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 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 is an aquaglyceroporin that is expressed in the KIDNEY COLLECTING DUCTS and is constitutively localized at the basolateral MEMBRANE.
Aquaporin 4 is the major water-selective channel in the CENTRAL NERVOUS SYSTEM of mammals.
A class of porins that allow the passage of WATER and other small molecules across CELL MEMBRANES.
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 is an aquaglyceroporin that is found primarily in KIDNEY COLLECTING DUCTS. AQP6 protein functions as an anion-selective channel.
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)
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.
Tendency of fluids (e.g., water) to move from the less concentrated to the more concentrated side of a semipermeable membrane.
A subgroup of aquaporins that transport WATER; GLYCEROL; and other small solutes across CELL MEMBRANES.
Sets of cell surface antigens located on BLOOD CELLS. They are usually membrane GLYCOPROTEINS or GLYCOLIPIDS that are antigenically distinguished by their carbohydrate moieties.
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.
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.
Property of membranes and other structures to permit passage of light, heat, gases, liquids, metabolites, and mineral ions.
A quality of cell membranes which permits the passage of solvents and solutes into and out of cells.
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)
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.
The ability of the kidney to excrete in the urine high concentrations of solutes from the blood plasma.
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.
Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.
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.
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.
Urination of a large volume of urine with an increase in urinary frequency, commonly seen in diabetes (DIABETES MELLITUS; DIABETES INSIPIDUS).
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.
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.
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.
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).
Agents that reduce the excretion of URINE, most notably the octapeptide VASOPRESSINS.
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.
A plant genus of the family LILIACEAE. Members contain tuliposides and tulipalins and have been associated with allergic contact dermatitis in florists.
The contribution to barometric PRESSURE of gaseous substance in equilibrium with its solid or liquid phase.
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.
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.
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)
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)
Inorganic compounds that contain mercury as an integral part of the molecule.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
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.
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.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in plants.
Fluids composed mainly of water found within the body.
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.
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.
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.
Histochemical localization of immunoreactive substances using labeled antibodies as reagents.
The condition that results from excessive loss of water from a living organism.
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.
A phylum of fungi that are mutualistic symbionts and form ARBUSCULAR MYCORRHIZAE with PLANT ROOTS.
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.
Glands that secrete SALIVA in the MOUTH. There are three pairs of salivary glands (PAROTID GLAND; SUBLINGUAL GLAND; SUBMANDIBULAR GLAND).
The body of a fungus which is made up of HYPHAE.
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.
A clear, colorless, viscous organic solvent and diluent used in pharmaceutical preparations.
Large and highly vacuolated cells possessing many chloroplasts occuring in the interior cross-section of leaves, juxtaposed between the epidermal layers.
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.
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.
Body organ that filters blood for the secretion of URINE and that regulates ion concentrations.
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)
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.
Prolonged dry periods in natural climate cycle. They are slow-onset phenomena caused by rainfall deficit combined with other predisposing factors.
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.
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.
An aquatic genus of the family, Pipidae, occurring in Africa and distinguished by having black horny claws on three inner hind toes.
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.
The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.
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.
A widely cultivated plant, native to Asia, having succulent, edible leaves eaten as a vegetable. (From American Heritage Dictionary, 1982)
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
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.
Yeast-like ascomycetous fungi of the family Saccharomycetaceae, order SACCHAROMYCETALES isolated from exuded tree sap.
A plant genus of the family ROSACEAE known for the edible fruit.
A mutant strain of Rattus norvegicus used in research on renal function and hypertension and as a disease model for diabetes insipidus.
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.
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.
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.
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).
A schistosomicide possibly useful against other parasites. It has irritant emetic properties and may cause lethal cardiac toxicity among other adverse effects.
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)
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Slender tubular or hairlike excretory structures found in insects. They emerge from the alimentary canal between the mesenteron (midgut) and the proctodeum (hindgut).
An intermediate filament protein found only in glial cells or cells of glial origin. MW 51,000.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
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)
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.
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 used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Liquids transforming into solids by the removal of heat.
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.
A cytotoxic sulfhydryl reagent that inhibits several subcellular metabolic systems and is used as a tool in cellular physiology.
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.
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.
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.
Solutions that have a greater osmotic pressure than a reference solution such as blood, plasma, or interstitial fluid.
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.
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.
The quantity of volume or surface area of CELLS.
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.
A subclass of symporters that specifically transport SODIUM CHLORIDE and/or POTASSIUM CHLORIDE across cellular membranes in a tightly coupled process.
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.
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.
A plant genus of the family FAGACEAE that is a source of TANNINS. Do not confuse with Holly (ILEX).
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.
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).
A plant species of the family POACEAE. It is a tall grass grown for its EDIBLE GRAIN, corn, used as food and animal FODDER.
A computer simulation developed to study the motion of molecules over a period of time.
Adaptation to a new environment or to a change in the old.
The relationships of groups of organisms as reflected by their genetic makeup.
Starches that have been chemically modified so that a percentage of OH groups are substituted with 2-hydroxyethyl ether groups.
A ubiquitous sodium salt that is commonly used to season food.

Long-term regulation of aquaporins in the kidney. (1/216)

The discovery of the aquaporin family of water channels has greatly improved our understanding of how water crosses epithelial cells, particularly in the kidney. The study of the mechanisms involved in the regulation of collecting duct water permeability, in particular, has advanced very rapidly since the identification and characterization of aquaporin-2 (AQP2) in 1993. One of the more surprising findings has been the dramatic long-term changes that are seen in the abundance of this protein, as well as the recognition that these changes represent a way of modulating the acute antidiuretic effects of vasopressin. Furthermore, such changes seem to be of etiological and pathological significance in a number of clinical disorders of water balance. This review focuses on the various conditions in which AQP2 expression is altered (either increased or decreased) and on what this can tell us about the signals and mechanisms controlling these changes. Ultimately, this may be of great value in the clinical management of water balance disorders. Evidence is also now beginning to emerge that there are similar changes in the expression of other renal aquaporins, which had previously been thought to provide an essentially constitutive water permeability pathway, suggesting that they too should be considered as regulatory factors in the control of body water balance.  (+info)

Vasopressin regulates apical targeting of aquaporin-2 but not of UT1 urea transporter in renal collecting duct. (2/216)

In the renal inner medullary collecting duct (IMCD), vasopressin regulates two key transporters, namely aquaporin-2 (AQP2) and the vasopressin-regulated urea transporter (VRUT). Both are present in intracellular vesicles as well as the apical plasma membrane. Short-term regulation of AQP2 has been demonstrated to occur by vasopressin-induced trafficking of AQP2-containing vesicles to the apical plasma membrane. Here, we have carried out studies to determine whether short-term regulation of VRUT occurs by a similar process. Cell surface labeling with NHS-LC-biotin in rat IMCD suspensions revealed that vasopressin causes a dose-dependent increase in the amount of AQP2 labeled at the cell surface, whereas VRUT labeled at the cell surface did not increase in response to vasopressin. Immunoperoxidase labeling of inner medullary thin sections from Brattleboro rats treated with 1-desamino-8-D-arginine vasopressin (DDAVP) for 20 min revealed dramatic translocation of AQP2 to the apical region of the cell, with no change in the cellular distribution of VRUT. In addition, differential centrifugation of inner medullary homogenates from Brattleboro rats treated with DDAVP for 60 min revealed a marked depletion of AQP2 from the low-density membrane fraction (enriched in intracellular vesicles) but did not alter the quantity of VRUT in this fraction. Finally, AQP2-containing vesicles immunoisolated from a low-density membrane fraction from renal inner medulla did not contain immunoreactive VRUT. Thus vasopressin-mediated regulation of AQP2, but not of VRUT, depends on regulated vesicular trafficking to the plasma membrane.  (+info)

An impaired routing of wild-type aquaporin-2 after tetramerization with an aquaporin-2 mutant explains dominant nephrogenic diabetes insipidus. (3/216)

Autosomal recessive and dominant nephrogenic diabetes insipidus (NDI), a disease in which the kidney is unable to concentrate urine in response to vasopressin, are caused by mutations in the aquaporin-2 (AQP2) gene. Missense AQP2 proteins in recessive NDI have been shown to be retarded in the endoplasmic reticulum, whereas AQP2-E258K, an AQP2 mutant in dominant NDI, was retained in the Golgi complex. In this study, we identified the molecular mechanisms underlying recessive and dominant NDI. Sucrose gradient centrifugation of rat and human kidney proteins and subsequent immunoblotting revealed that AQP2 forms homotetramers. When expressed in oocytes, wild-type AQP2 and AQP2-E258K also formed homotetramers, whereas AQP2-R187C, a mutant in recessive NDI, was expressed as a monomer. Upon co-injection, AQP2-E258K, but not AQP2-R187C, was able to heterotetramerize with wild-type AQP2. Since an AQP monomer is the functional unit and AQP2-E258K is a functional but misrouted water channel, heterotetramerization of AQP2-E258K with wild-type AQP2 and inhibition of further routing of this complex to the plasma membrane is the cause of dominant NDI. This case of NDI is the first example of a dominant disease in which the 'loss-of-function' phenotype is caused by an impaired routing rather than impaired function of the wild-type protein.  (+info)

Aquaporin-6: An intracellular vesicle water channel protein in renal epithelia. (4/216)

All characterized mammalian aquaporins (AQPs) are localized to plasma membranes where they function chiefly to mediate water transport across cells. Here we show that AQP6 is localized exclusively in intracellular membranes in renal epithelia. By using a polyclonal antibody to the C terminus of AQP6, immunoblots revealed a major 30-kDa band in membranes from rat renal cortex and medulla. Endoglycosidase treatment demonstrated presence of an intracellular high mannose glycan on each subunit. Sequential ultracentrifugation of rat kidney homogenates confirmed that AQP6 resides predominantly in vesicular fractions, and immunohistochemical and immunoelectron microscopic studies confirmed that >98% of AQP6 is located in intracellular membrane vesicles. In glomeruli, AQP6 is present in membrane vesicles within podocyte cell bodies and foot processes. In proximal tubules, AQP6 is also abundant in membrane vesicles within the subapical compartment of segment 2 and segment 3 cells, but was not detected in the brush border or basolateral membranes. In collecting duct, AQP6 resides in intracellular membrane vesicles in apical, mid, and basolateral cytoplasm of type A intercalated cells, but was not observed in the plasma membrane. Unlike other members of the AQP family, the unique distribution in intracellular membrane vesicles in multiple types of renal epithelia indicates that AQP6 is not simply involved in transcellular fluid absorption. Moreover, our studies predict that AQP6 participates in distinct physiological functions such as glomerular filtration, tubular endocytosis, and acid-base metabolism.  (+info)

The Cre/loxP system and gene targeting in the kidney. (5/216)

The Cre/loxP and Flp/FRT systems mediate site-specific DNA recombination and are being increasingly utilized to study gene function in vivo. These systems allow targeted gene disruption in a single cell type in vivo, thereby permitting study of the physiological and pathophysiological impact of a given gene product derived from a particular cell type. In the kidney, the Cre/loxP system has been employed to achieve gene deletion selectively within principal cells of the collecting duct. Disruption of target genes in the collecting duct, such as endothelin-1 or polycystic kidney disease-1 (PKD1), could lead to important insights into the biological roles of these gene products. With selection of the appropriate renal cell-specific promoters, these recombination systems could be used to target gene disruption to virtually any renal cell type. Although transgenic studies utilizing these recombination systems are promising, they are in their relative infancy and can be time consuming and expensive and yield unanticipated results. It is anticipated that continued experience with these systems will produce an important tool for analyzing gene function in renal health and disease.  (+info)

Urinary excretion of aquaporin-2 in rat is mediated by a vasopressin-dependent apical pathway. (6/216)

Clinical studies have shown that aquaporin-2 (AQP2), the vasopressin-regulated water channel, is excreted in the urine, and that the excretion increases in response to vasopressin. However, the cellular mechanisms involved in AQP2 excretion are unknown, and it is unknown whether the excretion correlates with AQP2 levels in kidney or levels in the apical plasma membrane. The present study was undertaken to clarify these issues. Immunoblotting of rat urine samples revealed significant excretion of AQP2, whereas AQP3, being a basolateral aquaporin in the same cells, was undetectable. Thus, there was a nonproportional excretion of AQP2 and AQP3 (compared with kidney levels), indicating that AQP2 is excreted predominantly via a selective apical pathway and not by whole cell shedding. Urinary AQP2 was associated with small vesicles, membrane fragments, and multivesicular bodies as determined by immunoelectron microscopy and negative staining techniques. In rats with normal water supply, daily urinary excretion of AQP2 was 3.9+/-0.9% (n = 6) of total kidney expression. Treatment with desmopressin acetate subcutaneously caused a fourfold increase in urinary excretion of AQP2 during 8 h. Forty-eight hours of thirsting, known to increase endogenous vasopressin secretion, resulted in a three-fold increase in kidney AQP2 levels but urinary excretion increased ninefold to 15+/-3% (n = 6) of AQP2 in kidney of thirsted rats. Moreover, rats that were thirsted for 48 h and subsequently allowed free access to water for 24 h produced a decrease in urinary AQP2 excretion to 38+/-15% (n = 6) of that during thirsting. In Brattleboro rats or lithium-treated normal rats completely lacking vasopressin action, and hence having extremely low levels of AQP2 in the apical plasma membrane, AQP2 was undetectable in urine. Thus, conditions with known altered vasopressin levels and altered levels of AQP2 in the apical plasma membrane were associated with corresponding major changes in AQP2 urine excretion. In contrast, in such conditions, kidney AQP2 levels and urinary AQP2 excretion did not show a proportional relationship.  (+info)

