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

Reduced water permeability and altered ultrastructure in thin descending limb of Henle in aquaporin-1 null mice. (1/469)

It has been controversial whether high water permeability in the thin descending limb of Henle (TDLH) is required for formation of a concentrated urine by the kidney. Freeze-fracture electron microscopy (FFEM) of rat TDLH has shown an exceptionally high density of intramembrane particles (IMPs), which were proposed to consist of tetramers of aquaporin-1 (AQP1) water channels. In this study, transepithelial osmotic water permeability (Pf) was measured in isolated perfused segments (0.5-1 mm) of TDLH in wild-type (+/+), AQP1 heterozygous (+/-), and AQP1 null (-/-) mice. Pf was measured at 37 degrees C using a 100 mM bath-to-lumen osmotic gradient of raffinose, and fluorescein isothiocyanate (FITC)-dextran as the luminal volume marker. Pf was (in cm/s): 0.26 +/- 0.02 ([+/+]; SE, n = 9 tubules), 0.21 +/- 0.01 ([+/-]; n = 12), and 0.031 +/- 0.007 ([-/-]; n = 6) (P < 0.02, [+/+] vs. [+/-]; P < 0.0001, [+/+] vs. [-/-]). FFEM of kidney medulla showed remarkably fewer IMPs in TDLH from (-/-) vs. (+/+) and (+/-) mice. IMP densities were (in microm-2, SD, 5-12 micrographs): 5,880 +/- 238 (+/+); 5,780 +/- 450 (+/-); and 877 +/- 420 (-/-). IMP size distribution analysis revealed mean IMP diameters of 8.4 nm ([+/+] and [+/-]) and 5.2 nm ([-/-]). These results demonstrate that AQP1 is the principal water channel in TDLH and support the view that osmotic equilibration along TDLH by water transport plays a key role in the renal countercurrent concentrating mechanism. The similar Pf and AQP1 expression in TDLH of (+/+) and (+/-) mice was an unexpected finding that probably accounts for the unimpaired urinary concentrating ability in (+/-) mice.  (+info)

Lung fluid transport in aquaporin-1 and aquaporin-4 knockout mice. (2/469)

The mammalian lung expresses water channel aquaporin-1 (AQP1) in microvascular endothelia and aquaporin-4 (AQP4) in airway epithelia. To test whether these water channels facilitate fluid movement between airspace, interstitial, and capillary compartments, we measured passive and active fluid transport in AQP1 and AQP4 knockout mice. Airspace-capillary osmotic water permeability (Pf) was measured in isolated perfused lungs by a pleural surface fluorescence method. Pf was remarkably reduced in AQP1 (-/-) mice (measured in cm/s x 0.001, SE, n = 5-10: 17 +/- 2 [+/+]; 6.6 +/- 0.6 AQP1 [+/-]; 1.7 +/- 0.3 AQP1 [-/-]; 12 +/- 1 AQP4 [-/-]). Microvascular endothelial water permeability, measured by a related pleural surface fluorescence method in which the airspace was filled with inert perfluorocarbon, was reduced more than 10-fold in AQP1 (-/-) vs. (+/+) mice. Hydrostatically induced lung interstitial and alveolar edema was measured by a gravimetric method and by direct measurement of extravascular lung water. Both approaches indicated a more than twofold reduction in lung water accumulation in AQP1 (-/-) vs. (+/+) mice in response to a 5- to 10-cm H2O increase in pulmonary artery pressure for five minutes. Active, near-isosmolar alveolar fluid absorption (Jv) was measured in in situ perfused lungs using 125I-albumin as an airspace fluid volume marker. Jv (measured in percent fluid uptake at 30 min, n = 5) in (+/+) mice was 6.0 +/- 0.6 (37 degrees C), increased to 16 +/- 1 by beta-agonists, and inhibited to less than 2.0 by amiloride, ouabain, or cooling to 23 degrees C. Jv (with isoproterenol) was not affected by aquaporin deletion (18.9 +/- 2.2 [+/+]; 16.4 +/- 1.5 AQP1 [-/-]; 16.3 +/- 1.7 AQP4 [-/-]). These results indicate that osmotically driven water transport across microvessels in adult lung occurs by a transcellular route through AQP1 water channels and that the microvascular endothelium is a significant barrier for airspace-capillary osmotic water transport. AQP1 facilitates hydrostatically driven lung edema but is not required for active near-isosmolar absorption of alveolar fluid.  (+info)

Developmental expression of aquaporin 1 in the rat renal vasculature. (3/469)

Aquaporin 1 (AQP-1) is a water channel protein that is constitutively expressed in renal proximal tubule and descending thin limb cells as well as in endothelial cells of the descending vasa recta. Studies in the developing rat kidney have demonstrated that AQP-1 is expressed in renal tubules before birth. However, nothing is known about the expression of AQP-1 in the renal vasculature during kidney development. The purpose of this study was to establish the distribution of AQP-1 in the renal vasculature of the developing rat kidney and follow the differentiation of the vascular system during kidney development. Kidneys from 16-, 17-, 18-, and 20-day-old fetuses and 1-, 4-, 7-, 14-, 21-, and 28-day-old pups were preserved and processed for immunohistochemical studies using a preembedding immunoperoxidase procedure. AQP-1 immunoreactivity was detected using affinity-purified rabbit polyclonal antibodies to AQP-1. AQP-1 was expressed throughout the arterial portion of the renal vasculature of the fetal and neonatal kidney from gestational age 17 days to 1 wk after birth. AQP-1 immunoreactivity gradually disappeared from the renal vasculature between 1 and 2 wk of age and remained only in the descending vasa recta. In contrast, AQP-1 immunoreactivity was not observed in lymphatic vessels until 3 wk of age and persisted in the adult kidney. AQP-1 was also expressed in a population of interstitial cells in the terminal part of the renal papilla at 3 wk of age as well as in the adult kidney. The transient expression of AQP-1 in the arterial portion of the renal vasculature in the developing rat kidney suggests that AQP-1 is important for fluid equilibrium and/or drainage in the developing kidney or, alternatively, plays a role in the regulation of growth and/or branching of the vascular tree during kidney development.  (+info)

Molecular identification and immunolocalization of the water channel protein aquaporin 1 in CBCECs. (4/469)

PURPOSE: Water channel proteins are important pathways for water movements across cell membranes, including those in the corneal endothelium that contribute to the fluid transport mechanism essential in maintaining corneal transparency. This study was conducted to identify and locate the water channel protein(s) in cultured bovine corneal endothelial cells (CBCECs). METHODS: Poly(A)+ RNA was isolated from CBCECs, and MMLV reverse transcriptase and random hexamer primers were used to generate a cDNA pool by reverse transcription-polymerase chain reaction (RT-PCR). Two specific degenerate primers were synthesized based on consensus sequences from the major intrinsic lens protein superfamily; a "touchdown" PCR protocol accommodated the degeneracy. Immunolocalization was performed by incubating sections of CBCECs with an antibody against human aquaporin 1 (AQP1). Cryosections (0.85 microm) of CBCECs were used for light microscopy, and 800-A ultrathin cryosections were used for electron microscopy (EM). RESULTS: A 372-bp fragment was isolated. Its encoded amino acid sequence was 100% identical with that of bovine AQP1 (AQP2_bovin). CBCECs reacted strongly with the anti-AQP1 antibody, and the labeling was selectively localized to the plasma membrane by light microscopy. Subcellular localization by EM revealed immunoreactivity with the inner leaflets of the plasma membrane. CONCLUSIONS: The identity of the aquaporin, its abundance, and its membrane location suggest that it is a major pathway for fluid flow across endothelial cell membranes. This is consistent with transcellular endothelial fluid transport.  (+info)

Novel method for evaluation of the oligomeric structure of membrane proteins. (5/469)

Assessment of the quaternary structure of membrane proteins by PAGE has been problematic owing to their relatively poor solubility in non-dissociative detergents. Here we report that several membrane proteins can be readily solubilized in their native quaternary structure with the use of the detergent perfluoro-octanoic acid (PFO). Further, PFO can be used with PAGE, thereby providing a novel, accessible tool with which to assess the molecular mass of homo-multimeric protein complexes.  (+info)

Regulation of aquaporin-1 and nitric oxide synthase isoforms in a rat model of acute peritonitis. (6/469)

The loss of ultrafiltration (UF) that accompanies acute peritonitis is a common problem in peritoneal dialysis (PD). It has been suggested that changes in nitric oxide (NO)-mediated vascular tone and permeability might be involved in the loss of UF, whereas channel-mediated water permeability should not be affected. This study used a model of acute peritonitis in rats to characterize changes in PD parameters, in correlation with: (1) expression studies of water channel aquaporin-1 and NO synthase (NOS) isoforms and (2) enzymatic assays for NOS in the peritoneum. Compared with controls, rats with peritonitis had a higher removal of plasma urea, a faster glucose absorption, and a loss of UF. Additional changes, including high protein loss, elevated leukocyte counts in dialysate, positive bacterial cultures, edema, and mononuclear infiltrates, were similar to those observed in PD patients with acute peritonitis. Acute peritonitis in rats induced a major increase in total NOS activity, which was inversely correlated with free-water permeability. The increased NOS activity was mediated by both inducible (Ca2+-independent) and endothelial (Ca2+-dependent) NOS isoforms and was reflected by increased peritoneal staining for nitrotyrosine. In contrast, aquaporin-1 expression was unchanged in rats with peritonitis. These findings cast light on the pathophysiology of permeability changes and loss of UF that characterize acute peritonitis. In particular, these data suggest that a local production of NO, mediated by different NOS isoforms, might play a key role in these changes.  (+info)

Micropuncture analysis of tubuloglomerular feedback regulation in transgenic mice. (7/469)

Micropuncture methods have been used widely as a means to define the function of single tubules and study the functional connection between tubules and afferent arterioles (so-called tubuloglomerular feedback [TGF]). Transgenic mouse strains have become a new research tool with the potential of shedding new light on the role of specific gene products in renal tubular and vascular function. The micropuncture approach has therefore been adapted to studies in the mouse kidney. Although the data presented here support the feasibility of using this technique in the mouse, technical improvements are desirable in the areas of anesthesia, ureteral urine collections, blood collections, volume replacement, and functional stability for extended time periods. During ketamine/inactin anesthesia, TGF responses could regularly be elicited in wild-type mice. In contrast, changes in loop flow did not alter stop-flow pressure in angiotensin II type 1A receptor and angiotensin-converting enzyme knockout mice. Infusion of angiotensin II in subpressor doses partially restored TGF responsiveness in angiotensin-converting enzyme knockout animals. Normal TGF responses compared to wild type were found in nitric oxide synthase I and thromboxane receptor knockout mice. Using free-flow micropuncture techniques, the proximal-distal single-nephron GFR difference was found to be augmented in aquaporin-1 and Na/H exchanger-3 knockout mice, suggesting TGF activation in these strains of mice. These results support an essential role of angiotensin II in TGF regulation mediated through the angiotensin II type 1A receptor. Chronic nitric oxide synthase I and thromboxane receptor deficiency did not change TGF responsiveness. Aquaporin-1 and Na/H exchanger-3 deficiency enhances TGF suppression of TGF probably by volume depletion-mediated TGF sensitization. The use of micropuncture methodology in transgenic mice combines old and new research tools in a way that promises to yield important new insights into single-nephron function in physiologic and pathophysiologic conditions.  (+info)

Safety and efficacy of adenovirus-mediated transfer of the human aquaporin-1 cDNA to irradiated parotid glands of non-human primates. (8/469)

This study evaluated the safety and efficacy of a single administration of a recombinant adenovirus encoding human aquaporin-1 (AdhAQP1) to the parotid glands of adult rhesus monkeys. In anticipation of possible clinical use of this virus to correct irradiation damage to salivary glands, AdhAQP1 was administered (at either 2 x 10(9) or 1 x 10(8) plaque-forming units/gland) intraductally to irradiated glands and to their contralateral nonirradiated glands. Radiation (single dose, 10 Gy) significantly reduced salivary flow in exposed glands. Virus administration resulted in gene transfer to irradiated and nonirradiated glands and was without untoward local (salivary) or systemic (sera chemistry, complete blood count) effects in all animals. However, the effect of AdhAQP1 administration varied and did not result in a consistent positive effect on salivary flow rates for all animals under these experimental conditions. We conclude that a single adenoviral-mediated gene transfer to primate salivary glands is well-tolerated, although its functional utility in enhancing fluid secretion from irradiated parotid glands is inconsistent.  (+info)

*Tetraethylammonium

E. M. Müller, J. S. Hub, H. Grubmüller, and B. L. de Groot (2008). "Is TEA an inhibitor for human Aquaporin-1?" Pflugers Arch. ... It has also been reported that TEA inhibits aquaporin (APQ) channels, but this still seems to be a disputed issue. A partial ...

