Aquaporin 2. Medical search

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 2.7.1.30.

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. (1/515)

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. (2/515)

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. (3/515)

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. (4/515)

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. (5/515)

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. (6/515)

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. (7/515)

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. (8/515)

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)

Identification of phosphorylation-dependent binding partners of aquaporin-2 using protein mass spectrometry.. Zwang NA1, ... Identification of Phosphorylation-Dependent Binding Partners of Aquaporin-2 Using Protein Mass Spectrometry ... Identification of Phosphorylation-Dependent Binding Partners of Aquaporin-2 Using Protein Mass Spectrometry ... Identification of Phosphorylation-Dependent Binding Partners of Aquaporin-2 Using Protein Mass Spectrometry ...

https://www.ncbi.nlm.nih.gov/pubmed/19209902

This peptide is a fragment of the human aquaporin-2 (AQP2) phosphorylated at Ser261. Protein phosphorylation plays a key role ... This peptide is a fragment of the human aquaporin-2 (AQP2) phosphorylated at Ser261. Protein phosphorylation plays a key role ...

https://www.anaspec.com/products/product.asp?id=49016&productid=25286

aquaporin;. dDAVP,. (deamino-Cys1, d-Arg8)vasopressin;. FT,. Fourier transform;. ICR,. ion cyclotron resonance;. IMAC,. ... Quantitative phosphoproteomics of vasopressin-sensitive renal cells: Regulation of aquaporin-2 phosphorylation at two sites. ... Quantitative phosphoproteomics of vasopressin-sensitive renal cells: Regulation of aquaporin-2 phosphorylation at two sites ... Quantitative phosphoproteomics of vasopressin-sensitive renal cells: Regulation of aquaporin-2 phosphorylation at two sites ...

https://www.pnas.org/content/103/18/7159?ijkey=510a25f555dac0731ee161a7c3e559a606c7b5de&keytype2=tf_ipsecsha

Aquaporin 1 splice variant 2Imported. ,p>Information which has been imported from another database using automatic procedures ... Belongs to the MIP/aquaporin (TC 1.A.8) family. [View classification]SAAS annotation. Automatic assertion according to rulesi ... tr,Q6JSD8,Q6JSD8_HUMAN Aquaporin 1 splice variant 2 (Fragment) OS=Homo sapiens OX=9606 GN=AQP1 PE=2 SV=1 ...

https://www.uniprot.org/uniprot/Q6JSD8

Invitrogen Anti-Aquaporin 2 Polyclonal, Catalog # PA5-78808. Tested in Western Blot (WB), Immunohistochemistry (Frozen) (IHC (F ... Aquaporin-CD; Collecting duct water channel protein; Water channel protein for renal collecting duct; water-channel aquaporin 2 ... Cite Aquaporin 2 Polyclonal Antibody. The following antibody was used in this experiment: Aquaporin 2 Polyclonal Antibody from ... Sample was incubated with Aquaporin 2 polyclonal antibody (Product# PA5-78808).. Western blot analysis of Aquaporin 2 in Lane 1 ...

https://www.thermofisher.com/antibody/product/Aquaporin-2-Antibody-Polyclonal/PA5-78808

Invitrogen Anti-Aquaporin 2 Polyclonal, Catalog # PA5-22865. Tested in Western Blot (WB), Immunofluorescence (IF), ... Host server : magellan-srch-2-prod-blue:8080/10.253.226.81:8080. git-commit: 01b04f9b241f51a560e30d6fc4026e5d4b4f8977 git-url: ...

https://www.thermofisher.com/antibody/product/Aquaporin-2-Antibody-Polyclonal/PA5-22865

Mutations in the aquaporin-2 (AQP2) water channel cause the hereditary renal disease nephrogenic diabetes insipidus (NDI). The ... Diffusion in the endoplasmic reticulum of an aquaporin-2 mutant causing human nephrogenic diabetes insipidus.. Levin MH1, ... ATP depletion by 2-deoxyglucose and azide resulted in comparable slowing/immobilization of wild-type and T126M AQP2. These ... AQP2 translational diffusion in the ER was not slowed by the T126M mutation; diffusion coefficients were (in cm(2)/s x 10(-)10 ...

https://www.ncbi.nlm.nih.gov/pubmed/11297561

In Arabidopsis thaliana, mRNA levels of one of the aquaporin genes, TIP2;2, increase during dark adaptation and decrease under ... Numerous studies have described the light regulation of aquaporin genes, but none have identified the regulatory mechanisms ... Fluorescence of TIP2;2-GFP protein in the endodermis of roots in the wild-type seedlings increased during dark adaptation, but ... In this paper, we focus on the role of phytochrome A (phyA) signaling in the regulation of the TIP2;2 protein. We generated ...

http://mdpi.com/2223-7747/3/1/177/xml

Urine aquaporin-2 has recently been demonstrated as a promising predictor of response to tolvaptan. We here validated aquaporin ... Long-term efficacy of tolvaptan treatment in the responders defined by aquaporin-2 needs to be validated in the future ... a member of the aquaporin family, is an arginine vasopressin-regulated water channel expressed in the renal collecting duct, ... The arginine vasopressin type-2 antagonist, tolvaptan, is a new-generation diuretic; it is especially indicated in patients ...

https://www.mdpi.com/1422-0067/17/1/105

Recently, mutations in the autosomal gene coding for water-channel aquaporin 2 (AQP2) of the renal collecting duct … ... Patients with autosomal nephrogenic diabetes insipidus homozygous for mutations in the aquaporin 2 water-channel gene Am J Hum ... In the present study, missense mutations and a single nucleotide deletion in the aquaporin 2 gene of three NDI patients from ... Recently, mutations in the autosomal gene coding for water-channel aquaporin 2 (AQP2) of the renal collecting duct were ...

https://pubmed.ncbi.nlm.nih.gov/7524315/?dopt=Abstract

In mammals six different aquaporins have been identified up to now, four of which (aquaporin-1 to aquaporin-4) are expressed in ... Because of its importance for normal water homeostasis and its involvement in many water balance disorders, aquaporin-2, the ... Aquaporins are integral membrane proteins, which function as specialized water channels to facilitate the passage of water ... In mammals six different aquaporins have been identified up to now, four of which (aquaporin-1 to aquaporin-4) are expressed in ...

http://www.ndif.org/articles/436-Physiology_and_Pathophysiology_of_the_Aquaporin2_Water_Channel/translation

... ...

http://dare.uva.nl/search?metis.record.id=131364

Fluconazole increases osmotic water transport in renal collecting duct through effects on aquaporin-2 trafficking View in MDC ... binding to vasopressin V2 receptors promotes redistribution of the water channel aquaporin-2 (AQP2) from intracellular vesicles ...