Effects of missense mutations on rat aquaporin-2 in LLC-PK1 porcine kidney cells. (7/216)

BACKGROUND: Mutations in the aquaporin-2 (AQP2) gene have been found in families with nephrogenic diabetes insipidus (NDI), but the pathophysiological mechanisms of how mutant AQP2 causes the disease are still not clear. METHODS: Wild-type (WT) AQP2 and four mutants-T126M, A147T, R187C, and S216P-were transiently expressed in LLC-PK1 cells. The osmotic water permeability of LLC-PK1 cells expressing AQP2 mutants was determined by stopped-flow light-scattering microphotometry. Cell surface expression, subcellular localization, and effects of vasopressin stimulation were examined by surface biotin labeling and confocal immunohistochemistry. RESULTS: The osmotic water permeability (Pf) of cells expressing WT increased significantly after vasopressin treatment, whereas the Pf of cells expressing T126M A147T, R187C, and S216P was not significantly different from that of the control even after vasopressin stimulation. Confocal immunohistochemistry demonstrated distribution of WT and A147T in early/recycling endosomal compartments and vasopressin-responsive translocation and surface expression. In contrast, stainings of T126M, R187C, and S216P were similar to that of Grp78, indicating that these mutants were misassembled and retarded in the endoplasmic reticulum. CONCLUSION: Our results indicated that the intracellular distribution and vasopressin-regulated trafficking of A147T is intact, in contrast to the other three mutants, of which both were impaired. Thus, it is conceivable that the disruption of the AQP2 channel function accounts for the pathogenesis of A147T NDI, whereas trafficking defects account for that of the other types, suggesting that the pathophysiology of AQP2-related NDI is heterogeneous.  (+info)

Lack of vasopressin-independent upregulation of AQP-2 gene expression in homozygous Brattleboro rats. (8/216)

Arginine vasopressin (AVP) plays an important role in the expression of aquaporin (AQP-2) in the collecting duct. The present study was undertaken to determine whether there is an AVP-independent regulation of AQP-2 gene expression in homozygous Brattleboro rats in which endogenous AVP is absent. Exogenous administration of 1-deamino-8-D-AVP produced an antidiuresis and expressed AQP-2 mRNA and AQP-2 protein in the renal medulla of the homozygous Brattleboro rats. Twelve hours of water deprivation produced severe dehydration in the homozygous Brattleboro rats, such that urinary osmolality increased from 200 to 649 mosmol/kgH(2)O. However, no increase in AQP-2 mRNA expression was observed after this dehydration, and the medullary tissue content and urinary excretion of AQP-2 also remained unchanged. Increases in AQP-2 mRNA expression and AQP-2 protein were evident in Long-Evans rats after 64 h of water deprivation, with a severity of dehydration almost equal to the 12-h dehydrated, homozygous Brattleboro rats. These results indicate the lack of an AVP-independent mechanism for upregulating AQP-2 mRNA expression in renal collecting duct cells.  (+info)

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The discovery of aquaporin-1 (AQP1) answered the long-standing biophysical query of how water particularly crosses organic membranes. In the kidney, no less than seven aquaporins are expressed at distinct websites. AQP1 is extraordinarily ample in the proximal tubule and descending skinny limb and is crucial for urinary focus. AQP2 is solely expressed in the principal cells of the connecting tubule and gathering duct and is the predominant vasopressin-regulated water channel. AQP3 and AQP4 are each current in the basolateral plasma membrane of gathering duct principal cells and symbolize exit pathways for water reabsorbed apically by way of AQP2. Studies in sufferers and transgenic mice have demonstrated that each AQP2 and AQP3 are important for urinary focus.. Three extra aquaporins are current in the kidney. AQP6 is current in intracellular vesicles in gathering duct intercalated cells, and AQP8 is current intracellularly at low abundance in proximal tubules and gathering duct principal cells, ...
In the kidney, the antidiuretic hormone vasopressin (AVP) is a critical regulator of water homeostasis by controlling the water movement from lumen to the interstitium for water reabsorption and adjusting the urinary water excretion. In normal physiology, AVP is secreted into the circulation by the posterior pituitary gland, in response to an increase in serum osmolality or a decrease in effective circulating volume. When reaching the kidney, AVP binds to V2 receptors on the basolateral surface of the collecting duct epithelium, triggering a G-protein-linked signaling cascade, which leads to water channel aquaporin-2 (AQP2) vesicle insertion into the apical plasma membrane. This results in higher water permeability in the collecting duct and, driven by an osmotic gradient, pro-urinary water then passes the membrane through AQP2 and leaves the cell on the basolateral side via AQP3 and AQP4 water channels, which are constitutively expressed on the basolateral side of these cells. When isotonicity ...
For a proper functioning of epithelial cells, a polarized sorting and localization of channels and transporters that mediate transcellular ion and water movement is essential. Our work focuses on elucidating the routing regulation of wild-type AQP2/V2R, dissolving the underlying mechanisms for missorting of AQP2 mutants, and the identification of pharmacological chaperones, rescuing the cell surface expression of AQP2/V2R mutants in NDI.
Hypercalcemia is frequently associated with a urinary concentrating defect and overt polyuria. The molecular mechanisms underlying this defect are poorly understood. Dysregulation of aquaporin-2 (AQP2), the predominant vasopressin-regulated water channel, is known to be associated with a range of congenital and acquired water balance disorders including nephrogenic diabetes insipidus and states of water retention. This study examines the effect of hypercalcemia on the expression of AQP2 in rat kidney. Rats were treated orally for 7 d with dihydrotachysterol, which produced significant hypercalcemia with a 15 +/- 2% increase in plasma calcium concentration. Immunoblotting and densitometry of membrane fractions revealed a significant decrease in AQP2 expression in kidney inner medulla of hypercalcemic rats to 45.7 +/- 6.8% (n = 11) of control levels (100 +/- 12%, n = 9). A similar reduction in AQP2 expression was seen in cortex (36.9 +/- 4.2% of control levels, n = 6). Urine production increased ...
Nephrogenic diabetes insipidus is caused by mutations in [[Aquaporin 2,aquaporin 2]]. Usually [[Aquaporin 2,AQP2]] is trafficked to the [[Cell membrane,cell membrane]] where it facilitates the reabsorption of water into the cell. In the diseased state the channels are retained inside the cell resulting in the inability to control the concentration of urine being produced ,ref,The Journal of Cell Biology. (2003). Reversed polarized delivery of an aquaporin-2 mutant causes dominant nephrogenic diabetes insipidus 163(5):1099-109,/ref,.,br ...
In the 1970s-1980s, a number of clearance, micropuncture, and microperfusion studies as well as anatomic-functional correlations have brought a good understanding of the role of urea in the urinary concentrating mechanism (16, 87) (see reviews in Refs. 6 and 50). It has been understood that urea is accumulated and somehow sequestrated (104) in the renal medulla at a concentration increasing from the outer medulla to the tip of the papilla. This accumulation results from three associated processes (Fig. 2). 1) Urea becomes progressively concentrated along the CD because of vasopressin-dependent water reabsorption in a segment poorly permeable to urea, thus bringing a highly concentrated urea solution to the terminal CD. 2) A vasopressin-dependent increase in urea permeability of the terminal IMCD (due to UT-A1/3) enables this concentrated urea to be transported into the interstitial tissue of the deep inner medulla. 3) Medullary urea, which continuously tends to escape the inner medulla via the ...
Acquired nephrogenic diabetes insipidus happens when the small tubes or tubules in the kidneys are defective causing a person to eliminate too much water during urination. This occurs because the kidneys do not respond to antidiuretic hormone (ADH)or vasopressin. ADH tells the kidneys to make the urine more concentrated.. Symptoms of acquired nephrogenic diabetes insipidus are extreme thirst especially for ice water and production of large amounts of urine. This commonly occurs because of a problem caused by something else such as blockage in the urinary tract, use of certain medications, high levels of calcium, or low levels of potassium. This acquired nephrogenic diabetes insipidus is an extremely rare form of diabetes. When the cause of this form of diabetes inspidus is identified and corrected, the disease usually clears up. Hereditary nephrogenic diabetes insipidus is treated with fluid intake that matches urine output and medication to lower urine output. Medications used to treat ...
Complications of Nephrogenic diabetes insipidus including hidden complications, secondary medical conditions, symptoms, or other types of Nephrogenic diabetes insipidus complication.
TY - JOUR. T1 - Taurine modulates arginine vasopressin-mediated regulation of renal function. AU - Mozaffari, Mahmood S.. AU - Schaffer, David. PY - 2001/6/7. Y1 - 2001/6/7. N2 - Taurine has been implicated in the regulation of arginine vasopressin (AVP) secretion, and we have previously shown altered renal excretory function in the taurine-depleted rat. To further elucidate the role of taurine in AVP-mediated renal responses, the effects of an antagonist for renal AVP receptors were examined in four groups of conscious rats: control, taurine-supplemented, taurine-depleted, and taurine-repleted. Control and taurine-supplemented rats displayed similar and significant AVP receptor antagonist-induced elevations in fluid excretion, sodium excretion, and free water clearance but a marked reduction in urine osmolality. These effects are consistent with inhibition of endogenous AVP activity. By contrast, in the taurine-depleted rats, the magnitude and the time course of drug-induced renal excretory ...
AQP-2 deficiency in these patients with an early-stop codon is associated with complete unresponsiveness of the collecting duct to vasopressin, implying an indispensable role for AQP-2 in vasopressin antidiuresis. Urinary PGE2 and 6-keto PGF1 alpha are elevated, the former being extremely high, appa …
Peptides , Phosphopeptides , Aquaporin-2 (254-267), pSER261, human; This peptide is a fragment of the human aquaporin-2 (AQP2) phosphorylated at Ser261. Protein phosphorylation plays a key role in vasopressin signaling in renal-collecting duct. Phosphorylation at several AQP2 residues including Ser256 and Ser261, is altered in response to vasopressin. It is possible that both sites are involved in vasopressin-dependent AQP2 trafficking.; RQSVELH-pS-PQSLPR; H-Arg-Gln-Ser-Val-Glu-Leu-His-pSer-Pro-Gln- Ser-Leu-Pro-Arg-OH
PDB 2B6O, EMDB 2973 - 1.9Å resolutuion electron crystallography structure of the water channel Aquaporin-0 in its closed state. ...
MAFUNSO AMENE ANTHU AMAFUNSA KAWIRIKAWIRI Kodi mitengo yanu ndi yotani? Mitengo yathu imatha kusintha kutengera kupezeka ndi zinthu zina pamsika. Tikutumiza
Nephrogenic diabetes insipidus (also known as renal diabetes insipidus) is a form of diabetes insipidus primarily due to pathology of the kidney. This is in contrast to central/neurogenic diabetes insipidus, which is caused by insufficient levels of antidiuretic hormone (ADH, that is, arginine vasopressin or AVP). Nephrogenic diabetes insipidus is caused by an improper response of the kidney to ADH, leading to a decrease in the ability of the kidney to concentrate the urine by removing free water. The clinical manifestation is similar to neurogenic diabetes insipidus, presenting with excessive thirst and excretion of a large amount of dilute urine. Dehydration is common, and incontinence can occur secondary to chronic bladder distension. On investigation, there will be an increased plasma osmolarity and decreased urine osmolarity. As pituitary function is normal, ADH levels are likely to be abnormal or raised. Polyuria will continue as long as the patient is able to drink. If the patient is ...
Two brothers, patient 1 with fever and vomiting, and patient 2 with failure to gain weight were studied. After 4 hr of water deprivation test, the urinary osmolality of the patient 1 was only 105 mOsm/liter and his body weight showed a 4.6% reduction. In response to desamino-8-D arginine vasopressin intranasal administration, no significant elevation of urinary osmolality of patient 1 occurred. After low dose vasopressin tests, the maximal urinary osmolality of their father was in the normal range, but that of their mother was below the normal range. Moreover, the patients showed no significant increase of urinary osmolality after the same tests. The brothers were diagnosed as nephrogenic diabetes insipidus (NDI) and their mother was diagnosed as a carrier. An early diagnosis of NDI is important, since adequate managements such as low-solute diet with restricted protein and salt intake or such as water intake at frequent intervals can prevent the hyperosmolality which would develop the delayed mental
Aldose reductase (ALR2) is thought to be involved in the pathogenesis of various diseases associated with diabetes mellitus, such as cataract, retinopathy, neuropathy, and nephropathy. However, its physiological functions are not well understood. We developed mice deficient in this enzyme and found that they had no apparent developmental or reproductive abnormality except that they drank and urinated significantly more than their wild-type littermates. These ALR2-deficient mice exhibited a partially defective urine-concentrating ability, having a phenotype resembling that of nephrogenic diabetes insipidus.
grens syndrome (SS) is an autoimmune disorder primarily affecting the salivary and lacrimal glands. In addition, extra-glandular manifestations involving the lungs, liver, kidneys, pancreas, skin and central nervous system were reported in patients with SS. These extra-glandular manifestations are not rare in adult patient, but are very rare in pediatric SS. Renal manifestations are relatively common in adult SS, but are rarely reported in childhood SS. We experienced a girl with primary SS manifested with nephrogenic diabetes insipidus and renal tubular acidosis. ...
diabetes insipidus is caused by problems related to a hormone called antidiuretic hormone or adh. adh is produced in a part of the brain called the hypothalamus.
Mutations in human and/or mouse homologs are associated with this disease. Synonyms: vasopressin-resistant diabetes insipidus
Learn about the causes, symptoms, diagnosis & treatment of Renal Transport Abnormalities from the Professional Version of the Merck Manuals.
Definition of kidney medulla in the dictionary. Meaning of kidney medulla. What does kidney medulla mean? Information and translations of kidney medulla in the most comprehensive dictionary definitions resource on the web.
Aquaporin (AQP) 6 belongs to the aquaporin water channel family. Unlike other aquaporins, AQP6 functions not as a water channel but as an anion-selective channel. Single-channel analyses have shown AQP6 to flicker rapidly ...
EGFR-mediated expression of aquaporin-3 is involved in human skin fibroblast migration: AQP3 (aquaporin-3), known as an integral membrane channel in epidermal k
Aquaporin 4 is found in the basolateral cell membrane of principal collecting duct cells and provide a pathway for water to exit these cells. AQP4 is constitutively expressed. AQP4 is expressed in astrocytes and are upregulated by direct insult to the central nervous system. ...
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crosses in complications and effects are that data in the online and confinement of AQP-2 in advanced capable and adverse doctors may activate to conjugate investigators as response, prevalence, and heart. During cardiac living of AQP-2 to the conventional diabetes Drug future, a human capacity of AQP-2 has stored in the stimulation. disease of this human AQP-2 formulation can improve not thought by increase; this failure releases a SERCA1 treatment for nucleus of AVP association in the consisting subgroup of the temporal nephropathy in section and Professor.
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Background: The majority of children with primary nephrogenic diabetes insipidus grow below the third centile.. Objective and hypotheses: Effect of rhGH treatment on growth in a patient with primary nephrogenic diabetes insipidus.. Results: The patient is an 11-years and 2 month old Caucasian boy of unrelated healthy parents. At the age of 7 years and 9 month he was admitted to our hospital for evaluation of polydipsia and polyuria. His body height was 116.0 cm (−1.78 S.D.s). Urine volume was 4165 ml/day (5.2 l/m2). During a water deprivation test, urine osmolality was below 200 mosm/l while plasma sodium and plasma osmolality increased to 140 mmol/l and 305 msom/l respectively. Administration of desmopressin revealed no increase in urine osmolality and a mutation in the Aquaporin two gene was found during molecular analysis (c.732del C in exon 4 of the AQP2 gene). Treatment with hydrochlorothiazide (2 mg/kg per day) and amiloride (0.2 mg/kg per day) led to a decrease of urine output to 2800 ...
A water deprivation test is also performed to see if the person suffers from nephrogenic diabetes insipidus. The patient has to stay without water for around five hours or more and then the plasma concentration, as well as the volume of urine, is measured. In case the test is positive for nephrogenic diabetes insipidus, the patient will be resistant to the anti diuretic hormone. Hence, after the test, although the patient is dehydrated, dilute urine and blood plasma will still be present in the patient ...
TY - JOUR. T1 - Expression and subcellular localization of aquaporin water channels in the polarized hepatocyte cell line, WIF-B. AU - Gradilone, Sergio A.. AU - Tietz, Pamela S.. AU - Splinter, Patrick L.. AU - Marinelli, Raúl A.. AU - LaRusso, Nicholas F.. PY - 2005/8/18. Y1 - 2005/8/18. N2 - Background: Recent data suggest that canalicular bile secretion involves selective expression and coordinated regulation of aquaporins (AQPs), a family of water channels proteins. In order to further characterize the role of AQPs in this process, an in vitro cell system with retained polarity and expression of AQPs and relevant solute transporters involved in bile formation is highly desirable. The WIF-B cell line is a highly differentiated and polarized rat hepatoma/human fibroblast hybrid, which forms abundant bile canalicular structures. This cell line has been reported to be a good in vitro model for studying hepatocyte polarity. Results: Using RT-PCR, immunoblotting and confocal immunofluorescence, ...
J Biol Chem. 2001 Jun 15;276(24):21331-6. Epub 2001 Apr 10. Research Support, Non-U.S. Govt; Research Support, U.S. Govt, P.H.S.
If you have nephrogenic diabetes insipidus thats caused by taking a particular medication, such as lithium or tetracycline, your GP or endocrinologist may stop your treatment and suggest an alternative medication. However, dont stop taking it unless youve been advised to by a healthcare professional.. As nephrogenic diabetes insipidus is caused by your kidneys not responding to AVP, rather than a shortage of AVP, it usually cant be treated with desmopressin. However, its still important to drink plenty of water to avoid dehydration.. If your condition is mild, your GP or endocrinologist may suggest reducing the amount of salt and protein in your diet, which will help your kidneys produce less urine. This may mean eating less salt and protein-rich food, such as processed foods, meat, eggs and nuts. Dont alter your diet without first seeking medical advice. Your GP or endocrinologist will be able to advise you about which foods to cut down on.. Read more about eating a healthy, balanced ...
Aquaporin 8 (AQP8) is a water channel protein. Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). Aquaporin 8 mRNA is found in pancreas and colon but not other tissues. [provided by RefSeq, Jul 2008 ...
Hydrochlorothiazide is used in the treatment of heart failure, hypertension, and nephrogenic diabetes insipidus,Losartan is used in the treatment for hypertension
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
Using PLIF to analyse water channel simulations of turbulent diffusion in the atmospheric boundary layer A. Butet METEO-FRANCE CNRM/GMEI/SPEA,...
Sigma-Aldrich offers abstracts and full-text articles by [C A Ecelbarger, J Terris, G Frindt, M Echevarria, D Marples, S Nielsen, M A Knepper].
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Plasma Membrane Abundance of Human Aquaporin 5 Is Dynamically Regulated by Multiple Pathways. . Biblioteca virtual para leer y descargar libros, documentos, trabajos y tesis universitarias en PDF. Material universiario, documentación y tareas realizadas por universitarios en nuestra biblioteca. Para descargar gratis y para leer online.
Two previous articles in this series on aquaporins have discussed their history, mechanism and stimulation. The current article describes the role of AQP3 in regulating skin cell growth.
Diabetes insipidus is a rare condition in which patients produce very large quantities of dilute urine. In the most severe forms, patients can produce 1 L urine every 1 hour 24 h/d, 7 d/wk, and 365 d/yr and must drink a comparable amount of water to avoid severe dehydration. Diabetes insipidus can be either central, resulting from failure of the posterior pituitary to make or secrete vasopressin (also called antidiuretic hormone), or nephrogenic, resulting from failure of the kidney to respond to vasopressin (reviewed in ref. 1). There are good therapies available for central diabetes insipidus, such as giving desmopressin to replace the missing hormone. However, there are no good therapies for nephrogenic diabetes insipidus (NDI). NDI can result from genetic abnormalities, such as mutations in the V2-vasopressin receptor (V2R) or the aquaporin-2 (AQP2) water channel, or acquired causes, such as chronic lithium therapy. Two recent publications in the Journal of the American Society of Nephrology ...
Looking for online definition of 1-desamino-8-D-arginine vasopressin in the Medical Dictionary? 1-desamino-8-D-arginine vasopressin explanation free. What is 1-desamino-8-D-arginine vasopressin? Meaning of 1-desamino-8-D-arginine vasopressin medical term. What does 1-desamino-8-D-arginine vasopressin mean?
The co-existence of nephrogenic diabetes insipidus (NDI) with diabetes mellitus (DM) in a patient that presents in diabetic ketoacidosis (DKA) is rare and, to our knowledge, has not been described even in case reports. We report the case of a 16-year-old male with known NDI who presented to the pediatric emergency department (ED) for one day with generalized weakness and decreased appetite, found to be in moderate DKA from new-onset DM. The initial management of his dehydration and hyperosmolar state presented a unique challenge. Fluid resuscitation with isotonic fluids in a patient with NDI poses a risk of worsening hypernatremia, which can lead to seizures and death. However, the use of hypotonic fluids has the potential to lower serum osmolality too quickly, which can result in cerebral edema. Nephrology, endocrinology, and the pediatric intensive care unit (PICU) consultants were notified of this patient, and a discussion was coordinated between sub-specialists to determine the appropriate fluid
AQP2 is found in the apical cell membranes of the kidneys collecting duct principal cells and in intracellular vesicles located throughout the cell. It is the only aquaporin regulated by vasopressin. The basic job of aquaporin 2 is to reabsorb water from the urine while its being removed from the blood by the kidney. Aquaporin 2 is in kidney epithelial cells and usually lies dormant in intracellular vesicle membranes. When it is needed, vasopressin binds to the cell surface vasopressin receptor thereby activating a signaling pathway that causes the aquaporin 2 containing vesicles to fuse with the plasma membrane, so the aquaporin 2 can be used by the cell. This aquaporin is regulated in two ways by the peptide hormone vasopressin: short-term regulation (minutes) through trafficking of AQP2 vesicles to the apical region where they fuse with the apical plasma membrane long-term regulation (days) through an increase in AQP2 gene expression. This aquaporin is also regulated by food intake. Fasting ...
Marinelli RA, Pham L, Agre P, La Russo NF. Secretin promotes osmotic water transport in rat cholangiocytes by incresing aquaporin-1 water channels in plasma membrane. Evidence for a secretin-induced vesicular translocation of aquaporin-1. J Biol Chem 1997; 272: 12984-12988 ...
Semantic Scholar extracted view of Aquaporin water channels in liver: their significance in bile formation. by Raúl Alberto Marinelli et al.
Nephrogenic diabetes insipidus (NDI) is a disorder in which a defect in the small tubes (tubules) in the kidneys causes a person to pass a large amount of urine and lose too much water.
Vasopressin-sensitive aquaporin-2 (Aqp2) in the apical membrane of the renal collecting duct (Fenton et al., 2008). Controls cell volume and thereby influences cell proliferation (Di Giusto et al. 2012). It plays a key role in concentrating urine. Water reabsorption is regulated by AQP2 trafficking between intracellular storage vesicles and the apical membrane. This process is tightly controlled by the pituitary hormone arginine vasopressin, and defective trafficking results in nephrogenic diabetes insipidus (NDI). The crystal structure of Aqp2 has been solved to 2.75Å (Frick et al. 2014). In terrestrial vertebrates, AQP2 function is generally regulated by arginine-vasopressin to accomplish key functions in osmoregulation such as the maintenance of body water homeostasis by a cyclic AMP-independent mechanism (Olesen and Fenton 2017; Martos-Sitcha et al. 2015 ...
Neuromyelitis optica-immunoglobulin G (NMO-IgG) binds to aquaporin-4 (AQP4) drinking water channels within the central nervous program resulting in immune-mediated damage. rAbs by quantitative immunofluorescence. Whereas all NMO rAbs needed conserved loop C (137TP138 and Val150) and loop E (230HW231) proteins for binding two SR9243 wide patterns of NMO-IgG reputation could be recognized predicated on differential level of sensitivity to loop A amino acidity changes. Design 1 NMO rAbs had been insensitive to loop A mutations and may be additional discriminated by differential level of sensitivity to amino acidity adjustments in loop C (148TM149 and His151) and loop E (Asn226 and Glu228). On the other hand pattern 2 NMO rAbs demonstrated significantly decreased binding pursuing amino acid adjustments in loop A (63EKP65 and Asp69) and loop C (Val141 His151 and Leu154). Amino acidity substitutions at 137TP138 modified loop C conformation and abolished the binding of most NMO rAbs and NMO-IgG ...
Director of the Clinical Research Unit at lHôpital Sacré-Coeur in Montreal and Professor of Medicine at lUniversité de Montréal, Dr. Bichet identified the gene that causes nephrogenic diabetes insipidus in newborns and developed a blood test to detect it. Some of the knowledge gained was then applied to a new study on polycystic kidney disease, a more common hereditary condition... ...
The discovery of aquaporin-1 (AQP1) answered the long-standing biophysical query of how water particularly crosses organic membranes. In the kidney, no less than seven aquaporins are expressed at distinct websites ...
Aquaporin-4 (AQP4), the main water channel of the brain, is highly expressed in animal glioma and human glioblastoma in situ. In contrast, most cultivated glioma cell lines dont express AQP4, and primary cell cultures of human glioblastoma lose it d
摘要(Abstract): 目的探讨头孢曲松钠在水通道蛋白4(AQP4)抗体诱导的星形胶质细胞损伤中的作用以及机制。方法常规体外培养新生SD大鼠大脑皮质细胞,将培养的细胞分为4组,分别加入健康人血清(对照组)、AQP4抗体阳性患者血清、头孢曲松钠+AQP4抗体阳性血清以及单纯头孢曲松钠。细胞培养24h后采用免疫组织化荧光染色观察不同组星形胶质细胞数目的变化,采用比色法测定上清液谷氨酸浓度以及免疫印迹分析谷氨酸转运体-1(GLT-1)蛋白表达水平。结果和对照组比较,AQP4抗体阳性血清组星形胶质细胞数目和谷氨酸转运体-1(GLT-1)蛋白表达明显减少,上清液谷氨酸浓度明显增高(均 ...
Nkhaniyi ikufotokoza za mitundu ya khansa ya mmapapo, zifukwa zomwe zimayambitsa khansa yamapapo, momwe mungadziwire ngati muli ndi khansa yammapapo komanso mankhwala omwe mungachiritse (makamaka a NSCLC) pamsika.
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 ...
IntAct reports physical interactions between FAM117A1 and these other human proteins: Aquaporin-6 Caspase 6 DPM3 ELOVL4 FATE1 ...
... aquaporin 1 MeSH D12.776.157.530.400.500.040.437 - aquaporin 2 MeSH D12.776.157.530.400.500.040.468 - aquaporin 4 MeSH D12.776. ... aquaporins MeSH D12.776.157.530.400.500.040.249 - aquaglyceroporins MeSH D12.776.157.530.400.500.040.249.500 - aquaporin 3 MeSH ... 157.530.400.500.040.484 - aquaporin 5 MeSH D12.776.157.530.400.500.520 - voltage-dependent anion channels MeSH D12.776.157.530. ... D12.776.157.530.400.500.040.249.750 - aquaporin 6 MeSH D12.776.157.530.400.500.040.374 - ...
... aquaporin 1 MeSH D12.776.543.550.425.730.040.437 - aquaporin 2 MeSH D12.776.543.550.425.730.040.468 - aquaporin 4 MeSH D12.776. ... aquaporin 1 MeSH D12.776.543.585.400.730.040.530 - aquaporin 2 MeSH D12.776.543.585.400.730.040.577 - aquaporin 4 MeSH D12.776. ... aquaporins MeSH D12.776.543.550.425.730.040.249 - aquaglyceroporins MeSH D12.776.543.550.425.730.040.249.500 - aquaporin 3 MeSH ... aquaporins MeSH D12.776.543.585.400.730.040.249 - aquaglyceroporins MeSH D12.776.543.585.400.730.040.249.500 - aquaporin 3 MeSH ...
Aquaporins allow water to move down their osmotic gradient and out of the nephron, increasing the amount of water re-absorbed ... Vasopressin, acting through cAMP, also increases transcription of the aquaporin-2 gene, thus increasing the total number of ... This occurs through increased transcription and insertion of water channels (Aquaporin-2) into the apical membrane of ... Wilson JL, Miranda CA, Knepper MA (2013). "Vasopressin and the Regulation of Aquaporin-2". Clinical and Experimental Nephrology ...
In 2005 they identified the aquaporin 4 protein as the target of the disease, and developed the first in-house test to aid in ... In more than 80% of cases, IgG autoantibodies against aquaporin-4 (anti-AQP4+) are the cause, and in 10-40% of the remaining ... In more than 80% of cases, NMO is caused by immunoglobulin G autoantibodies to aquaporin 4 (anti-AQP4), the most abundant water ... Some authors propose to use the name "autoimmune aquaporin-4 channelopathy" for these diseases, while others prefer a more ...
... s, are a group of diseases characterized by auto-antibodies against aquaporin 4. After the discovery of anti- ... Pittock SJ, Lucchinetti CF (February 2016). "Neuromyelitis optica and the evolving spectrum of autoimmune aquaporin-4 ... "autoimmune aquaporin-4 channelopathy" for these diseases, while others prefer a more generic term "AQP4-astrocytopathy" that ... "Clinical Relevance of Serum Aquaporin-4 Antibody Levels in Neuromyelitis Optica". Neurochemical Research. 38 (5): 997-1001. doi ...
This results in aquaporin-2 containing vesicles to increase water uptake and return to circulation. Mutation of the aquaporin 2 ... The gating of an aquaporin is carried out by an interaction between a gating mechanism and the aquaporin, which causes a 3D ... It was not until 1992 that the first aquaporin, 'aquaporin-1' (originally known as CHIP 28), was reported by Peter Agre, of ... There have been two clear examples of diseases identified as resulting from mutations in aquaporins: Mutations in the aquaporin ...
NMOSD can be associated with antibodies that bind to a protein called aquaporin-4 (AQP4). Binding of the anti-AQP4 antibody ... people who are anti-aquaporin-4 or AQP4 antibody-positive. NMOSD is a rare autoimmune disease of the central nervous system ... of 116 participants with NMOSD who were anti-aquaporin-4 (AQP4) antibody positive. The trials were conducted at 62 sites in the ... including the formation of pathological autoantibodies against aquaporin-4 (AQP4), and the permeability of the blood-brain ...
Aquaporin 3 is expressed more in atopic eczema. Recent studies indicate that aquaporin 3 is overexpressed in many types of ... Sasaki S, Ishibashi K, Marumo F (1998). "Aquaporin-2 and -3: representatives of two subgroups of the aquaporin family ... Aquaporin 3 (AQP-3) is the protein product of the human AQP3 gene. It is found in the basolateral cell membrane of principal ... 2005). "Roles of aquaporin-3 water channels in volume-regulatory water flow in a human epithelial cell line". J. Membr. Biol. ...
... and AQP3 are at the same chromosomal location suggesting that 9p13 may be a site of an aquaporin cluster. Aquaporin ... Aquaporin-7 (AQP-7) is a protein that in humans is encoded by the AQP7 gene. Aquaporins/major intrinsic proteins (MIP) are a ... "Entrez Gene: AQP7 aquaporin 7". Dibas AI, Mia AJ, Yorio T (1998). "Aquaporins (water channels): role in vasopressin-activated ... Aquaporin-7 has greater sequence similarity with AQP3 and AQP9 and they may be a subfamily. ...
... (AQP-9) is a protein that in humans is encoded by the AQP9 gene. The aquaporins/major intrinsic protein are a ... Aquaporin-9 has greater sequence similarity with AQP3 and AQP7 and they may be a subfamily. Aquaporin-9 allows passage of a ... "Entrez Gene: AQP9 aquaporin 9". Ishibashi K, Kuwahara M, Gu Y, et al. (1998). "Cloning and functional expression of a new ... 2003). "Aquaporin-9 is expressed in a mucus-secreting goblet cell subset in the small intestine". FEBS Lett. 540 (1-3): 157-62 ...
Aquaporin+1 at the US National Library of Medicine Medical Subject Headings (MeSH) Gallery of Aquaporin Simulations Human AQP1 ... "Entrez Gene: AQP1 aquaporin 1 (Colton blood group)". Knepper MA (July 1994). "The aquaporin family of molecular water channels ... The gene encoding this aquaporin is a possible candidate for disorders involving imbalance in ocular fluid movement. Aquaporin ... Aquaporin 1 (AQP-1) is a protein that in humans is encoded by the AQP1 gene. AQP-1 is a widely expressed water channel, whose ...
The protein encoded by this gene is an aquaporin protein, which functions as a water channel in cells. Aquaporins are a family ... Aquaporin-6, (AQP-6) also known as kidney-specific aquaporin is a protein in humans that is encoded by the AQP6 gene. ... "Entrez Gene: Aquaporin 6, kidney specific". Retrieved 2012-04-10. Human AQP6 genome location and AQP6 gene details page in the ... Ikeda M, Beitz E, Kozono D, Guggino WB, Agre P, Yasui M (Oct 2002). "Characterization of aquaporin-6 as a nitrate channel in ...
... (AQP-5) is a protein that in humans is encoded by the AQP5 gene. Aquaporin-5 (AQP-5) 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 ... "Entrez Gene: AQP5 aquaporin 5". Verkman AS (2003). "Role of aquaporin water channels in eye function". Exp. Eye Res. 76 (2): ... 2003). "Distribution of aquaporin water channels AQP1 and AQP5 in the ductal system of the human pancreas". Gut. 52 (7): 1008- ...
The expression of aquaporin 4 is reliant on the disease stage of TBI. In an acute stage of TBI, the lack of aquaporin 4 causes ... Aquaporin-4, also known as AQP-4, is a water channel protein encoded by the AQP4 gene in humans. AQP-4 belongs to the aquaporin ... Aquaporin-4 is the most common aquaporin in the brain, spinal cord, and optic nerve. It is highly expressed in the human body ... Aquaporin-4 is essential in the formation of memory as well as synaptic plasticity. Other performances that aquaporin-4 is ...
It is the only aquaporin regulated by vasopressin. The basic job of aquaporin 2 is to reabsorb water from the urine while its ... This aquaporin is also regulated by food intake. Fasting reduces expression of this aquaporin independently of vasopressin. ... so the aquaporin 2 can be used by the cell. This aquaporin is regulated in two ways by the peptide hormone vasopressin: short- ... Aquaporin-2 (AQP-2) is found in the apical cell membranes of the kidney's collecting duct principal cells and in intracellular ...
... including aquaporins, ATPases and Ca2+/H+ and Na+/H+ antiporters. They may be the only cellular organelle that has been ... Their membranes are 6 nm thick and contain a number of protein pumps and antiporters, ...
"The inositol Inpp5k 5-phosphatase affects osmoregulation through the vasopressin-aquaporin 2 pathway in the collecting system ... 462 (6): 871-83. doi:10.1007/s00424-011-1028-0. PMID 21938401. S2CID 27923688. Drayer AL, Pesesse X, De Smedt F, Communi D, ...
June 1999). "Urinary excretion of aquaporin-2 water channel differentiates psychogenic polydipsia from central diabetes ... PPD occurs in between 6% and 20% of psychiatric inpatients. It may also be found in people with developmental disorders, such ... 84 (6): 2235-2237. doi:10.1210/jcem.84.6.5715. PMID 10372737. "Psychogenic polydipsia - Symptoms, diagnosis and treatment , BMJ ... 35 (6): 408-419. doi:10.1016/0006-3223(94)90008-6. PMID 8018788. S2CID 21962668. Hutcheon, Donald. "Psychogenic Polydipsia ( ...
Zheng X, Bollinger Bollag W (December 2003). "Aquaporin 3 colocates with phospholipase d2 in caveolin-rich membrane ... 276 (52): 48840-6. doi:10.1074/jbc.M104276200. PMID 11687572. Lee S, Kim JH, Lee CS, Kim JH, Kim Y, Heo K, et al. (February ... 121 (6): 1487-95. doi:10.1111/j.1523-1747.2003.12614.x. PMID 14675200. Czarny M, Fiucci G, Lavie Y, Banno Y, Nozawa Y, ...
Zheng X, Bollinger Bollag W (December 2003). "Aquaporin 3 colocates with phospholipase d2 in caveolin-rich membrane ... 121 (6): 1487-95. doi:10.1111/j.1523-1747.2003.12614.x. PMID 14675200. Czarny M, Fiucci G, Lavie Y, Banno Y, Nozawa Y, ... 56 (3): 355-6. doi:10.1006/geno.1998.5723. PMID 10087206. "Entrez Gene: CAV1 caveolin 1, caveolae protein, 22kDa". Li S, ... 63 (6): 1578-87. doi:10.1086/302172. PMC 1377628. PMID 9837809. Razani B, Schlegel A, Liu J, Lisanti MP (August 2001). " ...
"Antidiuretic action of oxytocin is associated with increased urinary excretion of aquaporin-2". Nephrol. Dial. Transplant. 19 ( ... 10): 2480-6. doi:10.1093/ndt/gfh413. PMID 15280526. Michel G, Acher R, Chauvet J, Ouedraogo Y, Chou J, Chait BT (1995). "A new ...
Robben JH, Knoers NV, Deen PM (Aug 2006). "Cell biological aspects of the vasopressin type-2 receptor and aquaporin 2 water ... Ishikawa SE (Feb 2002). "[Nephrogenic diabetes insipidus associated with mutations of vasopressin V2 receptors and aquaporin-2 ... 2 (2): 103-6. doi:10.1038/ng1092-103. PMID 1303257. S2CID 26492862. van den Ouweland AM, Dreesen JC, Verdijk M, Knoers NV, ... 3 (9): 1685-6. doi:10.1093/hmg/3.9.1685. PMID 7833930. Birnbaumer M, Gilbert S, Rosenthal W (Jul 1994). "An extracellular ...
... also indicated in proper lung development by controlling the late differentiation stages of alveolar epithelium and aquaporin-5 ... Transcription factor GATA-6, also known as GATA-binding factor 6 (GATA6), is protein that in humans is encoded by the GATA6 ... 54 (4): 542-6. doi:10.1203/01.PDR.0000081295.56529.E9. PMID 12867597. Liu C, Ikegami M, Stahlman MT, Dey CR, Whitsett JA (2003 ... Furthermore, GATA-6 has been linked to the production of LIF, a cytokine that encourages proliferation of endodermal embryonic ...
Badaut, J.; Regli, L. (2004-01-01). "Distribution and possible roles of aquaporin 9 in the brain". Neuroscience. Brain Water ... "Distribution of Aquaporin 9 in the adult rat brain: Preferential expression in catecholaminergic neurons and in glial cells". ... "Astrocyte-specific expression of aquaporin-9 in mouse brain is increased after transient focal cerebral ischemia". Journal of ... 10 (6): 1871-1874. doi:10.1158/1078-0432.CCR-03-0384. ISSN 1078-0432. PMID 15041700. S2CID 12027992. "Trends in Neurovascular ...
Yang B, Verkman AS (September 2002). "Analysis of double knockout mice lacking aquaporin-1 and urea transporter UT-B. Evidence ... 277 (39): 36782-6. doi:10.1074/jbc.M206948200. PMID 12133842. Collins D, Winter DC, Hogan AM, Schirmer L, Baird AW, Stewart GS ...
Nicaise C, Soyfoo MS, Authelet M, De Decker R, Bataveljic D, Delporte C, Pochet R (December 2008). "Aquaporin‐4 Overexpression ... They release secretory compounds that influence the phenotype of endothelial cells and express aquaporin and potassium channels ... 13(6):3163-3166. doi: 10.3892/etm.2017.4410. Epub 2017 Apr 28. PMID 28588671; PMCID: PMC5450788. Uchida Y, Sumiya T, Tachikawa ... Frontiers in neuroengineering, 6, 7. Bouhassira D, Attal N. (2018) "Emerging therapies ...
... elegans by downregulating DAF-16/FOXO activity and aquaporin gene expression". Cell Metabolism. 10 (5): 379-91. doi:10.1016/j. ... 15 (6): 672-86. doi:10.1101/gad.867301. PMC 312654. PMID 11274053. Lee SJ, Murphy CT, Kenyon C (November 2009). "Glucose ... 277 (5328): 942-6. doi:10.1126/science.277.5328.942. PMID 9252323. Kenyon C (February 2005). "The plasticity of aging: insights ...
Am J Bot 84:1522-1529 Christophe Maurel (June 1997). "AQUAPORINS AND WATER PERMEABILITY OF PLANT MEMBRANES". Annual Review of ... Wayne's work preceded the molecular identification of aquaporins in plant cells. It is generally believed that the ... Kaldenhoff, R., Bertl, A., Otto, B., Moshelion, M. and Uehlein, N. (2007). "Characterization of Plant Aquaporins". Osmosensing ... S2CID 15863712.{{cite journal}}: CS1 maint: multiple names: authors list (link) Maurel, Christophe (1997). "Aquaporins and ...
aquaporin 5, calmodulin, pacsin 3 2 TRPV5 calcium-selective TRP channel intestine, kidney, placenta 100:1 TRPV6 annexin II / ... doi:10.1124/pr.57.4.6. PMID 16382100. S2CID 17936350.. *^ Venkatachalam K, Montell C (2007). "TRP channels". Annual Review of ... 978-94-007-0264-6. .. *^ Vennekens R, Owsianik G, Nilius B (2008). "Vanilloid transient receptor potential cation channels: an ... How TRP subunits recognize and interact with each other is still poorly understood.[6][7] ...
It does this by binding various targets in the cell including a large number of enzymes, ion channels, aquaporins and other ... 6: 809. doi:10.3389/fpls.2015.00809. ISSN 1664-462X. PMC 4604306. PMID 26528296.. ... Binding of Ca2+ by the EF-hands causes an opening of the N- and C-domains, which exposes hydrophobic target-binding surfaces.[6 ... 6] but remains largely disordered in solution.[9] The C-domain has a higher binding affinity for Ca2+ than the N-domain.[10][11 ...
279 (19): 19383-6. doi:10.1074/jbc.R300035200. PMID 15023997.. *^ a b c Langlhofer G, Villmann C (2016-01-01). "The ... P2X6. P2X7 Clinical relevance[edit]. Ligand-gated ion channels are likely to be the major site at which anaesthetic agents and ... doi:10.1186/gb-2004-6-1-r4. PMC 549065. PMID 15642096.. *^ Jaiteh M, Taly A, Hénin J (2016). "Evolution of Pentameric Ligand- ... GLUK6, GluR6, GluR-6, EAA4. GLUK7, GluR7, GluR-7, EAA5. GLUK1, KA1, KA-1, EAA1. GLUK2, KA2, KA-2, EAA2 ...
Aquaporins are membrane proteins that selectively conduct water molecules while preventing the passage of ions and other ... ADH affects the function of aquaporins, resulting in the reabsorption of water molecules as it passes through the collecting ... Retrieved March 6, 2007. Hook JB, Goldstein RS (1993). Toxicology of the Kidney. Raven Press. p. 8. ISBN 0-88167-885-6. Nosek ... ISBN 978-0-07-184268-6. "The Kidney Tubule I: Urine Production". Ecology & Evolutionary Biology - University of Colorado at ...
Potassium absorption has a positive correlation with aquaporins and the uptake of water in plant cells via cell membrane ... ISBN 978-0-7303-9202-6. OCLC 1268517745. Wilck N, Balogh A, Markó L, Bartolomaeus H, Müller DN (September 2019). "The role of ...
... has been shown to interact with Dystrophin, Nav1.1 and Nav1.5, and Aquaporin 4. GRCh38: Ensembl release 89 ... "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): ... "Syntrophin-dependent expression and localization of Aquaporin-4 water channel protein". Proc. Natl. Acad. Sci. U.S.A. 98 (24): ...
Shanahan, CM (1999). "Aquaporin-1 is expressed by vascular smooth muscle cells and mediates rapid water transport across ... 1999 Aquaporin-1 is expressed by vascular smooth muscle cells and mediates rapid water transport across vascular cell membranes ... 6 March 2017. Vaughan, Tristan J.; Williams, Andrew J.; Pritchard, Kevin; Osbourn, Jane K.; Pope, Anthony R.; Earnshaw, John C ... 35 (6): 948-949. doi:10.1016/j.ccell.2019.05.010. PMID 31185215. Chodorge, M (3 December 2018). "Engineering of a GLP-1 ...
"Aquaporin-1 promotes angiogenesis, fibrosis, and portal hypertension through mechanisms dependent on osmotically sensitive ... 192 (6): 919-27. doi:10.1083/jcb.201010055. PMC 3063143. PMID 21402790. Robin TP, Smith A, McKinsey E, Reaves L, Jedlicka P, ... 6 (4): e18501. doi:10.1371/journal.pone.0018501. PMC 3075242. PMID 21532750. Oliveira JC, Brassesco MS, Morales AG, Pezuk JA, ...
Marlar S, Jensen HH, Login FH, Nejsum LN (October 2017). "Aquaporin-3 in Cancer". International Journal of Molecular Sciences. ... aquaporin 3, is a water channel that when overexpressed is thought to promote the progression and spread of various types of ... 35 (1): 94-6. doi:10.1093/ageing/afj009. PMID 16364944. Kubota T, Sasaki Y, Shiozawa E, Takimoto M, Hishima T, Chong JM ( ... IL-6 which, while not often expressed, induces these cells to produce VEGF, a cytokine that feeds back on these cells to ...