*Major intrinsic proteins

The MIP superfamily includes three subfamilies: aquaporins, aquaglyceroporins and S-aquaporins. The aquaporins (AQPs) are water ... Aquaporin-1 (Aqp1) from the human red blood cell has been solved by electron crystallography to 3.8 Å resolution (PDB: 1FQY​). ... Aquaporins generally have the NPA motif in both halves, the glycerol facilitators generally have an NPA motif in the first ... Roles of aquaporins in human cancer have been reviewed as have their folding pathways. AQPs may act as transmembrane ...

*Secretin

Evidence for a secretin-induced vesicular translocation of aquaporin-1". The Journal of Biological Chemistry. 272 (20): 12984-8 ... translocation of aquaporin 2, or both are found. It has been suggested that "Secretin as a neurosecretory hormone from the ... "Secretin promotes osmotic water transport in rat cholangiocytes by increasing aquaporin-1 water channels in plasma membrane. ... 127 (1): 43-54. doi:10.1002/ijc.25028. PMID 19904746. Lee LT, Tan-Un KC, Pang RT, Lam DT, Chow BK (2004). "Regulation of the ...

*Secretin

Evidence for a secretin-induced vesicular translocation of aquaporin-1". The Journal of Biological Chemistry. 272 (20): 12984-8 ... translocation of aquaporin 2, or both are found.[9] It has been suggested that "Secretin as a neurosecretory hormone from the ... 90 (1-2): 47-52. doi:10.1159/000015658. PMID 11060443.. *^ 1947-, Costanzo, Linda S., (2006). Physiology (3rd ed.). ... "Secretin promotes osmotic water transport in rat cholangiocytes by increasing aquaporin-1 water channels in plasma membrane. ...

*GLUT1

... and aquaporin-1 in human erythrocyte membrane domains". Biochimica et Biophysica Acta. 1828 (3): 956-66. doi:10.1016/j.bbamem. ... ISBN 978-0-7167-7108-1.. [page needed] *^ Montel-Hagen A, Kinet S, Manel N, Mongellaz C, Prohaska R, Battini JL, Delaunay J, ... Glucose transporter 1 (or GLUT1), also known as solute carrier family 2, facilitated glucose transporter member 1 (SLC2A1), is ... GLUT 1 is highly conserved.[5] GLUT 1 of humans and mice have 98% identity at the amino acid level. GLUT 1 is encoded by the ...

*Andreas Engel

"Aquaporin water channels - from atomic structure to clinical medicine". The Journal of Physiology. 542 (1): 3-16. doi:10.1113/ ... Fujiyoshi and Engel solved the structure of Aquaporin-1 in collaboration with Agre. Together with Palczewski Engel's team ... 177 (1): 3-13. doi:10.1016/j.jsb.2011.11.013. PMID 22115996. "Farewell Symposium for Andreas Engel". unibas.ch. Retrieved 2015- ...

*Heterotetramer

Examples include haemoglobin (pictured), the NMDA receptor, some aquaporins, some AMPA receptors, as well as some enzymes. Ion- ... "Heterotetrameric Composition of Aquaporin-4 Water Channels". Biochemistry. 38 (34): 11156-63. doi:10.1021/bi990941s. PMID ... 426 (1): 199-214. doi:10.1016/j.jmb.2013.09.016. PMC 4047826 . PMID 24056174. Howarth, Mark; Chinnapen, Daniel J-F; Gerrow, ... Neely, John D.; Christensen, Birgitte M.; Nielsen, Søren; Agre, Peter (1 August 1999). " ...

*Secretina, a enciclopedia libre

Evidence for a secretin-induced vesicular translocation of aquaporin-1" (PDF). J. Biol. Chem. 272 (20): 12984-12988. PMID ... "Secretin promotes osmotic water transport in rat cholangiocytes by increasing aquaporin-1 water channels in plasma membrane. ... 1] *↑ 3,0 3,1 Kopin AS, Wheeler MB, Leiter AB (1990). "Secretin: structure of the precursor and tissue distribution of the mRNA ... 6,0 6,1 6,2 6,3 Chu JY, Lee LT, Lai CH, Vaudry H, Chan YS, Yung WH, Chow BK (2009). "Secretin as a neurohypophysial factor ...

*Vitreous body

Aquaporin-4 in Müller cell in rats, transports water to the vitreous body. The vitreous has many anatomical landmarks, ... "Aquaporin-4 water channel protein in the rat retina and optic nerve: polarized expression in Müller cells and fibrous ... 2010: 1-15. doi:10.1155/2010/190724. Nagelhus, EA; Veruki, ML; Torp, R; Haug, FM; Laake, JH; Nielsen, S; Agre, P; Ottersen, OP ... 1 March 2016. Velpandian, Thirumurthy (29 February 2016). "Pharmacology of Ocular Therapeutics". Springer - via Google Books. ...

*Mir-708 microRNA precursor family

"Aquaporin-1 Promotes Angiogenesis, Fibrosis, and Portal Hypertension Through Mechanisms Dependent on Osmotically Sensitive ... 70 (1): 36-45. doi:10.1158/0008-5472.CAN-09-3153. PMID 20028859. Schotte, D.; Chau, J. C. K.; Sylvester, G.; Liu, G.; Chen, C ... miR-708 is located on chromosome 11q14.1 and is endcoded in intron 1 of the ODZ4 gene. It is most highly expressed in the brain ...

*Lesional demyelinations of the central nervous system

Around active NMO lesions AQP4 may selectively be lost in the absence of aquaporin 1 (AQP1) loss or other structural damage ( ... 28 (1): 84-94. doi:10.1055/s-2007-1019130. Misu T, Höftberger R, Fujihara K, Wimmer I, Takai Y, Nishiyama S, Nakashima I, Konno ... 255 (1): 1-10. doi:10.1007/s00415-007-0754-x. Garrido C, Levy-Gomes A, Teixeira J, Temudo T (2004). "[Schilder's disease: two ... 1][permanent dead link]list of CCSVI publications Dawson J.W. (1916). "The histology of disseminated sclerosis". Trans Roy Soc ...

*Colton antigen system

The Co antigen is found on a protein called aquaporin-1 which is responsible for water homeostasis and urine concentration. The ... Agre P.Defective urinary-concentrating ability due to a complete deficiency of aquaporin-1. N Engl J Med. 2001 Jul 19;345(3): ...

*Neuromyelitis optica

Aquaporin 4 is found in the astrocytes that surround the blood-brain barrier (BBB), a system responsible for preventing ... In 2005 they identified the aquaporin 4 protein as the target of the disease, and developed a test to aid in the diagnosis of ... These antibodies target the protein aquaporin 4 in the cell membranes of astrocytes which acts as a channel for the transport ... Since the discovery of AQP-4 involvement, some research studies have focused on targeted treatment aimed at anti-aquaporin 4 ...

*AQP1 - Wicipedia

"Increased aquaporin 1 expression in the tunica albuginea of Peyronie's disease patients: an in vivo pilot study. ". Histol ... "Overexpression of Aquaporin 1 on cysts of patients with polycystic liver disease.". Rev Esp Enferm Dig. 2016. PMID 26838488. ... "Overexpression of Aquaporin-1 is a Prognostic Factor for Biochemical Recurrence in Prostate Adenocarcinoma. ". Pathol Oncol Res ... "Red blood cell aquaporin-1 expression is decreased in hereditary spherocytosis. ". Ann Hematol. 2016. PMID 27465156. ...

*Urea transporter

Yang B, Verkman AS (September 2002). "Analysis of double knockout mice lacking aquaporin-1 and urea transporter UT-B. Evidence ... UT-1 is activated by ADH, but is a passive transporter. It reabsorbs up to 70% of the original filtered load of urea. Urea ...

*Syntrophin, alpha 1

"In vivo requirement of the alpha-syntrophin PDZ domain for the sarcolemmal localization of nNOS and aquaporin-4". J. Cell Biol ... "Syntrophin-dependent expression and localization of Aquaporin-4 water channel protein". Proc. Natl. Acad. Sci. U.S.A. 98 (24): ... Alpha-1-syntrophin is a protein that in humans is encoded by the SNTA1 gene. Dystrophin is a large, rod-like cytoskeletal ... 12 Suppl 1: S110-7. doi:10.1016/S0960-8966(02)00091-3. PMID 12206805. Yang B, Jung D, Rafael JA, Chamberlain JS, Campbell KP ( ...

*Uterine epithelium

Lindsay, L. A., & Murphy, C. R. (2006). Redistribution of aquaporins 1 and 5 in the rat uterus is dependent on progesterone: a ... Lindsay, L. A., & Murphy, C. R. (2004). Redistribution of aquaporins in uterine epithelial cells at the time of implantation in ... Cell Physiology, 283(1), C142-C147. Enders, A. C., & Nelson, D. M. (1973). Pinocytotic activity of the uterus of the rat. ... The Journal of membrane biology, 206(1), 17-28. Tsang, L. L., Chan, L. N., Wang, X. F., So, S. C., Yuen, J. P., Fiscus, R. R ...

*Caveolin 1

Zheng, Xiangjian; Bollinger Bollag Wendy (December 2003). "Aquaporin 3 colocates with phospholipase d2 in caveolin-rich ... Caveolin-1 is a protein that in humans is encoded by the CAV1 gene. The scaffolding protein encoded by this gene is the main ... 271 (1): 568-73. doi:10.1074/jbc.271.1.568. PMID 8550621. Razani, B; Zhang X L; Bitzer M; von Gersdorff G; Böttinger E P; ... Feng, X; Gaeta M L; Madge L A; Yang J H; Bradley J R; Pober J S (March 2001). "Caveolin-1 associates with TRAF2 to form a ...

*கண்ணாடியுடனீர் - தமிழ் விக்கிப்பீடியா

"Aquaporin-4 water channel protein in the rat retina and optic nerve: polarized expression in Müller cells and fibrous ... இதன் அளவு மொத்த கண்ணின் அளவில் ஐந்தில் நான்கு பங்கு அளவு கொண்டதாகும்.[1] இதன் மைய பகுதிக்கு அருகாமையில் திரவ நிலையிலும், ... Nagelhus, EA; Veruki, ML; Torp, R; Haug, FM; Laake, JH; Nielsen, S; Agre, P; Ottersen, OP (1 April 1998). " ...

*Stanley Froehner

Syntrophin-dependent expression and localization of Aquaporin-4 water channel protein. vol. 98 no. 24. John D. Neely, 14108- ... 128-137 Delayed K+ clearance associated with aquaporin-4 mislocalization: Phenotypic defects in brains of α-syntrophin-null ...

*Marine life

Agre, P (2006). "The aquaporin water channels". Proceedings of the American Thoracic Society. 3 (1): 5-13. doi:10.1513/pats. ... 10 (1): 31-8. doi:10.1016/S0966-842X(01)02257-0. PMID 11755083. Hyde, K.D.; E.B.J. Jones; E. Leaño; S.B. Pointing; A.D. Poonyth ... 53 (1): 1377-1378. Jones, E.B.G., Hyde, K.D., & Pang, K.-L., eds. (2014). Freshwater fungi: and fungal-like organisms. Berlin/ ... 2006;117(1):156-84. doi:10.1016/j.virusres.2006.01.009. PMID 16494962. Sanjuán R, Nebot MR, Chirico N, Mansky LM, Belshaw R. ...

*Countercurrent multiplication

The thick ascending limb of the loop of Henle is the only part of the nephron lacking in aquaporin-a common transporter protein ... The ascending limb is impermeable to water (because of a lack of aquaporin, a common transporter protein for water channels in ... due to the presence of aquaporin 1 in its tubular wall. Thus water moves across the tubular wall into the medullary space, ...

*Glymphatic system

Two types of aquaporins are expressed in the CNS: aquaporin-1, which is expressed by specialized epithelial cells of the ... Aquaporins are membrane-bound channels that play critical roles in regulating the flux of water into and out of cells. Relative ... Aquaporin-4 expression in astrocytes is highly polarized to the endfoot processes ensheathing the cerebral vasculature. Up to ... Yool AJ (2007). "Aquaporins: multiple roles in the central nervous system". Neuroscientist. 13 (5): 470-85. doi:10.1177/ ...

*List of MeSH codes (D12.776.157)

... aquaporin 3 MeSH D12.776.157.530.400.500.040.249.750 -- aquaporin 6 MeSH D12.776.157.530.400.500.040.374 -- aquaporin 1 MeSH ... aquaporin 4 MeSH D12.776.157.530.400.500.040.484 -- aquaporin 5 MeSH D12.776.157.530.400.500.520 -- voltage-dependent anion ... aquaporins MeSH D12.776.157.530.400.500.040.249 -- aquaglyceroporins MeSH D12.776.157.530.400.500.040.249.500 -- ... File "2006 MeSH Trees".) MeSH D12.776.157.057.030.124 -- interferon regulatory factor-1 MeSH D12.776.157.057.030.249 -- ...

*List of MeSH codes (D12.776.543)

... aquaporin 3 MeSH D12.776.543.550.425.730.040.249.750 -- aquaporin 6 MeSH D12.776.543.550.425.730.040.374 -- aquaporin 1 MeSH ... aquaporin 3 MeSH D12.776.543.585.400.730.040.249.750 -- aquaporin 6 MeSH D12.776.543.585.400.730.040.436 -- aquaporin 1 MeSH ... aquaporin 4 MeSH D12.776.543.550.425.730.040.484 -- aquaporin 5 MeSH D12.776.543.550.425.730.520 -- voltage-dependent anion ... aquaporin 4 MeSH D12.776.543.585.400.730.040.600 -- aquaporin 5 MeSH D12.776.543.585.400.730.520 -- voltage-dependent anion ...

*Aphid

A. J. Shakesby; I. S. Wallace; H. V. Isaacs; J. Pritchard; D. M. Roberts; A. E. Douglas (2009). "A water-specific aquaporin ... Six generations in 1 year are not unusual in Canada, with succeeding generations often moving to new sites on the tree, ... 20: 1-13. CS1 maint: Explicit use of et al. (link) Henry G. Stroyan (1997). "Aphid". McGraw-Hill Encyclopedia of Science and ... 39 (1): 1-10. doi:10.1016/j.ibmb.2008.08.008. PMID 18983920. R. H. Dadd; T. E. Mittler (1965). "Studies on the artificial ...

