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.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

TY - JOUR. T1 - Decreased lipases and fatty acid and glycerol transporter could explain reduced fat in diabetic morbidly obese. AU - Ferrer, Roser. AU - Pardina, Eva. AU - Rossell, Joana. AU - Baena-Fustegueras, Juan Antonio. AU - Lecube, Albert. AU - Balibrea, José María. AU - Caubet, Enric. AU - González, Oscar. AU - Vilallonga, Ramón. AU - Fort, Jose Manuel. AU - Peinado-Onsurbe, Julia. PY - 2014/1/1. Y1 - 2014/1/1. N2 - © 2014 The Obesity Society. Objective: The possible differences were investigated in 32 morbidly obese patients depending on whether they were healthy or had dyslipidemia and/or type 2 diabetes. Methods: Lipid metabolism and insulin resistance were analyzed in subcutaneous (SAT) and visceral adipose tissue (VAT) before and during 6 and 12 months after Roux-en-Y gastric bypass. Results: Significant differences have been found in lipoprotein lipase (LPL) and hormone-sensitive lipase (HSL) activities in SAT from the different obese group versus normal weight (control) but ...
Aquaglyceroporins-aquaporin membrane channels (AQP) that conduct glycerol and other small neutral solutes in addition to water-play major roles in obesity. In adipocytes, aquaglyceroporins mediate glycerol uptake and release across the plasma membrane, which are two key steps for triacylglycerols (TAGs) synthesis (lipogenesis) and hydrolysis (lipolysis). The aim of this study was to assess both glycerol permeability and metabolism in undifferentiated 3T3-L1 cells (UDCs) as well as in untreated (CTL-DCs) versus lipopolysaccharide (LPS-DCs)-treated differentiated 3T3-L1 adipocytes. Glycerol release, TAGs content and whole membrane glycerol permeability were significantly increased in DCs as compared to UDCs. Moreover, in DCs, LPS treatment significantly increased TAGs content and decreased glycerol permeability. In addition, a significant reduction in whole membrane glycerol permeability was observed in LPS-DCs as compared to CTL-DCs. The relative contributions of AQP3, AQP7 and AQP9 (facilitated
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Background Water channel required to promote glycerol permeability and water transport across cell membranes. May contribute to water transport in the upper portion of small intestine. Isoform 2 is not permeable to urea and...
Glycerol-3-phosphate ABC transporter, permease protein UgpA (TC 3.A.1.1.3; K17321 glycerol transport system substrate-binding ...
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 ...
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Aquaporin 4 is found in the basolateral cell membrane of principal collecting duct cells and provide a pathway for water to exit these cells. AQP4 is constitutively expressed. AQP4 is expressed in astrocytes and are upregulated by direct insult to the central nervous system. ...
TY - JOUR. T1 - Aquaporin water channels - From atomic structure to clinical medicine. AU - Agre, Peter. AU - King, Landon S.. AU - Yasui, Masato. AU - Guggino, Wm B.. AU - Ottersen, Ole Petter. AU - Fujiyoshi, Yoshinori. AU - Engel, Andreas. AU - Nielsen, Søren. PY - 2002/7/1. Y1 - 2002/7/1. N2 - 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. AQP1 is selectively permeated by water driven by osmotic gradients. The atomic structure of human AQP1 has recently been defined. Each subunit of the tetramer contains an individual aqueous pore that permits single-file passage of water molecules but interrupts the hydrogen bonding needed for passage of protons. At least 10 mammalian aquaporins have been identified, and these are selectively permeated by water (aquaporins) or water plus glycerol (aquaglyceroporins). The sites of expression ...
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, ...
Transmembrane glycerol transport is an ancient biophysical property that evolved in selected subfamilies of water channel (aquaporin) proteins. Here, we conducted broad level genome (,550) and transcriptome (,300) analyses to unravel the duplication history of the glycerol-transporting channels (glps) in Deuterostomia. We found that tandem duplication (TD) was the major mechanism of gene expansion in echinoderms and hemichordates, which, together with whole genome duplications (WGD) in the chordate lineage, continued to shape the genomic repertoires in craniates. Molecular phylogenies indicated that aqp3-like and aqp13-like channels were the probable stem subfamilies in craniates, with WGD generating aqp9 and aqp10 in gnathostomes but aqp7 arising through TD in Osteichthyes. We uncovered separate examples of gene translocations, gene conversion, and concerted evolution in humans, teleosts, and starfishes, with DNA transposons the likely drivers of gene rearrangements in paleotetraploid ...