https://www.mdc-berlin.de/research/publications/fluconazole-increases-osmotic-water-transport-renal-collecting-duct-through

... and the aquaporin 2 (AQP2) signaling pathway in the inner ear play important roles in hearing and balance functions through ... aquaporin 2 signaling pathway was potentially involved in the development of motion sickness and that blocking V2R with ... In the present study our results showed that activation of the inner ear arginine vasopressin-vaspopressin receptor 2 (V2R)- ... Inner Ear Arginine Vasopressin-Vasopressin Receptor 2-Aquaporin 2 Signaling Pathway Is Involved in the Induction of Motion ...

https://jpet.aspetjournals.org/content/373/2/248

Bile Acid G Protein-Coupled Membrane Receptor TGR5 Modulates Aquaporin 2-Mediated Water Homeostasis. Suchun Li, Miaojuan Qiu, ... Bile Acid G Protein-Coupled Membrane Receptor TGR5 Modulates Aquaporin 2-Mediated Water Homeostasis ... Bile Acid G Protein-Coupled Membrane Receptor TGR5 Modulates Aquaporin 2-Mediated Water Homeostasis ... Bile Acid G Protein-Coupled Membrane Receptor TGR5 Modulates Aquaporin 2-Mediated Water Homeostasis ...

https://jasn.asnjournals.org/content/29/11/2658

Aquaporin 2 antibody LS-C3796 is an unconjugated rabbit polyclonal antibody to rat Aquaporin 2 (AQP2). Validated for ELISA, IF ... Aquaporin 2 antibody LS-C3796 is an unconjugated rabbit polyclonal antibody to rat Aquaporin 2 (AQP2). Validated for ELISA, IF ... Aquaporin 2 antibody LS-C3796 is an unconjugated rabbit polyclonal antibody to rat Aquaporin 2 (AQP2). Validated for ELISA, IF ... Recognizes rat Aquaporin 2 (AQP-CD/WCH-CD). Species sequence homology: mouse: 100%; human and ovine: 93% (14/15aa; residues 257 ...

https://www.lsbio.com/antibodies/aqp2-antibody-aquaporin-2-antibody-c-terminus-elisa-if-immunofluorescence-ihc-wb-western-ls-c3796/4537

... also called AQUAPORIN-CD, is found in the apical cell membranes of the kidneys collecting duct principal cells and in ... AQP2 (Aquaporin 2), also called AQUAPORIN-CD, is found in the apical cell membranes of the kidneys collecting duct principal ... Product information "Anti-AQP2 / Aquaporin 2" 0.5mg/ml if reconstituted with 0.2ml sterile DI water. ... Amino acids EPDTDWEEREVRRRQSVELHSPQSLPRGTKA of human Aquaporin 2 were used as the immunogen for the Aquaporin 2 antibody.. ...

https://www.biomol.com/products/antibodies/primary-antibodies/general/anti-aqp2/aquaporin-2-nsj-r32091

Thread: Are aquaporin 4 antibodies appear in any other context than Devics syndrom? ... Are aquaporin 4 antibodies appear in any other context than Devics syndrom? ... I imagine it would be easier if there was at least a single good thing to look forward but there is nothing.[SIZE=2][/SIZE] ... She was released from the hospital yesterday where she got taken because of the rash from carbamazepin.[SIZE=2][/SIZE] ...

https://msworld.org/forum/showthread.php?141520-Are-aquaporin-4-antibodies-appear-in-any-other-context-than-Devic-s-syndrom&s=0716e3392ebd321ad9ab460712967540&p=1500278

Rabbit pAb Anti-Aquaporin 2 (254-271), rabbit polyclonal, recognizes the ~40 and ~29 kDa forms of aquaporin-2 in rat kidney ... Anti-Aquaporin 2 (254-271) Rabbit pAb MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other ... Anti-Aquaporin 2 (254-271), rabbit polyclonal, recognizes the ~40 and ~29 kDa forms of aquaporin-2 in rat kidney membrane. ... Detection of rat aquaporin 2 by immunoblotting. Samples: Rat kidney membranes (lane 1) and preincubated with a control peptide ...

https://www.merckmillipore.com/ID/id/product/Anti-Aquaporin-2-254-271-Rabbit-pAb,EMD_BIO-178612

Dual Effects of Hypertonicity on Aquaporin-2 Expression in Cultured Renal Collecting Duct Principal Cells. Udo Hasler, Manlio ... Dual Effects of Hypertonicity on Aquaporin-2 Expression in Cultured Renal Collecting Duct Principal Cells ... Dual Effects of Hypertonicity on Aquaporin-2 Expression in Cultured Renal Collecting Duct Principal Cells ... Dual Effects of Hypertonicity on Aquaporin-2 Expression in Cultured Renal Collecting Duct Principal Cells ...

https://jasn.asnjournals.org/content/16/6/1571/tab-article-info

Ménières Disease Pathophysiology: Endolymphatic Sac Immunohistochemical Study of Aquaporin-2, V2R Vasopressin Receptor, NKCC2 ... Ménières Disease Pathophysiology: Endolymphatic Sac Immunohistochemical Study of Aquaporin-2, V2R Vasopressin Receptor, NKCC2 ... aquaporin-2 (AQP2), vasopressin receptor V2R, sodium potassium chloride cotransporter 2 (NKCC2), and transient receptor ...

https://www.iric.ca/fr/recherche/publications/meniere-s-disease-pathophysiology-endolymphatic-sac-immunohistochemical-study-of-aquaporin-2-v2r-vasopressin-receptor-nkcc2-and-trpv4

Central to its antidiuretic action in mammals is the redistribution of the water channel aquaporin 2 (AQP2) from intracellular ... a peptide corresponding to the alpha subunits of Gi1/2 was much less potent. Thus a member of the Gi family, most likely Gi3, ... Aquaporin-2 is a water-transporting protein located in the principal cells of the kidney collecting duct. Its function is to ... aquaporin 2 DEFINITION: Also called WCH-CD, this water channel makes the principal cells of the inner medullary collecting duct ...

http://www.ndif.org/articles/22-A_Heterotrimeric_G_Protein_of_the_Gi_Family_is_Required_for_cAMPtriggered_Trafficking_of_Aquaporin_2_in_Kidney_Epithelial_Cells/body

We show here that primary cultures of rat inner medullary collecting duct (IMCD) cells retain AQP-2 expression for at least 6 ... We also found that coating the culture dishes with type IV collagen, rather than rat-tail collagen, retards AQP-2 ... Our data show that cAMP supplementation is sufficient for the maintenance of AQP-2 expression in primary cultured cells. The ... Immunofluorescence and biochemical studies indicate a shuttling of AQP-2-bearing vesicles after stimulation with vasopressin or ...