*Category:Blood proteins

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*Olfactory glands

"Aquaporin pathways and mucin secretion of olfactory glands might protect the olfactory mucosa.", Chemical Senses, 37 (1): 35-46 ... 1-2): 229-240., doi:10.1016/S0167-4838(00)00167-9, PMID 11058764 Slide at ouhsc.edu. ... 1): 87-120., doi:10.1002/aja.1001210107, PMID 6052394 Solbu, T. T.; Holen, T. (2012), " ...
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 ...
Vasopressin is the key regulator of water homeostasis in vertebrates. Central to its antidiuretic action in mammals is the redistribution of the water channel aquaporin 2 (AQP2) from intracellular vesicles to the apical membrane of kidney epithelial cells, an event initiated by an increase in cAMP and activation of protein kinase A. The subsequent steps of the signaling cascade are not known. To identify proteins involved in the AQP2 shuttle we exploited a recently developed cell line (CD8) derived from the rabbit cortical collecting duct and stably transfected with rat AQP2 cDNA. Treatment of CD8 cells with pertussis toxin (PTX) inhibited both the vasopressin-induced increase in water permeability and the redistribution of AQP2 from an intracellular compartment to the apical membrane. ADP-ribosylation studies revealed the presence of at least two major PTX substrates. Correspondingly, two alpha subunits of PTX-sensitive G proteins, Galphai2 and Galphai3, were identified by Western blotting.
With Aquaporin Inside™ Reverse Osmosis membranes, water treatment can be done with lower energy consumption compared to conventional membrane technology. The benefit comes from the aquaporin proteins which are very efficient in transporting water. This enables the water treatment plant to increase the capacity of treated wastewater without increasing the energy consumption, or remaining at the same capacity level while lowering the energy consumption. At the same time, Aquaporin membranes has the potential to remove also small, neutral compounds such as micro pollutants/trace organics, improving re-use water quality.. Aquaporin Inside™ Forward Osmosis ...
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.
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.
Gentaur molecular products has all kinds of products like :search , FabGennix \ Aquaporin 8, Host species: Rabbit, Polyclonal antibody \ AQP-801AP for more molecular products just contact us
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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. ...
Hypertrophic cardiac myocytes, which are larger than normal, have more cytoplasm and larger nuclei than normal cells. The enlarged nuclei contain more DNA and RNA than their normal counterparts and generate more messenger RNA. The cytoplasm of hypertrophic myocytes contains more myofilaments and mitochondria, but the number of other cytoplasmic organelles is not increased. Water influx, which is typical of hydropic swelling, is not found in hypertrophy. ...
Aqp4 - Aqp4 (untagged) - Mouse aquaporin 4 (cDNA clone MGC:37514 IMAGE:4985265), (10ug) available for purchase from OriGene - Your Gene Company.
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, ...
Purpose: The expression of aquaporin water channel genes are shown to be affected in several pathological conditions of retina, such as in diabetic retinopathy, retinal ischemia and in autoimmune uveitis. Human native retinal pigment epithelial (RPE) cells and immortalized human RPEs are formerly shown to express aquaporins, still the expression of aquaporins in stem cell derived RPE have not been previously elucidated. The objective of this study was to determine the expression of several aquaporin genes (aquaporin1,- 3, -4, -5, -6, -7, -10, -11 and -12) and assess the localization of aquaporin 1 water channel protein in human embryonic (hESCs) and induced pluripotent stem cells (hiPSCs) derived RPE cells.. Methods: hESC- and hiPSC derived RPE cells were grown as monolayer in serum-free media. The expression of aquaporin genes was determined with qRT-PCR. The localization of AQP1-protein was studied with confocal microscopy. Finally, the functionality of aquaporins was assessed with dye ...
Aquaporin-5 is a protein that in humans is encoded by the AQP5 gene. Aquaporin 5 (AQP5) is a water channel protein. Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). Aquaporin 5 plays a role in the generation of saliva, tears and pulmonary secretions. AQP0, AQP2, AQP5, and AQP6 are closely related and all map to 12q13. Aquaporin GRCh38: Ensembl release 89: ENSG00000161798 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000044217 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse PubMed Reference:". Lee MD, Bhakta KY, Raina S, Yonescu R, Griffin CA, Copeland NG, Gilbert DJ, Jenkins NA, Preston GM, Agre P (Jun 1996). "The human Aquaporin-5 gene. Molecular characterization and chromosomal localization". J Biol Chem. 271 (15): 8599-604. doi:10.1074/jbc.271.15.8599. PMID 8621489. "Entrez Gene: AQP5 aquaporin 5". Verkman AS (2003). "Role of aquaporin water channels in eye function". Exp. Eye Res. 76 (2): 137-43. ...
Plant cells contain proteins that are members of the major intrinsic protein (MIP) family, an ancient family of membrane channel proteins characterized by six membrane-spanning domains and two asparagine-proline-alanine (NPA) amino acid motifs in the two halves of the protein. We recently demonstrated that [gamma]-TIP, one of the MIP homologs found in the vacuolar membrane of plant cells, is an aquaporin or water channel protein (C. Maurel, J. Reizer, J.I. Schroeder, M.J. Chrispeels [1993] EMBO J 12: 2241-2247). RD28, another MIP homolog in Arabidopsis thaliana, was first identified as being encoded by a turgor-responsive transcript. To find out if RD28 is a water channel protein, rd28 cRNA was injected into Xenopus laevis oocytes. Expression of RD28 caused a 10- to 15-fold increase in the osmotic water permeability of the oocytes, indicating that the protein creates water channels in the plasma membrane of the oocytes and is an aquaporin just like its homolog [gamma]-TIP. Although RD28 has ...
The pre-ovulatory hydration of the oocyte of marine teleosts, a unique process among vertebrates that occurs concomitantly with meiosis resumption (oocyte maturation), is a critical process for the correct development and survival of the embryo. Increasing information is available on the molecular mechanisms that control oocyte maturation in fish, but the identification of the cellular processes involved in oocyte hydration has remained long ignored. During the past few years, a number of studies have identified the major inorganic and organic osmolytes that create a transient intra-oocytic osmotic potential for hydrating the oocytes, whereas water influx was believed to occur passively. Recent work, however, has uncovered the role of a novel molecular water channel (aquaporin), designated aquaporin-1b (Aqp1b), which facilitates water permeation and resultant swelling of the oocyte. The Aqp1b belongs to a teleost-specific subfamily of water-selective aquaporins, similar to mammalian aquaporin-1 ...
Aquaporin membrane protein, molecular model. Computer illustration showing the structure of a molecule of the human aquaporin 1 protein (blue, and white ribbon). Aquaporins are membrane proteins that form channels (centre) that help water molecules (red and white spheres) pass in and out of cells. Unlike ion channels, aquaporins help prevent ions and other dissolved substances carrying electrical charge from entering the cell, as they only allow lone water molecules or certain uncharged solutes to pass through. This helps maintain the electrochemical potential of the cell membrane. - Stock Image C035/5236
Aquaporins (AQPs) are membrane proteins that enable water transport across cellular plasma membranes in response to osmotic gradients. Phenotypic analyses have revealed important physiological roles for AQPs, and the potential for AQP water channel modulators in various disease states has been proposed. For example, AQP1 is overexpressed in tumor microvessels, and this correlates with higher metastatic potential and aggressiveness of the malignancy. Chemical modulators would help in identifying the precise contribution of water channel activity in these disease states. These inhibitors would also be important therapeutically, e.g., in anti-cancer treatment. This perceived importance contrasts with the lack of success of high-throughput screens (HTS) to identify effective and specific inhibitors of aquaporins. In this paper, we have screened a library of 1500
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 ...
Purpose: : To demonstrate in the conjunctiva the presence of aquaporin type 5 (AQP5), a water channel homologue found in the apical membrane of several tissues including the cornea. Presently, there are no reports indicating as to which AQP might be expressed apically in the conjunctiva; only AQP3 has been identified in the lateral membranes of rat and human conjunctival epithelia. Because we had data from gene-expression microarray assays (Turner; ARVO 2004) indicating message for AQP5 in the human conjunctiva, tissue samples from human, as well as from rats and rabbits (given the ease of their procurement), were analyzed to confirm that the AQP5 protein was indeed expressed in mammalian conjunctivae. Methods: : Goat polyclonal IgG against AQP5 was purchased commercially and used in immunoblotting and immunohistochemical techniques to identify and localize the water channel in rat, rabbit and human epithelia. Results: : Immunoblot analysis of rabbit bulbar-plus-palpebral plasma membrane ...
Aquaporin 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
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
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
collections, groups of modules structured into books or course notes, or for other uses. Our open license allows for free use and reuse of all our content. ...
Significant progress in the understanding of imaging conditions and the interpretation of topographs recorded with the AFM has allowed the surface topography of bacteriorhodopsin to be correlated with the helixconnecting loops to a lateral resolution of 5 Å (Müller et al., 1999b). Here we have used this technology to study the surface of AqpZ, the first bacterial water channel identified (Calamita et al., 1995). Its overexpression, isolation and 2D crystallization have recently been described (Borgnia et al., 1999; Ringler et al., 1999).. 2D crystals adsorbed firmly and without folds or wrinkles to freshly cleaved mica in a high ionic strength buffer (Müller et al., 1997). Subsequent change to a buffer adjusted to compensate for van der Waals interactions allowed their height to be measured accurately (Müller and Engel, 1997). The result, 57 ± 4 Å, compares favorably with the height previously reported for AQP1, 58 ± 3 Å (Walz et al., 1996).. The p4212 crystals of AqpZ with unit cell ...
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 ...
Aquaporins are a family of water channel proteins that provide a major pathway for osmotically driven water transport through cell membranes. So far, 13 aquaporin isoforms (AQP0-AQP12) have been identified in mammalian species (Verkman, 2005). AQP4, the predominant isoform in adult brain, is primarily expressed at the border between brain parenchyma and major fluid compartments, including astrocyte foot processes and glia limitans, as well as ependymal cells and subependymal astrocytes (Venero et al., 2001). The bidirectional water channel AQP4 has an important role in water homeostasis in the brain. It probably helps in the redistribution and absorption of edema fluid, because disruption of AQP4 is found to contribute to the pathophysiology of brain edema (Zador et al., 2007). AQP4 knockout markedly reduced brain swelling in mouse models of cytotoxic brain edema, whereas it significantly worsened outcome in mouse models of vasogenic brain edema (Papadopoulos and Verkman, 2007). Thus, AQP4 ...
Aquaporins are transmembrane water channel proteins present in biological plasma membranes that aid in biological water filtration processes by transporting water molecules through at high speeds, while selectively blocking out other kinds of solutes. Aquaporin Z incorporated biomimetic membranes are envisaged to overcome the problem of high pressure needed, and holds great potential for use in water purification processes, giving high flux while keeping energy consumption low. The functionality of aquaporin Z in terms of osmotic permeability might be regulated by factors such as pH, temperature, crosslinking and hydrophobic thickness of the reconstituted bilayers. Hence, we reconstituted aquaporin Z into vesicles that are made from a series of amphiphilic block copolymers PMOXA-PDMS-PMOXAs with various hydrophobic molecular weights. The osmotic permeability of aquaporin Z in these vesicles was determined through a stopped-flow spectroscopy. In addition, the temperature and pH value of the vesicle
This paper strongly supports the conclusion that AQP0 has a high permeability mode and a low permeability mode. How do these two modes differ? Available structural data on the nature of the water-filled pore through AQP1 and the glycerol facilitator suggest a possible answer. For both, water and glycerol must move through the pore by single-file diffusion. The crystal structure and molecular dynamic simulations suggest that there are multiple water molecules in the pore. There are ∼6 waters seen in the narrow constriction of the pore in the X-ray structure (Sui et al., 2001), and molecular dynamic simulations suggest that there are ∼7 or 8 water molecules moving in concert in the single-file portion of the pore (Tajkhorshid et al., 2002; Zhu et al., 2004). The lack of passage of ionic current through AQP0 and AQP1 is explained by electrostatic considerations that strongly inhibit the movement of protons into the NPA region or hydroxyls into regions flanking either side of the NPA region (de ...
... (AQP4) inhibitor 2-(nicotinamide)-1,3,4-thiadiazole, TGN-020, inside a mouse style of focal cerebral ischemia using 7. research convincingly exhibited that pretreatment using the AQP4 inhibitor TGN-020 considerably reduced the quantity of mind edema connected with ischemic damage. Ischemic edema is usually thought to be initiated by influx of Na+ connected with energy failing. Higher osmolarity circumstances create the generating force for drinking water influx into cells, leading to ionic edema [17]. This early edema stage, so-called cytotoxic edema, is certainly thought to last a long time before mass leakage of drinking water into the human brain ensues, making so-called vasogenic edema [18]. AQP4 is certainly thought to play a substantial function in the real drinking water flux in both procedures. Flux through AQP4 is certainly buy 154992-24-2 bidirectional and solely reliant on osmolarity distinctions between your two spaces ...
Müller glial cells are important regulators of physiological function of retina. In a model disease of retinal inflammation and spontaneous recurrent uveitis in horses (ERU), we could show that retinal Müller glial cells significantly change potassium and water channel protein expression during autoimmune pathogenesis. The most significantly changed channel protein in neuroinflammatory ERU was aquaporin 11 (AQP11). Aquaporins (AQP, 13 members) are important regulators of water and small solute transport through membranes. AQP11 is an unorthodox member of this family and was assigned to a third group of AQPs because of its difference in amino acid sequence (conserved sequence is only 11 %) and especially its largely unknown function. In order to gain insight into the distribution, localization, and function of AQP11 in the retina, we first developed a novel monoclonal antibody for AQP11 enabling quantification, localization, and functional studies. In the horse retina, AQP11 was exclusively expressed
Background: Aquaporins are integral membrane proteins that facilitate the transport of water and small solutes across cell membranes. These proteins are vital for maintaining water homeostasis in living organisms. In mammals, thirteen aquaporins (AQP0-12) have been characterized, but in lower vertebrates, such as fish, the diversity, structure and substrate specificity of these membrane channel proteins are largely unknown. Results: The screening and isolation of transcripts from the zebrafish (Danio rerio) genome revealed eighteen sequences structurally related to the four subfamilies of tetrapod aquaporins, i.e., aquaporins (AQP0, -1 and -4), water and glycerol transporters or aquaglyceroporins (Glps; AQP3 and AQP7-10), a water and urea transporter (AQP8), and two unorthodox aquaporins (AQP11 and -12). Phylogenetic analyses of nucleotide and deduced amino acid sequences demonstrated dual paralogy between teleost and human aquaporins. Three of the duplicated zebrafish isoforms have unlinked ...
After producing a recombinant form of AqpZ in E. coli, the proteins were crystallized--capturing five water molecules inside--and then analyzed by state-of-the-art high-resolution X-ray diffraction techniques. The architecture of aquaporin Z is typical of aquaporins, with a spiral of eight oxygens providing water-binding sites inside the channel. The outer membrane and cytoplasmic ends of the channel are wider than the interior, which is long and narrow. This structure demonstrates that aquaporin selectivity arises in part from erecting a physical barrier: small molecules, like water, can easily pass, but larger ones simply cant fit. And the strategic positioning of amino acid residues with hydrophilic or hydrophobic properties along the channel helps police the influx of molecules based on their affinity for water. While it seems two amino acid chains located in the middle of the channel also provide a water-friendly surface, Stroud et al. say they play a more intriguing role. Noting that the ...
Aquaporin (AQP) proteins comprise a group of membrane intrinsic proteins (MIPs) that are responsible for transporting water and other small molecules, which is crucial for plant survival under stress conditions including salt stress. Despite the vital role of AQPs, little is known about them in cucumber (Cucumis sativus L.). In this study, we identified 39 aquaporin-encoding genes in cucumber that were separated by phylogenetic analysis into five sub-families (PIP, TIP, NIP, SIP, and XIP). Their substrate specificity was then assessed based on key amino acid residues such as the aromatic/Arginine (ar/R) selectivity filter, Frogers positions, and specificity-determining positions. The putative cis-regulatory motifs available in the promoter region of each AQP gene were analyzed and results revealed that their promoter regions contain many abiotic related cis-regulatory elements. Furthermore, analysis of previously released RNA-seq data revealed tissue- and treatment-specific expression patterns of
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.". ...
Polyclonal antibody for AQUAPORIN 3/AQP3 detection. Host: Rabbit.Size: 100μg/vial. Tested applications: IHC-P. Reactive species: Human. AQUAPORIN 3/AQP3 information: Molecular Weight: 31544 MW; Subcellular Localization: Basolateral cell membrane; Multi-pa
Aquaporin 10 antibody, C-term (aquaporin 10) for WB. Anti-Aquaporin 10 pAb (GTX45889) is tested in Human samples. 100% Ab-Assurance.
Looking for online definition of Aquaporin1 or what Aquaporin1 stands for? Aquaporin1 is listed in the Worlds largest and most authoritative dictionary database of abbreviations and acronyms
Structural data on AQPs, together with mutagenesis and molecular dynamics simulations, have indicated that single-file transport occurs through a narrow pore in each monomer, where water selectivity is conferred by electrostatic and steric factors (Hub et al., 2009; Khalali-Araghi et al., 2009). Glycerol-transporting AQPs, called aquaglyceroporins, have a less-constricted pore compared with that of water-selective AQPs (diameter of 3.4 Å compared with 2.8 Å, respectively), with relatively more hydrophobic residues lining the pore.. Many mammalian AQPs, including AQP1, AQP2, AQP4, AQP5 and AQP8, function primarily as bidirectional water-selective transporters. Cells expressing AQPs on their plasma membrane have an ~5- to 50-fold higher osmotic water permeability than membranes that do not (Verkman and Mitra, 2000). Water transport through single-file pores poses a biophysical limitation on the efficiency with which AQPs can transport water, so that AQPs must be present in the membrane at a high ...
plasma membrane intrinsic protein 2-7, PIP2;7, plasma membrane intrinsic protein 3, salt stress-induced major intrinsic protein, P93004, Q9ATM4 Plasma membrane aquaporin, PIP2;7 is water channel protein required for water transport across cell membrane
Brain. 2019 Jun 1;142(6):1598-1615. doi: 10.1093/brain/awz106.. Cotzomi E1,2, Stathopoulos P1,2, Lee CS1,2, Ritchie AM3, Soltys JN3, Delmotte FR2, Oe T2, Sng J2, Jiang R2, Ma AK4, Vander Heiden JA1, Kleinstein SH2,4,5, Levy M6, Bennett JL3, Meffre E2, OConnor KC1,2.. Neuromyelitis optica spectrum disorders (NMOSD) constitute rare autoimmune disorders of the CNS that are primarily characterized by severe inflammation of the spinal cord and optic nerve. Approximately 75% of NMOSD patients harbour circulating pathogenic autoantibodies targeting the aquaporin-4 water channel (AQP4). The source of these autoantibodies remains unclear, but parallels between NMOSD and other autoantibody-mediated diseases posit compromised B cell tolerance checkpoints as common underlying and contributing factors. Using a well established assay, we assessed tolerance fidelity by creating recombinant antibodies from B cell populations directly downstream of each checkpoint and testing them for polyreactivity and ...
INTERNET-DRAFT DTLS as a Transport Layer for RADIUS 9 October 2013 The above paragraph can be rephrased more generically. A session MUST be deleted when non-RADIUS traffic is received over it. This specification is for RADIUS, and there is no reason to allow non- RADIUS traffic over a RADIUS/DTLS connection. A session MUST be deleted when RADIUS traffic fails to pass security checks. There is no reason to permit insecure networks. A session SHOULD NOT be deleted when a well-formed, but "unexpected" RADIUS packet is received over it. Future specifications may extend RADIUS/DTLS, and we do not want to forbid those specifications. Once a DTLS session is established, a RADIUS/DTLS server SHOULD use DTLS Heartbeats [RFC6520] to determine connectivity between the two servers. A server SHOULD also use watchdog packets from the client to determine that the connection is still active. As UDP does not guarantee delivery of messages, RADIUS/DTLS servers which do not implement an application-layer watchdog ...
TY - JOUR. T1 - Involvement of aquaporin in thromboxane A2 receptor-mediated, G12/13/RhoA/NHE-sensitive cell swelling in 1321N1 human astrocytoma cells. AU - Saito, Masaki. AU - Tanaka, Hiroyuki. AU - Sasaki, Masako. AU - Kurose, Hitoshi. AU - Nakahata, Norimichi. PY - 2010/1/1. Y1 - 2010/1/1. N2 - The physiological role of the thromboxane A2 (TXA2) receptor expressed on glial cells remains unclear. We previously reported that 1321N1 human astrocytoma cells pretreated with dibutyryl cyclic AMP (dbcAMP) became swollen in response to U46619, a TXA2 analogue. In the present study, we examined the detailed mechanisms of TXA2 receptor-mediated cell swelling in 1321N1 cells. The cell swelling caused by U46619 was suppressed by expression of p115-RGS, an inhibitory peptide of Gα12/13 pathway and C3 toxin, an inhibitory protein for RhoA. The swelling was also inhibited by treatment with Y27632, a Rho kinase inhibitor and 5-(ethyl-N-isopropyl)amiloride (EIPA), a Na+/H+-exchanger inhibitor. Furthermore, ...
The collecting duct principle cells (PC) play a major role for concentration of urine and regulation of K+ homeostasis. Two water channels, AQP3 and AQP4, are expressed in the PC basolateral membrane (BLM). Here we present evidence that AQP4 participates in regulation of renal K+ transport. K+ enters the cell via Na+,K+-ATPase mediated transport in BLM. The presence of K+ channels in BLM, which is deeply infolded, thus providing a diffusion limited space, permits K+ recirculation, considered important for maintenance of membrane potential. Here we show with co-immunoprecipitation and GST pulldown assays, that in rat renal papilla, AQP4, but not AQP3, assembles with Na+,K+-ATPase and the K+ channel Kir7.1. This led us to hypothesize that AQP4, Na+,K+-ATPase and Kir7.1 form a K+ transporting microdomain, where AQP4 water transport maintains a favorable gradient for K+ efflux and stabilizes membrane potential. A mathematical model of K+ transport across an epithelial cells with a deeply infolded ...
Industrys need to predict the lifetime of adhesively bonded joints has been met by the development of a wide variety of techniques. One particular approach utilises the fact that adhesives and the joints they form can be susceptible to moisture attack. The ingress of moisture into, and through, an adhesive or polymer is termed water permeation. Such a phenomenon can be measured extremely accurately (e.g. through mass change, dielectric permittivity, etc) and it has been shown that for particular systems and environments, a good correlation can be made between the accelerated ageing protocol and in-service failure. This approach has been studied extensively for application within the electronics sector where adhesive/polymeric systems are used both to retain components and coat them. ...
Aquaporin 1 (CO2-, O2- and nitrous oxide-permeable and water-selective) (Zwiazek et al. 2017). Aquaporin-1 tunes pain perception by interacting with Na(v)1.8 Na+ channels in dorsal root ganglion neurons (Zhang and Verkman, 2010). It is upregulated in skeletal muscle in muscular dystrophy (Au et al. 2008). AQP1 has been reported to first insert as a four-helical intermediate, where helices 2 and 4 are not inserted into the membrane. In a second step this intermediate is folded into a six-helical topology. During this process, the orientation of the third helix is inverted, and it can shift out the membrane core (Virkki et al. 2014). Its synthesis is regluated by Kruppel-like factor 2 (KLF2; Q9Y5W3) which also interacts directly with Aqp1 (Fontijn et al. 2015). A nanoscale ion pump has been derived artificially from Aqp1 (Decker et al. 2017 ...
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
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].
I just got a new Betta. He is in a 15 gallon Column tank. (Tall) it came with a filter but after reading a little bit about Bettas I am wondering if I should leave it on there. Is it true that Bettas need very little water movement? Will the HOB filter cause too much water disturbance for him?
PhD Project - Permeable Pavement Engineering for Water Movement in Road Structures and Drainage Effects at University of Greenwich, listed on FindAPhD.com
Objective: It is well known that VEGFR expression is correlated with peritumoral brain edema in meningiomas. Also Aquaporin4 seems to induce the perifocal edema. In our study we analyzed the correlation of VEGFR1, VEGFR2 and Aquaporin4 to the brain edema. Additionally a potential correlation between[for full text, please go to the a.m. URL ...
Hi, Bit more than a month ago my mom developed burning sensation on her back and stomach, she went to a doc but he said its nothing lifetreatening and she waited for for her turn for the tests, it was like this for a week or two. Few weeks ago the burning sensation became too much to bear and my mom went to a hospital. They took her in and the next day she had issues walking and day later she couldnt walk on her own at all. After a few days they put her on some steroid IV thing for
Hi, Bit more than a month ago my mom developed burning sensation on her back and stomach, she went to a doc but he said its nothing lifetreatening and she waited for for her turn for the tests, it was like this for a week or two. Few weeks ago the burning sensation became too much to bear and my mom went to a hospital. They took her in and the next day she had issues walking and day later she couldnt walk on her own at all. After a few days they put her on some steroid IV thing for
Using Water Transport Short Essay On Global Warming, how to do an outline for an essay paper, ethical issues in the workplace case study, family involvement articles
The Corps of Engineers, Pittsburgh District has been forced to close several recreation areas due to high water following recent rainfall.
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.
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-
Please Note, The ebooks are not always PDF format, you might receive epub/kindle formats after purchase. This is Digital Version of (Ebook) 978-3
... from DW&PS allows customers to consistently filter high and variable solids while achieving high water recovery.
A new case report about a woman with a UTI who became ill from high water intake raises questions about doctors advice to drink plenty of fluids ...
Water excretion by the kidney is regulated by the peptide hormone vasopressin. Vasopressin increases the water permeability of the renal collecting duct cells, allowing more water to be reabsorbed from collecting duct urine to blood. Despite long-standing interest in this process, the mechanism of the water permeability increase has remained undetermined. Recently, a molecular water channel (AQP-CD) has been cloned whose expression appears to be limited to the collecting duct. Previously, we immunolocalized this water channel to the apical plasma membrane (APM) and to intracellular vesicles (IVs) of collecting duct cells. Here, we test the hypothesis that vasopressin increases cellular water permeability by inducing exocytosis of AQP-CD-laden vesicles, transferring water channels from IVs to APM. Rat collecting ducts were perfused in vitro to determine water permeability and subcellular distribution of AQP-CD in the same tubules. The collecting ducts were fixed for immunoelectron microscopy ...
Water deficit (WD) is a growing problem in agriculture. In citrus crops, genetically-determined characteristics of the rootstock are important factors in plant responses to WD. Aquaporins are involved in regulating the water supply to the plant by mediating water flow through the cell membranes. Recent studies support a direct role for aquaporins in plant water relations and demonstrate their involvement in tolerance to WD. This study investigates the relationship between photosynthetic and water-balance parameters with levels of expression of aquaporins in conditions of moderate WD in the rootstocks Poncirus trifoliata (L.) Raf. (PT), Cleopatra Mandarin (Citrus reshni Hort. ex Tan.) (CM) and 030115 (a hybrid of the two former rootstocks). Under conditions of WD, the hybrid 030115 drastically reduced aquaporin expression, accompanied by a loss of plant vigour but without reducing the net CO2 assimilation (ACO2). PT maintained the same level of aquaporin expression under WD as under normal ...
The methylotrophic yeast P. pastoris has, during the last decades, increased in popularity as a eukaryotic host for recombinant protein expression [7]. Numerous reports have described successful overexpression of soluble proteins as well as of membrane proteins in this system, but sufficient protein yields have not always been obtained. Several methods have been described that could be used to improve the outcome of expression trials, among which an optimisation of recombinant gene dosage has proven to be one of the most potent ones [21]. When it comes to the aquaporin family of membrane proteins, optimisation of the nucleotide sequence both regarding codon composition and AT content [38] and controlled growth in bioreactors [36] have been reported to improve the yields of heterologous protein. However, in no reports has a systematic examination of the effect of gene dosage on recombinant aquaporin expression in P. pastoris been done and results obtained for other membrane proteins [12, 15, 33] ...
In plant sexual reproduction, water and solute movement are tightly regulated, suggesting the involvement of aquaporins. We previously identified TIP5;1 and TIP1;3 as the only Arabidopsis aquaporin genes that are selectively and highly expressed in mature pollen, and showed that they can transport both water and urea when expressed in Xenopus oocytes. Here, we show that TIP5;1 has unusual characteristics, as its water transport activity is regulated by pH. Analysis of the water transport activity of a mutant version of TIP5;1 (TIP5;1-H131A) and amino acid alignment with other plant aquaporins regulated by pH suggested that a conserved motif is involved in pH sensing. GFP-TIP5;1 is located in the mitochondria of pollen tubes. The single mutants tip1;3 and tip5;1, as well as the tip1;3 tip5;1 double mutant, are fertile, but all mutants had shorter than normal pollen tubes when germinated in vitro in the absence of exogenous nitrogen. Thus, we propose that TIP5;1 and TIP1;3 are involved in nitrogen ...
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 ...
Peter Agre discovered the first aquaporin in 1992 in red blood cells and was awarded the 2003 Nobel Prize. Since then, 13 variants of aquaporin have been found in animals and humans and 35 in plants. There are thousands of these aquaporins in every cell membrane. Aquaporins contain a conduit that is so tiny that only a single water molecule at a time can pass through it. But this traffic can be lively indeed. In one second, several billion water molecules can get through. The direction of this water flow is contingent on the osmotic pressure. The water moves in a direction away from a low and toward a high concentration of salt and nutritional substances. But the conduit isnt always open. The Lund scientists have found out how it opens and closes. This was done in collaboration with a team at Chalmers University of Technology in Göteborg, Sweden, under the direction of Richard Neutze, and with Emad Tajkhorshid at the University of Illinois ...
While synthetic chemists have produced sophisticated architectures able to confine water clusters, most water channel based work is being conducted with natural protein channels as selectivity components, embedded in the diverse arrays of bio-assisted artificial systems. Such systems combine natural proteins that present high water conductance states under natural conditions with artificial lipidic or polymeric matrices. Experimental results have demonstrated that natural biomolecules can be used as bio-assisted building blocks for the construction of highly selective water transport through artificial channels. A next step is the design and construction of simpler compounds that maintain the high conduction activity obtained with natural compounds, leading to fully synthetic artificial biomimetic channels. Such studies aim to use constitutional artificial desalination membranes for highly selective water transport ...
While synthetic chemists have produced sophisticated architectures able to confine water clusters, most water channel based work is being conducted with natural protein channels as selectivity components, embedded in the diverse arrays of bio-assisted artificial systems. Such systems combine natural proteins that present high water conductance states under natural conditions with artificial lipidic or polymeric matrices. Experimental results have demonstrated that natural biomolecules can be used as bio-assisted building blocks for the construction of highly selective water transport through artificial channels. A next step is the design and construction of simpler compounds that maintain the high conduction activity obtained with natural compounds, leading to fully synthetic artificial biomimetic channels. Such studies aim to use constitutional artificial desalination membranes for highly selective water transport ...
Two aquaporins have been detected in the crystalline lens. AQP1 is confined to the mitotic epithelial cell layer that lines the anterior surface (14), whereas AQP0 is characteristic of the terminally differentiated fiber cells (33) that constitute the bulk of the lens mass. Although AQP1 is at least 10-fold more active as a water channel than its fiber cell counterpart (23), no spontaneous lens pathology has been associated with AQP1 deficiency in humans (25) or mice (20). In this study, we have shown that AQP0 accounts for ∼80% of the water permeability of mouse lens fiber cell plasma membranes and that heterozygous loss of this MIP is sufficient to compromise lens transparency. These observations suggest that although the lens can compensate for loss of AQP1 function, there is no such redundancy for AQP0 deficiency.. The relative loss of water permeability recorded in Aqp0+/− mouse lenses was similar in magnitude to that measured in the kidney proximal tubules of Aqp1+/− mice (20). This ...
PDB 2B6O, EMDB 2973 - 1.9Å resolutuion electron crystallography structure of the water channel Aquaporin-0 in its closed state. ...
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.
Homeostasis of the central nervous system (CNS) microenvironment is essential for its normal function and is maintained by the blood-brain barrier (BBB). The BBB proper is made up of endothelial cells (ECs) interconnected by tight junctions (TJs) that reveal a unique morphology and biochemical composition of the bodys vasculature. In this article, we focus on developmental aspects of the BBB and describe morphological as well as molecular special features of the neuro-vascular unit (NVU) involved in barrier induction. Recently, we and others identified the Wnt/b-catenin pathway as crucial for brain angiogenesis, TJ and BBB formation. Based on these findings we discuss other pathways and molecular interactions for BBB establishment and maintenance. At the morphological level, our concept favors a major role for polarized astrocytes (ACs) therein. Orthogonal arrays of particles (OAPs) that are the morphological correlate of the water channel protein aquaporin-4 (AQP4) are specifically formed in the
Sigma-Aldrich offers abstracts and full-text articles by [Xiao-Qiang Liu, Hideyuki Kobayashi, Zi-Bing Jin, Akihiko Wada, Nobuhis Nao-I].
Aquaporin-1 or Aquaporin1, Aqp1, of 258 aas and 6 TMSs. Three Aqp1 isoforms are differentially regluated by the function of the vasotocin (AVTR) and isotocin (ITR) receptors (Martos-Sitcha et al. 2015). Aqp1aa, one of two isoforms in teleosts, may play a role in spermatogenesis in Cynoglossus semilaevis (Guo et al. 2017 ...
The figure at the left displays the protein interaction network for human AQP2(red dot in center) as generated using STRING (4). Below is a pie chart depicting the biological processes that the proteins identified in this network are involved in. The ontologies of these interactors were visualized using PANTHER (5). The most dominant functional categories of the interacting proteins are involvement in cellular processes(including signal transduction), localization(including transport), multicellular organism processes, and biological regulation. One result of note is the inclusion of several other aquaporins within this network, including AQP1, AQP3, and AQP4. This opens the possibility for some overlap in coregulation of these different aquaporins ...
Anti-Aquaporin 3 Antibody (#AQP-003) from Alomone Labs is a highly specific rabbit polyclonal Ab directed against an epitope of rat AQP3. Applications: IFC, IHC, IP, WB. Free samples available. Control antigen included. Lyophilized. Global shipping at room temperature. Your top supplier for aquaporin research!
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Affiliation:Nagoya University of Arts and Sciences,栄養学部,教授, Research Field:Gastroenterology,Gastroenterology,General physiology, Keywords:CFTR,単離小葉間膵管,膵導管細胞,5-hydroxytriptamine,水チャネル,HCO_3^-分泌,aquaporin,Na^+-HCO_3^-共輸送体,pancreatic duct cell,細胞内Cl^-濃度, # of Research Projects:9, # of Research Products:0
Rabbit polyclonal Aquaporin 4 antibody validated for WB, ICC/IF and tested in Human, Mouse and Rat. Immunogen corresponding to synthetic peptide
Rabbit polyclonal Aquaporin 0 antibody validated for WB and tested in Human, Mouse and Rat. Immunogen corresponding to synthetic peptide
In Chapter 6, "The Hormonal Essence of the T-Rex?" author Cordelia Fine considers the biological dogma that testes, and the powerful hormones they exude, are the root of all sexual inequality.. 0 Comments. ...
From guiding branching neurons in the developing brain to maintaining a healthy heartbeat, there seems to be no job that the immune cells cant tackle.. 0 Comments. ...
For the mousse I used the same recipe I used for the Raspberry and Mascarpone Mousse Cakes, back in March. I replaced the lime with lemon and added cooked rhubarb to the mousse base. I dont really have a recipe to cook the rhubarb but I usually go for 1 cup of fruit to 1/3 cup sugar, cooked over low heat until the rhubarb softens and I still get chunks of fruit in there. The cake ring surrounding the mousse looks complicated and involved, but really it isnt. It is made with an almond cake batter very similar to ones used for jelly rolls called "ribbon sheet cake" or Joconde and a tuile cookie batter (also known as tulip paste) piped onto the baking sheet before you pour in the cake batter so while baking it leaves an imprint on your cake. If it were rocket science I would not be doing it....trust me. It is not more time consuming than baking a cake and I find the whole process tremendously more fun given the end result ...
Our results identify a water channel protein as the first defined autoantigen pertinent to an inflammatory demyelinating disorder of the human CNS. AQP4 is an integral protein of astrocytic plasma membranes (15-18), and is highly concentrated in foot process domains facing microvessels where it interacts with dystrophin-associated proteins (10, 17). The AQP4 channel is mercurial-insensitive, and is the predominant water channel in the CNS. It has a pathophysiologic role in brain edema formation following water intoxication (14, 19, 20) or focal cerebral ischemia (21). Brain edema occurring in oncologic contexts is attributed to the up-regulation of AQP4 in high-grade astrocytomas and in reactive astrocytes related to cerebral adenocarcinoma metastases (21, 22).. The present study is the first to implicate AQP4 in the pathogenesis of any autoimmune disorder. NMO may represent the first example of a novel class of autoimmune channelopathies. Unlike MS, the cerebrospinal fluid in patients who have ...
Aquaporins facilitate osmotically driven water movement across cell membranes. Aquaporin 4 (AQP4) is a major water channel in the central nervous system where it participates in cerebral water balance. AQP4 is also present in basolateral membranes of lower respiratory tract airway and renal collecting duct epithelial cells, gastric parietal cells and skeletal muscle cells. However, the distribution of AQP4 in many other tissues is still unknown. The aim of this study was to determine the expression and relative abundance of AQP4 in human Tissue MicroArrays (TMAs) and human protein microarrays by immunohistochemistry and chemiluminescence. In the central nervous system AQP4 was abundantly expressed in the cerebral cortex, cerebellar cortex (purkinje/granular layer), ependymal cell layer, hippocampus and spinal cord. Lower levels were detected in choroid plexus, white matter and meninges. In the musculoskeletal system AQP4 was highly expressed in the sarcolemma of skeletal muscle from the chest ...
In this study, we analyzed defined epitopes in the extracellular loops of AQP4 recognized by AQP4-IgG positive serum and CSF samples of 47 NMOSD patients. Overall, we found reduced binding to all mutations and AQP4-M1 compared to the AQP4-M23 isoform and distinguished two broad patterns of AQP4-IgG recognition, a loop A-dependent pattern A and a loop A-independent pattern B. Further, we observed reduced binding to multiple AQP4 mutants in the majority of all NMOSD patients indicating that the human AQP4 antibody response is defined by multiple epitopes. These findings are consistent with previous studies showing that serum autoantibodies bind to multiple targets including AQP4 peptides, monomers, and higher order arrays [15, 34]. A comparable study on conformational epitopes of the myelin oligodendrocyte glycoprotein (MOG) could show that the immune response can be directed against one single or multiple epitopes [33].. Introduction of a myc-tag in the extracellular loops A, C, and E reduced the ...
Plastic tree (oocytes HbPIP2;3 showed a high efficiency in increasing plasmalemma water conductance. the central regulatory role of in laticifer water balance and ethylene stimulation of latex production in Muell. Arg.)[1]. The latex represents the cytoplasmic content of laticifers which are organized as concentric mantels inside the secondary phloem of the tree trunk. Water accounts for 60%C70% of the latex upon each tapping [2]. Sufficient water supply is essential for both latex regeneration and latex flow [3, 4]. Therefore, any conditions favouring water supply of a rubber tree, especially water movement into phloem, could contribute to latex flow and production. The transmembrane water movement into cells was previously explained only by simple diffusion [5]. However, since it could not explain many phenomena, such as the high velocity of water exchange, the remarkable variations between different cell types and the transient change of water permeability subjected to the stimulation of some ...
Barnacles are sessile macro-invertebrates, found along rocky shores in coastal areas worldwide. The euryhaline bay barnacle Balanus improvisus (Darwin, 1854) (= Amphibalanus improvisus) can tolerate a wide range of salinities, but the molecular mechanisms underlying the osmoregulatory capacity of this truly brackish species are not well understood. Aquaporins are pore-forming integral membrane proteins that facilitate transport of water, small solutes and ions through cellular membranes, and that have been shown to be important for osmoregulation in many organisms. The knowledge of the function of aquaporins in crustaceans is, however, limited and nothing is known about them in barnacles. We here present the repertoire of aquaporins from a thecostracan crustacean, the barnacle B. improvisus, based on genome and transcriptome sequencing. Our analyses reveal that B. improvisus contains eight genes for aquaporins. Phylogenetic analysis showed that they represented members of the classical water ...
Sucrose as a product of photosynthesis is the major carbohydrate translocated from photosynthetic leaves to growing nonphotosynthetic organs such as roots and seeds. These growing tissues, besides carbohydrate supply, require uptake of water through aquaporins to enhance cell expansion during growth. Previous work revealed Sucrose Induced Receptor Kinase, SIRK1, to control aquaporin activity via phosphorylation in response to external sucrose stimulation. Here, we present the regulatory role of AT3G02880 (QSK1), a receptor kinase with a short external domain, in modulation of SIRK1 activity. Our results suggest that SIRK1 autophosphorylates at Ser-744 after sucrose treatment. Autophosphorylated SIRK1 then interacts with and transphosphorylates QSK1 and QSK2. Upon interaction with QSK1, SIRK1 phosphorylates aquaporins at their regulatory C-terminal phosphorylation sites. Consequently, in root protoplast swelling assays, the qsk1qsk2 mutant showed reduced water influx rates under iso-osmotic ...
It is well-known that the rapid now of water into and out of cells is controlled by membrane proteins called aquaporins (AQPs). However, the mechanisms that allow cells to quickly respond to a changing osmotic environment are less well established. Using GFP-AQP fusion proteins expressed in HEK293 cells, we demonstrate the reversible manipulation of cellular trafficking of AQP1. AQP1 trafficking was mediated by the tonicity of the cell environment in a specific PKC- and microtubule-dependent manner. This suggests that the increased level of water transport following osmotic change may be due it phosphorylation-dependent increase in the level of AQP1 trafficking resulting in membrane localization.. ...
Although the functionality of the lens water channels, AQP1 (epithelium) and AQP0 (fiber cells), are well established less is known about the role of AQP5 in the lens. Since in other tissues AQP5 functions as a regulated water channel with a water permeability (PH2O) some 20x higher than AQP0, AQP5 could function to modulate PH2O in lens fiber cells. To test this possibility a fluorescence dye dilution assay was used to calculate the relative PH2O of epithelial cells and fiber membrane vesicles isolated from either the mouse or rat lens, in the absence and presence of HgCl2 - an inhibitor of AQP1 and AQP5 ...
Investigator: Nancy Glober. Mentor: Murat Digicaylioglu, MD, PhD. Abstract: Edema secondary to Traumatic Brain Injury (TBI) causes morbidity and mortality. Aquaporin 4 (AQP4) is a water channel expressed in the central nervous system (CNS) that regulates edema formation, however, the regulation of AQP4 in the CNS remains poorly understood. We show that AQP4 mRNA increases in cultured astrocytes after 12 h of oxygen-glucose deprivation (OGD), whereas AQP4 protein increases after 48 h of OGD. In addition, we show that miRNA-210 may be involved in the regulation of AQP4 mRNA. AQP4 membrane distribution in astrocytes subjected to OGD changed from a diffuse distribution to a clustered one. However, astrocytes that were mechanically stretched did not show the same distribution pattern. Treatment with Acetazolamide inhibited the changes in distribution of AQP4 caused by OGD, and mice treated with Acetazolamide after TBI demonstrated less cytotoxic edema than controls, suggesting a possible clinical ...
Read "Regulation of water permeability of collecting ducts in mouse kidney during postnatal development, Russian Journal of Developmental Biology" on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips.
pT47: cancer out into or onto pleural surface with intra-pleural skip foci beyond direct extension; through & out on the free pleural surface implys the set-up for an incipient [T08-54] malignant effusion (pT4) ...but is it the same (6th ed. AJCC has a clinical malignant effusion as cT4)? AJCC 6th not clear on this for chest7 but is clear that its pT4 for colon cancer in abdomen. But, the pleura can be pulled down into the tumor and invasively penetrated (pT2) & sealed off down in this interior closed space with no call for adjuvant radiation [LMC-07-3392] but may, therefore, call for chemotherapy ...
Background Water channel required to promote glycerol permeability and water transport across cell membranes. May contribute to water transport in the upper portion of small intestine. Isoform 2 is not permeable to urea and...
Liquid Level Contents Gauges - - Shipbuilding & Water Transport - Maritime by Seetru Limited. Gauges for the Ship Building & Offshore IndustriesWe have the following Liquid Level Contents Gauges For Ship Building & Offshore use, the G35 and G31 mod...
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 ...
Screening assays designed to probe ligand and drug-candidate regulation of membrane proteins responsible for ion-translocation across the cell membrane are wide spread, while efficient means to screen membrane-protein facilitated transport of uncharged solutes are sparse. We report on a microfluidic-based system to monitor transport of uncharged solutes across the membrane of multiple (,100) individually resolved surface-immobilized liposomes. This was accomplished by rapidly switching (,10 ms) the solution above dye-containing liposomes immobilized on the floor of a microfluidic channel. With liposomes encapsulating the pH-sensitive dye carboxyfluorescein (CF), internal changes in pH induced by transport of a weak acid (acetic acid) could be measured at time scales down to 25 ms. The applicability of the set up to study biological transport reactions was demonstrated by examining the osmotic water permeability of human aquaporin (AQP5) reconstituted in proteoliposomes. In this case, the rate of ...
Aquaporins and ABC transporters were the major transporters identified in our study. ABC transporters are known to transport fatty acids that are required for proper cuticle development in leaves [45]. The cuticle plays an important role in maintaining the structural integrity of salt glands. Under saline conditions, it becomes important for the salt glands to form a thick cuticular layer to prevent water loss and also diffusion of ions into neighbouring cells [6]. The observed high level of expression of ABC transporters in the salt gland-rich tissue could explain this in Avicennia salt gland cells. Aquaporins are known to regulate water movement across the membranes. During drought and salt exposure, aquaporins are known to maintain water balance in the cells [46] and have been shown to play a crucial role in salt secretion of A. officinalis [9]. Although aquaporins have been identified from the leaves of other salt secretors [41], its precise function in regulating water movement during ...
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 ...

Fatal anti-aquaporin-4 seropositive neuromyelitis optica spectrum disorder in tuberculosis | BMC Infectious Diseases | Full TextFatal anti-aquaporin-4 seropositive neuromyelitis optica spectrum disorder in tuberculosis | BMC Infectious Diseases | Full Text

This is the first reported case of anti-aquaporin-4 antibody-positive NMO spectrum disorder in a patient with active ... It shows the usefulness of testing for anti-aquaporin-4 antibodies while evaluating neurological deterioration in patients with ... Spinal imaging and anti-aquaporin-4 antibody positivity established a diagnosis of neuromyelitis optica spectrum disorder. ... We report a fatal case of anti-aquaporin-4 antibody positive NMO spectrum disorder in a patient who was receiving treatment for ...
more infohttps://bmcinfectdis.biomedcentral.com/articles/10.1186/1471-2334-14-470

AHRO : Austin Health Research Online: Neuromyelitis Optica Spectrum Disorder and Anti-Aquaporin 4 Channel Immunoglobulin in an...AHRO : Austin Health Research Online: Neuromyelitis Optica Spectrum Disorder and Anti-Aquaporin 4 Channel Immunoglobulin in an...

aquaporin-4. myelin oligodendrocyte glycoprotein. neuromyelitis optica. neuropathy. pediatric. Appears in Collections:. Journal ... Neuromyelitis optica spectrum disorder is uncommon in children, and often seronegative for aquaporin-4 immunoglobulin G (AQP4- ... Neuromyelitis Optica Spectrum Disorder and Anti-Aquaporin 4 Channel Immunoglobulin in an Australian Pediatric Demyelination ... Of the remaining 4 children, 3 had a monophasic course and 1 a relapsing course. Two were tested for anti-myelin ...
more infohttp://ahro.austin.org.au/austinjspui/handle/1/22299

Aquaporin 1 - WikipediaAquaporin 1 - Wikipedia

The gene encoding this aquaporin is a possible candidate for disorders involving imbalance in ocular fluid movement. Aquaporin ... Aquaporin 1 is a protein that in humans is encoded by the AQP1 gene. AQP1 is a widely expressed water channel, whose ... Aquaporin 1 at the US National Library of Medicine Medical Subject Headings (MeSH) Gallery of Aquaporin Simulations Human AQP1 ... It is not regulated by vasopressin (ADH). Aquaporins are a family of small integral membrane proteins related to the major ...
more infohttps://en.wikipedia.org/wiki/Aquaporin_1

IJMS | Free Full-Text | Fragment Screening of Human Aquaporin 1IJMS | Free Full-Text | Fragment Screening of Human Aquaporin 1

... to identify effective and specific inhibitors of aquaporins. In this paper, we have screened a library of 1500 ... Aquaporins (AQPs) are membrane proteins that enable water transport across cellular plasma membranes in response to osmotic ... This article belongs to the Special Issue Aquaporin) View Full-Text , Download PDF [9881 KB, uploaded 25 March 2016] , Browse ... Aquaporins (AQPs) are membrane proteins that enable water transport across cellular plasma membranes in response to osmotic ...
more infohttp://www.mdpi.com/1422-0067/17/4/449

Aquaporin-1 - Proteopedia, life in 3DAquaporin-1 - Proteopedia, life in 3D

Aquaporins Aquaporin-1 (AQP1) was first discovered in human red blood cell membranes by Gheorghe Bengas research group in 1986 ... Water selective aquaporins are AQP1, -2, -4, -5, -6, -8, -12, and -0. A subgroup of aquaporins called aquaglycerporins allow ... Aquaporins are integral membrane proteins that specialize in the regulation of cellular water flow across the cell membrane.[3] ... Aquaporin-1 Structure Aquaporin-1 is an integral membrane protein that is considered to have an "open" structure. Despite being ...
more infohttp://proteopedia.org/wiki/index.php/Aquaporin-1

AQP1 - Aquaporin 1 splice variant 2 - Homo sapiens (Human) - AQP1 gene & proteinAQP1 - Aquaporin 1 splice variant 2 - Homo sapiens (Human) - AQP1 gene & protein

Aquaporin 1 splice variant 2Imported. ,p>Information which has been imported from another database using automatic procedures ... Belongs to the MIP/aquaporin (TC 1.A.8) family. [View classification]SAAS annotation. Automatic assertion according to rulesi ... tr,Q6JSD8,Q6JSD8_HUMAN Aquaporin 1 splice variant 2 (Fragment) OS=Homo sapiens OX=9606 GN=AQP1 PE=2 SV=1 ... 1.20.1080.10, 1 hit. InterProi. View protein in InterPro. IPR023271 Aquaporin-like. IPR034294 Aquaporin_transptr. IPR000425 ...
more infohttps://www.uniprot.org/uniprot/Q6JSD8

Aquaporin 1
     Summary Report | CureHunterAquaporin 1 Summary Report | CureHunter

Aquaporin 1 forms a water-specific channel that is constitutively expressed at the PLASMA MEMBRANE of ERYTHROCYTES and KIDNEY ... Aquaporin-CHIP; CHIP28 Protein; Channel-Forming Integral Membrane Protein Of 28 kDa; AQP CHIP Protein; Aquaporin CHIP; Channel ... Aquaporin 1. Subscribe to New Research on Aquaporin 1 Aquaporin 1 forms a water-specific channel that is constitutively ... 01/01/2012 - "In this study, we were going to elucidate the involvement of aquaporin 1 and 4 (AQP1,4) in the metastasis of lung ...
more infohttp://www.curehunter.com/public/keywordSummaryD051398.do

Central diabetes insipidus associated with impaired renal aquaporin-1 expression in mice lacking liver X receptor β | PNASCentral diabetes insipidus associated with impaired renal aquaporin-1 expression in mice lacking liver X receptor β | PNAS

2008) Aquaporin 1 is important for maintaining secretory granule biogenesis in endocrine cells. Mol Endocrinol 22:1924-1934. ... 1994) Requirement of human renal water channel aquaporin-2 for vasopressin-dependent concentration of urine. Science 264:92-95. ... 2007) Nephrogenic diabetes insipidus in mice caused by deleting COOH-terminal tail of aquaporin-2. Am J Physiol Renal Physiol ... The persistent high urine volume after AVP administration was traced to a reduction in aquaporin-1 expression in the kidney of ...
more infohttps://www.pnas.org/content/109/8/3030

Reconstitution of CO2 Regulation of SLAC1 Anion Channel and Function of CO2-Permeable PIP2;1 Aquaporin as CARBONIC ANHYDRASE4...Reconstitution of CO2 Regulation of SLAC1 Anion Channel and Function of CO2-Permeable PIP2;1 Aquaporin as CARBONIC ANHYDRASE4...

A) The aquaporin PIP2;1 was identified as a βCA4-interacting protein by screening a split ubiquitin yeast two-hybrid library. ... Wang C1, Hu H2, Qin X3, Zeise B3, Xu D4, Rappel WJ5, Boron WF3, Schroeder JI6. ... PIP2;1 alone served as a negative control.. (C) PIP2;1-G103W impaired the CO2 permeability of PIP2;1 as measured by changes in ... B) and (C) Split YFP (B) and reversible split luciferase complementation assays (C) showed that βCA4 interacts with PIP2;1 at ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed?term=26764375

IJMS | Free Full-Text | Immunohistochemical Expression of Aquaporin-1 in Fluoro-Edenite-Induced Malignant Mesothelioma: A...IJMS | Free Full-Text | Immunohistochemical Expression of Aquaporin-1 in Fluoro-Edenite-Induced Malignant Mesothelioma: A...

The immunohistochemical expression of aquaporin-1 (AQP1) in asbestos-related malignant pleural mesothelioma (MPM) is emerging ... Immunohistochemical Expression of Aquaporin-1 in Fluoro-Edenite-Induced Malignant Mesothelioma: A Preliminary Report. Giuseppe ... "Immunohistochemical Expression of Aquaporin-1 in Fluoro-Edenite-Induced Malignant Mesothelioma: A Preliminary Report." Int. J. ... The Aquaporin 1 Inhibitor Bacopaside II Reduces Endothelial Cell Migration and Tubulogenesis and Induces Apoptosis ...
more infohttp://www.mdpi.com/1422-0067/19/3/685

anti-Aquaporin 1 antibody [7D11]  | GeneTexanti-Aquaporin 1 antibody [7D11] | GeneTex

Anti-Aquaporin 1 mAb (GTX11025) is tested in Human, Mouse, Rat samples. 100% Ab-Assurance. ... Aquaporin 1 antibody [7D11] (aquaporin 1) for ELISA, FACS, IHC-P, WB. ... aquaporin 1. Background. integral membrane protein that is a major water transport molecule in the kidney proximal tubule and ... Aqp1 Antibody , CHIP28 Antibody , aquaporin 1 Antibody. Specificity. This antibody recognizes an epitope within an ...
more infohttp://www.genetex.com/Aquaporin-1-antibody-7D11-GTX11025.html

Frontiers | The Importance of Aquaporin 1 in Pancreatitis and Its Relation to the CFTR Cl- Channel | PhysiologyFrontiers | The Importance of Aquaporin 1 in Pancreatitis and Its Relation to the CFTR Cl- Channel | Physiology

Aquaporins (AQPs) facilitate the transepithelial water flow involved in epithelial fluid secretion in numerous tissues; however ... Aquaporins (AQPs) facilitate the transepithelial water flow involved in epithelial fluid secretion in numerous tissues; however ... in Capan-1 cells. The presence of AQP1 and CFTR in the mice and human pancreas were investigated by immunohistochemistry. ... in Capan-1 cells. The presence of AQP1 and CFTR in the mice and human pancreas were investigated by immunohistochemistry. ...
more infohttps://www.frontiersin.org/articles/10.3389/fphys.2018.00854/full

Aquaporin-1 in plasma membrane and caveolae provides mercury-sensitive water channels across lung endothelium.  - PubMed - NCBIAquaporin-1 in plasma membrane and caveolae provides mercury-sensitive water channels across lung endothelium. - PubMed - NCBI

1996 Jan;270(1 Pt 2):H416-22. Comparative Study; Research Support, Non-U.S. Govt; Research Support, U.S. Govt, P.H.S. ... Aquaporin-1 in plasma membrane and caveolae provides mercury-sensitive water channels across lung endothelium.. Schnitzer JE1, ... Immunoblotting of these fractions showed that the transmembrane water channel protein aquaporin-1 was amply expressed on the ... Just like certain epithelia, endothelia might express physiologically relevant amounts of aquaporin-1 on their cell surface to ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/8769778?dopt=Abstract

Safety of a Single Administration of AAV2hAQP1, an Adeno-Associated Viral Vector Encoding Human Aquaporin-1 to One Parotid...Safety of a Single Administration of AAV2hAQP1, an Adeno-Associated Viral Vector Encoding Human Aquaporin-1 to One Parotid...

Safety of a Single Administration of AAV2hAQP1, an Adeno-Associated Viral Vector Encoding Human Aquaporin-1 to One Parotid ... Early responses to adenoviral-mediated transfer of the aquaporin-1 cDNA for radiation-induced salivary hypofunction. Proc Natl ... Increased fluid secretion after adenoviral-mediated transfer of the aquaporin-1 cDNA to irradiated rat salivary glands. Proc ... AAV2-mediated transfer of the human aquaporin-1 cDNA restores fluid secretion from irradiated miniature pig parotid glands. ...
more infohttps://www.clinicaltrials.gov/ct2/show/study/NCT02446249?term=dry+mouth&fund=0&rank=15

Safety of a Single Administration of AAV2hAQP1, an Adeno-Associated Viral Vector Encoding Human Aquaporin-1 to One Parotid...Safety of a Single Administration of AAV2hAQP1, an Adeno-Associated Viral Vector Encoding Human Aquaporin-1 to One Parotid...

Safety of a Single Administration of AAV2hAQP1, an Adeno-Associated Viral Vector Encoding Human Aquaporin-1 to One Parotid ... Early responses to adenoviral-mediated transfer of the aquaporin-1 cDNA for radiation-induced salivary hypofunction. Proc Natl ... Increased fluid secretion after adenoviral-mediated transfer of the aquaporin-1 cDNA to irradiated rat salivary glands. Proc ... AAV2-mediated transfer of the human aquaporin-1 cDNA restores fluid secretion from irradiated miniature pig parotid glands. ...
more infohttps://www.clinicaltrials.gov/ct2/show/NCT02446249?term=Saliva+and+Salivary+Gland+Disorders&recrs=a&fund=0&rank=4

Aquaporin 1 Antibody - Affinity purified polyclonal antibody WB - Buy Now! |AbgentAquaporin 1 Antibody - Affinity purified polyclonal antibody WB - Buy Now! |Abgent

Aquaporin 1 Antibody, Affinity purified polyclonal antibody validated in WB (AG1048-025), Abgent ... home , Products , Primary Antibodies , Signal Transduction , Aquaporin 1 Antibody Aquaporin 1 Antibody. Affinity purified ... Aquaporin 1 (AQP-1) belongs to a family of membrane proteins that allow passage of water and certain other solutes through ... Aquaporin-1, AQP-1, Aquaporin-CHIP, Urine water channel, Water channel protein for red blood cells and kidney proximal tubule, ...
more infohttp://www.abgent.com/products/AG1048-Aquaporin-1-Antibody

Renal medullary gene expression in aquaporin-1 null mice - NDI FoundationRenal medullary gene expression in aquaporin-1 null mice - NDI Foundation

aquaporin-1 DEFINITION: Also known as CHIP-28, aquaporin-1 is the major water channel of the red blood cells. In the kidneys, ... aquaporin-1 DEFINITION: Also known as CHIP-28, aquaporin-1 is the major water channel of the red blood cells. In the kidneys, ... Mice that do not have the aquaporin-1 (AQP1) gene are unable to concentrate urine. Brooks, et al., examined mice lacking AQP1 ... Renal medullary gene expression in aquaporin-1 null mice Authors: Brooks, Heddwen L.; McReynolds, Matthew R.; Garcia-Taylor, ...
more infohttp://www.ndif.org/proceedings/147-Renal_medullary_gene_expression_in_aquaporin1_null_mice/abstract

Inhibition of Human Aquaporin-1 Water Channel Activity by Carbonic Anhydrase Inhibitors | IOVS | ARVO JournalsInhibition of Human Aquaporin-1 Water Channel Activity by Carbonic Anhydrase Inhibitors | IOVS | ARVO Journals

Purpose:: Aquaporins are a family of water channel proteins that facilitates water transport across the plasma membrane. ... R. Patil, S. Xu, A. Rusinko, N. A. Sharif, M. B. Wax, R. T. Mathias, K. Varadaraj; Inhibition of Human Aquaporin-1 Water ... Inhibition of Human Aquaporin-1 Water Channel Activity by Carbonic Anhydrase Inhibitors ... Inhibition of Human Aquaporin-1 Water Channel Activity by Carbonic Anhydrase Inhibitors ...
more infohttps://iovs.arvojournals.org/article.aspx?articleid=2385533

Frontiers | Molecular Characterization of Aquaporin 1 and Aquaporin 3 from the Gills of the African Lungfish, Protopterus...Frontiers | Molecular Characterization of Aquaporin 1 and Aquaporin 3 from the Gills of the African Lungfish, Protopterus...

Aquaporins (Aqps) are a superfamily of integral membrane proteins which generally facilitate the permeation of water through ... Aquaporins (Aqps) are a superfamily of integral membrane proteins which generally facilitate the permeation of water through ... Figure 5. The gene expression of (A) aquaporin 1 (aqp1) and (B) aquaporin 3 (aqp3) in various tissues/organs of Protopterus ... Figure 2. A multiple amino acid alignment of aquaporin 3 (Aqp3) from Protopterus annectens with Danio rerio Aqp3a (AAH44188.1 ...
more infohttps://www.frontiersin.org/articles/10.3389/fphys.2016.00532/full

Kuang K et al. (2001), 
		
		
			Mercurial sensitivity of aquaporin 1 endofacial... -
		
		Xenbase Paper
	Kuang K et al. (2001), Mercurial sensitivity of aquaporin 1 endofacial... - Xenbase Paper

aquaporin-1. (. AQP1. ) has two asparagine-proline-alanine (NPA) repeats on loops B and E. From recent structural information, ... Mercurial sensitivity of aquaporin 1 endofacial loop B residues. Kuang K , Haller JF , Shi G , Kang F , Cheung M , Iserovich P ...
more infohttp://www.xenbase.org/literature/article.do?method=display&articleId=8676

Reconstitution of CO2 Regulation of SLAC1 Anion Channel and Function of CO2-Permeable PIP2;1 Aquaporin as CARBONIC ANHYDRASE4...Reconstitution of CO2 Regulation of SLAC1 Anion Channel and Function of CO2-Permeable PIP2;1 Aquaporin as CARBONIC ANHYDRASE4...

2 aquaporin displays CO2 permeability in yeast (Heckwolf et al., 2011). Four barley PIP2 aquaporins were recently shown to ... It has been widely demonstrated that CO2 is transported across membranes via aquaporins: The AQP1 aquaporin from tobacco ... A) The aquaporin PIP2;1 was identified as a βCA4-interacting protein by screening a split ubiquitin yeast two-hybrid library. ... The aquaporins Nt-AQP1 from tobacco, PIP1;2 from Arabidopsis, and four PIP2 proteins in barley (Hordeum vulgare) have been ...
more infohttp://www.plantcell.org/content/28/2/568

Aquaporin 1 Positive Mesenchymal Cell Imply Existence Of Cornea Limbal Niche Cells | IOVS | ARVO JournalsAquaporin 1 Positive Mesenchymal Cell Imply Existence Of Cornea Limbal Niche Cells | IOVS | ARVO Journals

We stained the sections with N-cadherin and keratin 15 (Limbal basal epithelial layer), aquaporin 1 (AQP1; subepithelial cells ... Aquaporin 1 Positive Mesenchymal Cell Imply Existence Of Cornea Limbal Niche Cells ... Aquaporin 1 Positive Mesenchymal Cell Imply Existence Of Cornea Limbal Niche Cells ... Kazunari Higa, Naoko Kato, Satoru Yoshida, Yoko Ogawa, Jun Shimazaki, Kazuo Tsubota, Shigeto Shimmura; Aquaporin 1 Positive ...
more infohttps://iovs.arvojournals.org/article.aspx?articleid=2361460

Localization of aquaporin-1 water channel in glial cells of the human peripheral nervous systemLocalization of aquaporin-1 water channel in glial cells of the human peripheral nervous system

... ... The aquaporins (AQPs) are a family of water channel proteins with at least 13 mammalian members (AQPs 0-12) expressed in ... Aquaporin expression in the peripheral nervous system is poorly studied. Here we report that the AQP1 water channel is ...
more infohttps://insights.ovid.com/glia/200605000/01445424-200605000-00012

Functional reconstitution of a rice aquaporin water channel, PIP1; 1, by a micro-batchwise methodology.Functional reconstitution of a rice aquaporin water channel, PIP1; 1, by a micro-batchwise methodology.

Assessing the selectivity, regulation and physiological relevance of aquaporin membrane channels (AQPs) requires structural and ... PIP1;1 was produced as a histidine-tagged form, 10His-OsPIP1;1, in an Escherichia coli-based expression system. The recombinant ... PIP1;1 proteoliposomes and control empty liposomes had good size homogeneity as seen by quasi-elastic light scattering and ... Write a short (1 or 2 sentence) testimonial describing your experience with GenScript products or services. If your testimonial ...
more infohttps://www.genscript.com/reference_peer-reviewed_literature_11221.html?journal=Plant%2520Physiol%2520Biochem.&pubmed_id=

REGULATION OF AQUAPORIN-1 ION CHANNEL FUNCTION BY INTRACELLULAR SIGNALING PATHWAYS - OpenThesisREGULATION OF AQUAPORIN-1 ION CHANNEL FUNCTION BY INTRACELLULAR SIGNALING PATHWAYS - OpenThesis

Aquaporins serve as pores for water thus allowing enhanced water permeability in biological membranes (Preston, et al., 1992). ... REGULATION OF AQUAPORIN-1 ION CHANNEL FUNCTION BY INTRACELLULAR SIGNALING PATHWAYS. by Birdsell, Dawn Nice. ... A subset of Aquaporin proteins behave as ion channels regulated by intracellular signaling pathways (Anthony, et al., 2000; ... The Carboxyl (C) -terminus of Aqp1 encodes a PSD-95/DLG/ZO- 1 (PDZ) ligand binding domain and a number of putative regulatory ...
more infohttp://www.openthesis.org/documents/Regulation-aquaporin-1-ion-channel-68065.html
  • Previously classified as a subtype of multiple sclerosis, NMO is now considered to be a distinct clinical, pathological, and immunological entity [ 1 ]. (biomedcentral.com)
  • Neuromyelitis optica (NMO) is an autoimmune inflammatory condition of the central nervous system that is characterized by circulating anti-aquaporin-4 antibodies, transverse myelitis and optic neuritis. (biomedcentral.com)
  • A key diagnostic test for NMO spectrum disorders is the presence of anti-aquaporin-4 (anti-Aqp-4) IgG antibodies in patient serum [ 2 ]. (biomedcentral.com)
  • It shows the usefulness of testing for anti-aquaporin-4 antibodies while evaluating neurological deterioration in patients with tuberculosis. (biomedcentral.com)
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