Semantic Scholar extracted view of Aquaporin water channels in liver: their significance in bile formation. by Raúl Alberto Marinelli et al.
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 ...
We recently demonstrated that the aquaglyceroporins (AQGPs) could act as potent transporters for orthosilicic acid (H4SiO4). Although interesting, this finding raised the question of whether water and H4SiO4, the transportable form of Si, permeate AQGPs by interacting with the same region of the pore, especially in view of the difference in molecular radius between the two substrates. Here, our goal was to identify residues that endow the AQGPs with the ability to facilitate Si diffusion by examining the transport characteristics of mutants in which residues were interchanged between a water-permeable but Si-impermeable channel (aquaporin 1 [AQP1]) and a Si-permeable but water-impermeable channel (AQP10). Our results indicate that the composition of the arginine filter (XX/R), known to include three residues that play an important role in water transport, may also be involved in Si selectivity. Interchanging the identities of the nonarginine residues within this filter causes Si transport to ...
Resveratrol and gallic acid were co-loaded in phospholipid vesicles aiming at protecting the skin from external injuries, such as oxidative stress and microbial infections. Liposomes were prepared using biocompatible phospholipids dispersed in water. To improve vesicle stability and applicability, the phospholipids and the phenols were dispersed in water/propylene glycol or water/glycerol, thus obtaining PEVs and glycerosomes, respectively. The vesicles were characterized by size, morphology, physical stability, and their therapeutic efficacy was investigated in vitro. The vesicles were spherical, unilamellar and small in size: liposomes and glycerosomes were around 70 nm in diameter, while PEVs were larger (∼170 nm). The presence of propylene glycol or glycerol increased the viscosity of the vesicle systems, positively affecting their stability. The ability of the vesicles to promote the accumulation of the phenols (especially gallic acid) in the skin was demonstrated, as well as their ...
Aquaporin 1: Aquaporin 1 forms a water-specific channel that is constitutively expressed at the PLASMA MEMBRANE of ERYTHROCYTES and KIDNEY TUBULES, PROXIMAL. It provides these cells with a high permeability to WATER. In humans polymorphisms of this protein result in the Colton blood group antigen.
Aquaporin A/S is a global cleantech company located in Kongens Lyngby, Denmark. Aquaporin is dedicated to revolutionizing water purification through the use of industrial biotechn
Aquaporin 8 (AQP8) is a water channel protein. Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). Aquaporin 8 mRNA is found in pancreas and colon but not other tissues. [provided by RefSeq, Jul 2008 ...
Plasma Membrane Abundance of Human Aquaporin 5 Is Dynamically Regulated by Multiple Pathways. . 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.
The researchers showed that this technique was successful in monitoring gene expression in a brain tumor in mice. After implanting the tumor, they gave the mice a drug to trigger the tumor cells to express the aquaporin reporter gene, which made the tumor look darker in MRI images.. Overexpression of aquaporin has no negative impact on cells because it is exclusive to water and simply allows the molecules to go back and forth across the cell membrane, Shapiro says. Under normal physiological conditions the number of water molecules entering and exiting an aquaporin-expressing cell is the same, so that the total amount of water in each cell does not change. Aquaporin is a very convenient way to genetically change the way that cells look under MRI.. Though the work was done in mice, it has the potential for clinical translation, according to Shapiro. Aquaporin is a naturally occurring gene and will not cause an immune reaction. Previously developed reporter genes for MRI have been much more ...
C. elegans AQP-4 protein; contains similarity to Pfam domain PF00230 (Major intrinsic protein)contains similarity to Interpro domains IPR000425 (Major intrinsic protein), IPR012269 (Aquaporin ...
collections, groups of modules structured into books or course notes, or for other uses. Our open license allows for free use and reuse of all our content. ...
Stahlberg, H.; Braun, T.; de Groot, B. L.; Philippsen, A.; Borgnia, M. J.; Agre, P.; Kuehlbrandt, W.; Engel, A.: The 6.9Å Structure of GlpF: A Basis for Homology Modeling of the Glycerol Channel from Escherichia coli. Journal of Structural Biology 132, pp. 133 - 141 (2000 ...
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 ...
TY - JOUR. T1 - Conditional osmotic stress in yeast. T2 - a system to study transport through aquaglyceroporins and osmostress signaling. AU - Karlgren, Sara. AU - Pettersson, Nina. AU - Nordlander, Bodil. AU - Mathai, John C.. AU - Brodsky, Jeffrey L.. AU - Zeidel, Mark L.. AU - Bill, Roslyn M.. AU - Hohmann, Stefan. N1 - © 2005 The American Society for Biochemistry and Molecular Biology, Inc.. PY - 2005/2/25. Y1 - 2005/2/25. N2 - The accumulation and transport of solutes are hallmarks of osmoadaptation. In this study we have employed the inability of the Saccharomyces cerevisiae gpd1Δ gpd2Δ mutant both to produce glycerol and to adapt to high osmolarity to study solute transport through aquaglyceroporins and the control of osmostress-induced signaling. High levels of different polyols, including glycerol, inhibited growth of the gpd1Δ gpd2Δ mutant. This growth inhibition was suppressed by expression of the hyperactive allele Fps1-AΔ of the osmogated yeast aquaglyceroporin, Fps1. The ...
TY - JOUR. T1 - Role of Aquaporin 0 in lens biomechanics. AU - Sindhu Kumari, S.. AU - Gupta, Neha. AU - Shiels, Alan. AU - FitzGerald, Paul G. AU - Menon, Anil G.. AU - Mathias, Richard T.. AU - Varadaraj, Kulandaiappan. PY - 2015/4/19. Y1 - 2015/4/19. N2 - Abstract Maintenance of proper biomechanics of the eye lens is important for its structural integrity and for the process of accommodation to focus near and far objects. Several studies have shown that specialized cytoskeletal systems such as the beaded filament (BF) and spectrin-actin networks contribute to mammalian lens biomechanics; mutations or deletion in these proteins alters lens biomechanics. Aquaporin 0 (AQP0), which constitutes ∼45% of the total membrane proteins of lens fiber cells, has been shown to function as a water channel and a structural cell-to-cell adhesion (CTCA) protein. Our recent ex vivo study on AQP0 knockout (AQP0 KO) mouse lenses showed the CTCA function of AQP0 could be crucial for establishing the refractive ...
After producing a recombinant form of AqpZ in E. coli, the proteins were crystallized--capturing five water molecules inside--and then analyzed by state-of-the-art high-resolution X-ray diffraction techniques. The architecture of aquaporin Z is typical of aquaporins, with a spiral of eight oxygens providing water-binding sites inside the channel. The outer membrane and cytoplasmic ends of the channel are wider than the interior, which is long and narrow. This structure demonstrates that aquaporin selectivity arises in part from erecting a physical barrier: small molecules, like water, can easily pass, but larger ones simply cant fit. And the strategic positioning of amino acid residues with hydrophilic or hydrophobic properties along the channel helps police the influx of molecules based on their affinity for water. While it seems two amino acid chains located in the middle of the channel also provide a water-friendly surface, Stroud et al. say they play a more intriguing role. Noting that the ...
Aquaporins facilitate the diffusion of water across cell membranes. We previously showed that acid pH or low Ca2+ increase the water permeability of bovine AQP0
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Aqp4 - Aqp4 (untagged) - Mouse aquaporin 4 (cDNA clone MGC:37514 IMAGE:4985265), (10ug) available for purchase from OriGene - Your Gene Company.
Aquaporin-5 is a protein that in humans is encoded by the AQP5 gene. Aquaporin 5 (AQP5) is a water channel protein. Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). Aquaporin 5 plays a role in the generation of saliva, tears and pulmonary secretions. AQP0, AQP2, AQP5, and AQP6 are closely related and all map to 12q13. Aquaporin GRCh38: Ensembl release 89: ENSG00000161798 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000044217 - