveness of the malignancy. Chemical modulators would help in identifying the precise contribution of water channel activity in these disease states. These inhibitors would also be important therapeutically, e.g., in anti-cancer treatment. This perceived importance contrasts with the lack of success of high-throughput screens (HTS) to identify effective and specific inhibitors of aquaporins. In this paper, we have screened a library of 1500
Differential expression of Kir4.1 and aquaporin 4 in the retina from endotoxin-induced uveitis rat. | Sigma-AldrichDifferential expression of Kir4.1 and aquaporin 4 in the retina from endotoxin-induced uveitis rat. | Sigma-Aldrich
Sigma-Aldrich offers abstracts and full-text articles by [Xiao-Qiang Liu, Hideyuki Kobayashi, Zi-Bing Jin, Akihiko Wada, Nobuhis Nao-I].
TCDB » SEARCHTCDB » SEARCH
Aquaporin-1 or Aquaporin1, Aqp1, of 258 aas and 6 TMSs. Three Aqp1 isoforms are differentially regluated by the function of the vasotocin (AVTR) and isotocin (ITR) receptors (Martos-Sitcha et al. 2015). Aqp1aa, one of two isoforms in teleosts, may play a role in spermatogenesis in Cynoglossus semilaevis (Guo et al. 2017 ...
AnatomyOrganismsDiseasesChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesDisciplines and OccupationsTechnology, Industry, AgricultureHumanitiesInformation Science
Aquaporin 1Aquaporin 5Aquaporin 3Aquaporin 4AquaporinsAquaporin 2Aquaporin 6WaterMercuric ChlorideOsmosisAquaglyceroporinsBlood Group AntigensWater-Electrolyte BalanceGlycerolPermeabilityCell Membrane PermeabilityPlant TranspirationKidney Tubules, CollectingKidney Concentrating AbilityDiabetes Insipidus, NephrogenicPlant ProteinsIon ChannelsNeuromyelitis OpticaPolyuriaBiological TransportXenopus laevisOsmotic PressureOocytesAntidiuretic AgentsMolecular Sequence DataTulipaVapor PressureAmino Acid SequenceCistaceaePlant RootsBrain EdemaMercury CompoundsCell MembraneMembrane ProteinsLens, CrystallineGene Expression Regulation, PlantEye ProteinsBody WaterRenal AgentsAnguillaOsmolar ConcentrationVasopressinsImmunohistochemistryDehydrationRNA, MessengerGlomeromycotaMicroscopy, Electron, Scanning TransmissionSalivary GlandsMyceliumDeamino Arginine VasopressinPropylene GlycolMesophyll CellsMesembryanthemumKidney MedullaKidneySubmandibular GlandReceptors, VasopressinDroughtsAstrocytesReverse Transcriptase Polymerase Chain ReactionXenopusMercuryGene ExpressionNobel PrizeRats, Sprague-DawleySpinacia oleraceaGlycerol KinaseProtein TransportPichiaFragariaRats, BrattleboroPlant StomataProteolipidsBlotting, WesternSaline Solution, HypertonicAntimony Potassium TartratePlant LeavesBase SequenceMalpighian TubulesGlial Fibrillary Acidic ProteinSequence Homology, Amino AcidRNA, ComplementaryImmunoblottingPhloretinMicroscopy, ImmunoelectronModels, MolecularFreezingSolute Carrier Family 12, Member 14-ChloromercuribenzenesulfonateMice, KnockoutDNA PrimersUreaHypertonic SolutionsArabidopsisGene Expression RegulationCell SizeMorulaSodium-Potassium-Chloride SymportersDNA, ComplementaryEpithelial CellsQuercusCloning, MolecularProtein ConformationZea maysMolecular Dynamics SimulationAcclimatizationPhylogenyHydroxyethyl Starch DerivativesSodium Chloride
PLD2PLD2
Zheng X, Bollinger Bollag W (December 2003). "Aquaporin 3 colocates with phospholipase d2 in caveolin-rich membrane ... 467 (2-3): 326-32. doi:10.1016/s0014-5793(00)01174-1. PMID 10675563. Kim JH, Lee S, Park JB, Lee SD, Kim JH, Ha SH, Hasumi K, ... 467 (2-3): 326-32. doi:10.1016/S0014-5793(00)01174-1. PMID 10675563. Lee C, Kim SR, Chung JK, Frohman MA, Kilimann MW, Rhee SG ... N-(2-(1-(3-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]decan-8-yl)ethyl)-2-naphthamide: 75-fold selective versus PLD1, IC50 = 20 ...
Caveolin 1Caveolin 1
Zheng, Xiangjian; Bollinger Bollag Wendy (December 2003). "Aquaporin 3 colocates with phospholipase d2 in caveolin-rich ... 467 (2-3): 326-32. doi:10.1016/S0014-5793(00)01174-1. ISSN 0014-5793. PMID 10675563. Vargas, Leonardo; Nore Beston F; Berglof ... 56 (3): 355-6. doi:10.1006/geno.1998.5723. PMID 10087206. "Entrez Gene: CAV1 caveolin 1, caveolae protein, 22kDa". Li, Shengwen ...
GLUT1GLUT1
... and aquaporin-1 in human erythrocyte membrane domains". Biochimica et Biophysica Acta. 1828 (3): 956-66. doi:10.1016/j.bbamem. ... 18 (3): 183-93. doi:10.1080/09687680110072140. PMID 11681785.. *. Baumann MU, Deborde S, Illsley NP (October 2002). "Placental ... Other mutations, like GLY314SER, ALA275THR, ASN34ILE, SER95ILE, ARG93TRP, ARG91TRP, a 3-bp insertion (TYR292) and a 12-bp ... Certain mutations, like GLY286ASP and a 3-bp deletion in ILE435/436, cause Stomatin-deficient cryohydrocytosis with neurologic ...
Wernickes encephalopathyWernicke's encephalopathy
... and the Aquaporin 4 channel. Focal lactic acidosis also causes secondary oedema, oxidative stress, inflammation and white ... 17 (3): 348-55. doi:10.1111/j.1468-1331.2009.02917.x. PMID 20050893. Kondo, K.; Fujiwara, M.; Murase, M.; Kodera, Y.; Akiyama, ... 55 (1-3): 129-35. doi:10.1016/j.neuint.2009.02.020. PMID 19428817. Hazell AS, Todd KG, Butterworth RF (June 1998). "Mechanisms ... 42 (3): 226-31. doi:10.1136/jnnp.42.3.226. PMC 490724 . PMID 438830. Torviket al., 1982; Blansjaar and Van Dijk, 1992 Lana- ...
Glymphatic systemGlymphatic system
Two types of aquaporins are expressed in the CNS: aquaporin-1, which is expressed by specialized epithelial cells of the ... Aquaporins are membrane-bound channels that play critical roles in regulating the flux of water into and out of cells. Relative ... Aquaporin-4 expression in astrocytes is highly polarized to the endfoot processes ensheathing the cerebral vasculature. Up to ... Yool AJ (2007). "Aquaporins: multiple roles in the central nervous system". Neuroscientist. 13 (5): 470-85. doi:10.1177/ ...
Major intrinsic proteinsMajor intrinsic proteins
The MIP superfamily includes three subfamilies: aquaporins, aquaglyceroporins and S-aquaporins. The aquaporins (AQPs) are water ... Aquaporin-1 (Aqp1) from the human red blood cell has been solved by electron crystallography to 3.8 Å resolution (PDB: 1FQY​). ... Aquaporins generally have the NPA motif in both halves, the glycerol facilitators generally have an NPA motif in the first ... Roles of aquaporins in human cancer have been reviewed as have their folding pathways. AQPs may act as transmembrane ...
Marine lifeMarine life
Agre, P (2006). "The aquaporin water channels". Proceedings of the American Thoracic Society. 3 (1): 5-13. doi:10.1513/pats. ... For about 3 billion years, most organisms were microscopic, and bacteria and archaea were the dominant forms of life. Although ... 29 (3): 456-463. doi:10.1016/j.ympev.2003.07.018. ISSN 1055-7903. PMID 14615186. Mayhew, Peter J. (August 2007). "Why are there ... 47 (3): 370-382. Bibcode:1980E&PSL..47..370M. doi:10.1016/0012-821X(80)90024-2. ISSN 0012-821X. Schopf, J. William; Kudryavtsev ...
Аквапорин-1 - ВікіпедіяАквапорин-1 - Вікіпедія
Аквапорин-1, AQP1 (англ. Aquaporin 1 (Colton blood group)) - білок, який кодується геном AQP1, розташованим у людей на ... de Groot B.L., Engel A., Grubmueller H. (2001). A refined structure of human aquaporin-1.. FEBS Lett. 504: 206 - 211. PubMed ... AQP1, AQP-CHIP, CHIP28, CO, aquaporin 1 (Colton blood group). Зовнішні ІД. OMIM: 107776 MGI: 103201 HomoloGene: 68051 GeneCards ... Сполуки, які фізично взаємодіють з Aquaporin 1 переглянути/редагувати посилання на ВікіДаних. ...
Syndrome of inappropriate antidiuretic hormone secretionSyndrome of inappropriate antidiuretic hormone secretion
... via activation of aquaporins, the site of the ADH receptors - back into the circulation. This has two consequences. First, in ... aquaporin 2), and their insertion into the cells' luminal membranes. Excessive ADH causes an inappropriate increase in the ... "Physiology and pathophysiology of renal aquaporins". Seminars in nephrology. 21 (3): 231-8. doi:10.1053/snep.2001.21647. PMID ... inherited mutations that cause aquaporins always to be "turned on"; and 6) miscellaneous largely transient conditions. ...
Wernicke encephalopathyWernicke encephalopathy
... and the Aquaporin 4 channel.[47] Focal lactic acidosis also causes secondary oedema, oxidative stress, inflammation and white ... 50 (3): 329-33. doi:10.1590/S0004-282X1992000300012. PMID 1308411.. *^ a b Xin, Y.; Wan, D. H.; Chu, Q.; Li, A. M.; Gao, X. J ... WE is more likely to occur in males than females.[35] Among the minority who are diagnosed, mortality can reach 17%.[3] The ... When it occurs simultaneously with alcoholic Korsakoff syndrome it is known as Wernicke-Korsakoff syndrome.[2][3] ...
List of MeSH codes (D12.776.157)List of MeSH codes (D12.776.157)
... aquaporin 6 MeSH D12.776.157.530.400.500.040.374 -- aquaporin 1 MeSH D12.776.157.530.400.500.040.437 -- aquaporin 2 MeSH ... aquaporins MeSH D12.776.157.530.400.500.040.249 -- aquaglyceroporins MeSH D12.776.157.530.400.500.040.249.500 -- aquaporin 3 ... D12.776.157.530.400.500.040.468 -- aquaporin 4 MeSH D12.776.157.530.400.500.040.484 -- aquaporin 5 MeSH D12.776.157.530.400.500 ... glucose transporter type 3 MeSH D12.776.157.530.500.500.937 -- glucose transporter type 4 MeSH D12.776.157.530.500.500.968 -- ...
Tricho-hepato-enteric syndromeTricho-hepato-enteric syndrome
... aquaporin 7, sodium iodide symporter and hydrogen potassium adenosine triphosphatase) showed reduced expression or ... Hum Mutat 32(3):277-281. doi:10.1002/humu.21420. Hartley JL, Zachos NC, Dawood B, Donowitz M, Forman J, Pollitt RJ, Morgan NV, ... 57 (3): 212-6. doi:10.1136/adc.57.3.212. PMC 1627586 . PMID 7073301. Goulet O, Vinson C, Roquelaure B, Brousse N, Bodemer C, ... 3: 6. doi:10.1186/1750-1172-3-6. PMC 2279108 . PMID 18304370. Verloes A, Lombet J, Lambert Y, et al. (February 1997). "Tricho- ...
Index of biophysics articlesIndex of biophysics articles
Mershin Andrew Huxley Animal locomotion Animal locomotion on the water surface Anita Goel Antiporter Aquaporin 2 Aquaporin 3 ... Aquaporin 4 Archibald Hill Ariel Fernandez Arthropod exoskeleton Arthropod leg Avery Gilbert BEST2 BK channel Bacterial outer ... alpha 3 Cyclic nucleotide-gated channel alpha 4 Cyclic nucleotide-gated ion channel Cyclic nucleotide gated channel beta 3 Cys- ... Aggregate modulus Aharon Katzir Alan Lloyd Hodgkin Alexander Rich Alexander van Oudenaarden Allan McLeod Cormack Alpha-3 beta-4 ...
List of MeSH codes (D12.776.543)List of MeSH codes (D12.776.543)
... aquaporin 6 MeSH D12.776.543.550.425.730.040.374 -- aquaporin 1 MeSH D12.776.543.550.425.730.040.437 -- aquaporin 2 MeSH ... aquaporin 6 MeSH D12.776.543.585.400.730.040.436 -- aquaporin 1 MeSH D12.776.543.585.400.730.040.530 -- aquaporin 2 MeSH ... aquaporins MeSH D12.776.543.550.425.730.040.249 -- aquaglyceroporins MeSH D12.776.543.550.425.730.040.249.500 -- aquaporin 3 ... aquaporins MeSH D12.776.543.585.400.730.040.249 -- aquaglyceroporins MeSH D12.776.543.585.400.730.040.249.500 -- aquaporin 3 ...
AquaporinAquaporin
The gating of an aquaporin is carried out by an interaction between a gating mechanism and the aquaporin, which causes a 3D ... It was not until 1992 that the first aquaporin, 'aquaporin-1' (originally known as CHIP 28), was reported by Peter Agre, of ... There have been two clear examples of diseases identified as resulting from mutations in aquaporins: Mutations in the aquaporin ... aquaporins. In addition to the maintenance of normal cytosolic osmolarity, aquaporins can play a major role in extension growth ...
HyponatremiaHyponatremia
... occurs in one of two ways: either the osmoreceptor-aquaporin feedback loop is overwhelmed, or it is interrupted. ... 163 (3): ITC1-19. doi:10.7326/aitc201508040. PMID 26237763.. *^ a b c d e f g h i j k l m n o Lee, JJ; Kilonzo, K; Nistico, A; ... ISBN 978-3-540-79565-0.. *^ a b c Rondon-Berrios, Helbert; Berl, Tomas (2017). "Vasopressin Receptor Antagonists in ... "Physiology and pathophysiology of renal aquaporins". Seminars in nephrology. 21 (3): 231-8. doi:10.1053/snep.2001.21647. PMID ...
Neuromyelitis opticaNeuromyelitis optica
Aquaporin 4 is found in the astrocytes that surround the blood-brain barrier (BBB), a system responsible for preventing ... In 2005 they identified the aquaporin 4 protein as the target of the disease, and developed a test to aid in the diagnosis of ... These antibodies target the protein aquaporin 4 in the cell membranes of astrocytes which acts as a channel for the transport ... Since the discovery of AQP-4 involvement, some research studies have focused on targeted treatment aimed at anti-aquaporin 4 ...