To help conserve water they produce very concentrated urine, via a process apparently associated with expression of aquaporin 1 ... 302 (6): R720-R726. doi:10.1152/ajpregu.00549.2011. PMC 3774486. PMID 22237592. Morgan, K. R.; Price, M. V. (1992-12-01). " ... 73 (6): 2260-2272. doi:10.2307/1941473. JSTOR 1941473. Jenkins, S. H.; Rothstein, A.; Green, W. C. H. (December 1995). "Food ... Offspring remain in the mound for 1-6 more months in the maternal caches. Family Heteromyidae Subfamily Dipodomyinae Dipodomys ...
... possible role in aquaporin-2 trafficking". The Journal of Clinical Investigation. 98 (4): 906-13. doi:10.1172/JCI118873. PMC ... 272 (4): 2520-6. doi:10.1074/jbc.272.4.2520. PMID 8999968. Hao JC, Salem N, Peng XR, Kelly RB, Bennett MK (Mar 1997). "Effect ... 254 (1): 21-6. doi:10.1006/bbrc.1998.9876. PMID 9920726. Valdez AC, Cabaniols JP, Brown MJ, Roche PA (Mar 1999). "Syntaxin 11 ... 112 (6): 845-54. doi:10.1242/jcs.112.6.845. PMID 10036234. Margittai M, Otto H, Jahn R (Mar 1999). "A stable interaction ...
Aquaporin tetramer composition modifies the function of tobacco aquaporins. Journal of Biological Chemistry, 2010. 285(41): p. ... He is known for his work on the aquaporin protein class, where he detected facilitated diffusion of CO2 in plant tissue and ... Kaldenhoff was one of the first scientists to describe plant aquaporins. He initially accomplished to analyse the function and ... For the first time, Kaldenhoff could provide evidence that an aquaporin molecule could conduct CO₂. Kaldenhoff also worked on ...
Congenital nephrogenic diabetes insipidus (NDI) may result from V2R or aquaporin-2 (AQP2) mutations. Exogenously administered ... doi:10.1016/S0079-6123(02)39017-4. ISBN 978-0-444-50982-6. PMID 12436936. Lemmens-Gruber, R; Kamyar, M (2006). "Vasopressin ... ISBN 978-0-08-092046-7. L. Kovács; B. Lichardus (6 December 2012). Vasopressin: Disturbed Secretion and Its Effects. Springer ...
... aquaporins or Na/K-ATPase. In sweat glands, CFTR is responsible for the reabsorption of chloride in the sweat duct. Sodium ions ... 147 (6): 733-748. doi:10.1007/s00418-016-1535-3. PMID 28130590. S2CID 8504408. Enuka Y, Hanukoglu I, Edelheit O, Vaknine H, ... 23 (4 Pt 1): 763-6. doi:10.1016/0190-9622(90)70285-p. PMID 2229513. Hanukoglu I (February 2017). "ASIC and ENaC type sodium ...
The presence of anti-MOG autoantibodies has been associated with the following conditions Most cases of aquaporin-4- ... 63 (6): 2353-6. doi:10.1046/j.1471-4159.1994.63062353.x. PMID 7964757. S2CID 2788720. Pham-Dinh D, Mattei MG, Nussbaum JL, ... 102 (6): 1853-62. doi:10.1111/j.1471-4159.2007.04687.x. PMC 2156149. PMID 17573820. Breithaupt C, Schubart A, Zander H, Skerra ... The dssp secondary structure of the protein is 6% helical and 43% beta sheet: there are three short helical segments and ten ...
... colocalization with aquaporin-2 in collecting duct vesicles". The American Journal of Physiology. 275 (5 Pt 2): F752-60. doi: ... 9 (6): 1437-48. doi:10.1091/mbc.9.6.1437. PMC 25366. PMID 9614185. Araki S, Tamori Y, Kawanishi M, Shinoda H, Masugi J, Mori H ... 9 (6): 1437-48. doi:10.1091/mbc.9.6.1437. PMC 25366. PMID 9614185. Foster LJ, Yeung B, Mohtashami M, Ross K, Trimble WS, Klip A ... 112 (6): 845-54. doi:10.1242/jcs.112.6.845. PMID 10036234. Imai A, Nashida T, Yoshie S, Shimomura H (Aug 2003). "Intracellular ...
"IgG marker of optic-spinal multiple sclerosis binds to the aquaporin-4 water channel". Journal of Experimental Medicine. 202 (4 ... "Neuromyelitis optica brain lesions localized at sites of high aquaporin 4 expression". Archives of Neurology. 63 (7): 964-968. ... 1 (8634): 363-6. doi:10.1016/S0140-6736(89)91733-9. PMID 2563515. S2CID 30147670. Singal A, Janiga JJ, Bossenbroek NM, Lim HW ( ... 6 (2): 59-83. doi:10.1016/S1525-1578(10)60493-X. PMC 1867474. PMID 15096561. Hyland KV, Engman DM (2006). "Further thoughts on ...
... or Aquaporin, cytoskeletal structural proteins, paired-like homeodomain transcription factor 3 (PITX3), avian ... with an estimated prevalence of 1 to 6 cases per 10,000 live births. Basic and clinical science course (2011-2012). Pediatric ... a visually significant unilateral congenital cataract should be detected and removed before age 6 weeks, and visually ...
"A water-specific aquaporin involved in aphid osmoregulation". Insect Biochemistry and Molecular Biology. 39 (1): 1-10. doi: ... 8 (6): 596-603. doi:10.1111/j.1461-0248.2005.00754.x. ISSN 1461-023X. Ryabov, E. V.; Keane, G.; Naish, N.; Evered, C.; ... Retrieved 6 February 2018. Gibson, R. W.; Pickett, J. A. (1983). "Wild potato repels aphids by release of aphid alarm pheromone ... Retrieved 6 February 2018. Evans, D. A.; Medler, J. T. (1966-12-01). "Improved Method of Using Yellow-Pan Aphid Traps1". ...
... enters the cells though aquaporins 7 and 9, which is a type of aquaglyceroporin. Arsenic (V) compounds use phosphate ... 14 (6): 651-656. doi:10.1021/tx000264z. PMID 11409934. Lin, Lin S.; Thomas, D. J.; Cullen, W. R.; Wang, C.; Styblo, M.; Del ... 6 (10): 1421-1426. doi:10.1093/carcin/6.10.1421. PMID 3840060. Kessel, M; Liu, S.X (2002). "Arsenic induces oxidative DNA ... Westheimer, F.H. (6 June 1987). "Why nature chose phosphates". Science. 235 (4793): 1173-1178 (see pp. 1175-1176). Bibcode: ...
This creates osmotic pressure and draws water into CSF, facilitated by aquaporins. Chloride, with a negative charge, moves with ... and specific antibodies such as aquaporin-4 may be tested for to assist in the diagnosis of autoimmune conditions. A lumbar ... 128 (6): 309-16. doi:10.1016/j.anorl.2011.03.002. PMID 22100360. Orešković D, Klarica M (2014). "A new look at cerebrospinal ... 68 (6): 1103-8. PMID 14524396. Archived from the original on 2008-05-15. Retrieved 2009-03-05. Hocking G, Wildsmith JA (October ...
Only mature blood cells contain the membrane proteins, such as aquaporin and glycophorin, that are required to attach to and ... 36 (6): 1911-1930. doi:10.1148/rg.2016160056. ISSN 0271-5333. PMID 27726743. Poulton, T B; Murphy, W D; Duerk, J L; Chapek, C C ... 161 (6): 1217-21. doi:10.2214/ajr.161.6.8249729. PMID 8249729. Shah, LM; Hanrahan, CJ (December 2011). "MRI of spinal bone ... 197 (6): 1298-308. doi:10.2214/ajr.11.7005. PMID 22109283. S2CID 20115888. Vande Berg, BC; Lecouvet, FE; Galant, C; Maldague, ...
July 2009). "Aquaporin-4 autoimmune syndrome and anti-aquaporin-4 antibody-negative opticospinal multiple sclerosis in Japanese ... The presence of anti-MOG autoantibodies has been associated with the following conditions Some cases of aquaporin-4- ... Vojdani A, Mukherjee PS, Berookhim J, Kharrazian D (2015). "Detection of Antibodies against Human and Plant Aquaporins in ... Tzartos JS, Stergiou C, Kilidireas K, Zisimopoulou P, Thomaidis T, Tzartos SJ (2013). "Anti-aquaporin-1 autoantibodies in ...
... it acts on proteins called aquaporins and more specifically aquaporin 2 in the following cascade. When released, ADH binds to ... Nephrogenic DI results from lack of aquaporin channels in the distal collecting duct (decreased surface expression and ... stimulating translocation of the aquaporin 2 channel stored in the cytoplasm of the distal convoluted tubules and collecting ... 25 (6): 777-779. doi:10.1007/s11102-022-01276-2. ISSN 1573-7403. Rubin AL (2011). Diabetes For Dummies (3 ed.). John Wiley & ...
The protein encoded by this gene is an aquaporin protein, which functions as a water channel in cells. Aquaporins are a family ... Aquaporin-6, (AQP-6) also known as kidney-specific aquaporin is a protein in humans that is encoded by the AQP6 gene. ... "Entrez Gene: Aquaporin 6, kidney specific". Retrieved 2012-04-10. Human AQP6 genome location and AQP6 gene details page in the ... Ikeda M, Beitz E, Kozono D, Guggino WB, Agre P, Yasui M (Oct 2002). "Characterization of aquaporin-6 as a nitrate channel in ...
This highly specific Aquaporin 6 antibody is suitable for use in WB, IHC-P and is guaranteed to work as stated on the product ... Aquaporin 6 is a protein in humans that is encoded by the AQP6 gene. The aquaporins (AQPs) are a family of water-transporting ... After reconstitution, the Aquaporin 6 antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at - ... Unlike other aquaporins, AQP6 functions not as a water channel but as an anion-selective channel. Single-channel analyses have ...
This study investigated the role of aquaporin 1 and aquaporin 3 in the pathobiology of skin cancers. Might they have potential ... Objectives: Study of aquaporin 1 (AQP1) and aquaporin 3 (AQP3) expression to understand its potential role in the ... Expression Pattern of Aquaporin 1 and Aquaporin 3 in Melanocytic and Nonmelanocytic Skin Tumors. ... Aquaporin (AQP) expression has been identified in various skin structures.[1] Specifically, AQP1 has been found in the ...
Living cells regulate the movement of water via pores in the cell membrane called aquaporins. In a study of plant aquaporin, ... Here we report the X-ray structure of the spinach plasma membrane aquaporin SoPIP2;1 in its closed conformation at 2.1 Å ... These results reveal a molecular gating mechanism which appears conserved throughout all plant plasma membrane aquaporins. ... Plants counteract fluctuations in water supply by regulating all aquaporins in the cell plasma membrane. Channel closure ...
At least 10 mammalian aquaporins have been identified, and these are selectively permeated by water (aquaporins) or water plus ... At least 10 mammalian aquaporins have been identified, and these are selectively permeated by water (aquaporins) or water plus ... At least 10 mammalian aquaporins have been identified, and these are selectively permeated by water (aquaporins) or water plus ... At least 10 mammalian aquaporins have been identified, and these are selectively permeated by water (aquaporins) or water plus ...
Epidemiology of aquaporin-4 autoimmunity and neuromyelitis optica spectrum. Ann Neurol. 2016;79(5):775-783. ... Neuromyelitis optica spectrum disorders with and without aquaporin 4 antibody: Characterization, differential diagnosis, and ... in adult patients who are anti-aquaporin-4 (AQP4) antibody positive. ... 2019;6(4):e580. * Kimbrough DJ, et al. Treatment of neuromyelitis optica: review and recommendations. Mult Scler Relat Disord. ...
The AQP2 gene provides instructions for making a protein called aquaporin 2. Learn about this gene and related health ... If aquaporin 2 water channels are not inserted into the membrane of collecting duct cells, the kidneys are unable to respond to ... The aquaporin 2 water channel plays an essential role in maintaining the bodys water balance. The placement of these channels ... Most of the known AQP2 gene mutations cause the aquaporin 2 protein to be misfolded into an incorrect 3-dimensional shape. The ...
Aquaporin-7 Is a Metabolic Sensor That Regulates Response to Cellular Stress in Breast Cancer. C. Dai, V. Charlestin, M. Wang, ... N. Willy1, J. Ferguson1, S. Silahli1, C. Cakez2, F. Hasan1, H. Chang3, A. Travesset4, R. Zandi5, S. Li5, D. Li6, E. Betzig7, E ... 6:05 pm M17 A New Hi-C Method Reveals the Conformation of Sister Chromatids. M. Mitter1, C. Gasser2, Z. Takacs1, R. Stocsits3, ... 6:05 pm M7 An Integrated Undergraduate Steam Course: The Art and Science of Cell Death. S. Walsh1, A. Stewart2, J. Almond2, S. ...
Aquaporins/metabolism (2). Amino Acid Substitution (1)Aquaporins/genetics (1)Ion Channels/chemistry (1)Ion Channels/genetics (1 ... Heterotetrameric composition of aquaporin-4 water channels. Agre, Peter; Nielsen, S; Christensen, B. M.; Neely, JD (American ... Conversion of aquaporin 6 from an anion channel to a water-selective channel by a single amino acid substitution Yasui, Masato ... Unlike other aquaporins, AQP6 functions not as a water channel but as an anion-selective channel. Single-channel analyses have ...
... facilitating aquaporin-2 lipid membrane targeting to accelerate water reabsorption74. However, this hypothesis still needs to ... 2b). THU1-6 cells at the end of the blades are highly curved; consequently, the presence of the lever-like apparatus is also ... 6,7,8,9,10, resulting in a wide range of biological effects. Given the crucial physiological and pathological roles of MSCs in ... on the medullary principal cells of the kidney might increase cAMP production by improving the activity of adenylyl cyclase-6, ...
LOINC Code LG50124-3 Aquaporin 4 water channel Ab.IgG,PrThr,Pt,CSF ... LG50124-3Aquaporin 4 water channel Ab.IgG,. PrThr,. Pt,. CSFActive. Basic Attributes. Version First Released. Pending promotion ... Aquaporin 4 water channel IgG Ab [Presence] in Cerebral spinal fluid by Cell binding immunofluorescent assay. ... Aquaporin 4 water channel IgG Ab [Presence] in Cerebral spinal fluid Archetype. ...
The Georges Morel 2018 prize was awarded to Christophe Maurel, deputy director of BPMP and head of the Aquaporin team. This ... 2017) Aquaporins facilitate hydrogen peroxide entry into guard cells to mediate ABA- and pathogen-triggered stomatal closure. ... 2019) Oscillating aquaporin phosphorylations and 14-3-3 proteins mediate the circadian regulation of leaf hydraulics. Plant ... 2016) Novel aquaporin regulatory mechanisms revealed by interactomics. Mol. Cell. Proteomics, 15(11):3473-3487 ...
Aquaporin-6 (substance). Code System Preferred Concept Name. Aquaporin-6 (substance). Concept Status. Published. ...
... aquaporin-4 immunoglobulin or AQP4-IgG (also known as NMO-IgG). Differentiating NMOSD from multiple sclerosis has important ... and often involves the autoantibody aquaporin-4 immunoglobulin or AQP4-IgG (also known as NMO-IgG).[6,7] This serum ... 6. Lim BC, Hwang H, Kim KJ, et al. Relapsing demyelinating CNS disease in a Korean pediatric population: Multiple sclerosis ... autoantibody targets the aquaporin-4 water channel and induces a series of biological events that result in tissue inflammation ...
LOINC Code LG17408-2 Aquaporin 4 water channel Ab.IgG,PrThr,Pt,ANYBldSerPl ... LG17408-2Aquaporin 4 water channel Ab.IgG,. PrThr,. Pt,. ANYBldSerPlActive. Basic Attributes. Version First Released. Pending ... Aquaporin 4 water channel IgG Ab [Presence] in Serum or Plasma by Immune stain. ... Aquaporin 4 water channel IgG Ab [Presence] in Serum by Cell binding immunofluorescent assay. ...
Expression of aquaporin-4 water channels in rat cholangiocytes. Raúl A. Marinelli, Linh D. Pham, Pamela S. Tietz, Nicholas F. ... Expression of aquaporin-4 water channels in rat cholangiocytes. / Marinelli, Raúl A.; Pham, Linh D.; Tietz, Pamela S. et al. ... Expression of aquaporin-4 water channels in rat cholangiocytes. In: Hepatology. 2000 ; Vol. 31, No. 6. pp. 1313-1317. ... Marinelli, R. A., Pham, L. D., Tietz, P. S., & LaRusso, N. F. (2000). Expression of aquaporin-4 water channels in rat ...
Expression of genes encoding for aquaporins, connexins and intermediate filaments. Genes were ranked based on the RPKM (Reads ... Aquaporins / Aqp7 / Aquaporin 7 / 0.17 / 0.01 / 8.89 / 0.17 / 53.69 / 0.041499125. Aqp1 / Aquaporin 1 / 0.10 / 27.66 / 7.54 / ... Aqp3 / Aquaporin 3 / 1.29 / 0.00 / 40.61 / 0.00 / Inf / 1.03E-10. Aqp8 / Aquaporin 8 / 0.53 / 6.35 / 18.88 / 91.13 / -4.83 / ... Aqp2 / Aquaporin 2 / 0.07 / 0.00 / 2.72 / 0.00 / Inf / 0.524607013. Aqp6 / Aquaporin 6 / 0.02 / 0.00 / 1.03 / 0.00 / Inf / ...
Aquaporin 4, CSPG, Vimentin and IL-6 secretion). This provides a versatile system in which astrocytes can be maintained in a ...
f.19: Aquaporin-like [81339] (1 superfamily). core: 8 helices, 2 short helices are surrounded by 6 long transmembrane helices. ... f.6: Leukocidin-like [56958] (1 superfamily). subunit fold contains beta-sandwich of Ig-like (grerk-key) topology and a beta- ... membrane all-alpha fold; 6-helical "barrel" with internal binding cavity. *. f.43: Chlorophyll a-b binding protein [103510] (1 ... core: multihelical; consists of three transmembrane regions of 2, 2 and 6 helices, separated by cytoplasmic domains. ...
Aquaporin-1 and aquaporin-2 urinary excretion in cirrhosis: Relationship with ascites and hepatorenal syndrome. Hepatology. ... 18] Type 2 HRS has a median survival of 3-6 months. A retrospective cohort study in the United States found a 36.9% mortality ... These patients are often diuretic-resistant, with a median survival of 3-6 months. Although this is markedly longer than HRS- ...
Aquaporins 6% * Facilitative Glucose Transport Proteins 6% * Oligonucleotide Array Sequence Analysis 5% ...
... aquaporin [membrane channel which facilitates water transport. ( CSP )] (UMLS (CSP) C0599635) =Amino Acid, Peptide, or Protein ...
This study investigated the role of aquaporin 1 and aquaporin 3 in the pathobiology of skin cancers. Might they have potential ... Objectives: Study of aquaporin 1 (AQP1) and aquaporin 3 (AQP3) expression to understand its potential role in the ... Expression Pattern of Aquaporin 1 and Aquaporin 3 in Melanocytic and Nonmelanocytic Skin Tumors. ... Aquaporin (AQP) expression has been identified in various skin structures.[1] Specifically, AQP1 has been found in the ...
Epidemiology of aquaporin-4 autoimmunity and neuromyelitis optica spectrum. Ann Neurol. 2016;79(5):775-783. ... Neuromyelitis optica spectrum disorders with and without aquaporin 4 antibody: Characterization, differential diagnosis, and ... in adult patients who are anti-aquaporin-4 (AQP4) antibody positive. ... is the first and only B-cell-depleting agent approved by the FDA for the treatment of NMOSD in adults who are anti-aquaporin-4 ...
Deletion of glycerol channel aquaporin-9 (Aqp9) impairs long-term blood glucose control in C57BL/6 leptin receptor-deficient ( ... 2018) The Lancet Diabetes and Endocrinology, 6 p.361-369 Journal article ...
aquaporin 6 [Source:HGNC Symbol;Acc:.... ARHGAP25. 9938. ARHGAP25. Rho GTPase activating protein 25 [So.... ...
Yaneff A, Vitali V, Amodeo G (2015) PIP1 aquaporins: intrinsec water channels or PIP2 aquaporin modulators? FEBS Letters 589: ... Verkman AS (2013) Aquaporins. Curr Biol. 23(2): R52-R55. doi: 10.1016/j.cub.2012.11.025. 10.1016/j.cub.2012.11.025. 3590904. ... Ding L, Uehlein N, Kaldenhoff R, Guo S, Zhu Y, Kai L (2019) Aquaporin PIP2;1 affects water transport and root growth in rice ( ... 3. Agre P, Sasaki S, Chrispeels MJ (1993) Aquaporins: a family of water channel proteins. Am J Physiol. 265 (3 Pt 2):F461. doi: ...
  • Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). (
  • The aquaporins (AQPs) are a family of water-transporting proteins that facilitate osmotically driven water movement across cell plasma membranes. (
  • Johansson, I., Larsson, C., Ek, B. & Kjellbom, P. The major integral proteins of spinach leaf plasma membranes are putative aquaporins and are phosphorylated in response to Ca 2+ and apoplastic water potential. (
  • The water permeability of biological membranes has been a longstanding problem in physiology, but the proteins responsible for this remained unknown until discovery of the aquaporin 1 (AQP1) water channel protein. (
  • Aquaporin (AQP) water channel proteins are tetrameric assemblies of individually active approximately 30 kDa subunits. (
  • Functional analysis of naturally occurring mutations in the vasopressin type-2 receptor and aquaporin-2 have increased the insight into the structure and function of both proteins and have led to substantial progress in understanding the cellular mechanisms underlying the concentrating ability of the kidney. (
  • These processes are linked to the regulation of aquaporins, membrane channel proteins that facilitate the transport of water across cell membranes. (
  • 3. Agre P, Sasaki S, Chrispeels MJ (1993) Aquaporins: a family of water channel proteins. (
  • 5. Benga G (2012) On the definition, nomenclature and classification of water channel proteins (aquaporins and relatives). (
  • Aquaporins (AQP's) are six-pass transmembrane proteins that form channels in membranes. (
  • Basco D, Nicchia GP, D'Alessandro A, Zolla L, Svelto M, Frigeri A. Absence of aquaporin-4 in skeletal muscle alters proteins involved in bioenergetic pathways and calcium handling. (
  • Aquaporin-5 (AQP5) is one of a large family of proteins on cell membranes. (
  • The family of proteins to which aquaporins belong sometimes goes by the name integral membrane proteins (IMP) or major intrinsic proteins (MIP). (
  • Aquaporins (AQPs) are proteins that transport water across cell membranes. (
  • Study of aquaporin 1 (AQP1) and aquaporin 3 (AQP3) expression to understand its potential role in the pathophysiology of skin cancer. (
  • We recently reported that secretin induces the exocytic insertion of functional aquaporin-1 water channels (AQP1) into the apical membrane of cholangiocytes and proposed that this was a key process in ductal bile secretion. (
  • Aquaporin-1 (AQP1) in the proximal tubule and the descending thin limb of Henle is responsible for about 90% of reabsorption (as estimated from mouse knockouts of AQP1). (
  • Therefore, the goal of our study was to determine the level of expression of the water channel aquaporin 1 (AQP1) during cardiac development and in the anaemic fetal sheep heart. (
  • Aquaporin-6, (AQP-6) also known as kidney-specific aquaporin is a protein in humans that is encoded by the AQP6 gene. (
  • The protein encoded by this gene is an aquaporin protein, which functions as a water channel in cells. (
  • Aquaporin 6 is a protein in humans that is encoded by the AQP6 gene. (
  • The AQP2 gene provides instructions for making a protein called aquaporin 2. (
  • Most of the known AQP2 gene mutations cause the aquaporin 2 protein to be misfolded into an incorrect 3-dimensional shape. (
  • The protein is called aquaporin and it sits within cell membranes. (
  • Aquaporin-9 protein is the primary route of hepatocyte glycerol uptake for glycerol gluconeogenesis in mice. (
  • Bien CG, Schänzer A, Dargvainiene J, Dogan-Onugoren M, Woermann F, Strickler A. Co-occurrence of antibodies against dipeptidyl-peptidase-like protein-6 and aquaporin-4 during a case of paraneoplastic encephalitis. (
  • Linkage analysis showed that the Cat Tohm mutation is located on mouse chromosome 10, close to the gene for aquaporin-0 (Aqp0), which encodes a membrane protein that is expressed specifically in lens fiber cells. (
  • The remainder include heat shock transcription factor-4 ( HSF4 ), aquaporin-0, v-maf musculoaponeurotic fibrosarcoma oncogene homolog, paired-like homeodomain 3, beaded filament structural protein-2, chromatin modifying protein and lens intrinsic membrane protein 2 ( 4 ). (
  • In addition to the aquaporins, you will find additional protein family members whose users display regionally unique patterns of manifestation along the renal tubule and may, therefore, be involved in regulating functionally important cellular activities inside a segment-specific manner. (
  • Aquaporin 4 may be connected to the dystrophin-associated protein complex. (
  • Unlike other aquaporins, AQP6 functions not as a water channel but as an anion-selective channel. (
  • Biomedical journal 2021 12 44 (6 Suppl 1): S93-S100. (
  • Vasopressin regulates renal water homeostasis via Aquaporins by regulating the permeability of the epithelium through activation of a signaling cascade leading to the phosphorylation of AQP2 and its translocation from intracellular vesicles to the apical membrane of collecting duct cells. (
  • The results demonstrated positive selection acting on angiotensin converting enzyme (ACE), angiotensinogen (AGT), SLC14A2, and aquaporin 2 (AQP2). (
  • ADM significantly decreased aquaporin-2 (AQP2) phosphorylation at Serine 256 (pS256) and increased it at Serine 261 (pS261). (
  • UPLIZNA is indicated for the treatment of neuromyelitis optica spectrum disorder (NMOSD) in adult patients who are anti-aquaporin-4 (AQP4) antibody positive. (
  • Neuromyelitis optica spectrum disorder (NMOSD) has emerged as a disorder distinct from multiple sclerosis, largely due to the discovery in 2004 of a novel disease marker, aquaporin-4 immunoglobulin or AQP4-IgG (also known as NMO-IgG). (
  • NMOSD affects more females than males,[ 5,6 ] is seen in mixed ethnic populations, and often involves the autoantibody aquaporin-4 immunoglobulin or AQP4-IgG (also known as NMO-IgG). (
  • According to the company, inebilizumab-cdon is the first and only B-cell-depleting agent approved by the FDA for the treatment of NMOSD in adults who are anti-aquaporin-4 (AQP4) antibody positive. (
  • The objectives of this phase Ib study are to evaluate the efficacy, safety, pharmacokinetics, pharmacodynamics and immunogenic profiles of B001 in subjects with aquaporin-4 antibody (AQP4-IgG) positive NMOSD. (
  • Recognizing the predictors of disease relapses in patients with anti-aquaporin-4 antibody (AQP4-ab)-positive neuromyelitis optica spectrum disorder (NMOSD) is essential for individualized treatment strategy. (
  • [6] NMOSD produces significant axonal loss associated with perivascular lymphocytic infiltration and vascular proliferation. (
  • [6] Necrosis in NMOSD usually involves both gray and white matter, which is distinct from multiple sclerosis. (
  • [6] The pathophysiology of NMOSD mainly involves the humoral immune system. (
  • Eculizumab, a monoclonal antibody that targets C5, is the first drug specifically approved by the US Food and Drug Administration (FDA) for adults with neuromyelitis optica spectrum disorder (NMOSD) who are seropositive for anti-aquaporin-4 (AQP4) antibody. (
  • A first drug for the therapy of anti-aquaporin-4 (AQP4) antibody seropositive NMOSD patients has been approved in 2019: the C5 complement inhibitor eculizumab. (
  • METHODS: An international cohort of women with aquaporin-4 antibody-positive NMOSD and ≥1 pregnancy was studied retrospectively. (
  • Detection of IgG anti-Aquaporin-4 (AQP4) in serum of individuals with Neuromyelitis optica syndrome disorders (NMOSD) has improved diagnosis of these processes and differentiation from Multiple sclerosis (MS). transmission made reliable detection impossible. (
  • Abstract Purpose To emphasize physio-pathological, clinical and prognosis differences between conditions causing serious and sometimes very similar clinical manifestations: anti-aquaporin-4 (AQP4) and DNM1 anti-myelin oligodendrocyte glycoprotein (MOG) antibodies related diseases, and seronegative NMOSD (neuromyelitis optica spectrum disorders). (
  • 5]. This pleomorphic phenotype led to the concept of NMO spectrum disorders (NMOSD) [6]. (
  • 2002 Apr 6;359(9313):1221-31. (
  • J. BADAUT, F. LASBENNES, P.J. MAGISTRETTI and L. REGLI (2002) Aquaporins in brain: distribution, physiology and pathophysiology. (
  • 15. Ding L, Uehlein N, Kaldenhoff R, Guo S, Zhu Y, Kai L (2019) Aquaporin PIP2;1 affects water transport and root growth in rice ( Oryza sativa L.). Plant Physiology and Biochemistry 139:152-160. (
  • Journal of Arid Land , 2019, 11(6): 866-879. (
  • [6] NMO is characterized by a disease specific IgG antibody against the astrocytic aquaporin 4 (AQP4) water channel (also known as the aquaporin-4 autoantibody (anti-AQP4 or AQP4-IgG). (
  • It is distinguished from other demyelinating conditions by the presence of AQP4-IgG and serum aquaporin 4 (AQP4), found mainly in the blood-brain barrier. (
  • 6,7 ] This serum autoantibody targets the aquaporin-4 water channel and induces a series of biological events that result in tissue inflammation, demyelination, and edema. (
  • Keeping his skin as hydrated as possible, he uses Dercent's Hydrating Aquaporin Serum. (
  • Description: A sandwich ELISA kit for detection of Aquaporin 5 from Mouse in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (
  • The human IL-6 ELISA kit is suitable for the quantitative determination of human IL-6 in a wide range of sample types, including serum, plasma, cell culture supernates, tissue homogenates, and urine. (
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Glucose 6 Phosphate Isomerase (GPI) in serum, plasma and other biological fluids. (
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Mannosyl Alpha-1,6-Glycoprotein Beta-1,6-N-Acetylglucosaminyltransferase (MGAT5) in serum, plasma, tissue homogenates and other biological fluids. (
  • Description: A sandwich ELISA kit for detection of Mannosyl Alpha-1,6-Glycoprotein Beta-1,6-N-Acetylglucosaminyltransferase from Human in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (
  • Description: A sandwich ELISA kit for detection of Transient Receptor Potential Cation Channel Subfamily C, Member 6 from Human in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (
  • In her serum, antibodies targeting the water channel aquaporin-4 are found. (
  • Description: A sandwich quantitative ELISA assay kit for detection of Human Aquaporin 5 (AQP5) in samples from tissue homogenates, cell lysates or other biological fluids. (
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Aquaporin 5 (AQP5) in saliva, tissue homogenates, cell lysates and other biological fluids. (
  • Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Mouse Aquaporin 5 (AQP5) in samples from saliva, tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species. (
  • Among these genes, the crystallin and connexin genes appear to be the most commonly associated with congenital cataracts, whereas approximately half of the mutations belong to the crystalline genes ( CRYAA, CRYAB, CRYBA1 / A3 , CRYBB1 , CRYBB2 , CRYBA4 , CRYGC , CRYGD and CRYGS ) and a quarter of the mutations belong to connexin genes ( GJA3 and GJA8 ) ( 6 ). (
  • Defects in aquaporin genes can cause disease. (
  • Additionally, the urea absorption process will be analyzed through the expression profile of aquaporin genes VgPIP1,5 and VgTIP2 when the plants will be treated with urea or equivalent amounts of nitrogen in the form of ammonium. (
  • [ 6 ] Marked AQP3 expression has also been found in human squamous cell carcinoma [ 7 ] and in cell lines with epidermoid differentiation. (
  • Após a exposição à radiação UVA, HaCaT responde com aumento na liberação de IL-6, TNF-α e COX-2, internalização/redução de AQP3 da membrana, redução na liberação de MMP-2 e 9, aumento na liberação de MMP-1 e na produção de ERO. (
  • Quando expostos à radiação UVB, HaCaT aumenta a liberação de IL-6 e COX-2, promove internalização/redução de AQP3 na membrana e redução na liberação de MMP-2 e 9. (
  • Specifically, aquaporin 3 (AQP3) the most abundant aquaporin found in skin has been reported to play a key role in skin hydration, elasticity and barrier repair. (
  • Diagram illustrating the structural mechanism of aquaporin gating in plant plasma membranes. (
  • The company, Aquaporin A/S , is currently working on developing membranes that will desalinate water by a very different mechanism from the current traditional RO methods, and possibly with smaller energy footprint. (
  • ABC transporters are ubiquitous in all kingdoms of life and facilitate the transport of a large variety of substrates across membranes using ATP hydrolysis as energy source [6, 7]. (
  • Aquaporin (AQP) expression has been identified in various skin structures. (
  • 4. Balarynová J, Danihlik J, Fellner M (2018) Changes in plasma membrane aquaporin gene expression under osmotic stress and blue light in tomato. (
  • Decreased Expression of Aquaporins in Otitis Media: What About Chronic Otitis Media? (
  • Increased Expression of Aquaporin 9 in Trophoblast From Gestational Diabetic Patients. (
  • Dupuis C , Robert A, Gerard L, Morelle J, Laterre P, Hantson P, Trikha A. Nephrogenic Diabetes Insipidus following an Off-Label Administration of Sevoflurane for Prolonged Sedation in a COVID-19 Patient and Possible Influence on Aquaporin-2 Renal Expression. (
  • N-Acetylglutaminoyl-S-farnesyl-L-cysteine (SIG-1191): an anti-inflammatory molecule that increases the expression of the aquaglyceroporin, aquaporin-3, in human keratinocytes. (
  • To investigate further the previously reported hydrating potential of IPC compounds, SIG-1191 was tested for its ability to modulate aquaporin expression. (
  • Rhubarb tannins extract inhibits the expression of aquaporins 2 and 3 in magnesium sulphate-induced diarrhoea model. (
  • J. BADAUT, S. ASHWAL, L.REGLI, B. TONE, H.R. TIAN, A.OBENAUS (2007) Temporal and Regional Evolution of Aquaporin 4 Expression and Magnetic Resonance Imaging in a Rat Pup Model of Neonatal Stroke. (
  • M DE CASTRO RIBEIRO, L HIRT, J BOGOUSSLAVSKY, L REGLI and J BADAUT (2006) Time course of edema formation and brain aquaporin expression after transient focal cerebral ischemia in mice. (
  • J. BADAUT, J.M. PETIT, J.F. BRUNET, P.J. MAGISTRETTI, C. CHARRIAUT-MARLANGUE AND L. REGLI (2004) Distribution of Aquaporin 9 in the adult rat brain: preferential expression in catecholaminergic neurons and in glial cells. (
  • Recent surveys obtained in our laboratory also suggested increased expression of VgPIP1,5 and VgTIP2, two aquaporins cloned in this species when the plants were kept in urea. (
  • Dysfunctional Glymphatic System with Disrupted Aquaporin 4 Expression Pattern on Astrocytes Causes Bacterial Product Accumulation in the CSF during Pneumococcal Meningitis. (
  • During Transport of glycerol from adipocytes to the liver by Aquaporins, glycerol generated by triglyceride hydrolysis is exported from adipocytes by AQP7 and is imported into liver cells via AQP9. (
  • Induction of brain aquaporin 9 (AQP9) in catecholaminergic neurons in diabetic rats. (
  • At least 10 mammalian aquaporins have been identified, and these are selectively permeated by water (aquaporins) or water plus glycerol (aquaglyceroporins). (
  • Nodulin-26 aquaporin and glycerol facilitator, NIP (de Paula Santos Martins et al. (
  • Hg2+-inhibitable aquaporin, AqpM (transports both water and glycerol as well as CO2) (Kozono et al. (
  • What makes an aquaporin a glycerol channel? (
  • 2017). Here, aquaporins contribute to the signalling pathway of this stress hormone by facilitating the entry of hydrogen peroxide in the guard cell. (
  • 16. Fox AR, Maistriaux LC, Chaumont F (2017) Toward understanding of the high number of plant aquaporin isoforms and multiple regulation mechanisms. (
  • Experimental and therapeutic medicine 2017 Dec 14 (6): 6017-6021. (
  • Whole-exome sequencing reveals the major genetic factors contributing to neuromyelitis optica spectrum disorder in Chinese patients with aquaporin 4-IgG seropositivity. (
  • Neuromyelitis optica spectrum disorder is an autoimmune astrocytopathy of the CNS with secondary demyelination, which can be associated with a specific auto-antibody against the antigen aquaporin-4 (AQP4) in 50-90% of cases ( 4 ). (
  • Pregnancy outcomes in aquaporin-4-positive neuromyelitis optica spectrum disorder. (
  • Here, we demonstrate a new IPC compound, N-acetylglutaminoyl-S-farnesyl-L-cysteine (SIG-1191), which inhibits UVB-induced inflammation blocking pro-inflammatory cytokine interleukin-6 (IL-6) and tumor necrosis factor alpha (TNF-α) production. (
  • Bolstering the case for inflammation, a 2005 paper reported that the tear fluid of keratoconus patients contained inflammatory mediators, such as interleukin-6, tumor necrosis factor-alpha (TNF-a) and matrix mettaloproteinase-9 (MMP-9). (
  • Children aged three months to two years, who are no longer provided with maternal antibodies derived from pas- sive immunization and do not possess mature immune systems, are highly sus- Online platform Binary option cash back Sandnes Aquaporins and Water Transport in the Cornea Alan S. (
  • British Journal of Dermatology, vol.131(6): 856-861. (
  • 6. Benga G (2013) Comparative studies of water permeability of red blood cells from humans and over 30 animal species: an overview of 20 years of collaboration with Philip Kuchel. (
  • Localization and ordering of lipids around Aquaporin-0: Proteinand lipid mobility effects. (
  • While rules of Na+ homeostasis requires the orchestrated work of multiple Na+ transporters along the nephron, water IACS-9571 reabsorption across the tubular epithelium is almost entirely dependent on the activity of water channels, aquaporins (AQPs). (
  • Loonen AJ, Knoers NV, van Os CH, Deen PM. Aquaporin 2 mutations in nephrogenic diabetes insipidus. (
  • Robben JH, Knoers NV, Deen PM. Cell biological aspects of the vasopressin type-2 receptor and aquaporin 2 water channel in nephrogenic diabetes insipidus. (
  • In humans, mutations in the aquaporin-2 gene lead to hereditary nephrogenic diabetes insipidus. (
  • Aquaporin-4 and MOG autoantibody discovery in idiopathic transverse myelitis epidemiology. (
  • Characterization of aquaporin-6 as a nitrate channel in mammalian cells. (
  • Aquaporin-4 (Aqp4), an astrocytic transmembrane water channel, is an important molecular contributor to cerebral edema formation. (
  • J.BADAUT, S. ASHWAL, A ADAMI, B TONE, B RECKER, B TERNON, A. OBENAUS (2010) Brain water mobility decreases after astrocytic aquaporin-4 inhibition using RNA interference. (
  • Aquaporin 11 insufficiency modulates kidney susceptibility to oxidative stress. (
  • Patients in the rituximab group were treated with 100 mg on day 1, followed by 500 mg on day 2, continuing at that dose every 6 months. (
  • 4-6 Patients with NMO have a life-long exposure to the uncontrolled complement activation due to chronic autoimmune attack, and most patients experience an unpredictable, relapsing course of disease with cumulative disability, as each attack adds to the neurologic disability. (
  • The single nucleotide polymorphism site of aquaporin-4 gene in patients with neuromyelitis optica. (
  • 10. Bienert GP, Chaumont F (2014) Aquaporin-facilitated transmembrane diffusion of hydrogen peroxide. (
  • 11. Bienert GP, Heinen RB, Berny MC, Chaumont F (2014) Maize plasma membrane aquaporin ZmPIP2;5, but not ZmPIP1;2, facilitates transmembrane diffusion of hydrogen peroxide. (
  • Aquaporin-4 (Aqp4) is a passive transmembrane water channel that in the central nervous system (CNS) is exclusively expressed by astrocytes, and is an important molecular contributor to cerebral edema formation after cerebral ischemia [ 27 - 31 ]. (
  • The amount of synthesized colored products are positively related to the analyte of interest in the sample.This human IL-6 ELISA kit has been described in up to 143 publications. (
  • The main questions it aims to answer are: Does the time to corticosteroid treatment affect the visual outcome at 6 months in subjects with acute multiple sclerosis (MS)-, aquaporin 4-IgG positive (AQP4-IgG+) and myelin-oligodendrocyte-glycoprotein-IgG positive (MOG-IgG+) ON? (
  • Agre, P. & Kozono, D. Aquaporin water channels: molecular mechanisms for human diseases. (
  • Morishita, Y., Sakube, Y., Sasaki, S. & Ishibashi, K. Molecular mechanisms and drug development in aquaporin water channel diseases: aquaporin superfamily (superaquaporins): expansion of aquaporins restricted to multicellular organisms. (
  • Dysregulated IL-6 has been associated with the pathogenesis of autoimmune and inflammatory diseases, metabolic abnormalities, and cancer. (
  • Targeting IL-6 has shown to be potential for the treatment of various immune-mediated diseases. (
  • In recent decades, there is an increasing interest in research on functional foods and dietary supplements for different diseases [ 3 - 6 ]. (
  • A few mutations result in the production of functional aquaporin 2 water channels, but these channels are misrouted within the cell and do not reach the cell membrane. (
  • Mutations in the gene encoding the vasopressin type-2 receptor cause the X-chromosomal form of the disease, whereas mutations in the gene encoding the vasopressin-dependent water channel aquaporin-2 are responsible for the autosomal recessive, and (in some cases) an autosomal dominant type of the disease. (
  • In mice, mutations in the aquaporin-0 gene lead to congenital cataracts. (
  • 6. Cellular detoxification mechanisms of arsenic compounds. (
  • More than 200 members of the aquaporin family have been found in plants, microbials, invertebrates and vertebrates, and their importance to the physiology of these organisms is being uncovered. (
  • Experimental physiology , 88 (6), 691-698. (
  • American Journal of Physiology: Cell Physiology , 321 (6), 1060-1069. (
  • Previous studies performed in the Plant Development Physiology Laboratory showed a high preference for urea by the tank-bromeliad Vriesea gigantea and its possible transport via aquaporins. (
  • An amino acid sequence from the C-terminus of human Aquaporin 6 (EPLKKESQPGSGAVEMESV) was used as the immunogen for this Aquaporin 6 antibody. (
  • 15/23210-6 - Analysis of urea assimilation in Vriesea gigantea (Bromeliaceae) plants with low urease activity: is mandatory the urea hydrolysis for its assimilation? (
  • Crystal structure of a yeast aquaporin at 1.15 angstrom reveals a novel gating mechanism. (
  • Requirement of human renal water channel aquaporin-2 for vasopressin-dependent concentration of urine. (
  • Serous-acinar cells express the tight junction marker zona occludens-1 and measurements of transepithelial electrical resistance (TEER) demonstrate exceptional tight junction formation [routinely >2000 omega(ohms)/cm2] in a relatively short period of time (6-8 days) in Transwell inserts. (
  • Water transport activity of the plasma membrane aquaporin PM28A is regulated by phosphorylation. (
  • In addition to regulating immune and inflammatory reactions, IL-6 also plays an important role in hematopoiesis, metabolism, and organ development. (
  • To assess the potential of this system as a model of reactive gliosis, astrocytes in 3D were activated with TGFbeta1 to a ramified, reactive phenotype (elevated GFAP, Aquaporin 4, CSPG, Vimentin and IL-6 secretion). (
  • This hormone triggers chemical reactions that ultimately insert aquaporin 2 water channels into the membrane of collecting duct cells. (
  • Without signals from ADH, aquaporin 2 water channels are removed from the membrane of collecting duct cells. (
  • If aquaporin 2 water channels are not inserted into the membrane of collecting duct cells, the kidneys are unable to respond to signals from ADH. (
  • prior 6-8 cells of stimulation promotes associated responsiveness which involves N-glycosylated to negatively 300 Needs of andwith per methylase. (
  • The interleukin-6 receptor inhibitor satralizumab and anti-CD19 antibody inebilizumab have published positive phase III trial results and await approval in the near future. (