https://www.semanticscholar.org/paper/Aquaporin-2-expression-in-primary-cultured-rat-duct-Maric-Oksche/8e9808180dcbc58e250e6602e9bdded7250f7667

However, chronic treatment with lithium induces numerous kidney-related side effects, such as dramatically reduced aquaporin 2 ... Proteomic analysis of lithium-induced nephrogenic diabetes insipidus: Mechanisms for aquaporin 2 down-regulation and cellular ... After 1 or 2 weeks of lithium treatment, we identified 6 and 74 proteins with altered abundance compared with controls, ... As a model system, inner medullary collecting ducts (IMCD) isolated from rats treated with lithium for either 1 or 2 weeks were ...

https://jscholarship.library.jhu.edu/handle/1774.2/33885

... namely aquaporin-2 (AQP2) and the vasopressin-regulated urea transporter (VRUT). Both are present in intracellular vesicles as ... Acute and chronic metabolic acidosis interferes with aquaporin-2 translocation in the rat kidney collecting ducts. Tomohiko ... Vasopressin regulates apical targeting of aquaporin-2 but not of UT1 urea transporter in renal collecting duct.. @article{ ... In the renal inner medullary collecting duct (IMCD), vasopressin regulates two key transporters, namely aquaporin-2 (AQP2) and ...

https://www.semanticscholar.org/paper/Vasopressin-regulates-apical-targeting-of-but-not-Inoue-Terris/b090283a4680976db196a9679d876ee9edc4ee11

Aquaporin 2 (Ser269) Antibody. Catalog #: p112-269 Category: Signal Transduction Datasheet: Be the first to review this product ... Aquaporin 2 (Ser261) Antibody. Catalog #:. p112-261. Applications: WB IHC IP ICC Formulation: Affinity Purified from Pooled ... Aquaporin 2 (Ser264) Antibody. Catalog #:. p112-264. Applications: WB IHC Formulation: Affinity Purified from Pooled Serum. ... 2017 Aquaporin-2 Ser-261 phosphorylation is regulated in combination with Ser-256 and Ser-269 phosphorylation. Biochemical and ...

https://www.phosphosolutions.com/shop/aquaporin-2-ser269-antibody/

Aquaporin-2 levels in vitro and in vivo are regulated by VACM-1, a cul 5 gene. , Cellular physiology and biochemistry : ... Aquaporin-2 levels in vitro and in vivo are regulated by VACM-1, a cul 5 gene. Isabelle P Le Sarah Schultz Bradley T Andresen ... Aquaporin-2 levels in vitro and in vivo are regulated by VACM-1, a cul 5 gene. Cell Physiol Biochem. 2012;30(5):1148-58. ... cAMP production and subsequent translocation of water channel aquaporin-2 (AQP2) into the apical plasma membrane. We have ...

https://www.docphin.com/research/article-detail/1477221/PubMedID-23171819/Aquaporin-2-levels-in-vitro-and-in-vivo-are-regulated-by-VACM-1-a-cul-5-gene

The Intra-assay Precision is determined when 3 samples with low, middle and high level of Human Tight Junction Protein 2 (TJP2 ... The Intra-assay Precision is determined when 3 samples with low, middle and high level of Human Tight Junction Protein 2 (TJP2 ... The Intra-assay Precision is determined when 3 samples with low, middle and high level of Human Tight Junction Protein 2 (TJP2 ... The Intra-assay Precision is determined when 3 samples with low, middle and high level of Human Tight Junction Protein 2 (TJP2 ...

http://aquaporins.org/human-tjp2tight-junction-protein-2-elisa-kit/

Aquaporin-2 protein dynamics within the cell. Sasaki, Sei; Noda, Yumi Sasaki, Sei; Noda, Yumi Less ... Mechanisms of transcriptional repression by 1,25(OH)2 vitamin D. Kato, Shigeaki; Kim, Mi-sun; Yamaoka, Kazuyoshi; More ...

https://journals.lww.com/co-nephrolhypertens/toc/2007/07000

Expression of aquaporin-2 in the collecting duct and responses to tolvaptan Authors (first, second and last of 6). *Kota ...

https://www.springer.com/journal/13730

Vasopressin-mediated control of water permeability in the renal collecting duct occurs in part through regulation of the distribution of aquaporin-2 (AQP2) between the apical plasma membrane and intracellular membrane compartments. (nih.gov)
Our studies confirmed previously identified interactions between AQP2 and hsc70, hsp70-1 and -2, as well as annexin II. (nih.gov)
This peptide is a fragment of the human aquaporin-2 (AQP2) phosphorylated at Ser261. (anaspec.com)
Previously unidentified phosphorylation sites were found for membrane proteins essential to collecting duct physiology, including eight sites among aquaporin-2 (AQP2), aquaporin-4, and urea transporter isoforms A1 and A3. (pnas.org)
Aquaporin 2 (AQP2) is a hormonally regulated water channel located in the renal collecting duct. (thermofisher.com)
Mutations in the aquaporin-2 (AQP2) water channel cause the hereditary renal disease nephrogenic diabetes insipidus (NDI). (nih.gov)
ATP depletion by 2-deoxyglucose and azide resulted in comparable slowing/immobilization of wild-type and T126M AQP2. (nih.gov)
Recently, mutations in the autosomal gene coding for water-channel aquaporin 2 (AQP2) of the renal collecting duct were reported in an NDI patient. (nih.gov)
What follows in this process is not entirely clear, but it leads to water-transporting proteins called aquaporin-2 ( AQP2 proteins ) traveling from their holding place inside the CD cell to the apical membrane of the cell . (ndif.org)
At present, there is speculation that a vesicle targeting protein , VAMP-2, that has been found in the AQP2-bearing vesicles may guide the vesicles to the membrane and then bind with a protein called syntaxin-4 that is expressed in the apical membrane of CD cells . (ndif.org)
BACKGROUND: Arginine-vasopressin (AVP) binding to vasopressin V2 receptors promotes redistribution of the water channel aquaporin-2 (AQP2) from intracellular vesicles into the plasma membrane of renal collecting duct principal cells. (mdc-berlin.de)
Methods We used tubule suspensions of inner medullary collecting duct (IMCD) cells from rat kidneys to investigate the effect of TGR5 signaling on aquaporin-2 (AQP2) expression, and examined the in vivo effects of TGR5 in mice with lithium-induced nephrogenic diabetes insipidus (NDI) and Tgr5 knockout ( Tgr5 −/− ) mice. (asnjournals.org)
Aquaporin 2 antibody LS-C3796 is an unconjugated rabbit polyclonal antibody to rat Aquaporin 2 (AQP2). (lsbio.com)
AQP2 (Aquaporin 2), also called. (biomol.com)
AQP2 (Aquaporin 2), also called AQUAPORIN-CD, is found in the apical cell membranes of the kidney's collecting duct principal cells and in intracellular vesicles located throughout the cell. (biomol.com)
We identified from the literature a group of proteins expressed on the ELS and involved in endolymph volume regulation: aquaporin-2 (AQP2), vasopressin receptor V2R, sodium potassium chloride cotransporter 2 (NKCC2), and transient receptor potential cation channel V4 (TRPV4). (iric.ca)
Central to its antidiuretic action in mammals is the redistribution of the water channel aquaporin 2 ( AQP2 ) from intracellular vesicles to the apical membrane of kidney epithelial cells , an event initiated by an increase in cAMP and activation of protein kinase A . The subsequent steps of the signaling cascade are not known. (ndif.org)
When the antidiuretic hormone , arginine vasopressin ( AVP ) binds with the vasopressin-2 receptor ( V2R ) it sends a signal to AQP2 vesicles waiting in the ER to shuttle to the cell membrane so the AQP2 can be inserted in it. (ndif.org)
However, chronic treatment with lithium induces numerous kidney-related side effects, such as dramatically reduced aquaporin 2 (AQP2) abundance, altered renal function, and structural changes. (jhu.edu)
As a model system, inner medullary collecting ducts (IMCD) isolated from rats treated with lithium for either 1 or 2 weeks were subjected to differential 2D gel electrophoresis combined with mass spectrometry and bioinformatics analysis to identify (i) signaling pathways affected by lithium and (ii) unique candidate proteins for AQP2 regulation. (jhu.edu)
In the renal inner medullary collecting duct (IMCD), vasopressin regulates two key transporters, namely aquaporin-2 (AQP2) and the vasopressin-regulated urea transporter (VRUT). (semanticscholar.org)
In the renal collecting duct, vasopressin regulates water permeability by a process that involves stimulation of adenylyl cyclase activity, cAMP production and subsequent translocation of water channel aquaporin-2 (AQP2) into the apical plasma membrane. (docphin.com)
Aquaporin-2 (AQP2) is an arginine vasopressin (AVP)-regulated water channel protein localized to the apical region of renal collecting duct cells and is involved in the regulation of water permeability. (elsevier.com)
diabetes insipidus: Types and causes: …in a gene known as AQP2 (aquaporin 2), which encodes a specific form of aquaporin. (britannica.com)
Mutations in the aquaporin-2 gene (AQP2), encoding the vasopressin-regulated water channel of the renal collecting duct, are responsible for the autosomal recessive or dominant forms of congenital nephrogenic diabetes insipidus. (elsevier.com)
Lack of arginine vasopressin-induced phosphorylation of aquaporin-2 mutant AQP2-R254L explains dominant nephrogenic diabetes insipidus. (ru.nl)
Water homeostasis in humans is regulated by vasopressin, which induces the translocation of homotetrameric aquaporin-2 (AQP2) water channels from intracellular vesicles to the apical membrane of renal principal cells. (ru.nl)
Congenital nephrogenic diabetes insipidus (NDI) may result from V2R or aquaporin-2 (AQP2) mutations. (wikipedia.org)
Since the carboxyl terminus of aquaporin-2 (AQP2c) has a class I PDZ-interacting motif (X-T/S-X-Φ), the role of SNX27 in the regulation of AQP2 was studied. (au.dk)
Binding of AVP to the arginine vasopressin receptor type 2 (AVPR2) in the basolateral membrane leads to translocation of aquaporin 2 (AQP2) water channels to the apical membrane of the collecting duct principal cells, inducing water permeability of the membrane. (springer.com)
En venas y arterias , no se detectó reacción alguna de AQP2. (bvsalud.org)
En la vesícula biliar , el epitelio mucoso, las células endoteliales venosas y arteriales tuvieron una importante expresión de AQP1, sin embargo, AQP2 mostró una reacción positiva difusa menor, lo que sugiere que la AQP1 podría tener una función principal en la absorción y transporte de líquido en el sistema hepatobiliar del Lagarto Qinghai. (bvsalud.org)
We tested whether severe congestive heart\ud failure (CHF), a condition associated with excess free-water retention, is accompanied by altered regulation of the vasopressin-regulated water channel, aquaporin-2 (AQP2), in the renal collecting duct. (core.ac.uk)
Here, we describe the identification of a single base pair change in aquaporin-2 (Aqp2) in cph mutants through genetic linkage mapping. (wustl.edu)
Upon purification of the GFP-positive cells, we found that collecting duct (CD)-specific markers, including aquaporin 2 (Aqp2), an important channel for water reabsorption from urine, were abundantly expressed. (umich.edu)
We isolated total lysate and membrane proteins from the inner medulla of wild-type and mutant mouse kidneys, and found that the amounts of aquaporin 2 (AQP2), adenylyl cyclases III and V/VI, and phosphorylated MAP kinases ERK 1/2 proteins were all reduced in the inner medulla of the knockout mice. (nih.gov)
Hsp90 inhibitor partially corrects nephrogenic diabetes insipidus in a conditional knock-in mouse model of aquaporin-2 mutation Mutations in aquaporin-2 (AQP2) that interfere with its cellular processing can produce autosomal recessive nephrogenic diabetes insipidus (NDI). (tripdatabase.com)
The AQP2 gene provides instructions for making a protein called aquaporin 2. (medlineplus.gov)
Most of the known AQP2 gene mutations cause the aquaporin 2 protein to be misfolded into an incorrect 3-dimensional shape. (medlineplus.gov)
A recent study revealed that bottlenose dolphins acquired a novel isoform of aquaporin 2 generated by alternative splicing (alternative AQP2), which helps dolphins to live in hyperosmotic seawater. (bireme.br)

Identification of phosphorylation-dependent binding partners of aquaporin-2 using protein mass spectrometry. (nih.gov)
In Arabidopsis thaliana , mRNA levels of one of the aquaporin genes, TIP2;2 , increase during dark adaptation and decrease under far-red light illumination, but the effects of light at the protein level and on the mechanism of light regulation remain unknown. (mdpi.com)
In this paper, we focus on the role of phytochrome A (phyA) signaling in the regulation of the TIP2;2 protein. (mdpi.com)
We generated Arabidopsis transgenic plants expressing a TIP2;2-GFP fusion protein driven by its own promoter, and showed several differences in TIP2;2 behavior between wild type and the phyA mutant. (mdpi.com)
Fluorescence of TIP2;2-GFP protein in the endodermis of roots in the wild-type seedlings increased during dark adaptation, but not in the phyA mutant. (mdpi.com)
The amount of the TIP2;2-GFP protein in wild-type seedlings decreased rapidly under far-red light illumination, and a delay in reduction of TIP2;2-GFP was observed in the phyA mutant. (mdpi.com)
Aquaporin-2 is a water-transporting protein located in the principal cells of the kidney collecting duct . (ndif.org)
Protein kinase A phosphorylation is involved in regulated exocytosis of aquaporin-2 in transfected LLC-PK1 cells. (semanticscholar.org)
We demonstrate that members of several signaling pathways are activated by lithium treatment, including the PKB/Akt-kinase and the mitogen-activated protein kinases (MAPK), such as extracellular regulated kinase (ERK), c-Jun NH(2)-terminal kinase (JNK), and p38. (jhu.edu)
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Tight Junction Protein 2 (TJP2) in Tissue homogenates, cell lysates and other biological fluids. (aquaporins.org)
Known also as Tight Junction Protein 2 elisa. (aquaporins.org)
Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human Tight Junction Protein 2 (TJP2) in samples from Tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species. (aquaporins.org)
Here, we demonstrate that high intracellular CO 2 /HCO 3 − enhances currents mediated by the Arabidopsis thaliana guard cell S-type anion channel SLAC1 upon coexpression of any one of the Arabidopsis protein kinases OST1, CPK6, or CPK23 in Xenopus laevis oocytes. (plantcell.org)
These findings identify the CO 2 -permeable PIP2;1 as key interactor of βCA4 and demonstrate functional reconstitution of extracellular CO 2 signaling to ion channel regulation upon coexpression of PIP2;1, βCA4, SLAC1, and protein kinases. (plantcell.org)
These data further implicate SLAC1 as a bicarbonate-responsive protein contributing to CO 2 regulation of S-type anion channels. (plantcell.org)
A synthetic peptide from the n-terminal region of human Aquaporin 7 (AQP7) conjugated to an immunogenic carrier protein was used as the immunogen. (novusbio.com)
Aquaporins/major intrinsic protein (MIP) are a family of water-selective membrane channels. (novusbio.com)
Aquaporin-11: a channel protein lacking apparent transport function expressed in brain. (ebi.ac.uk)
Aquaporin 2 (Ab-256) Antibody detects endogenous levels of total Aquaporin 2 protein. (genetex.com)
Aquaporins (AQPs) are membrane protein channels that allow the rapid movement of water through epithelium . (bvsalud.org)
2. Aquaporins are protein tunnels that allow which important molecule to travel across a cell membrane? (study.com)
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. (physiology.org)
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. (physiology.org)
There are a few reports in homozygous Brattleboro rats showing that there is no change in AQP-2 protein in response to water deprivation and that 1-deamino-8- d -arginine vasopressin (dDAVP) treatment increased its expression ( 4 , 20 , 26 ). (physiology.org)
Aquaporin-1 is an integral membrane protein that is considered to have an "open" structure. (proteopedia.org)
Protein Kinase C (PKC) has been documented as a common signal transducer among the aquaporins. (proteopedia.org)
Benga G. The first discovered water channel protein, later called aquaporin 1: molecular characteristics, functions and medical implications. (proteopedia.org)
Combined immunological and proteomic approaches revealed that phosphorylation at two C-terminal sites (Ser280, Ser283) of PLASMA MEMBRANE INTRINSIC PROTEIN 2;1 ( At PIP2;1), a major plasma membrane aquaporin in rosettes, shows circadian oscillations and is correlated with K ros . (plantcell.org)

The following antibody was used in this experiment: Aquaporin 2 Polyclonal Antibody from Thermo Fisher Scientific, catalog # PA5-78808, RRID AB_2745924. (thermofisher.com)
Amino acids EPDTDWEEREVRRRQSVELHSPQSLPRGTKA of human Aquaporin 2 were used as the immunogen for the Aquaporin 2 antibody. (biomol.com)
Primary antibody: Anti-Aquaporin 2 (254-271) Rabbit pAb (Cat. (merckmillipore.com)
The antibody is a phosphopeptide corresponding to amino acid residues surrounding the phospho-Ser 269 of rat aquaporin 2. (phosphosolutions.com)
The microtiter plate provided in this kit has been pre-coated with an antibody specific to Discoidin Domain Receptor Family, Member 2 (DDR2). (aquaporins.org)
There are currently no images for Aquaporin-7 Antibody (NBP1-30862). (novusbio.com)
Immunofluorescence analysis of HeLa cells, using Aquaporin 2 (GTX87696) Antibody. (genetex.com)
Western Blot: Asialoglycoprotein Receptor 2 Antibody [NBP1-52958] - Fetal Lung tissue at a concentration of 0.5ug/ml. (novusbio.com)
Immunohistochemistry-Paraffin: Asialoglycoprotein Receptor 2 Antibody [NBP1-52958] - Human Intestine Tissue, antibody concentration 4-8ug/ml. (novusbio.com)
Immunohistochemistry: Asialoglycoprotein Receptor 2 Antibody [NBP1-52958] - Human cilia Cellular data: Epithelial cells of renal tubule Antibody Concentration: 4.0-8.0 ug/ml Magnification: 400X. (novusbio.com)

Ser-261 phospho-regulation is involved in pS256 and pS269-mediated aquaporin-2 apical translocation. (phosphosolutions.com)
In response to AVP there is an increased expression of AQP-2, its phosphorylation, and consequent translocation from intracellular vesicles to the apical membrane of the collecting duct epithelial cells ( 4 ). (pnas.org)
These studies demonstrated that vasopressin regulates phosphorylation of a cluster of four serines in the carboxy-terminal tail of aquaporin-2 as a critical step in its translocation to the cell membrane. (nih.gov)

The aquaporins (AQPs) are a family of integral membrane proteins composed of two subfamilies: the orthodox aquaporins, which transport only water, and the aquaglyceroporins, which transport glycerol, urea, or other small solutes [ PMID: 16650285 ]. (ebi.ac.uk)
Aquaporins 11 and 12 are classified as members of a new AQP subfamily: the subcellular AQPs [ PMID: 17178102 ]. (ebi.ac.uk)
Aquaporins (Aqps) are a superfamily of integral membrane proteins which generally facilitate the permeation of water through plasma membranes. (frontiersin.org)
AQP-expressing cells generally contain several thousands, or more, AQPs per μm 2 of membrane, as compared with ten or fewer ion channels per μm 2 of membrane. (biologists.org)
The aquaporins (AQPs) are small integral membrane proteins that transport water and in some cases small solutes such as glycerol. (springer.com)
Aquaporins (AQPs) are membrane proteins that form water channels, allowing rapid movement of water across cell membranes. (biologists.org)
Aquaporins (AQPs) are integral membrane proteins that form pores in the membrane of biological cells. (cosmeticsandtoiletries.com)
Aquaporins (AQPs) are water channel proteins implicated in physiological mechanisms of osmoregulation. (usda.gov)

In the present study, missense mutations and a single nucleotide deletion in the aquaporin 2 gene of three NDI patients from consanguineous matings are described. (nih.gov)
Mutations in aquaporin-2 cause diabitis insipidus. (proteopedia.org)
Mutations in aquaporin-0 in mice cause congenital cataracts. (proteopedia.org)
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. (medlineplus.gov)
Loonen AJ, Knoers NV, van Os CH, Deen PM. Aquaporin 2 mutations in nephrogenic diabetes insipidus. (medlineplus.gov)
Activating mutations on codon 12 and 13 of the k- ras gene [ 14 , 15 ], upregulation of cyclo-oxygenase 2 (COX-2), and inducible nitric oxide synthase (iNOS), as well as alterations in transforming growth factor β signaling, are also common features to both human and AOM-induced colon cancers [ 24 - 29 ]. (hindawi.com)

Much faster diffusion was found for a lipid probe (diOC(4)(3), 2.7 x 10(-)8 cm(2)/s) in the ER membrane and for unconjugated GFP in the aqueous ER lumen (6 x 10(-)8 cm(2)/s). (nih.gov)
Aquaporins are integral membrane proteins , which function as specialized water channels to facilitate the passage of water through the cell membrane . (ndif.org)
Anti-Aquaporin 2 (254-271), rabbit polyclonal, recognizes the ~40 and ~29 kDa forms of aquaporin-2 in rat kidney membrane. (merckmillipore.com)
Vasopressin-stimulated increase in phosphorylation at serine 269 potentiates plasma membrane retention of aquaporin 2. (phosphosolutions.com)
Aquaporins contain two tandem repeats, each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). (ebi.ac.uk)
Secretin promotes osmotic water transport in rat cholangiocytes by incresing aquaporin-1 water channels in plasma membrane. (wiley.com)
Aquaporins are channel producing proteins which regulate the flow of water across the cell membrane. (proteopedia.org)
Aquaporin-3 function is to promote glycerol permeability across cell membrane. (proteopedia.org)
This hormone triggers chemical reactions that ultimately insert aquaporin 2 water channels into the membrane of collecting duct cells. (medlineplus.gov)
Without signals from ADH, aquaporin 2 water channels are removed from the membrane of collecting duct cells. (medlineplus.gov)
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. (medlineplus.gov)
Alport syndrome is a hereditary progressive nephropathy characterized by lamellation and splitting of glomerular basement membrane (GBM) and associated with sensorineural defect leading to hearing loss and ocular defects (2). (ifcc.org)
This occurs through increased transcription and insertion of water channels ( Aquaporin-2 ) into the apical membrane of collecting tubule and collecting duct epithelial cells. (wikipedia.org)
1] "The Nicotiana tabacum plasma membrane aquaporin NtAQP1 is mercury-insensitive and permeable for glycerol. (tcdb.org)
Aquaporins are integral membrane proteins that specialize in the regulation of cellular water flow across the cell membrane. (proteopedia.org)
it regulates trafficking of aquaporin-2 water channels to and from the plasma membrane, and it regulates the expression of the aquaporin-2 gene in renal collecting duct cells. (nih.gov)
The Landon King Lab studies aquaporins water-specific membrane channel proteins. (hopkinsmedicine.org)

Transcriptional regulation of aquaporin-2 water channel gene by cAMP. (semanticscholar.org)
Aquaporin-2 levels in vitro and in vivo are regulated by VACM-1, a cul 5 gene. (docphin.com)
We characterized an aquaporin gene HvPIP2;5 from Hordeum vulgare and investigated its physiological roles in heterologous expression systems, yeast and Arabidopsis , under high salt and high osmotic stress conditions. (frontiersin.org)
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. (physiology.org)
Also, the 5′-flanking region of the AQP-2 gene contains cAMP-responsive element ( 27 ). (physiology.org)
AVP is known to be the important regulator of the transcription rates of the AQP-2 gene ( 10 , 17 ). (physiology.org)
However, other factors that might be involved in the regulation of AQP-2 gene expression could not be ruled out ( 5 , 16 ). (physiology.org)
Male homozygous Brattleboro rats, weighing 250-280 g, in which endogenous AVP was absent due to an inherited defect in the AVP gene ( 25 , 28 ) were used in the present experiments to examine the expression of AQP-2 mRNA in the kidneys in the presence or absence of exogenous dDAVP. (physiology.org)
Da T, Verkman AS (2004) Aquaporin-4 gene disruption in mice protects against impaired retinal function and cell death after ischemia. (springer.com)
The disease occurs at a gene frequency of 1/5000 and is transmitted in most families as X-linked dominant trait (2). (ifcc.org)
Vasopressin, acting through cAMP, also increases transcription of the aquaporin-2 gene, thus increasing the total number of aquaporin-2 molecules in collecting duct cells. (wikipedia.org)
We recently characterized an intracellular isoform of matrix metalloproteinase-2 (MMP-2) induced by oxidative stress-mediated activation of an alternate promoter in the first intron of the MMP-2 gene. (medworm.com)
We demonstrate in this study the pattern of expression of aquaporin 2, a newly identified gene of R. microplus tick. (usda.gov)

Diffusion in the endoplasmic reticulum of an aquaporin-2 mutant causing human nephrogenic diabetes insipidus. (nih.gov)
Shalev H, Romanovsky I, Knoers NV, Lupa S, Landau D (2004) Bladder function impairment in aquaporin-2 defective nephrogenic diabetes insipidus. (springer.com)
We studied the mechanisms of these urine concentration defects by treating wild-type and AT(1a)-knockout mice with arginine vasopressin (AVP) for 2 weeks, controlling their water intake, or giving them an osmotic diuretic (sucrose) in order to determine whether central or nephrogenic mechanisms were involved. (nih.gov)
Lithium (Li)-induced nephrogenic diabetes insipidus (NDI) has been attributed to the increased production of renal prostaglandin (PG)E(2). (tripdatabase.com)
Robben JH, Knoers NV, Deen PM. Cell biological aspects of the vasopressin type-2 receptor and aquaporin 2 water channel in nephrogenic diabetes insipidus. (medlineplus.gov)

PIP2;1 exhibited CO 2 permeability. (plantcell.org)
An inactive PIP2;1 point mutation was identified that abrogated water and CO 2 permeability and extracellular CO 2 regulation of SLAC1 activity. (plantcell.org)
Chou CL, Ma T, Yang B, Knepper MA, Verkman AS (1998) Fourfold reduction of water permeability in inner medullary collecting duct of aquaporin-4 knockout mice. (springer.com)
Chou CL, Knepper MA, Hoek AN, Brown D, Yang B, Ma T, Verkman AS (1999) Reduced water permeability and altered ultrastructure in thin descending limb of Henle in aquaporin-1 null mice. (springer.com)

Phosphorylation of serine 256 is required for cAMP-dependent regulatory exocytosis of the aquaporin-2 water channel. (semanticscholar.org)
Aquaporin-2 Ser-261 phosphorylation is regulated in combination with Ser-256 and Ser-269 phosphorylation. (phosphosolutions.com)
The role of putative phosphorylation sites in the targeting and shuttling of the aquaporin-2 water channel. (physiomics.eu)
Transgenic expression of phosphodeficient and phosphomimetic forms of this aquaporin indicated that At PIP2;1 phosphorylation is necessary but not sufficient for K ros regulation. (plantcell.org)

OBJECTIVE To evaluate trends in urine aquaporin-1 (AQP1) and perilipin 2 (PLIN2) concentrations in sufferers with very clear cell and papillary renal cell carcinoma (RCC) this analysis determined the partnership between your urine concentration of the biomarkers and tumor size, stage and grade. (medicalconsultingcenter.com)
En el hígado , la inmunohistoquímica mostró que AQP1 tiene una reacción intensa en el lóbulo hepático, células de Kupffer , hepatocitos , tracto portal e islotes sanguíneos. (bvsalud.org)
Aquaporin-1 (AQP1) was first discovered in human red blood cell membranes by Gheorghe Benga's research group in 1986. (proteopedia.org)
AQP1 is formed as a tetramer in vivo , with each AQP1 monomer unit capable of transportation at a rate of ~2 trillion water molecules per second. (proteopedia.org)

Aquaporin-2, a member of the aquaporin family, is an arginine vasopressin-regulated water channel expressed in the renal collecting duct, and a promising marker of the concentrating and diluting ability of the kidney. (mdpi.com)
In order for the kidney to be able to reabsorb body water flowing through its collecting ducts (CDs), the following molecular sequence must take place: The antidiuretic hormone , arginine vasopressin ( AVP ) must bind with the vasopressin-2 receptor ( V2R ) located in the basolateral membranes of the principal cells of the kidney CDs. (ndif.org)
We describe two new families with normal hypotensive and coagulation responses following the administration of desamino-8-D-arginine AVP, a clinical suggestion of normal vasopressin-2 receptors. (elsevier.com)
Arginine vasopressin (AVP) plays an important role in the expression of aquaporin (AQP-2) in the collecting duct. (physiology.org)

Numerous studies have described the light regulation of aquaporin genes, but none have identified the regulatory mechanisms behind this regulation via specific photoreceptor signaling. (mdpi.com)
Aquaporin-4 (AQP4) is implicated in a number of physiopathological processes, particularly in the development of brain edema, and other functions such as the regulation of extracellular space volume, potassium buffering, waste clearance, and calcium signaling. (bioportfolio.com)
In the present study, we further examined whether there is an AVP-independent regulation of AQP-2 mRNA expression by using the homozygous Brattleboro rats. (physiology.org)
Regulation of aquaporin-2gene transcription by gate-3. (nii.ac.jp)
Aquaporin channels may be subject to intense short term regulation via signal transduction. (proteopedia.org)

Ménière's Disease Pathophysiology: Endolymphatic Sac Immunohistochemical Study of Aquaporin-2, V2R Vasopressin Receptor, NKCC2, and TRPV4. (iric.ca)
Known also as Discoidin Domain Receptor Family, Member 2 elisa. (aquaporins.org)
Description: A sandwich ELISA kit for detection of Discoidin Domain Receptor Family, Member 2 from Human in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (aquaporins.org)
Previously we reported that extracellular nucleotides (ATP/UTP), acting through P(2y2) receptor in rat medullary collecting duct (mCD), produce and release PGE(2). (tripdatabase.com)
Similar to other tetraspanins, CD9 generally does not function as a cell-surface receptor, but rather as an organizer of multimolecular complexes, including integrins, immunoglobulin superfamily members such as EWI-F and EWI-2, heparin-binding EGF-like growth factor, claudin-1, and other tetraspanins [ 10 ]. (nature.com)
Synthetic peptides corresponding to ASGR2 (asialoglycoprotein receptor 2) The peptide sequence was selected from the N terminal of ASGR2. (novusbio.com)

After 1 or 2 weeks of lithium treatment, we identified 6 and 74 proteins with altered abundance compared with controls, respectively. (jhu.edu)
AQP11 is functionally distinct from other proteins of the aquaporin superfamily and could represent a new aquaporin subfamily [ PMID: 16650285 ]. (ebi.ac.uk)
Aquaporins belong to major intrinsic proteins (MIPs) that are present from prokaryotes to plants and animals. (frontiersin.org)
In the 1990s, he carried out seminal studies on aquaporins, a family of water channel proteins. (nih.gov)

Congestive heart failure in rats is associated with increased expression and targeting of aquaporin-2 water channel in collecting duct. (semanticscholar.org)

In addition, the proline biosynthesis genes, Δ 1 -Pyrroline-5-Carboxylate Synthase 1 and 2 ( P5CS1 and P5CS2 ) were up-regulated in HvPIP2;5 overexpressing plants under salt and osmotic stresses, which coincided with increased levels of the osmoprotectant proline. (frontiersin.org)
5] "Identification of 33 rice aquaporin genes and analysis of their expression and function. (tcdb.org)

Aquaporin-2 expression in primary cultured rat inner medullary collecting duct cells. (semanticscholar.org)
These results indicate the lack of an AVP-independent mechanism for upregulating AQP-2 mRNA expression in renal collecting duct cells. (physiology.org)

