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 18.104.22.168.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.
Long-term regulation of aquaporins in the kidney. (1/216)The discovery of the aquaporin family of water channels has greatly improved our understanding of how water crosses epithelial cells, particularly in the kidney. The study of the mechanisms involved in the regulation of collecting duct water permeability, in particular, has advanced very rapidly since the identification and characterization of aquaporin-2 (AQP2) in 1993. One of the more surprising findings has been the dramatic long-term changes that are seen in the abundance of this protein, as well as the recognition that these changes represent a way of modulating the acute antidiuretic effects of vasopressin. Furthermore, such changes seem to be of etiological and pathological significance in a number of clinical disorders of water balance. This review focuses on the various conditions in which AQP2 expression is altered (either increased or decreased) and on what this can tell us about the signals and mechanisms controlling these changes. Ultimately, this may be of great value in the clinical management of water balance disorders. Evidence is also now beginning to emerge that there are similar changes in the expression of other renal aquaporins, which had previously been thought to provide an essentially constitutive water permeability pathway, suggesting that they too should be considered as regulatory factors in the control of body water balance. (+info)
Vasopressin regulates apical targeting of aquaporin-2 but not of UT1 urea transporter in renal collecting duct. (2/216)In the renal inner medullary collecting duct (IMCD), vasopressin regulates two key transporters, namely aquaporin-2 (AQP2) and the vasopressin-regulated urea transporter (VRUT). Both are present in intracellular vesicles as well as the apical plasma membrane. Short-term regulation of AQP2 has been demonstrated to occur by vasopressin-induced trafficking of AQP2-containing vesicles to the apical plasma membrane. Here, we have carried out studies to determine whether short-term regulation of VRUT occurs by a similar process. Cell surface labeling with NHS-LC-biotin in rat IMCD suspensions revealed that vasopressin causes a dose-dependent increase in the amount of AQP2 labeled at the cell surface, whereas VRUT labeled at the cell surface did not increase in response to vasopressin. Immunoperoxidase labeling of inner medullary thin sections from Brattleboro rats treated with 1-desamino-8-D-arginine vasopressin (DDAVP) for 20 min revealed dramatic translocation of AQP2 to the apical region of the cell, with no change in the cellular distribution of VRUT. In addition, differential centrifugation of inner medullary homogenates from Brattleboro rats treated with DDAVP for 60 min revealed a marked depletion of AQP2 from the low-density membrane fraction (enriched in intracellular vesicles) but did not alter the quantity of VRUT in this fraction. Finally, AQP2-containing vesicles immunoisolated from a low-density membrane fraction from renal inner medulla did not contain immunoreactive VRUT. Thus vasopressin-mediated regulation of AQP2, but not of VRUT, depends on regulated vesicular trafficking to the plasma membrane. (+info)
An impaired routing of wild-type aquaporin-2 after tetramerization with an aquaporin-2 mutant explains dominant nephrogenic diabetes insipidus. (3/216)Autosomal recessive and dominant nephrogenic diabetes insipidus (NDI), a disease in which the kidney is unable to concentrate urine in response to vasopressin, are caused by mutations in the aquaporin-2 (AQP2) gene. Missense AQP2 proteins in recessive NDI have been shown to be retarded in the endoplasmic reticulum, whereas AQP2-E258K, an AQP2 mutant in dominant NDI, was retained in the Golgi complex. In this study, we identified the molecular mechanisms underlying recessive and dominant NDI. Sucrose gradient centrifugation of rat and human kidney proteins and subsequent immunoblotting revealed that AQP2 forms homotetramers. When expressed in oocytes, wild-type AQP2 and AQP2-E258K also formed homotetramers, whereas AQP2-R187C, a mutant in recessive NDI, was expressed as a monomer. Upon co-injection, AQP2-E258K, but not AQP2-R187C, was able to heterotetramerize with wild-type AQP2. Since an AQP monomer is the functional unit and AQP2-E258K is a functional but misrouted water channel, heterotetramerization of AQP2-E258K with wild-type AQP2 and inhibition of further routing of this complex to the plasma membrane is the cause of dominant NDI. This case of NDI is the first example of a dominant disease in which the 'loss-of-function' phenotype is caused by an impaired routing rather than impaired function of the wild-type protein. (+info)
Aquaporin-6: An intracellular vesicle water channel protein in renal epithelia. (4/216)All characterized mammalian aquaporins (AQPs) are localized to plasma membranes where they function chiefly to mediate water transport across cells. Here we show that AQP6 is localized exclusively in intracellular membranes in renal epithelia. By using a polyclonal antibody to the C terminus of AQP6, immunoblots revealed a major 30-kDa band in membranes from rat renal cortex and medulla. Endoglycosidase treatment demonstrated presence of an intracellular high mannose glycan on each subunit. Sequential ultracentrifugation of rat kidney homogenates confirmed that AQP6 resides predominantly in vesicular fractions, and immunohistochemical and immunoelectron microscopic studies confirmed that >98% of AQP6 is located in intracellular membrane vesicles. In glomeruli, AQP6 is present in membrane vesicles within podocyte cell bodies and foot processes. In proximal tubules, AQP6 is also abundant in membrane vesicles within the subapical compartment of segment 2 and segment 3 cells, but was not detected in the brush border or basolateral membranes. In collecting duct, AQP6 resides in intracellular membrane vesicles in apical, mid, and basolateral cytoplasm of type A intercalated cells, but was not observed in the plasma membrane. Unlike other members of the AQP family, the unique distribution in intracellular membrane vesicles in multiple types of renal epithelia indicates that AQP6 is not simply involved in transcellular fluid absorption. Moreover, our studies predict that AQP6 participates in distinct physiological functions such as glomerular filtration, tubular endocytosis, and acid-base metabolism. (+info)
The Cre/loxP system and gene targeting in the kidney. (5/216)The Cre/loxP and Flp/FRT systems mediate site-specific DNA recombination and are being increasingly utilized to study gene function in vivo. These systems allow targeted gene disruption in a single cell type in vivo, thereby permitting study of the physiological and pathophysiological impact of a given gene product derived from a particular cell type. In the kidney, the Cre/loxP system has been employed to achieve gene deletion selectively within principal cells of the collecting duct. Disruption of target genes in the collecting duct, such as endothelin-1 or polycystic kidney disease-1 (PKD1), could lead to important insights into the biological roles of these gene products. With selection of the appropriate renal cell-specific promoters, these recombination systems could be used to target gene disruption to virtually any renal cell type. Although transgenic studies utilizing these recombination systems are promising, they are in their relative infancy and can be time consuming and expensive and yield unanticipated results. It is anticipated that continued experience with these systems will produce an important tool for analyzing gene function in renal health and disease. (+info)
Urinary excretion of aquaporin-2 in rat is mediated by a vasopressin-dependent apical pathway. (6/216)Clinical studies have shown that aquaporin-2 (AQP2), the vasopressin-regulated water channel, is excreted in the urine, and that the excretion increases in response to vasopressin. However, the cellular mechanisms involved in AQP2 excretion are unknown, and it is unknown whether the excretion correlates with AQP2 levels in kidney or levels in the apical plasma membrane. The present study was undertaken to clarify these issues. Immunoblotting of rat urine samples revealed significant excretion of AQP2, whereas AQP3, being a basolateral aquaporin in the same cells, was undetectable. Thus, there was a nonproportional excretion of AQP2 and AQP3 (compared with kidney levels), indicating that AQP2 is excreted predominantly via a selective apical pathway and not by whole cell shedding. Urinary AQP2 was associated with small vesicles, membrane fragments, and multivesicular bodies as determined by immunoelectron microscopy and negative staining techniques. In rats with normal water supply, daily urinary excretion of AQP2 was 3.9+/-0.9% (n = 6) of total kidney expression. Treatment with desmopressin acetate subcutaneously caused a fourfold increase in urinary excretion of AQP2 during 8 h. Forty-eight hours of thirsting, known to increase endogenous vasopressin secretion, resulted in a three-fold increase in kidney AQP2 levels but urinary excretion increased ninefold to 15+/-3% (n = 6) of AQP2 in kidney of thirsted rats. Moreover, rats that were thirsted for 48 h and subsequently allowed free access to water for 24 h produced a decrease in urinary AQP2 excretion to 38+/-15% (n = 6) of that during thirsting. In Brattleboro rats or lithium-treated normal rats completely lacking vasopressin action, and hence having extremely low levels of AQP2 in the apical plasma membrane, AQP2 was undetectable in urine. Thus, conditions with known altered vasopressin levels and altered levels of AQP2 in the apical plasma membrane were associated with corresponding major changes in AQP2 urine excretion. In contrast, in such conditions, kidney AQP2 levels and urinary AQP2 excretion did not show a proportional relationship. (+info)
Effects of missense mutations on rat aquaporin-2 in LLC-PK1 porcine kidney cells. (7/216)BACKGROUND: Mutations in the aquaporin-2 (AQP2) gene have been found in families with nephrogenic diabetes insipidus (NDI), but the pathophysiological mechanisms of how mutant AQP2 causes the disease are still not clear. METHODS: Wild-type (WT) AQP2 and four mutants-T126M, A147T, R187C, and S216P-were transiently expressed in LLC-PK1 cells. The osmotic water permeability of LLC-PK1 cells expressing AQP2 mutants was determined by stopped-flow light-scattering microphotometry. Cell surface expression, subcellular localization, and effects of vasopressin stimulation were examined by surface biotin labeling and confocal immunohistochemistry. RESULTS: The osmotic water permeability (Pf) of cells expressing WT increased significantly after vasopressin treatment, whereas the Pf of cells expressing T126M A147T, R187C, and S216P was not significantly different from that of the control even after vasopressin stimulation. Confocal immunohistochemistry demonstrated distribution of WT and A147T in early/recycling endosomal compartments and vasopressin-responsive translocation and surface expression. In contrast, stainings of T126M, R187C, and S216P were similar to that of Grp78, indicating that these mutants were misassembled and retarded in the endoplasmic reticulum. CONCLUSION: Our results indicated that the intracellular distribution and vasopressin-regulated trafficking of A147T is intact, in contrast to the other three mutants, of which both were impaired. Thus, it is conceivable that the disruption of the AQP2 channel function accounts for the pathogenesis of A147T NDI, whereas trafficking defects account for that of the other types, suggesting that the pathophysiology of AQP2-related NDI is heterogeneous. (+info)
Lack of vasopressin-independent upregulation of AQP-2 gene expression in homozygous Brattleboro rats. (8/216)Arginine vasopressin (AVP) plays an important role in the expression of aquaporin (AQP-2) in the collecting duct. The present study was undertaken to determine whether there is an AVP-independent regulation of AQP-2 gene expression in homozygous Brattleboro rats in which endogenous AVP is absent. Exogenous administration of 1-deamino-8-D-AVP produced an antidiuresis and expressed AQP-2 mRNA and AQP-2 protein in the renal medulla of the homozygous Brattleboro rats. Twelve hours of water deprivation produced severe dehydration in the homozygous Brattleboro rats, such that urinary osmolality increased from 200 to 649 mosmol/kgH(2)O. However, no increase in AQP-2 mRNA expression was observed after this dehydration, and the medullary tissue content and urinary excretion of AQP-2 also remained unchanged. Increases in AQP-2 mRNA expression and AQP-2 protein were evident in Long-Evans rats after 64 h of water deprivation, with a severity of dehydration almost equal to the 12-h dehydrated, homozygous Brattleboro rats. These results indicate the lack of an AVP-independent mechanism for upregulating AQP-2 mRNA expression in renal collecting duct cells. (+info)
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In the kidney, the antidiuretic hormone vasopressin (AVP) is a critical regulator of water homeostasis by controlling the water movement from lumen to the interstitium for water reabsorption and adjusting the urinary water excretion. In normal physiology, AVP is secreted into the circulation by the posterior pituitary gland, in response to an increase in serum osmolality or a decrease in effective circulating volume. When reaching the kidney, AVP binds to V2 receptors on the basolateral surface of the collecting duct epithelium, triggering a G-protein-linked signaling cascade, which leads to water channel aquaporin-2 (AQP2) vesicle insertion into the apical plasma membrane. This results in higher water permeability in the collecting duct and, driven by an osmotic gradient, pro-urinary water then passes the membrane through AQP2 and leaves the cell on the basolateral side via AQP3 and AQP4 water channels, which are constitutively expressed on the basolateral side of these cells. When isotonicity ...
For a proper functioning of epithelial cells, a polarized sorting and localization of channels and transporters that mediate transcellular ion and water movement is essential. Our work focuses on elucidating the routing regulation of wild-type AQP2/V2R, dissolving the underlying mechanisms for missorting of AQP2 mutants, and the identification of pharmacological chaperones, rescuing the cell surface expression of AQP2/V2R mutants in NDI.
Nephrogenic diabetes insipidus is caused by mutations in [[Aquaporin 2,aquaporin 2]]. Usually [[Aquaporin 2,AQP2]] is trafficked to the [[Cell membrane,cell membrane]] where it facilitates the reabsorption of water into the cell. In the diseased state the channels are retained inside the cell resulting in the inability to control the concentration of urine being produced ,ref,The Journal of Cell Biology. (2003). Reversed polarized delivery of an aquaporin-2 mutant causes dominant nephrogenic diabetes insipidus 163(5):1099-109,/ref,.,br ...
In the 1970s-1980s, a number of clearance, micropuncture, and microperfusion studies as well as anatomic-functional correlations have brought a good understanding of the role of urea in the urinary concentrating mechanism (16, 87) (see reviews in Refs. 6 and 50). It has been understood that urea is accumulated and somehow "sequestrated" (104) in the renal medulla at a concentration increasing from the outer medulla to the tip of the papilla. This accumulation results from three associated processes (Fig. 2). 1) Urea becomes progressively concentrated along the CD because of vasopressin-dependent water reabsorption in a segment poorly permeable to urea, thus bringing a highly concentrated urea solution to the terminal CD. 2) A vasopressin-dependent increase in urea permeability of the terminal IMCD (due to UT-A1/3) enables this concentrated urea to be transported into the interstitial tissue of the deep inner medulla. 3) Medullary urea, which continuously tends to escape the inner medulla via the ...
Acquired nephrogenic diabetes insipidus happens when the small tubes or tubules in the kidneys are defective causing a person to eliminate too much water during urination. This occurs because the kidneys do not respond to antidiuretic hormone (ADH)or vasopressin. ADH tells the kidneys to make the urine more concentrated.. Symptoms of acquired nephrogenic diabetes insipidus are extreme thirst especially for ice water and production of large amounts of urine. This commonly occurs because of a problem caused by something else such as blockage in the urinary tract, use of certain medications, high levels of calcium, or low levels of potassium. This acquired nephrogenic diabetes insipidus is an extremely rare form of diabetes. When the cause of this form of diabetes inspidus is identified and corrected, the disease usually clears up. Hereditary nephrogenic diabetes insipidus is treated with fluid intake that matches urine output and medication to lower urine output. Medications used to treat ...
Complications of Nephrogenic diabetes insipidus including hidden complications, secondary medical conditions, symptoms, or other types of Nephrogenic diabetes insipidus complication.
Peptides , Phosphopeptides , Aquaporin-2 (254-267), pSER261, human; This peptide is a fragment of the human aquaporin-2 (AQP2) phosphorylated at Ser261. Protein phosphorylation plays a key role in vasopressin signaling in renal-collecting duct. Phosphorylation at several AQP2 residues including Ser256 and Ser261, is altered in response to vasopressin. It is possible that both sites are involved in vasopressin-dependent AQP2 trafficking.; RQSVELH-pS-PQSLPR; H-Arg-Gln-Ser-Val-Glu-Leu-His-pSer-Pro-Gln- Ser-Leu-Pro-Arg-OH
PDB 2B6O, EMDB 2973 - 1.9Å resolutuion electron crystallography structure of the water channel Aquaporin-0 in its closed state. ...
Nephrogenic diabetes insipidus (also known as renal diabetes insipidus) is a form of diabetes insipidus primarily due to pathology of the kidney. This is in contrast to central/neurogenic diabetes insipidus, which is caused by insufficient levels of antidiuretic hormone (ADH, that is, arginine vasopressin or AVP). Nephrogenic diabetes insipidus is caused by an improper response of the kidney to ADH, leading to a decrease in the ability of the kidney to concentrate the urine by removing free water. The clinical manifestation is similar to neurogenic diabetes insipidus, presenting with excessive thirst and excretion of a large amount of dilute urine. Dehydration is common, and incontinence can occur secondary to chronic bladder distension. On investigation, there will be an increased plasma osmolarity and decreased urine osmolarity. As pituitary function is normal, ADH levels are likely to be abnormal or raised. Polyuria will continue as long as the patient is able to drink. If the patient is ...
Two brothers, patient 1 with fever and vomiting, and patient 2 with failure to gain weight were studied. After 4 hr of water deprivation test, the urinary osmolality of the patient 1 was only 105 mOsm/liter and his body weight showed a 4.6% reduction. In response to desamino-8-D arginine vasopressin intranasal administration, no significant elevation of urinary osmolality of patient 1 occurred. After low dose vasopressin tests, the maximal urinary osmolality of their father was in the normal range, but that of their mother was below the normal range. Moreover, the patients showed no significant increase of urinary osmolality after the same tests. The brothers were diagnosed as nephrogenic diabetes insipidus (NDI) and their mother was diagnosed as a carrier. An early diagnosis of NDI is important, since adequate managements such as low-solute diet with restricted protein and salt intake or such as water intake at frequent intervals can prevent the hyperosmolality which would develop the delayed mental
Aldose reductase (ALR2) is thought to be involved in the pathogenesis of various diseases associated with diabetes mellitus, such as cataract, retinopathy, neuropathy, and nephropathy. However, its physiological functions are not well understood. We developed mice deficient in this enzyme and found that they had no apparent developmental or reproductive abnormality except that they drank and urinated significantly more than their wild-type littermates. These ALR2-deficient mice exhibited a partially defective urine-concentrating ability, having a phenotype resembling that of nephrogenic diabetes insipidus.
diabetes insipidus is caused by problems related to a hormone called antidiuretic hormone or adh. adh is produced in a part of the brain called the hypothalamus.