Aquaporin 3Aquaporin 3
... is found in the basolateral cell membrane of principal collecting duct cells and provide a pathway for water to ... 2005). "Roles of aquaporin-3 water channels in volume-regulatory water flow in a human epithelial cell line". J. Membr. Biol. ... 2007). "Expression of aquaporin 3 in the human prostate". Int. J. Urol. 14 (12): 1088-92; discussion 1092. doi:10.1111/j.1442- ... 2007). "Expression of aquaporin 3 (AQP3) in normal and neoplastic lung tissues". Hum. Pathol. 38 (1): 171-8. doi:10.1016/j. ...
Aquaporin 2Aquaporin 2
It is the only aquaporin regulated by vasopressin. The basic job of aquaporin 2 is to reabsorb water from the urine while its ... This aquaporin is also regulated by food intake. Fasting reduces expression of this aquaporin independently of vasopressin. ... so the aquaporin 2 can be used by the cell. This aquaporin is regulated in two ways by the peptide hormone vasopressin: short- ... Aquaporin 2 is in kidney epithelial cells and usually lies dormant in intracellular vesicle membranes. When it is needed, ...
Aquaporin 4Aquaporin 4
The expression of aquaporin 4 is reliant on the disease stage of TBI. In an acute stage of TBI, the lack of aquaporin 4 causes ... Aquaporin-4, also known as AQP4, is a water channel protein encoded by the AQP4 gene in humans. AQP4 belongs to the aquaporin ... Aquaporin-4 is essential in the formation of memory as well as synaptic plasticity. Other performances that aquaporin-4 is ... "Aquaporin-4 autoimmune syndrome and anti-aquaporin-4 antibody-negative opticospinal multiple sclerosis in Japanese". Multiple ...
Aquaporin 1Aquaporin 1
... at the US National Library of Medicine Medical Subject Headings (MeSH) Gallery of Aquaporin Simulations Human AQP1 ... The gene encoding this aquaporin is a possible candidate for disorders involving imbalance in ocular fluid movement. Aquaporin ... AQP1 aquaporin 1 (Colton blood group)". Knepper MA (1994). "The aquaporin family of molecular water channels". Proc. Natl. Acad ... Aquaporin 1 is a protein that in humans is encoded by the AQP1 gene. AQP1 is a widely expressed water channel, whose ...
AQP6AQP6
The protein encoded by this gene is an aquaporin protein, which functions as a water channel in cells. Aquaporins are a family ... Ikeda M, Beitz E, Kozono D, Guggino WB, Agre P, Yasui M (Oct 2002). "Characterization of aquaporin-6 as a nitrate channel in ... Wang W, Hart PS, Piesco NP, Lu X, Gorry MC, Hart TC (Mar 2003). "Aquaporin expression in developing human teeth and selected ... Aquaporin 6, kidney specific is a protein in humans that is encoded by the AQP6 gene. ...
Andreas EngelAndreas Engel
"Aquaporin water channels - from atomic structure to clinical medicine". The Journal of Physiology. 542 (1): 3-16. doi:10.1113/ ... Fujiyoshi and Engel solved the structure of Aquaporin-1 in collaboration with Agre. Together with Palczewski Engel's team ... 177 (1): 3-13. doi:10.1016/j.jsb.2011.11.013. PMID 22115996. "Farewell Symposium for Andreas Engel". unibas.ch. Retrieved 2015- ...
Lesional demyelinations of the central nervous systemLesional demyelinations of the central nervous system
Around active NMO lesions AQP4 may selectively be lost in the absence of aquaporin 1 (AQP1) loss or other structural damage ( ... 246 (3): 880-6. doi:10.1148/radiol.2463070486. PMID 18195384. Calabrese M, Filippi M, Rovaris M, Mattisi I, Bernardi V, Atzori ... 72 (3): 385-94. doi:10.1002/ana.23621. PMID 23034911. Lucchinetti C. F.; et al. (2008). "Clinical and radiographic spectrum of ... 2 (3): 295-301. doi:10.1002/acn3.164. PMC 4369279 . PMID 25815356. Young NP, Weinshenker BG, Parisi JE, Scheithauer B, Giannini ...
Congenital cataractCongenital cataract
... or Aquaporin, cytoskeletal structural proteins, paired-like homeodomain transcription factor 3 (PITX3), avian ... Any central opacity or surrounding cortical distortion greater than 3 mm can be assumed to be visually significant. Laboratory ...
Category:Blood proteinsCategory:Blood proteins
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AnatomyOrganismsDiseasesChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesDisciplines and OccupationsTechnology, Industry, AgricultureHumanitiesInformation Science
Aquaporin 1Aquaporin 5Aquaporin 3Aquaporin 4AquaporinsAquaporin 2Aquaporin 6WaterMercuric ChlorideOsmosisAquaglyceroporinsBlood Group AntigensWater-Electrolyte BalanceGlycerolPermeabilityCell Membrane PermeabilityPlant TranspirationKidney Tubules, CollectingKidney Concentrating AbilityDiabetes Insipidus, NephrogenicPlant ProteinsIon ChannelsNeuromyelitis OpticaPolyuriaBiological TransportXenopus laevisOsmotic PressureOocytesAntidiuretic AgentsMolecular Sequence DataTulipaVapor PressureAmino Acid SequenceCistaceaePlant RootsBrain EdemaMercury CompoundsCell MembraneMembrane ProteinsLens, CrystallineGene Expression Regulation, PlantEye ProteinsBody WaterRenal AgentsAnguillaOsmolar ConcentrationVasopressinsImmunohistochemistryDehydrationRNA, MessengerGlomeromycotaMicroscopy, Electron, Scanning TransmissionSalivary GlandsMyceliumDeamino Arginine VasopressinPropylene GlycolMesophyll CellsMesembryanthemumKidney MedullaKidneySubmandibular GlandReceptors, VasopressinDroughtsAstrocytesReverse Transcriptase Polymerase Chain ReactionXenopusMercuryGene ExpressionNobel PrizeRats, Sprague-DawleySpinacia oleraceaGlycerol KinaseProtein TransportPichiaFragariaRats, BrattleboroPlant StomataProteolipidsBlotting, WesternSaline Solution, HypertonicAntimony Potassium TartratePlant LeavesBase SequenceMalpighian TubulesGlial Fibrillary Acidic ProteinSequence Homology, Amino AcidRNA, ComplementaryImmunoblottingPhloretinMicroscopy, ImmunoelectronModels, MolecularFreezingSolute Carrier Family 12, Member 14-ChloromercuribenzenesulfonateMice, KnockoutDNA PrimersUreaHypertonic SolutionsArabidopsisGene Expression RegulationCell SizeMorulaSodium-Potassium-Chloride SymportersDNA, ComplementaryEpithelial CellsQuercusCloning, MolecularProtein ConformationZea maysMolecular Dynamics SimulationAcclimatizationPhylogenyHydroxyethyl Starch DerivativesSodium Chloride
Aquaporin 3 - WikipediaAquaporin 3 - Wikipedia
Aquaporin 3 is found in the basolateral cell membrane of principal collecting duct cells and provide a pathway for water to ... 2005). "Roles of aquaporin-3 water channels in volume-regulatory water flow in a human epithelial cell line". J. Membr. Biol. ... 2007). "Expression of aquaporin 3 in the human prostate". Int. J. Urol. 14 (12): 1088-92; discussion 1092. doi:10.1111/j.1442- ... 2007). "Expression of aquaporin 3 (AQP3) in normal and neoplastic lung tissues". Hum. Pathol. 38 (1): 171-8. doi:10.1016/j. ...
en.wikipedia.org
Anti-Aquaporin 3 antibody (ab15117) | AbcamAnti-Aquaporin 3 antibody (ab15117) | Abcam
Rabbit polyclonal Aquaporin 3 antibody. Validated in WB, ELISA, IHC and tested in Rat. Cited in 1 publication(s). Independently ... Primary - Rabbit Anti-Aquaporin 3 antibody (ab15117) WB, ELISA, IHC-Fr Secondary - Goat Anti-Rabbit IgG H&L (HRP) (ab205718) ... Anti-Aquaporin 3 antibody (ab15117). Rabbit polyclonal Aquaporin 3 antibody. Validated in WB, ELISA, IHC and tested in Rat. ... Hi, I would like to know if antibody aquaporin 3 cat#ab15117 is an extracellular antibody and can it be used for FACS? Thanks ...
abcam.com
Anti-Aquaporin 3 antibody (ab15117) | AbcamAnti-Aquaporin 3 antibody (ab15117) | Abcam
Rabbit polyclonal Aquaporin 3 antibody. Validated in WB, ELISA, IHC and tested in Rat. Cited in 1 publication(s). Independently ... Hi, I would like to know if antibody aquaporin 3 cat#ab15117 is an extracellular antibody and can it be used for FACS? Thanks ... Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the ... Predicted molecular weight: 32 kDa.Can be blocked with Aquaporin 3 peptide (ab80550). ...
abcam.com
Aquaporin-3: Regulating Skin Cell GrowthAquaporin-3: Regulating Skin Cell Growth
Two previous articles in this series on aquaporins have discussed their history, mechanism and stimulation. The current article ... Aquaporins (AQPs) are integral membrane proteins that form pores in the membrane of biological cells. At least 13 mammalian ... 4. M Hara-Chikuma and AS Verkman, Roles of Aquaporin-3 in the epidermis, (In press at J Invest Derm) ... For this explanation and for the role that an aquaporin plays, we turn to cell physiologist Wendy B. Bollag, PhD, of the ...
cosmeticsandtoiletries.com
Aquaporin-3 water channel localization and regulation in rat kidney. | Sigma-AldrichAquaporin-3 water channel localization and regulation in rat kidney. | Sigma-Aldrich
Aquaporin-3 water channel localization and regulation in rat kidney.. [C A Ecelbarger, J Terris, G Frindt, M Echevarria, D ... Anti-Water Channel Aquaporin 3 antibody produced in rabbit, affinity isolated antibody pricing ... The aquaporins are a family of water channels expressed in several water-transporting tissues, including the kidney. We have ... affinity-purified polyclonal antibody to aquaporin-3 (AQP-3) to investigate its localization and regulation in the kidney. ...
sigmaaldrich.com
The Correlation between Aquaporin-4 Antibody and the Visual Function of Patients with Demyelinating Optic Neuritis at Onset :...The Correlation between Aquaporin-4 Antibody and the Visual Function of Patients with Demyelinating Optic Neuritis at Onset :...
pediatric cases; #serum from multiple ethnicity of White, Asian, Black, Hispanic, Mestizo, Middle Eastern, and Native Argentinean; ##serum from Austria, Denmark, France, Germany, Italy, and Turkey ...
hindawi.com
Frontiers | Molecular Characterization of Aquaporin 1 and Aquaporin 3 from the Gills of the African Lungfish, Protopterus...Frontiers | Molecular Characterization of Aquaporin 1 and Aquaporin 3 from the Gills of the African Lungfish, Protopterus...
Aquaporins (Aqps) are a superfamily of integral membrane proteins which generally facilitate the permeation of water through ... Aquaporins (Aqps) are a superfamily of integral membrane proteins which generally facilitate the permeation of water through ... Figure 5. The gene expression of (A) aquaporin 1 (aqp1) and (B) aquaporin 3 (aqp3) in various tissues/organs of Protopterus ... Table 1. Primers used for PCR, RACE, and qPCR of aquaporin 1 (aqp1) and aquaporin 3 (aqp3) from the gills of Protopterus ...
frontiersin.org
CiNii 論文 - Tissue Distribution, Effects of Salinity Acclimation, and Ontogeny of Aquaporin 3...CiNii 論文 - Tissue Distribution, Effects of Salinity Acclimation, and Ontogeny of Aquaporin 3...
Immunolocalisation of aquaporin 3 in the gill and the gastrointestinal tract of the European eel Anguilla anguilla (L.) LIGNOT ... Glycosylation is not essential for vasopressin-dependent routing of aquaporin 2 in transfected Madin-Darby canine kidney cells ... Aquaporin-3 expressed in the basolateral membrane of gill chloride cells in Mozambique tilapia Oreochromis mossambicus adapted ... Evidence for stabilization of aquaporin 2 folding mutants by N-linked glycosylation in endoplasmic reticulum BUCK TM ...
ci.nii.ac.jp
Interferon gamma decreases intestinal epithelial aquaporin 3 expression through downregulation of constitutive transcription |...Interferon gamma decreases intestinal epithelial aquaporin 3 expression through downregulation of constitutive transcription |...
Abstract Aquaporin (AQP) 3 expression is altered in inflammatory bowel diseases, although the exact mechanisms regulating AQP ... Zhao G, Li J, Wang J, Shen X, Sun J (2014) Aquaporin 3 and 8 are down-regulated in TNBS-induced rat colitis. Biochem Biophys ... Zhang W, Xu Y, Chen Z, Xu Z, Xu H (2011) Knockdown of aquaporin 3 is involved in intestinal barrier integrity impairment. FEBS ... Aquaporin (AQP) 3 expression is altered in inflammatory bowel diseases, although the exact mechanisms regulating AQP abundance ...
rd.springer.com
The human CFTR protein expressed in CHO cells activates aquaporin-3 in a cAMP-dependent pathway: study by digital holographic...The human CFTR protein expressed in CHO cells activates aquaporin-3 in a cAMP-dependent pathway: study by digital holographic...
2007). Structural basis of aquaporin inhibition by mercury. J. Mol. Biol. 368, 607-617. doi:10.1016/j.jmb.2007.02.070. ... 2000). Aquaporin 3 cloned from Xenopus laevis is regulated by the cystic fibrosis transmembrane conductance regulator. FEBS ... Water transport is associated with an aquaporin, AQP3. The above data with genistein and MBP-91 indicated that Cl− and water ... et al.(2008). Role of NHERF1, cystic fibrosis transmembrane conductance regulator, and cAMP in the regulation of aquaporin 9. J ...
jcs.biologists.org
Relationship of aquaporins 3 (AQP3), 7 (AQP7), and 11 (AQP11) with boar sperm resilience to withstand freeze-thawing procedures...Relationship of aquaporins 3 (AQP3), 7 (AQP7), and 11 (AQP11) with boar sperm resilience to withstand freeze-thawing procedures...
Relationship of aquaporins 3 (AQP3), 7 (AQP7), and 11 (AQP11) with boar sperm resilience to withstand freeze-thawing procedures ... In this context, the hypothesis of this study was that aquaporins AQP3, AQP7, and AQP11 could be linked to boar sperm ...
sigmaaldrich.com
AQP3 / Aquaporin 3 Antibody (C-Terminus) for ELISA, IF/Immunofluorescence,AQP3 / Aquaporin 3 Antibody (C-Terminus) for ELISA, IF/Immunofluorescence,
Aquaporin 3 antibody LS-C3804 is an unconjugated rabbit polyclonal antibody to rat Aquaporin 3 (AQP3). Validated for ELISA, IF ... Aquaporin 3 antibody LS-C3804 is an unconjugated rabbit polyclonal antibody to rat Aquaporin 3 (AQP3). Validated for ELISA, IF ... Aquaporin 3 antibody LS-C3804 is an unconjugated rabbit polyclonal antibody to rat Aquaporin 3 (AQP3). Validated for ELISA, IF ...
lsbio.com
Oscillating Aquaporin Phosphorylation and 14-3-3 Proteins Mediate the Circadian Regulation of Leaf Hydraulics | Plant CellOscillating Aquaporin Phosphorylation and 14-3-3 Proteins Mediate the Circadian Regulation of Leaf Hydraulics | Plant Cell
The circadian fluctuations in aquaporin transcript abundance suggest that aquaporin water channels play a role in these ... 2002). Plasma membrane aquaporins in the motor cells of Samanea saman: Diurnal and circadian regulation. Plant Cell 14: 727-739 ... Oscillating Aquaporin Phosphorylation and 14-3-3 Proteins Mediate the Circadian Regulation of Leaf Hydraulics. Karine Prado, ... 2014). Aquaporins: Highly regulated channels controlling plant water relations. Plant Physiol. 164: 1600-1618. ...
plantcell.org
AQP3 / Aquaporin 3 Antibody (C-Terminus) for ELISA, IHC, WB/WesternAQP3 / Aquaporin 3 Antibody (C-Terminus) for ELISA, IHC, WB/Western
Aquaporin 3 antibody LS-C3802 is an unconjugated rabbit polyclonal antibody to rat Aquaporin 3 (AQP3). Validated for ELISA, IHC ... Aquaporin 3 antibody LS-C3802 is an unconjugated rabbit polyclonal antibody to rat Aquaporin 3 (AQP3). Validated for ELISA, IHC ... Aquaporin 3 antibody LS-C3802 is an unconjugated rabbit polyclonal antibody to rat Aquaporin 3 (AQP3). Validated for ELISA, IHC ... Recognizes rat Aquaporin 3 (AQP3/GLIP). Species sequence homology: mouse 92%, human 85%. ...
lsbio.com
Glycolic acid attenuates UVB-induced aquaporin-3, matrix metalloproteinase-9 expression, and collagen degradation in...Glycolic acid attenuates UVB-induced aquaporin-3, matrix metalloproteinase-9 expression, and collagen degradation in...
aquaporin-3; GA, glycolic acid; IL, interleukin; MAPK, mitogen-activated protein kinase; MCP-1, monocyte chemoattractant ... GA reverted and dose-dependently increased the level of aquaporin-3 (AQP3), the expression of which was down-regulated by UVB. ... Glycolic acid attenuates UVB-induced aquaporin-3, matrix metalloproteinase-9 expression, and collagen degradation in ... Glycolic acid attenuates UVB-induced aquaporin-3, matrix metalloproteinase-9 expression, and collagen degradation in ...
biochemj.org
Anti-Psoriatic Drug Monomethylfumarate Increases Nuclear Factor Erythroid 2-Related Factor 2 Levels and Induces Aquaporin-3...Anti-Psoriatic Drug Monomethylfumarate Increases Nuclear Factor Erythroid 2-Related Factor 2 Levels and Induces Aquaporin-3...
On the other hand, the expression and membranous localization of aquaporin-3 (AQP3), a glycerol channel implicated in ... Anti-Psoriatic Drug Monomethylfumarate Increases Nuclear Factor Erythroid 2-Related Factor 2 Levels and Induces Aquaporin-3 ... Assunto(s): Aquaporina 3/biossíntese Fumaratos/farmacologia Maleatos/farmacologia Fator 2 Relacionado a NF-E2/biossíntese ... Aquaporina 3/genética Sequência de Bases Células Cultivadas Expressão Gênica Queratinócitos/efeitos dos fármacos Queratinócitos ...
pesquisa.bvsalud.org
Aquaporin-3 in Keratinocytes and Skin: Its Role and Interaction With Phospholipase D2Aquaporin-3 in Keratinocytes and Skin: Its Role and Interaction With Phospholipase D2
Aquaporin 3 (AQP3) is an aquaglyceroporin that transports water and glycerol and is expressed in the epidermis, among other ... Aquaporin-3 in Keratinocytes and Skin: Its Role and Interaction With Phospholipase D2 Arch Biochem Biophys. 2011 Apr 15;508(2): ... Aquaporin 3 (AQP3) is an aquaglyceroporin that transports water and glycerol and is expressed in the epidermis, among other ...
pubmed.ncbi.nlm.nih.gov
Oncotarget | Potential role of aquaporin 3 in gastric intestinal metaplasiaOncotarget | Potential role of aquaporin 3 in gastric intestinal metaplasia
Potential role of aquaporin 3 in gastric intestinal metaplasia. Haijian Zhao _, Xiaojun Yang, Yangchun Zhou, Weiming Zhang, Yao ... Keywords: gastric intestinal metaplasia, aquaporin 3, gastric cancer, pathology. Received: June 25, 2015 Accepted: August 30, ... Aquaporin 3 (AQP3) has been found to be expressed in goblet cells rather than mucus-secreting glands. To investigate the ... Haijian Zhao1,2, Xiaojun Yang3, Yangchun Zhou1,4, Weiming Zhang5, Yao Wang1, Jianfei Wen1, Zhihong Zhang5, Lizong Shen1 ...
oncotarget.com
Anti-Aquaporin 3 AntibodyAnti-Aquaporin 3 Antibody
AQUAPORIN 3/AQP3 information: Molecular Weight: 31544 MW; Subcellular Localization: Basolateral cell membrane; Multi-pa ... Polyclonal antibody for AQUAPORIN 3/AQP3 detection. Host: Rabbit.Size: 100μg/vial. Tested applications: IHC-P. Reactive species ... also known as aquaporin 0. Aquaporin 3 is localized at the basal lateral membranes of collecting duct cells in the kidney. In ... Aquaporin-3;AQP-3;Aquaglyceroporin-3;AQP3;. Research Areas. ,signal transduction,metabolism,plasma membrane,channels, ...
bosterbio.com
Aquaporin-3 facilitates epidermal cell migration and proliferation during wound healing<...Aquaporin-3 facilitates epidermal cell migration and proliferation during wound healing<...
Aquaporin-3 facilitates epidermal cell migration and proliferation during wound healing. / Hara-Chikuma, Mariko; Verkman, A. S. ... Aquaporin-3 facilitates epidermal cell migration and proliferation during wound healing. Journal of Molecular Medicine. 2008 ... Hara-Chikuma, M & Verkman, AS 2008, Aquaporin-3 facilitates epidermal cell migration and proliferation during wound healing, ... Hara-Chikuma, Mariko ; Verkman, A. S. / Aquaporin-3 facilitates epidermal cell migration and proliferation during wound healing ...
keio.pure.elsevier.com
Aquaporin-3 (AQP3) Antibody ReviewAquaporin-3 (AQP3) Antibody Review
This type of aquaporin transports not only water but also neutral solutes, including cell-permeating cryoprotectants. PMID: ... Aquaporin-1,3 were widely expressed in the cochlea and endolymphatic sac of guinea pig. PMID: 16494013 ... Aquaporin-3 is expressed in developmental zebrafish embryos (Danio rerio). PMID: 15533783 ... By using immunohistochemical techniques applied to confocal microscopy, the presence of aquaporin 3 water channel in the ...
antibodybeyond.com
Gentaur Molecular :EIAab \ CLIA Aqp3,AQP-3,Aquaglyceroporin-3,Aquaporin-3,Mouse,Mus musculus \ U0581mGentaur Molecular :EIAab \ CLIA Aqp3,AQP-3,Aquaglyceroporin-3,Aquaporin-3,Mouse,Mus musculus \ U0581m
Aquaporin-3,Mouse,Mus musculus \ U0581m for more molecular products just contact us ... Aquaporin-3,Mouse,Mus musculus mus musculus murine CLIA Aqp3,AQP-3,Aquaglyceroporin-3,Aquaporin-3,Mouse,Mus musculus detects ... Aquaporin-3,Mouse,Mus musculus / Product Detail : U0581m CLIA Aqp3,AQP-3,Aquaglyceroporin-3,Aquaporin-3,Mouse,Mus musculus. ... Aquaporin-3,Mouse,Mus musculus. Related products : CLIA Aqp3,AQP-3,Aquaglyceroporin-3,Aquaporin-3,Mouse,Mus musculus ...
antibody-antibodies.com
A subgroup of plant aquaporins facilitate the bi-directional diffusion of As(OH) 3 and Sb(OH) 3 across membranes | BMC Biology ...A subgroup of plant aquaporins facilitate the bi-directional diffusion of As(OH) 3 and Sb(OH) 3 across membranes | BMC Biology ...
Plasmids expressing aquaporin homologs rAQP9, AtNIP5;1, Atnip5;1Δ2-67, AtNIP6;1, Atnip6;1Δ2-29, Atnip6;1Δ2-69, AtNIP7;1 or ... Expression of Arabidopsis aquaporin homologs improves yeast growth in the presence of arsenate (As(V)). Δfps1 Δacr3 Δycf1 ... N-terminal truncation is required for functional expression in yeast of specific Lotus japonicus aquaporin homologs. Δfps1 Δ ... Yeast expressing specific Arabidopsis aquaporin homologs display sensitivity to arsenite (As(III)) and antimonite (Sb(III)). Δ ...
bmcbiol.biomedcentral.com
Recombinant Zea mays Aquaporin NIP2-3(NIP2-3) - CusabioRecombinant Zea mays Aquaporin NIP2-3(NIP2-3) - Cusabio
Purchase Recombinant Zea mays Aquaporin NIP2-3(NIP2-3). It is produced in in vitro E.coli expression system. High purity. Good ... Recombinant Zea mays Aquaporin NIP2-3(NIP2-3),partial ( Yeast-CSB-YP861006ZAX1 E.coli-CSB-EP861006ZAX1 Baculovirus-CSB- ... Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.. ... MIP/aquaporin (TC 1.A.8) family, NIP (TC 1.A.8.12) subfamily. ... Recombinant Zea mays Aquaporin NIP2-3(NIP2-3). *in vitro E.coli ...
cusabio.com
Anti-Aquaporin 3/AQP3 Antibody | KO Validated | Alomone LabsAnti-Aquaporin 3/AQP3 Antibody | KO Validated | Alomone Labs
Anti-Aquaporin 3 Antibody (#AQP-003) from Alomone Labs is a highly specific rabbit polyclonal Ab directed against an epitope of ... The aquaporins can be divided into two functional groups based on their permability characteristics: the aquaporins that are ... Aquaporin 3 (AQP-3) belongs to a family of membrane proteins that allow the passage of water and certain other solutes through ... Anti-Aquaporin 3 Antibody (#AQP-003) is a highly specific antibody directed against an epitope of the rat protein. The antibody ...
alomone.com
AnatomyOrganismsDiseasesChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesDisciplines and OccupationsTechnology, Industry, AgricultureHumanitiesInformation Science
Aquaporin 1Aquaporin 5Aquaporin 3Aquaporin 4AquaporinsAquaporin 2Aquaporin 6WaterMercuric ChlorideOsmosisAquaglyceroporinsBlood Group AntigensWater-Electrolyte BalanceGlycerolPermeabilityCell Membrane PermeabilityPlant TranspirationKidney Tubules, CollectingKidney Concentrating AbilityDiabetes Insipidus, NephrogenicPlant ProteinsIon ChannelsNeuromyelitis OpticaPolyuriaBiological TransportXenopus laevisOsmotic PressureOocytesAntidiuretic AgentsMolecular Sequence DataTulipaVapor PressureAmino Acid SequenceCistaceaePlant RootsBrain EdemaMercury CompoundsCell MembraneMembrane ProteinsLens, CrystallineGene Expression Regulation, PlantEye ProteinsBody WaterRenal AgentsAnguillaOsmolar ConcentrationVasopressinsImmunohistochemistryDehydrationRNA, MessengerGlomeromycotaMicroscopy, Electron, Scanning TransmissionSalivary GlandsMyceliumDeamino Arginine VasopressinPropylene GlycolMesophyll CellsMesembryanthemumKidney MedullaKidneySubmandibular GlandReceptors, VasopressinDroughtsAstrocytesReverse Transcriptase Polymerase Chain ReactionXenopusMercuryGene ExpressionNobel PrizeRats, Sprague-DawleySpinacia oleraceaGlycerol KinaseProtein TransportPichiaFragariaRats, BrattleboroPlant StomataProteolipidsBlotting, WesternSaline Solution, HypertonicAntimony Potassium TartratePlant LeavesBase SequenceMalpighian TubulesGlial Fibrillary Acidic ProteinSequence Homology, Amino AcidRNA, ComplementaryImmunoblottingPhloretinMicroscopy, ImmunoelectronModels, MolecularFreezingSolute Carrier Family 12, Member 14-ChloromercuribenzenesulfonateMice, KnockoutDNA PrimersUreaHypertonic SolutionsArabidopsisGene Expression RegulationCell SizeMorulaSodium-Potassium-Chloride SymportersDNA, ComplementaryEpithelial CellsQuercusCloning, MolecularProtein ConformationZea maysMolecular Dynamics SimulationAcclimatizationPhylogenyHydroxyethyl Starch DerivativesSodium Chloride
AQP3ProteinsProteinPermeabilityPMIDAQP1MembraneLocalizationMembranesGeneAntibodyEpithelial cellsAQP5KeratinocytesMutationsAQPsMolecularAbstractRole of aquaporinNeuromyelitis opticaRenalUreaAquaglyceroporinsPlant aquaporinsKidneyMammalian20011999TissuesCollecting ductHumanVasopressin2018PermeableVesiclesRegulationTransporterEpidermalKeratinocyteRatsFound that aquaporinReceptors2016GenesCellsAQP4PhospholipaseDifferentiationAQP0
AQP318
Proteins31
Protein35
Permeability5
PMID2
  • Aquaporins 11 and 12 are classified as members of a new AQP subfamily: the subcellular AQPs [ PMID: 17178102 ]. (ebi.ac.uk)
  • PMID 3049610 King LS, Choi M, Fernandez PC, Cartron JP, Agre P.Defective urinary-concentrating ability due to a complete deficiency of aquaporin-1. (wikipedia.org)
AQP15
  • Background: The immunohistochemical expression of aquaporin-1 (AQP1) in asbestos-related malignant pleural mesothelioma (MPM) is emerging as a useful prognostic indicator of improved survival. (mdpi.com)
  • A limited number of aquaporins are found within the central nervous system (CNS): AQP1, 3, 4, 5, 8, 9, and 11, but more exclusive representation of AQP1, 4, and 9 are found in the brain and spinal cord. (wikipedia.org)
  • For example, p f for human aquaporin-1 (AQP1) ranges from 1 × 10 −14 to 16 × 10 −14 cm 3 s −1 ( 5 ). (sciencemag.org)
  • Of the nine other aquaporin genes identified in mammals, at least six (AQP1-4, AQP6, and AQP7) are expressed in the kidney ( 3 ), an organ largely devoted to high rates of active fluid transport. (physiology.org)
  • Around active NMO lesions AQP4 may selectively be lost in the absence of aquaporin 1 (AQP1) loss or other structural damage (lesion type 4). (wikipedia.org)
Membrane23
  • Aquaporin 3 is found in the basolateral cell membrane of principal collecting duct cells and provide a pathway for water to exit these cells. (wikipedia.org)
  • Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). (abcam.com)
  • AQP-2 and -3 circumferentially lined the epithelial cell membranes except for the apical membrane of the epithelial cells adjacent to the lumens of both ureter and bladder. (antibodybeyond.com)
  • PIP1;3 is a plasma membrane aquaporine which facilitates trasport of water across cell membrane. (agrisera.com)
  • Regulation of Plasma Membrane Nanodomains of the Water Channel Aquaporin-3 Revealed by Fixed and Live Photoactivated Localization Microscopy. (nih.gov)
  • Aharon R, Shahak Y, Wininger S, Bendov R, Kapulnik Y, Galili G (2003) Overexpression of a plasma membrane aquaporin in transgenic tobacco improves plant vigor under favorable growth conditions but not under drought or salt stress. (springer.com)
  • We hypothesized that aquaporin 3 is involved in the regulation of keratinocyte function by a mechanism involving the interaction between aquaporin 3 and phospholipase D. Using sucrose gradient centrifugation, immunoprecipitation analysis, and confocal microscopy, we found that aquaporin 3 and phospholipase D 2 colocalized in caveolin-rich membrane microdomains. (elsevier.com)
  • Zheng, X & Bollag, WB 2003, ' Aquaporin 3 Colocates with Phospholipase D 2 in Caveolin-Rich Membrane Microdomains and Is Downregulated Upon Keratinocyte Differentiation ', Journal of Investigative Dermatology , vol. 121, no. 6, pp. 1487-1495. (elsevier.com)
  • When it is needed, vasopressin binds to the cell surface vasopressin receptor thereby activating a signaling pathway that causes the aquaporin 2 containing vesicles to fuse with the plasma membrane, so the aquaporin 2 can be used by the cell. (wikipedia.org)
  • This aquaporin is regulated in two ways by the peptide hormone vasopressin: short-term regulation (minutes) through trafficking of AQP2 vesicles to the apical region where they fuse with the apical plasma membrane long-term regulation (days) through an increase in AQP2 gene expression. (wikipedia.org)
  • The aquaporin-4 tetramers accumulate to transform into orthogonal arrays of particle (OAPs) in the cell plasma membrane. (wikipedia.org)
  • Membrane topology of aquaporin CHIP. (wikipedia.org)
  • Plasma membrane aquaporin activity can affect the rate of apoptosis but is inhibited after apoptotic volume decrease. (semanticscholar.org)
  • We obtained high-precision p f values by (i) having measured the abundance of the reconstituted aquaporins in the vesicular membrane via fluorescence correlation spectroscopy and via high-speed atomic force microscopy, and (ii) having acquired the vesicular water efflux from scattered light intensities via our new adaptation of the Rayleigh-Gans-Debye equation. (sciencemag.org)
  • Aquaporins are membrane-bound channels that play critical roles in regulating the flux of water into and out of cells. (wikipedia.org)
  • ADH activates V2 receptors on the basolateral membrane of principal cells in the renal collecting duct, initiating a cyclic AMP-dependent process that culminates in increased production of water channels (aquaporin 2), and their insertion into the cells' luminal membranes. (wikipedia.org)
  • 7(1): p. 87-95 Biela, A., K. Grote, B. Otto, S. Hoth, R. Hedrich, and R. Kaldenhoff, The Nicotiana tabacum plasma membrane aquaporin NtAQP1 is mercury-insensitive and permeable for glycerol. (wikipedia.org)
  • Otto, B. and R. Kaldenhoff, Cell-specific expression of the mercury-insensitive plasma-membrane aquaporin NtAQP1 from Nicotiana tabacum. (wikipedia.org)
  • This occurs through increased transcription and insertion of water channels (Aquaporin-2) into the apical membrane of collecting tubule and collecting duct epithelial cells. (wikipedia.org)
  • It works at the level of the renal collecting duct by binding to V2 receptors, which signal for the translocation of aquaporin channels via cytosolic vesicles to the apical membrane of the collecting duct. (wikipedia.org)
  • The presence of these aquaporin channels in the distal nephron causes increasing water reabsorption from the urine, which becomes passively re-distributed from the nephron to systemic circulation by way of basolateral membrane channels. (wikipedia.org)
  • The increased intracellular cAMP in the kidney in turn triggers fusion of aquaporin-2-bearing vesicles with the apical plasma membrane of the collecting duct principal cells, increasing water reabsorption. (wikipedia.org)
  • It is not known how mitochondria maintain osmotic balance across the inner mitochondrial membrane, although the membrane contains aquaporins that are believed to be conduits for regulated water transport. (wikipedia.org)
Localization5
Membranes6
  • Subcellular fractionation of membranes, using progressively higher centrifugation speeds, revealed that AQP-3 is present predominantly in the 4,000 and 17,000 g pellets and, in contrast to AQP-2, is virtually absent in the high-speed (200,000 g) pellet that contains small intracellular vesicles. (sigmaaldrich.com)
  • Aquaporins facilitate the transport of water and small neutral solutes across cell membranes. (cusabio.com)
  • Membranes were washed 5 times with TBS-T, each time in a fresh polystyrene box and probed with anti-PIPs1;3 antibodies (AS09 504, 1:1000 , 1h) and secondary anti-rabbit ( 1:2000, 1 h). (agrisera.com)
  • The cell membranes of a variety of different bacteria, fungi, animal and plant cells contain aquaporins through which water can flow more rapidly into and out of the cell than by diffusing through the phospholipid bilayer. (wikipedia.org)
  • Aquaporin 2 is in kidney epithelial cells and usually lies dormant in intracellular vesicle membranes. (wikipedia.org)
  • Significant water (but not glycerol) transport has been attributed to MIP in lens fiber cell membranes ( 32 ), and this pH- and calcium-sensitive water channel ( 23 ) is commonly referred to as aquaporin-0 (AQP0). (physiology.org)
Gene10
Antibody6
Epithelial cells2
  • Skin dryness alters the ability of epithelial cells to migrate and cover the wound site and reduces the supply of white blood cells and nutrients, which are essentials to form new tissues and protect skin against infections [ 3 ]. (hindawi.com)
  • Two types of aquaporins are expressed in the CNS: aquaporin-1, which is expressed by specialized epithelial cells of the choroid plexus, and aquaporin-4 (AQP4), which is expressed by astrocytes. (wikipedia.org)
AQP51
Keratinocytes3
Mutations3
  • Mutations in HNF1α and HNF4α are the causes of the type 3 and type 1 forms of maturity-onset diabetes of the young (MODY3 and MODY1), a genetic disorder of the insulin-secreting pancreatic beta cells characterized by the onset of diabetes mellitus before 25 years of age and an autosomal dominant pattern of inheritance ( 19 ). (sciencemag.org)
  • Mutations in aquaporin-2 cause diabitis insipidus. (proteopedia.org)
  • Mutations in aquaporin-0 in mice cause congenital cataracts. (proteopedia.org)
AQPs5
Molecular5
Abstract1
Role of aquaporin1
Neuromyelitis optica5
Renal4
  • Long-term regulation of four renal aquaporins in rats. (findaphd.com)
  • What are the 3 parts of the renal tubule? (brainscape.com)
  • This concentration depends on the accumulation of urea in the renal medulla, permitted by an intrarenal recycling of urea among collecting ducts, vasa recta and thin descending limbs, all equipped with specialized, facilitated urea transporters (UTs) (UT-A1 and 3, UT-B, and UT-A2, respectively). (physiology.org)
  • citation needed] Braun, Eldon (April 1998), "Comparative renal function in reptiles, birds, and mammals", Seminars in Avian and Exotic Pet Medicine, 7 (2): 62-71, doi:10.1016/S1055-937X(98)80044-3 Sembulingam, K (2016). (wikipedia.org)
Urea5
  • Aquaporin 7 facilitates water, glycerol and urea transport. (novusbio.com)
  • There are also roles for other water channels, including aquaporins 1, 3, and 4, and for urea transporters in urinary concentration. (asnjournals.org)
  • Humans have 13 different aquaporins that allow water to pass at different speeds and have different selectivity behaviour (e.g. for glycerol and urea). (findaphd.com)
  • and 3 ) species differences among mice, rats, and humans related to their very different body size and metabolic rate, leading to considerably larger needs to excrete and to concentrate urea in smaller species (urea excretion per unit body weight in mice is 5 times that in rats and 23 times that in humans). (physiology.org)
  • Urea transporter 3 transports urea into the interstitium of the Inner Medullary Collecting Duct. (wikipedia.org)
Aquaglyceroporins2
Plant aquaporins2
  • In the present chapter, we discussed roles of plant aquaporins in salinity stress and exploitating the same for genetic engineering approach. (springer.com)
  • Kaldenhoff was one of the first scientists to describe plant aquaporins. (wikipedia.org)
Kidney4
Mammalian3
20011
19992
  • In 1999, together with other research teams, Agre reported the first high-resolution images of the three-dimensional structure of an aquaporin, namely, aquaporin-1. (wikipedia.org)
  • Caselli RJ in 1999 reported five patients, age 54 to 80 years, presented between 3 weeks and 18 months after symptomatic onset of progressive cognitive decline, psychosis, and unsteady gait that proved to be due to a steroid-responsive nonvasculitic autoimmune inflammatory meningoencephalitic syndrome. (wikipedia.org)
Tissues2
Collecting duct2
Human10
Vasopressin4
20185
Permeable2
Vesicles1
  • In contrast to previous findings with AQP-2, there was only limited AQP-3 labeling of intracellular vesicles, suggesting that this water channel is not regulated acutely through vesicular trafficking. (sigmaaldrich.com)
Regulation5
  • Transgenic expression of phosphodeficient and phosphomimetic forms of this aquaporin indicated that At PIP2;1 phosphorylation is necessary but not sufficient for K ros regulation. (plantcell.org)
  • Phosphatidylglycerol, as a bioactive lipid, could potentially mediate the effects of the aquaporin 3-phospholipase D 2 signaling module, with aquaporin 3 as a modulatory unit, in the regulation of keratinocyte function. (elsevier.com)
  • Regulation of aquaporin-2gene transcription by gate-3. (nii.ac.jp)
  • Other performances that aquaporin-4 is involved in are synaptic plasticity, astrocyte migration, regulation of extracellular space volume, and the homeostasis of potassium. (wikipedia.org)
  • Regulation of aquaporin (AQP) water channels in relation to brain edema. (uio.no)
Transporter2
Epidermal2
Keratinocyte2
  • Bollag WB, Xie D, Zheng X, Zhong X (2007) A potential role for the phospholipase D2-aquaporin-3 signaling module in early keratinocyte differentiation: production of a phosphatidylglycerol signaling lipid. (springer.com)
  • Whether aquaporin 3 and its glycerol transporting capacity are involved in regulating keratinocyte function, we have previously shown that phospholipase D 2 can metabolize phospholipids in the presence of glycerol to yield phosphatidylglycerol. (elsevier.com)
Rats3
  • Agren J, Zelenin S, Hakansson M, Eklof AC, Aperia A, Nejsum LN, Nielsen S, Sedin G (2003) Transepidermal water loss in developing rats: role of aquaporins in the immature skin. (springer.com)
  • Both GSK-3β/CRMP2 and CDK5/CRMP2 pathways participate in the protection of dexmedetomidine against propofol-induced learning and memory impairment in neonatal rats. (nih.gov)
  • Aquaporin-4 in Müller cell in rats, transports water to the vitreous body. (wikipedia.org)
Found that aquaporin1
  • I think it will be found that aquaporin 3 will be the item of interest (1). (alzforum.org)
Receptors1
  • Excessive ADH causes an inappropriate increase in the reabsorption in the kidneys of solute-free water ("free water"): excess water moves from the distal convoluted tubules (DCT)s and collecting tubules of the nephrons - via activation of aquaporins, the site of the ADH receptors - back into the circulation. (wikipedia.org)
20161
  • Afzal Z, Howton TC, Sun Y, Mukhtar MS (2016) The roles of aquaporins in plant stress responses. (springer.com)
Genes1
  • Specifically, aquaporin 3 and filaggrin genes were enhanced by 20 and 58%, respectively. (hindawi.com)
Cells9
  • Aquaporins differentially regulate cell-cell adhesion in MDCK cells. (nih.gov)
  • Aquaporin 3 maintains the stemness of CD133+ hepatocellular carcinoma cells by activating STAT3. (nih.gov)
  • Immunocytochemistry showed strong aquaporin (AQP)-4 water channel expression in Müller cells in mouse retina and fibrous astrocytes in optic nerve. (arvojournals.org)
  • In many solid malignancies, including head and neck squamous cell carcinoma (HNSCC), an increased infiltration of cytotoxic CD8 + T cells into the tumor mass is often associated with good prognosis and response to therapy ( 1 - 3 ). (sciencemag.org)
  • Aquaporin 9 changes in pyramidal cells before and is expressed in astrocytes after delayed neuronal death in the ischemic hippocampal CA1 region of the gerbil. (ebi.ac.uk)
  • RNA interference influenced the proliferation and invasion of XWLC-05 lung cancer cells through inhibiting aquaporin 3. (nih.gov)
  • In addition to regulating intracellular and extracellular pH, Na + -coupled HCO − 3 -transport, Na + /H + -exchange, and anion-exchange also contribute to water and electrolyte balance in cells and systemically. (frontiersin.org)
  • Desmopressin (DDAVP) stimulates the release of von Willebrand factor (vWF) from the Weibel-Palade bodies of endothelial cells, thereby increasing the levels of vWF (as well as coagulant factor VIII) 3 to 5-fold. (wikipedia.org)
  • This causes water to flow out from those cells by osmosis through aquaporin channels, making them lose turgor, which is the force that is applied onto the cell wall by water within the cell. (wikipedia.org)
AQP43
  • 3 Studies of brain edema in AQP4-null mice implied an important role for AQP4 in fluid balance, 20 supporting the possibility that AQP4 may participate in the maintenance of retinal water balance during synaptic transmission and retinal edema. (arvojournals.org)
  • In the CNS, AQP4 is the most prevalent aquaporin channel, specifically located at the perimicrovessel astrocyte foot processes, glia limitans, and ependyma. (wikipedia.org)
  • Similar to other aquaporin channels, the monomers of AQP4 assemble into tetramers. (wikipedia.org)
Phospholipase1
Differentiation1
AQP01
  • At 3 wk of age (postnatal day 21 ), lenses from null mice ( Aqp0 −/− ) contained polymorphic opacities, whereas lenses from heterozygous mice ( Aqp0 +/− ) were transparent and did not develop frank opacities until ∼24 wk of age. (physiology.org)