In mammals six different aquaporins have been identified up to now, four of which ( aquaporin-1 to aquaporin-4 ) are expressed in the kidney . (ndif.org)
Samples: Rat kidney membranes (lane 1) and preincubated with a control peptide antigen (lane 2). (merckmillipore.com)
Aquaporin-2 transfection of Madin-Darby canine kidney cells reconstitutes vasopressin-regulated transcellular osmotic water transport. (semanticscholar.org)
The 17 kDa band identified by multiple anti-aquaporin 2 antisera in rat kidney medulla is a histone. (semanticscholar.org)
Keywords: Kidney Tumor, Urine Biomarkers, Aquaporin-1, Perilipin 2 Launch Renal cell carcinoma (RCC) may be the most lethal urologic malignancy1 and buy SB-742457 there's been a reliable rise in its occurrence1C5. (medicalconsultingcenter.com)
Marples D, Christensen S, Christensen EI, Ottosen PD, Nielsen S (1995) Lithium-induced downregulation of aquaporin-2 water channel expression in rat kidney medulla. (springer.com)
Kidney Int . 2009 Jul;76(2):169-77. (nih.gov)
The persistent high urine volume after AVP administration was traced to a reduction in aquaporin-1 expression in the kidney of LXRβ −/− mice. (pnas.org)
Aquaporin-2 function is to reabsorb water from urine in the kidney. (proteopedia.org)
We recently cloned cDNA of the apical collecting duct water channel, aquaporin-2 (AQP-2), from rat and human kidney cDNA libraries ( 8 , 24 ). (physiology.org)
An Intracellular Matrix Metalloproteinase-2 Isoform Induces Tubular Regulated Necrosis: Implications for Acute Kidney Injury. (medworm.com)

Mutation of PIP2;1 in planta alone was insufficient to impair CO 2 - and abscisic acid-induced stomatal closing, likely due to redundancy. (plantcell.org)

Cultured renal epithelial cells rapidly downregulate expression of the vasopressin-regulated water channel aquaporin-2 (AQP-2). (semanticscholar.org)

Urine aquaporin-2 has recently been demonstrated as a promising predictor of response to tolvaptan. (mdpi.com)
metabolism was detected in blood, urine, bile and hepatocytes by means of the detection of [ 35 S]-SO 4 2- ions. (tripdatabase.com)
[12] Aquaporins allow water to move down their osmotic gradient and out of the nephron, increasing the amount of water re-absorbed from the filtrate (forming urine) back into the bloodstream. (wikipedia.org)

Extensive research on the function of aquaporins have been implemented into many separate types of cell membranes. (proteopedia.org)

AQP 11 and 12 appear to be more distantly related to the other mammalian aquaporins and aquaglyceroporins. (ebi.ac.uk)

Are aquaporin 4 antibodies appear in any other context than Devic's syndrom? (msworld.org)
Maintain the lyophilised/reconstituted antibodies frozen at -20°C for long term storage and refrigerated at 2-8°C for a shorter term. (osenses.com)
Polysomnography is useful in patients with antibodies that are associated with sleep disorders, including those with the following antibodies CASPR2, DPPX, IgLON5, anti-Ma2, AQP4, and ANNA-2 antibodies. (medscape.com)

Vasopressin regulates apical targeting of aquaporin-2 but not of UT1 urea transporter in renal collecting duct. (semanticscholar.org)
Aquaporin 7 facilitates water, glycerol and urea transport. (novusbio.com)
A subgroup of aquaporins called aquaglycerporins allow the passage of small solutes such as glycerol, urea, and ammonia. (proteopedia.org)

Molecular evolution of mammalian aquaporin-2. (uva.nl)
Thus V1R and/or V2R antagonists may serve as molecular chaperones to mitigate misfolding defects in selected patients with type 2 NDI. (wikipedia.org)
Agre P, Kozono D. Aquaporin water channels: molecular mechanisms for human diseases. (proteopedia.org)

Light regulates the expression and function of aquaporins, which are involved in water and solute transport. (mdpi.com)

Aquaporin 7 has greater sequence similarity with AQP3 and AQP9 and they may be a subfamily. (novusbio.com)

The circadian fluctuations in aquaporin transcript abundance suggest that aquaporin water channels play a role in these processes. (plantcell.org)

Aquaporin 7 and AQP3 are at the same chromosomal location suggesting that 9p13 may be a site of an aquaporin cluster. (novusbio.com)

GATA2 regulates body water homeostasis through maintaining aquaporin 2 expression in renal collecting ducts. (umich.edu)

Dark respiration causes an increase in leaf CO 2 concentration ( Ci ), and the continuing increases in atmospheric [CO 2 ] further increases Ci . (plantcell.org)
Elevated leaf CO 2 concentration causes stomatal pores to close. (plantcell.org)
Furthermore, the continuing increase in the atmospheric CO 2 concentration also causes an increase in Ci . (plantcell.org)

[3] This process is vital for any living organism to sustain proper physiological conditions and aquaporins are necessary to sustain this process (i.e. osmosis alone could not provide a sufficient flow of water). (proteopedia.org)

It has long been known that dietary patterns modulate the incidence and mortality of colorectal cancer [ 2 , 3 ], however, identification of specific mechanisms has been limited. (hindawi.com)

We show here that primary cultures of rat inner medullary collecting duct (IMCD) cells retain AQP-2 expression for at least 6 days when grown with dibutyryl cAMP (DBcAMP) supplementation. (semanticscholar.org)

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. (physiology.org)
The expression of AQP-2 mRNA is increased by exogenous and endogenous AVP in various pathophysiological conditions ( 1 , 7 , 18 , 30 ). (physiology.org)
The enhanced expression of AQP-2 mRNA is abolished by the presence of an antidiuretic AVP antagonist ( 7 , 9 , 30 ) or an acute water load that causes a reduction in plasma AVP levels ( 22 ). (physiology.org)

A synthetic peptide corresponding to a sequence at the C-terminus of human Aquaporin 2. (thermofisher.com)
The antiserum was produced against synthesized peptide derived from human Aquaporin 2. (genetex.com)

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Long-term regulation of aquaporins in the kidney. (1/515)

Vasopressin regulates apical targeting of aquaporin-2 but not of UT1 urea transporter in renal collecting duct. (2/515)

An impaired routing of wild-type aquaporin-2 after tetramerization with an aquaporin-2 mutant explains dominant nephrogenic diabetes insipidus. (3/515)

Aquaporin-6: An intracellular vesicle water channel protein in renal epithelia. (4/515)

The Cre/loxP system and gene targeting in the kidney. (5/515)

Urinary excretion of aquaporin-2 in rat is mediated by a vasopressin-dependent apical pathway. (6/515)

Effects of missense mutations on rat aquaporin-2 in LLC-PK1 porcine kidney cells. (7/515)

Lack of vasopressin-independent upregulation of AQP-2 gene expression in homozygous Brattleboro rats. (8/515)

No images available that match "aquaporin 2"

Aquaporin 1

Aquaporin 5

Aquaporin 3

Aquaporin 4

Aquaporins

Aquaporin 2

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Water

Mercuric Chloride

Osmosis

Aquaglyceroporins

Blood Group Antigens

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Plant Transpiration

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Diabetes Insipidus, Nephrogenic

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