Mutations in human and/or mouse homologs are associated with this disease. Synonyms: vasopressin-resistant diabetes insipidus
Learn about the causes, symptoms, diagnosis & treatment of Renal Transport Abnormalities from the Professional Version of the Merck Manuals.
Definition of kidney medulla in the Definitions.net dictionary. Meaning of kidney medulla. What does kidney medulla mean? Information and translations of kidney medulla in the most comprehensive dictionary definitions resource on the web.
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 ...
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 ...
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
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. ...
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A water deprivation test is also performed to see if the person suffers from nephrogenic diabetes insipidus. The patient has to stay without water for around five hours or more and then the plasma concentration, as well as the volume of urine, is measured. In case the test is positive for nephrogenic diabetes insipidus, the patient will be resistant to the anti diuretic hormone. Hence, after the test, although the patient is dehydrated, dilute urine and blood plasma will still be present in the patient ...
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, ...
J Biol Chem. 2001 Jun 15;276(24):21331-6. Epub 2001 Apr 10. Research Support, Non-U.S. Govt; Research Support, U.S. Govt, P.H.S.
If you have nephrogenic diabetes insipidus thats caused by taking a particular medication, such as lithium or tetracycline, your GP or endocrinologist may stop your treatment and suggest an alternative medication. However, dont stop taking it unless youve been advised to by a healthcare professional.. As nephrogenic diabetes insipidus is caused by your kidneys not responding to AVP, rather than a shortage of AVP, it usually cant be treated with desmopressin. However, its still important to drink plenty of water to avoid dehydration.. If your condition is mild, your GP or endocrinologist may suggest reducing the amount of salt and protein in your diet, which will help your kidneys produce less urine. This may mean eating less salt and protein-rich food, such as processed foods, meat, eggs and nuts. Dont alter your diet without first seeking medical advice. Your GP or endocrinologist will be able to advise you about which foods to cut down on.. Read more about eating a healthy, balanced ...
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 ...
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
... A. Butet METEO-FRANCE CNRM/GMEI/SPEA,...
Sigma-Aldrich offers abstracts and full-text articles by [C A Ecelbarger, J Terris, G Frindt, M Echevarria, D Marples, S Nielsen, M A Knepper].
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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.
Two previous articles in this series on aquaporins have discussed their history, mechanism and stimulation. The current article describes the role of AQP3 in regulating skin cell growth.
Looking for online definition of 1-desamino-8-D-arginine vasopressin in the Medical Dictionary? 1-desamino-8-D-arginine vasopressin explanation free. What is 1-desamino-8-D-arginine vasopressin? Meaning of 1-desamino-8-D-arginine vasopressin medical term. What does 1-desamino-8-D-arginine vasopressin mean?
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 ...
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 ...
Semantic Scholar extracted view of Aquaporin water channels in liver: their significance in bile formation. by Raúl Alberto Marinelli et al.
Nephrogenic diabetes insipidus (NDI) is a disorder in which a defect in the small tubes (tubules) in the kidneys causes a person to pass a large amount of urine and lose too much water.
Vasopressin-sensitive aquaporin-2 (Aqp2) in the apical membrane of the renal collecting duct (Fenton et al., 2008). Controls cell volume and thereby influences cell proliferation (Di Giusto et al. 2012). It plays a key role in concentrating urine. Water reabsorption is regulated by AQP2 trafficking between intracellular storage vesicles and the apical membrane. This process is tightly controlled by the pituitary hormone arginine vasopressin, and defective trafficking results in nephrogenic diabetes insipidus (NDI). The crystal structure of Aqp2 has been solved to 2.75Å (Frick et al. 2014). In terrestrial vertebrates, AQP2 function is generally regulated by arginine-vasopressin to accomplish key functions in osmoregulation such as the maintenance of body water homeostasis by a cyclic AMP-independent mechanism (Olesen and Fenton 2017; Martos-Sitcha et al. 2015 ...
Neuromyelitis optica-immunoglobulin G (NMO-IgG) binds to aquaporin-4 (AQP4) drinking water channels within the central nervous program resulting in immune-mediated damage. rAbs by quantitative immunofluorescence. Whereas all NMO rAbs needed conserved loop C (137TP138 and Val150) and loop E (230HW231) proteins for binding two SR9243 wide patterns of NMO-IgG reputation could be recognized predicated on differential level of sensitivity to loop A amino acidity changes. Design 1 NMO rAbs had been insensitive to loop A mutations and may be additional discriminated by differential level of sensitivity to amino acidity adjustments in loop C (148TM149 and His151) and loop E (Asn226 and Glu228). On the other hand pattern 2 NMO rAbs demonstrated significantly decreased binding pursuing amino acid adjustments in loop A (63EKP65 and Asp69) and loop C (Val141 His151 and Leu154). Amino acidity substitutions at 137TP138 modified loop C conformation and abolished the binding of most NMO rAbs and NMO-IgG ...
Director of the Clinical Research Unit at lHôpital Sacré-Coeur in Montreal and Professor of Medicine at lUniversité de Montréal, Dr. Bichet identified the gene that causes nephrogenic diabetes insipidus in newborns and developed a blood test to detect it. Some of the knowledge gained was then applied to a new study on polycystic kidney disease, a more common hereditary condition... ...
Aquaporin-4 (AQP4), the main water channel of the brain, is highly expressed in animal glioma and human glioblastoma in situ. In contrast, most cultivated glioma cell lines dont express AQP4, and primary cell cultures of human glioblastoma lose it d
Lithium is the most common cause of nephrogenic diabetes insipidus (Li-NDI). Hydrochlorothiazide (HCTZ) combined with amiloride is the mainstay treatment in Li-NDI. The paradox antidiuretic action of HCTZ in Li-NDI is generally attributed to increased sodium and water uptake in proximal tubules as a compensation for increased volume loss due to HCTZ inhibition of the NaCl-co-transporter (NCC), but alternative actions for HCTZ have been suggested. Here, we investigated whether HCTZ exerted an NCC-independent effect in Li-NDI. In polarized mouse cortical collecting duct (mpkCCD) cells, HCTZ treatment attenuated the Li-induced downregulation of the Aquaporin-2 (AQP2) water channel abundance. In these cells, amiloride reduces cellular Li influx through the epithelial sodium channel ENaC. HCTZ also reduced Li influx, but to a lower extent. HCTZ increased AQP2 abundance on top of that of amiloride and did not affect the ENaC-mediated transcellular voltage. MpkCCD cells did not express NCC mRNA or ...
Lithium therapy frequently induces nephrogenic diabetes insipidus; amiloride appears to prevent its occurrence in some clinical cases. Amiloride blocks the epithelial sodium channel (ENaC) located in the apical membrane of principal cells; hence one possibility is that ENaC is the main entry site for lithium and the beneficial effect of amiloride may be through inhibiting lithium entry. Using a mouse collecting duct cell line, we found that vasopressin caused an increase in Aquaporin 2 (AQP2) expression which was reduced by clinically relevant lithium concentrations similar to what is seen with in vivo models of this disease. Further amiloride or benzamil administration prevented this lithium-induced downregulation of AQP2. Amiloride reduced transcellular lithium transport, intracellular lithium concentration, and lithium-induced inactivation of glycogen synthase kinase 3beta. Treatment of rats with lithium downregulated AQP2 expression, reduced the principal-to-intercalated cell ratio, and ...
What can cause diabetes insipidus depends on that number of this particular condition youve.. Diabetes insipidus can be an unheard of health condition which usually develops whenever a individuals filtering system just cant preserve drinking water every time they execute their particular purpose of selection someones blood vessels. The amount of h2o generally is actually governed simply by ADH, that is really a good antidiuretic hormonal known as vasopressin.. The aim of vasopressin would be to constantly handle the amount of h2o which is within the body through governing the level of pee your own renal system help make. In case the degree of h2o with your method is lower, the anterior pituitary gland generates vasopressin in order to make use of much less h2o and lower the creation of pee.. Nonetheless, should you have DI, generally vasopressin is not able to correctly handle your bodys drinking water amounts, that allows a significant amount of pee to obtain created and also given out from ...
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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.". ...
There is disturbance in renal concentrating mechanism, resulting in polyuria nad inability to produce hypertonic urine. DI is due to absence of an ADH effect, either because of impaired or failed secretion (cranial or central DI) or lack of end organ response to ADH (nephrogenic DI). Most of the inherited nephrogenic DI have mutation in ADH V2 receptor, there is also down regulation of AQP2 in acquired forms of DI ...
The relation between the expressed amounts and conferred water permeabilities of AQP2-S256D-F. Of oocytes, injected with 0.1, 0.2, 0.3, or 0.4 ng of AQP2-S256D-
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. ...
... 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. ...
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 ...
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 ...
12] Aquaporins allow water to move down their osmotic gradient and out of the nephron, increasing the amount of water re- ... Insertion of aquaporin-2 (AQP2) channels (water channels). This allows water to be reabsorbed down an osmotic gradient, and so ... This occurs through increased transcription and insertion of water channels (Aquaporin-2) into the apical membrane of ... Vasopressin, acting through cAMP, also increases transcription of the aquaporin-2 gene, thus increasing the total number of ...
... aquaporin 1 MeSH D12.776.157.530.400.500.040.437 -- aquaporin 2 MeSH D12.776.157.530.400.500.040.468 -- aquaporin 4 MeSH ... aquaporins MeSH D12.776.157.530.400.500.040.249 -- aquaglyceroporins MeSH D12.776.157.530.400.500.040.249.500 -- aquaporin 3 ... D12.776.157.530.400.500.040.484 -- aquaporin 5 MeSH D12.776.157.530.400.500.520 -- voltage-dependent anion channels MeSH ... MeSH D12.776.157.530.400.500.040.249.750 -- aquaporin 6 MeSH D12.776.157.530.400.500.040.374 -- ...
... aquaporin 1 MeSH D12.776.543.550.425.730.040.437 -- aquaporin 2 MeSH D12.776.543.550.425.730.040.468 -- aquaporin 4 MeSH ... aquaporin 1 MeSH D12.776.543.585.400.730.040.530 -- aquaporin 2 MeSH D12.776.543.585.400.730.040.577 -- aquaporin 4 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 ...
June 1999). "Urinary excretion of aquaporin-2 water channel differentiates psychogenic polydipsia from central diabetes ... 35 (6): 408-419. doi:10.1016/0006-3223(94)90008-6. Hedges, D.; Jeppson, K.; Whitehead, P. (2003). "Antipsychotic medication and ... PPD occurs in between 6% and 20% of psychiatric inpatients. It may also be found in people with developmental disorders, such ... 84 (6): 2235-2237. doi:10.1210/jc.84.6.2235. PMID 10372737. "Primary polydipsia - General Practice Notebook". GPnotebook. ...
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 ...
"Aquaporin-2 and -3: representatives of two subgroups of the aquaporin family colocalized in the kidney collecting duct". Annu. ... 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- ...
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, ...
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 ...
... 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 ...
Aquaporin 7 and AQP3 are at the same chromosomal location suggesting that 9p13 may be a site of an aquaporin cluster. Aquaporin ... Aquaporin-7 is a protein that in humans is encoded by the AQP7 gene. Aquaporins/major intrinsic protein (MIP) are a family of ... "Entrez Gene: AQP7 aquaporin 7". Dibas AI, Mia AJ, Yorio T (1998). "Aquaporins (water channels): role in vasopressin-activated ... Aquaporin 7 has greater sequence similarity with AQP3 and AQP9 and they may be a subfamily. ...
... including aquaporins, ATPases and Ca2+/H+ and Na+/H+ antiporters. They may be the only cellular organelle that has been ... Their membranes are 6 nm thick and contain a number of protein pumps and antiporters, ...
"The inositol Inpp5k 5-phosphatase affects osmoregulation through the vasopressin-aquaporin 2 pathway in the collecting system ... 462 (6): 871-83. doi:10.1007/s00424-011-1028-0. PMID 21938401. Drayer AL, Pesesse X, De Smedt F, Communi D, Moreau C, Erneux C ...
Aquaporin-5 is a protein that in humans is encoded by the AQP5 gene. Aquaporin 5 (AQP5) is a water channel protein. Aquaporins ... "Entrez Gene: AQP5 aquaporin 5". Verkman AS (2003). "Role of aquaporin water channels in eye function". Exp. Eye Res. 76 (2): ... 2003). "Distribution of aquaporin water channels AQP1 and AQP5 in the ductal system of the human pancreas". Gut. 52 (7): 1008- ... 2007). "Stimulation of aquaporin-5 and transepithelial water permeability in human airway epithelium by hyperosmotic stress". ...
Aquaporin-9 is a protein that in humans is encoded by the AQP9 gene. The aquaporins/major intrinsic protein are a family of ... Aquaporin 9 has greater sequence similarity with AQP3 and AQP7 and they may be a subfamily. Aquaporin 9 allows passage of a ... AQP9 aquaporin 9". Ishibashi K, Kuwahara M, Gu Y, et al. (1998). "Cloning and functional expression of a new aquaporin (AQP9) ... 2003). "Aquaporin-9 is expressed in a mucus-secreting goblet cell subset in the small intestine". FEBS Lett. 540 (1-3): 157-62 ...
2004). „Antidiuretic action of oxytocin is associated with increased urinary excretion of aquaporin-2". Nephrology, Dialysis, ...
"Antidiuretic action of oxytocin is associated with increased urinary excretion of aquaporin-2". Nephrol. Dial. Transplant. 19 ( ... 20 (6): 729-36. doi:10.1016/0361-9230(88)90084-6. PMID 3409054. Acher R, Chauvet J (1988). "Structure, processing and evolution ... 10): 2480-6. doi:10.1093/ndt/gfh413. PMID 15280526. Michel G, Acher R, Chauvet J, Ouedraogo Y, Chou J, Chait BT (1995). "A new ...
Aquaporin 1. *Arachidonate 5-lipoxygenase. *Atrophin 1. *BH3 interacting-domain death agonist ... DescriptionIdeogram house mouse chromosome 6.svg. English: Ideogram of house mouse (Mus musculus) chromosome. Chromosome 6 ... File:Ideogram house mouse chromosome 6.svg. From Wikipedia, the free encyclopedia ... Chromosome 6 highlighted.}} ,Source=GRCm38.p4 (GCF_000001635.24) at NCBI's [http://www.ncbi.nlm.nih.gov/genome/tools/gdp/ ...
Robben JH, Knoers NV, Deen PM (Aug 2006). "Cell biological aspects of the vasopressin type-2 receptor and aquaporin 2 water ... Ishikawa SE (Feb 2002). "[Nephrogenic diabetes insipidus associated with mutations of vasopressin V2 receptors and aquaporin-2 ... 2 (2): 103-6. doi:10.1038/ng1092-103. PMID 1303257. van den Ouweland AM, Dreesen JC, Verdijk M, Knoers NV, Monnens LA, Rocchi M ... 3 (9): 1685-6. doi:10.1093/hmg/3.9.1685. PMID 7833930. Birnbaumer M, Gilbert S, Rosenthal W (Jul 1994). "An extracellular ...
Zheng X, Bollinger Bollag W (December 2003). "Aquaporin 3 colocates with phospholipase d2 in caveolin-rich membrane ... 276 (52): 48840-6. doi:10.1074/jbc.M104276200. PMID 11687572. Lee S, Kim JH, Lee CS, Kim JH, Kim Y, Heo K, Ihara Y, Goshima Y, ... 121 (6): 1487-95. doi:10.1111/j.1523-1747.2003.12614.x. PMID 14675200. Czarny M, Fiucci G, Lavie Y, Banno Y, Nozawa Y, ...
... also indicated in proper lung development by controlling the late differentiation stages of alveolar epithelium and aquaporin-5 ... Transcription factor GATA-6, also known as GATA-binding factor 6 (GATA6), is protein that in humans is encoded by the GATA6 ... 54 (4): 542-6. doi:10.1203/01.PDR.0000081295.56529.E9. PMID 12867597. Liu C, Ikegami M, Stahlman MT, Dey CR, Whitsett JA (2003 ... Furthermore, GATA-6 has been linked to the production of LIF, a cytokine that encourages proliferation of endodermal embryonic ...
Yang B, Verkman AS (September 2002). "Analysis of double knockout mice lacking aquaporin-1 and urea transporter UT-B. Evidence ... 277 (39): 36782-6. doi:10.1074/jbc.M206948200. PMID 12133842. Collins D, Winter DC, Hogan AM, Schirmer L, Baird AW, Stewart GS ...
2007) Anti-aquaporin-4 antibody is involved in the pathogenesis of NMO: A study on antibody titre. Brain 130:1235-1243. ... 2007) Loss of aquaporin 4 in lesions of neuromyelitis optica: Distinction from multiple sclerosis. Brain 130:1224-1234. ... 2008) Mechanisms of disease: Aquaporin-4 antibodies in neuromyelitis optica. Nat Clin Pract Neurol 4:202-214. ... 2008) Antibody to aquaporin-4 in the long-term course of neuromyelitis optica. Brain 131:3072-3080. ...
Buena vista" hypothesis suggests that changes in the sizes of eyes, rather than a shift from fins to limbs, led fish to transition to land more than 300 million years ago. 1 Comment. ...
... known as aquaporins, are transmembrane proteins that mediate osmotic water permeability. The discovery of aquaporin (AQP) has… ... The discovery of aquaporin (AQP) has made a great impact on life sciences. AQPs are a family of homologous water channels ... Lenti ORF particles, Aqp6 (Myc-DDK-tagged ORF) - Rat aquaporin 6, kidney specific (Aqp6), 200 uL, ,10^7 TU/mL. Not available. ... Lenti ORF particles, AQP6 (Myc-DDK tagged) - Human aquaporin 6, kidney specific (AQP6) , 200 uL, ,10^7 TU/mL. Not available. ...
All characterized mammalian aquaporins (AQPs) are localized to plasma membranes where they function chiefly to mediate water ...
Aquaporin 6, WB control \ PC-AQP6 for more molecular products just contact us ... Aquaporin adipose) (AQPap) (Aquaporin-7-like). [TIP1-1 AQP.1 At2g36830 T1J8.1] Aquaporin TIP1-1 (Aquaporin TIP) (Gamma- ... AQP5] Aquaporin-5 (AQP-5). [MIP] Lens fiber major intrinsic protein (Aquaporin-0) (MIP26) (MP26). [AQP1 GW7_07092] Aquaporin-1 ... Aqp5] Aquaporin-5 (AQP-5). [PIP1-1 PIP1A At3g61430 F2A19.30] Aquaporin PIP1-1 (AtPIP1;1) (Plasma membrane aquaporin-1) (Plasma ...
Aquaporin 4 , Aquaporins , Bacteria , Ear , Ear, Middle , Hearing , Hearing Loss , Hearing Loss, Sensorineural , Homeostasis , ... Aquaporins (AQPs) are integral membrane proteins engaged in the modulation of water homeostasis, but the roles they play in ... Aquaporins / Ear / Ear, Middle Type of study: Incidence_studies Clinical aspect: Prognosis Language: English Journal: Clinical ... Decreased Aquaporin 4 and 6 mRNAs in Patients With Chronic Otitis Media With Otorrhea ...
Rabbit Polyclonal Anti-Aquaporin-7 Antibody. Validated: WB, ICC/IF, IHC, IHC-Fr. Tested Reactivity: Human, Mouse, Porcine, and ... Aquaporin 7 and AQP3 are at the same chromosomal location suggesting that 9p13 may be a site of an aquaporin cluster. Aquaporin ... Aquaporin-7 Antibody Summary. Immunogen. A synthetic peptide from the n-terminal region of human Aquaporin 7 (AQP7) conjugated ... Blogs on Aquaporin-7. There are no specific blogs for Aquaporin-7, but you can read our latest blog posts. ...
Aquaporin-4 antibodies (AQP4-Ab) are associated with neuromyelitis optica spectrum disorder (NMOSD) and typically this disorder ... Neuroophthalmologie Aquaporin 4 Serumstatus Neuromyelitis-optica-spektrum-erkrankung Visual outcome Acute optic neuritis ... Aquaporin-4 antibodies (AQP4-Ab) are associated with neuromyelitis optica spectrum disorder (NMOSD) and typically this disorder ... Visual outcome 6 months after an acute episode of optic neuritis appears uninfluenced by aquaporin-4 serostatus. ...
Aquaporin-6 is expressed along the rat gastrointestinal tract and upregulated by feeding in the small intestine. BMC Physiology ... Aquaporin-6 is expressed along the rat gastrointestinal tract and upregulated by feeding in the small intestine. In: BMC ... Aquaporin-6 is expressed along the rat gastrointestinal tract and upregulated by feeding in the small intestine. / Laforenza, ... Aquaporin-6 localization at the apical pole of the superficial epithelial cells and its upregulation by feeding suggest that it ...
Aquaporin 9 antibody Rabbit Polyclonal Hu, Ms, Pig, Rat, Shp, Bov ELISA, IHC-P, WB ... Aquaporin 6 antibody(FITC) Rabbit Polyclonal Hu, Ms, Rat, Shp, Bov ELISA, IP, WB ... Aquaporin 6 antibody Rabbit Polyclonal Hu, Ms, Rat, Shp, Bov ELISA, IP, WB ... Aquaporin 9 antibody Rabbit Polyclonal Hu, Ms, Rat, Shp, Bov IHC, WB ...
Lesions Caused by Intracerebral Injection of Aquaporin-4 Immunoglobulin G Lesions Caused by Intracerebral Injection of ... Objective]To investigate the pathological damage caused by aquaporin-4 antibody extracted from patients with neuromyelitis ... from aquaporin-4(AQP4)IgG positive patients and healthy human complement(hC)were injected in the brain parenchyma(EAE+AQP4-IgG+ ... Aquaporin-4 Immunoglobulin G / 中山大学学报(医学科学版) ...
Arrows indicate different positions of the glycosylated and oligomerization forms of aquaporin-6 as previously assigned. ... and aquaporin-6 (right panel). Protein expression in 2 individual platelet units is shown. ... Figure 6. Effect of exogenous broad-spectrum metalloproteinase inhibitor on platelet N-terminome during storage. Platelets were ...
One way is through the use of aquaporins. Use this assessment to assess how well you understand the functions of aquaporins. ... 2. Aquaporins are protein tunnels that allow which important molecule to travel across a cell membrane?. ... For an effective review, complete the related lesson Aquaporins: Definition & Functions. Use this review to prepare for ... Information recall - access the knowledge youve gained regarding the functions of aquaporins ...
Aquaporin/glycerol facilitator of 294 aas and 6 TMSs. May play a role in freeze tolerance (Hirota et al. 2015).. ...
Aquaporin-B, AqpB of 294 aas and 6 TMSs. Tyr216 in loop D is a key residue in gating, possibly involving phosphorylation. ... 1] "Functional characterization of a novel aquaporin from Dictyostelium discoideum amoebae implies a unique gating mechanism." ...
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. ...
Contractile vacuole aquaporin of 295 aas and 6 TMSs, Aqp. Shown to transport water, accounting for the high water permeability ...
Aquaporin-1 or Aquaporin1, Aqp1, of 258 aas and 6 TMSs. Three Aqp1 isoforms are differentially regluated by the function of the ...
aquaporin 8 Gene. Mus musculus. Under-expressed. 11865. Arntl. aryl hydrocarbon receptor nuclear translocator-like Gene. Mus ... aquaporin 6 Gene. Mus musculus. Over-expressed. 11833. Aqp8. ...
Aquaporin water channels in the bladder urothelium as novel targets for treatment of lower urinary tract pathophysiology at ... Aquaporins at a glance. J Cell Sci. 2011 Jul 1;124(Pt 13):2107-12. 7. Terris J, Ecelbarger CA, Nielsen S, Knepper MA. Long-term ... Thus, aquaporins are exciting new potential targets for the treatment of UI and nocturia. The aim is to investigate the ... Aquaporin water channels in the bladder urothelium as novel targets for treatment of lower urinary tract pathophysiology ...
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 ...
Aquaporins Aquaporin-1 (AQP1) was first discovered in human red blood cell membranes by Gheorghe Bengas research group in 1986 ... Aquaporin-1 Structure Aquaporin-1 is an integral membrane protein that is considered to have an "open" structure. Despite being ... Aquaporin-1 Regulation Aquaporin channels may be subject to intense short term regulation via signal transduction. Transducers ... 12 other isoforms of aquaporin-1 have been discovered and each have been classified under the family known as Aquaporins. ...
Anti-aquaporin-4 antibody is involved in the pathogenesis of NMO: a study on antibody titre. Brain 2007;130:1235-43. 5. Chihara ... Aquaporin-4 antibodies (AQP4-IgG), pathogenic antibodies, are detected in at least two-thirds of NMOSD patients. AQP4-IgG is ... Aquaporin-4 antibody-negative neuromyelitis optica: Distinct assay sensitivity-dependent entity. Neurology 2013;80:2194-200. 4 ... SAkuraSky study is a global phase III clinical study for NMOSD patients including aquaporin-4 antibodies (AQP4-IgG) ...
2014 Dec 17;84(6):1226-39. doi: 10.1016/j.neuron.2014.12.014. Erratum in: Neuron. 2015 Jan 7;85(1):228. Neuron. 2015 Jan 7;85(1 ... Adenylate cyclase 6 determines cAMP formation and aquaporin-2 phosphorylation and trafficking in inner medulla. ... 2014 Jan 2;94(1):80-6. doi: 10.1016/j.ajhg.2013.11.015. Epub 2013 Dec 19. ...
M. Pohl, M.-T. Fischer, S. Mader et al., "Pathogenic T cell responses against aquaporin 4," Acta Neuropathologica, vol. 122, no ... 6. ±. 1. .. 2. versus 7. .. 1. ±. 1. .. 5. , 𝑃. =. N. S. ), ΔEDSS and residual EDSS were dramatically reduced in the PLEX- ... T. Takahashi, K. Fujihara, I. Nakashima et al., "Anti-aquaporin-4 antibody is involved in the pathogenesis of NMO: a study on ... 6. versus 2. .. 6. ±. 2. .. 4. , 𝑃. ,. 0. .. 0. 1. ) were significantly lower in the PLEX-treated group than in the steroid- ...
PMIDProteinsMembraneAQP1AntibodyAQPsMembranesPermeabilityRole of aquaporinsAnti-aquaporinCharacterizationAQP2LocalizationNeuromyelitis opticaAQP5Function of aquaporins2002Aqp6TransmembraneMammalianTMSsEpithelial CellsBelongs to the aquaporinExpression of aquaporinsIsoforms1997Plant aquaporinsKidneyIntegralSelectivelyPathwayAgrePermeableAQP3AQP9Molecular weightAstrocytesChromosomeAQP4-AbHumanGene expressionOsmoticResearch on AquaporinUreaRegulationVesicleMRNAArabidopsis
- December 1997), "Subacute bacterial endocarditis masquerading as type III essential mixed", Journal of the American Society of Nephrology, 8 (12): 1971-6, PMID 9402102 Autoimmune Diseases at the US National Library of Medicine Medical Subject Headings (MeSH) Kárpáti F, Dénes L, Büttner K (1975). (wikipedia.org)
- Water channel proteins, known as aquaporins, are transmembrane proteins that mediate osmotic water permeability. (acris-antibodies.com)
- Aquaporins (AQPs) are integral membrane proteins engaged in the modulation of water homeostasis, but the roles they play in chronic otitis media (COM) have not been well investigated. (bvsalud.org)
- Several aquaporins (a family of integral membrane proteins) have been recently identified in the mammalian gastrointestinal tract, and their involvement in the movement of fluid and small solutes has been suggested. (elsevier.com)
- Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). (wikipedia.org)
- Aquaporins (AQPs) are integral membrane proteins that form pores in the membrane of biological cells. (cosmeticsandtoiletries.com)
- Aquaporins are integral membrane proteins that specialize in the regulation of cellular water flow across the cell membrane. (proteopedia.org)
- Aquaporins are specialized water transport proteins that play an essential role in brain edema. (hindawi.com)
- Aquaporins also called water channels, are integral membrane proteins from a larger family of major intrinsic proteins that form pores in the membrane of biological cells, mainly facilitating transport of water between cells. (wikipedia.org)
- Also known as water channels, aquaporins are integral membrane pore proteins. (wikipedia.org)
- Aquaporin proteins are composed of a bundle of six transmembrane α-helices. (wikipedia.org)
- and (6) AQP8s, or metazoan aquaporin 8 proteins. (tcdb.org)
- Benga G (2009) Water channel proteins (later called aquaporins) and relatives: past, present, and future. (springer.com)
- AQP4 belongs to the aquaporin family of integral membrane proteins that conduct water through the cell membrane. (wikipedia.org)
- also called aquaporins) are membrane channel proteins initially discovered as water channels, but their roles in the transport of small neutral solutes, metal ions, and gasses are now well established. (springer.com)
- Aquaporin 1 (AQP1), aquaporin 2 (AQP2) and the mercury-insensitive water channel (MIWC) are water-selective channel proteins, whereas the fourth, referred to as aquaporin 3 (AQP3), permits transport of urea and glycerol as well. (springer.com)
- Aquaporins (AQP) are water-specific membrane channel proteins. (jhu.edu)
- Aquaporin water channel proteins mediate the transport of water across cell membranes in numerous species. (jhu.edu)
- The eye contains numerous water channel proteins and the roles of AQPs (aquaporins) in the retina are blurred, especially under disease conditions. (portlandpress.com)
- AQPs (aquaporins) are hydrophobic membrane proteins and the narrowest diameter of the pore of AQPs is 2.8 Å (1 Å=0.1 nm) [ 16 ]. (portlandpress.com)
- Additionally we are shipping Aquaporin 5 Kits (45) and Aquaporin 5 Proteins (4) and many more products for this protein. (antibodies-online.com)
- Many organisms lacking a specific aquaporin have an unobtrusive phenotype, which suggests that aquaporins are unimportant or can be substituted by homolog proteins or compensatory mechanisms. (plantcell.org)
- Aquaporins are integral membrane proteins of the tonoplast and the plasma membrane that facilitate the passage of water through these membranes. (plantphysiol.org)
- The membranes of the small vesicles as well as the membrane of the CV have aquaporin proteins embedded in them. (wikipedia.org)
- The presence of aquaporin proteins in both CV and the small vesicles suggests that water collection occurs both through the CV membrane itself as well as through the function of the vesicles. (wikipedia.org)
- Pioneering was Kaldenhoff's discovery that under investigation some of the aquaporin proteins facilitate the diffusion of CO₂ in plant tissues and cells and in chloroplasts respectively. (wikipedia.org)
- Aquaporins, membrane proteins involved in the channeling of water, have also been shown to play a key role in E. solidaginis' freezing tolerance. (wikipedia.org)
- Clearance of soluble proteins, waste products, and excess extracellular fluid is accomplished through convective bulk flow of the ISF, facilitated by astrocytic aquaporin 4 (AQP4) water channels. (wikipedia.org)
- Studies of enterocyte brush-border ion transporter proteins (sodium-hydrogen exchanger 2, sodium-hydrogen exchanger 3, aquaporin 7, sodium iodide symporter and hydrogen potassium adenosine triphosphatase) showed reduced expression or mislocalization in all patients with different profiles for each. (wikipedia.org)
- Major intrinsic protein is a member of the water-transporting aquaporins as well as the original member of the MIP family of channel proteins. (wikipedia.org)
- Acetazolamide can bind to Aquaporin 1 and inhibit the water movement across the plasma membrane. (acris-antibodies.com)
- Immunoblotting analysis of brush border membrane vesicle preparations showed an intense signal for aquaporin-6 protein. (elsevier.com)
- In the latter regions, immunohistochemistry revealed strong aquaporin-6 labelling in the apical membrane of the surface epithelial cells, while weak or no labelling was observed in the crypt cells. (elsevier.com)
- Aquaporins/major intrinsic protein (MIP) are a family of water-selective membrane channels. (novusbio.com)
- 2. Aquaporins are protein tunnels that allow which important molecule to travel across a cell membrane? (study.com)
- Aquaporin-1 is an integral membrane protein that is considered to have an "open" structure. (proteopedia.org)
- Aquaporins actively transport water across the membrane e. (coursehero.com)
- 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)
- 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)
- 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)
- Vasopressin-mediated control of water permeability in the renal collecting duct occurs in part through regulation of the distribution of aquaporin-2 (AQP2) between the apical plasma membrane and intracellular membrane compartments. (nih.gov)
- Secretin promotes osmotic water transport in rat cholangiocytes by incresing aquaporin-1 water channels in plasma membrane. (wiley.com)
- Human red cell AQP1 is the first functionally defined member of the aquaporin family of membrane water channels. (shapeways.com)
- Aquaporin 1 forms a water-specific channel that is constitutively expressed at the PLASMA MEMBRANE of ERYTHROCYTES and KIDNEY TUBULES, PROXIMAL. (curehunter.com)
- 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)
- Aquaporins (AQP) were originally regarded as plasma membrane channels that are freely permeated by water or small uncharged solutes but not by ions. (jhu.edu)
- Mannitol-induced water imbalance resulted in increased protein amounts in tonoplast fractions and a shift in protein distribution to other membrane fractions, suggesting aquaporin relocalization. (plantphysiol.org)
- The tobacco plasma membrane aquaporin NtAQP1 was used to elucidate this issue. (plantcell.org)
- However, determining the impact of plasma membrane-located aquaporins for whole plant or organ water transport efficiency proved difficult in this model plant because of its small size. (plantcell.org)
- We chose the well-characterized tobacco plasma membrane-located aquaporin NtAQP1 for these studies. (plantcell.org)
- aquaporin, amniotic fluid, fetal membrane. (prolekare.cz)
- Placental and membrane aquaporin water channels: Correlation with amniotic fluid volume and composition. (prolekare.cz)
- In vivo silencing of aquaporin-1 by RNA interference inhibits angiogenesis in the chicken embryo chorioallantoic membrane assai. (prolekare.cz)
- Glucagon induces the plasma membrane insertion of functional aquaporin-8 water channels in isolated rat hepatocytes. (prolekare.cz)
- showed that TobRB7, a putative plasma membrane aquaporin of tobacco, is highly expressed in the meristem and in the immature central cylinder of roots. (plantphysiol.org)
- analyzed the expression pattern of the aquaporin MIP A in roots of Mesembryanthenum crystallinum and found that this plasma membrane aquaporin is preferentially expressed in the epidermis and in the youngest portions of the xylem. (plantphysiol.org)
- showed that AthH2, a plasma membrane aquaporin, is highly expressed in newly formed tissues and organs. (plantphysiol.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)
- These antibodies target the protein aquaporin 4 in the cell membranes of astrocytes which acts as a channel for the transport of water across the cell membrane. (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)
- 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)
- Aquaporins are membrane-bound channels that play critical roles in regulating the flux of water into and out of cells. (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 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)
- Aquaporin-1 or Aquaporin1, Aqp1, of 258 aas and 6 TMSs. (tcdb.org)
- Aquaporin-1 (AQP1) was first discovered in human red blood cell membranes by Gheorghe Benga's research group in 1986. (proteopedia.org)
- Aqp1 of 270 aas and 6 TMSs. (tcdb.org)
- 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)
- Aquaporin 1 is a protein that in humans is encoded by the AQP1 gene. (wikipedia.org)
- The human genes encoding AQP1 and AQP2 have been cloned, permitting deduction of their amino acid sequence, prediction of their two-dimensional structure by hydropathy analysis, speculations on their way of functioning and DNA analysis in patients with diseases possibly caused by mutant aquaporins. (springer.com)
- The aquaporin-1 (AQP1) water channel protein is known to facilitate the rapid movement of water across cell membranes, but a proposed secondary role as an ion channel is still unsettled. (jhu.edu)
- Aquaporin channel-forming integral protein (CHIP) is the first characterized water channel protein (genome symbol AQP1), but the molecular structure of the aqueous pathway through CHIP remains undefined. (jhu.edu)
- Expression of aquaporin 1 (AQP1) in chorioallantoic membranes of near term ovine foetuses with induced hypoxia. (prolekare.cz)
- 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)
- We also demonstrate that interleukin 6 (IL-6), shown to be increased in NMO, enhanced the survival of PB as well as their AQP4-Ab secretion, whereas the blockade of IL-6 receptor (IL-6R) signaling by anti-IL-6R antibody reduced the survival of PB in vitro. (pnas.org)
- Anti-Aquaporin 6 antibody , (1:200). (acris-antibodies.com)
- 2. Anti-Aquaporin 6 antibody, preincubated with the control peptide antigen. (acris-antibodies.com)
- Objective]To investigate the pathological damage caused by aquaporin-4 antibody extracted from patients with neuromyelitis optica spectrum disorders(NMOSD)and the influence of systemic immune status on the local disease focus. (bvsalud.org)
- There are currently no images for Aquaporin-7 Antibody (NBP1-30862). (novusbio.com)
- The NMO-IgG antibody is IgG1 directed against protein aquaporin-4 (AQP4) [ 6 ]. (hindawi.com)
- Anti-aquaporin-4 antibody is involved in the pathogenesis of NMO: a study on antibody titre. (springer.com)
- Rabbit polyclonal Aquaporin 3 antibody. (abcam.com)
- NMO occupies a unique position in the spectrum of inflammatory central nervous system demyelinating disorders in that it is the only such disorder that has an associated disease-specific antibody, aquaporin-4 antibody (AQP4 Ab), or NMO-IgG. (hindawi.com)
- All characterized mammalian aquaporins (AQPs) are localized to plasma membranes where they function chiefly to mediate water transport across cells. (jhu.edu)
- Seven AQPs are expressed in the kidney ( 6 ). (pnas.org)
- The distribution and function of aquaporins (AQPs) have not previously been defined in sweat glands. (jhu.edu)
- Aquaporins (AQPs) play a pivotal role in the cellular transport of water and many other small solutes, influencing many physiological and developmental processes in plants. (mdpi.com)
- We computationally determined the diffusional (PD) and osmotic (Pf) water permeability coefficients for the mammalian CDE based on in silico simulations of cochlear water dynamics integrating previously derived in vivo experimental data on fluid flow with expression sites of molecular water channels (aquaporins, AQPs). (nih.gov)
- The aquaporins (AQPs) are water selective. (wikipedia.org)
- Extensive research on the function of aquaporins have been implemented into many separate types of cell membranes. (proteopedia.org)
- 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)
- Os CH van, Deen PMT, Dempster JA (1994) Aquaporins: water selective channels in biological membranes. (springer.com)
- The water permeability of cell membranes differs by orders of magnitude, and most of this variability reflects the differential expression of aquaporin water channels. (jhu.edu)
- The summary about aquaporins which were first described as channels increased permeability of lipid membranes to water in response to osmotic and/or hydrostatic gradients. (prolekare.cz)
- Their membranes are 6 nm thick and contain a number of protein pumps and antiporters, including aquaporins, ATPases and Ca2+/H+ and Na+/H+ antiporters. (wikipedia.org)
- Relative to simple diffusion, the presence of aquaporins in biological membranes facilitates a 3-10 fold increase in water permeability. (wikipedia.org)
- Aquaporin-6 (AQP6) has recently been identified as an intracellular vesicle water channel with anion permeability that is activated by low pH or HgCl2. (jhu.edu)
- Water permeability of the mammalian cochlea: functional features of an aquaporin-facilitated water shunt at the perilymph-endolymph barrier. (nih.gov)
- The aim is to investigate the physiological role of aquaporins and vasopressin receptors in porcine and rat urinary bladders. (findaphd.com)
- 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)
- Zholkevich, V. 2008-10-31 00:00:00 To elucidate the role of aquaporins in the control of the root pressure, we tested the effects of HgCl2 (aquaporin blocker) at concentrations from 10−8 to 10−2 M on the exudation rate (J w). (deepdyve.com)
- Hence, the discussion about the role of aquaporins in the majority of multicellular organisms remains open ( Chrispeels and Maurel, 1994 ). (plantcell.org)
- Because of the potential role of aquaporins in regulating water flow in plants, a number of studies have focused on the sites of aquaporin gene expression. (plantphysiol.org)
- Here we show that an ancient aquaporin gene cluster evolved specifically in the sarcopterygian lineage, and subsequently diverged into paralogous forms of AQP2, -5, or -6 to mediate water conservation in extant Tetrapoda. (nih.gov)
- Teleost and tetrapod subclusters are shaded according to the aquaporin grade, except for sarcopterygian Aqp2, -5, and -6 paralogs, which are shaded in pink. (nih.gov)
- Congenital nephrogenic diabetes insipidus (NDI) may result from V2R or aquaporin-2 (AQP2) mutations. (wikipedia.org)
- This gene has been mapped among aquaporins AQP2, AQP5, and AQP6, in a potential gene cluster at 12q13. (wikipedia.org)
- In this direction we investigated, in some regions of the rat gastrointestinal tract, the presence and localization of aquaporin-6, given its peculiar function as an ion selective channel. (elsevier.com)
- Aquaporin-6 localization at the apical pole of the superficial epithelial cells and its upregulation by feeding suggest that it may be involved in movements of water and anions through the epithelium of the villi. (elsevier.com)
- Expression, localization, and regulation of aquaporin-1 to -3 in rat urothelia. (findaphd.com)
- Neuromyelitis optica (NMO) is an inflammatory disease affecting the optic nerve and spinal cord, in which autoantibodies against aquaporin 4 (AQP4) water channel protein probably play a pathogenic role. (pnas.org)
- Aquaporin-4 antibodies (AQP4-Ab) are associated with neuromyelitis optica spectrum disorder (NMOSD) and typically this disorder has a poor visual prognosis as a result of optic neuritis (ON). (neurodiem.de)
- Aquaporin 4 and neuromyelitis optica. (springer.com)
- Genetic defects involving aquaporin genes have been associated with several human diseases including nephrogenic diabetes insipidus and neuromyelitis optica. (wikipedia.org)
- Aquaporin-4 is the predominant autoimmune target in neuromyelitis optica, or NMO, since a specific AQP4 IgG autoantibody, or NMO-IgG, binds to the extracellular surface of AQP4. (wikipedia.org)
- Currently two principal causes are accepted: In NMO-IgG positive patients, the cause of the neuromyelitis optica (understood as the syndrome) is an autoimmune aquaporin-4 channelopathy, due to these specific autoantibodies. (wikipedia.org)
- Nevertheless, this model is questioned by recent reports that found astrocyte damage, similar to the one found in aquaporin-seropositive neuromyelitis optica. (wikipedia.org)
- Expression of aquaporin-5 (AQP5), studied by immunofluorescence and confocal microscopy, showed an increase in parallel with the increase in P f following hyperosmotic stress. (springer.com)
- Aquaporin-5 (AQP5) is a water channel protein expressed in lung, salivary gland, and lacrimal gland epithelia. (jhu.edu)
- Aquaporin 5 (AQP5) is a water channel protein. (antibodies-online.com)
- Findings show that overexpression of aquaporin 5 (AQP5 ) activated epithelial-mesenchymal transition ( EMT (show ITK Antibodies )) in colorectal cancer ( CRC (show CALR Antibodies )) cells. (antibodies-online.com)
- Osmotic water permeabilities of aquaporins AQP4 (show AQP4 Antibodies ), AQP5 , and GlpF from near-equilibrium simulations have been presented. (antibodies-online.com)
- Based on previous research using mice and rats, researchers looked towards the role of aquaporin 5 (AQP5), a water channel protein, in human individuals with primary focal hyperhidrosis. (wikipedia.org)
- AQP6 is located on human 12q13 chromosome and exhibit significant homology with other aquaporin protein. (acris-antibodies.com)
- Aquaporin 6, kidney specific is a protein in humans that is encoded by the AQP6 gene. (wikipedia.org)
- Unlike other aquaporins, AQP6 functions not as a water channel but as an anion-selective channel. (jhu.edu)
- This is supported by the fact that the bladder urothelium expresses the transmembrane water channels (aquaporins). (findaphd.com)
- Cheung KH, Leung CT, Leung GP, Wong PY (2003) Synergistic effects of cystic fibrosis transmembrane conductance regulator and aquaporin-9 in the rat epididymis. (springer.com)
- With the exception of the yeast protein (627 amino acyl residues), all characterized members of the family are of 256-285 residues in length and exhibit 6-8 putative transmembrane α-helical spanners (TMSs). (wikipedia.org)
- Arima H, Yamamoto N, Sobue K, Umenishi F, Tada T, Katsuya H, Asai K (2003) Hyperosmolar mannitol simulates expression of aquaporins 4 and 9 through a p38 mitogen-activated protein kinase-dependent pathway in rat astrocytes. (springer.com)
- Expression of aquaporins in bronchial tissue and lung parenchyma of patients with chronic obstructive pulmonary disease. (abcam.com)
- Increased expression of aquaporins in placenta of the late gestation mouse fetus. (prolekare.cz)
- Expression of aquaporins in the renal connecting tubule. (prolekare.cz)
- Early work of Nobel Prize winner, Peter Agre and his group first clone a 269 amino acid protein from RBC and kidney libraries that has a 6 TMD (1). (acris-antibodies.com)
- The persistent high urine volume after AVP administration was traced to a reduction in aquaporin-1 expression in the kidney of LXRβ −/− mice. (pnas.org)
- The basic job of aquaporin 2 is to reabsorb water from the urine while its being removed from the blood by the kidney. (wikipedia.org)
- Aquaporins selectively conduct water molecules in and out of the cell, while preventing the passage of ions and other solutes. (wikipedia.org)
- Aquaporins selectively transport water (but not glycerol) while glycerol facilitators selectively transport glycerol but not water. (tcdb.org)
- Aquaporins are selectively permeable to water but exclude cations e.g. (coursehero.com)
- Here we show that NMO-IgG binds selectively to the aquaporin-4 water channel, a component of the dystroglycan protein complex located in astrocytic foot processes at the blood-brain barrier. (rupress.org)
- Aquaporins selectively transport glycerol as well as water while glycerol facilitators selectively transport glycerol but not water. (wikipedia.org)
- Future research on renal water transport will focus on the search for other aquaporins, structure-function relationship of aquaporins, the development of aquaporin inhibitors and their possible use as diuretics, and further elucidation of the renal vasopressin pathway. (springer.com)
- Hydrogen-rich solution against myocardial injury and aquaporin expression via the PI3K/Akt signaling pathway during cardiopulmonary bypass in rats. (abcam.com)
- The 2003 Nobel Prize in Chemistry was awarded jointly to Peter Agre for the discovery of aquaporins, and Roderick MacKinnon for his work on the structure and mechanism of potassium channels. (wikipedia.org)
- It was not until 1992 that the first aquaporin, 'aquaporin-1' (originally known as CHIP 28), was reported by Peter Agre, of Johns Hopkins University. (wikipedia.org)
- 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)
- Agre said he discovered aquaporins "by serendipity. (wikipedia.org)
- Agre P (2006) The aquaporin water channels. (springer.com)
- Amiry-Moghaddam M, Williamson A, Palomba M, Eid T, De Lanerolle NC, Nagelhus EA, Adams ME, Froehner SC, Agre P, Ottersen OP (2003) Delayed K + clearance associated with aquaporin-4 mislocalization: phenotypic defects in brains of α-syntrophin-null mice. (springer.com)
- Ampah-Korsah H, Sonntag Y, Engfors A, Kirscht A, Kjellbom P, Johanson U (2017) Single amino acid substitutions in the selectivity filter render NbXIP1;1α aquaporin water permeable. (springer.com)
- Aquaglyceroporins form the subset of the aquaporin water channel family that is permeable to glycerol and certain small, uncharged solutes. (jhu.edu)
- In the CNS lesions of NMO, reduced expression of AQP4 on astrocytes is evident even during the early stage ( 6 ), which is followed by the occurrence of vasculocentric destruction of astrocytes associated with perivascular deposition of complement and IgG ( 7 ). (pnas.org)
- However, the rapid swelling of astrocytes in ischemic brain injury contributes to astrocyte dysfunction during stroke, and this rapid swelling is induced by aquaporins [ 4 , 5 ]. (hindawi.com)
- Aquaporin-4 is highly expressed in the human body primarily at the end-feet of astrocytes. (wikipedia.org)
- NMO is associated with the NMO-IgG biomarker, which targets the aquaporin-4 water channel on astrocytes. (hindawi.com)
- Aquaporin 4 is found in the astrocytes that surround the blood-brain barrier (BBB), a system responsible for preventing substances in the blood from crossing into the brain. (wikipedia.org)
- Researchers have long known that astrocytes express water channels called aquaporins. (wikipedia.org)
- Aquaporin-4 expression in astrocytes is highly polarized to the endfoot processes ensheathing the cerebral vasculature. (wikipedia.org)
- A synthetic peptide from the n-terminal region of human Aquaporin 7 (AQP7) conjugated to an immunogenic carrier protein was used as the immunogen. (novusbio.com)
- Expression and localisation of aquaporin water channels in human urothelium in situ and in vitro. (findaphd.com)
- One year later, a Chesebrough-Ponds patent 6 disclosing cosmetic compositions containing phytovitamin D 3 contained a discussion of keratinocytes, which constitute 75-80% of the total number of cells in the human epidermis. (cosmeticsandtoiletries.com)
- Aquaglyceroporin aquaporin (AQP)3 is the major glycerol channel in human and rat erythrocytes. (jhu.edu)
- Bellemere G, Von Stetten O, Oddos T (2008) Retinoic acid increases aquaporin 3 expression in normal human skin. (springer.com)
- Human red cell aquaporin CHIP. (wikipedia.org)
- The human Aquaporin-5 gene. (jhu.edu)
- A replication-deficient, recombinant adenovirus encoding human aquaporin-1 (hAQP1), the archetypal water channel, was constructed. (jhu.edu)
- Aoki K, Uchihara T, Tsuchiya K, Nakamura A, Ikeda K, Wakayama Y (2003) Enhanced expression of aquaporin 4 in human brain infarction. (springer.com)
- Aquaporin-4 (AQP4), the main water channel of the brain, is highly expressed in animal glioma and human glioblastoma in situ. (biomedsearch.com)
- Roles of aquaporins in human cancer have been reviewed as have their folding pathways. (wikipedia.org)
- Gene expression profile studies of human keratoconus cornea for NEIBank: a novel cornea-expressed gene and the absence of transcripts for aquaporin 5" (PDF). (wikipedia.org)
- Aquaporins are selective water/glycerol channels involved in the maintenance of volume homeostasis and ionic/osmotic balance. (acris-antibodies.com)
- Aquaporin protein regulation and redistribution in response to osmotic stress was investigated. (plantphysiol.org)
- Aquaporins allow water to move down their osmotic gradient and out of the nephron, increasing the amount of water re-absorbed from the filtrate (forming urine) back into the bloodstream. (wikipedia.org)
- Long-term regulation of four renal aquaporins in rats. (findaphd.com)
- Aquaporin channels may be subject to intense short term regulation via signal transduction. (proteopedia.org)
- 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)
- Alexandersson E, Fraysse L, Sjövall-Larsen S, Gustavsson S, Fellert M, Karlsson M et al (2005) Whole gene family expression and drought stress regulation of aquaporins. (springer.com)
- The purpose of this study was to focuse on aquaporins and their role in the regulation of amniotic fluid circulation. (prolekare.cz)
- The present review summarizes the results of clinical and experimental research on aquaporins and the regulation of amniotic fluid circulation. (prolekare.cz)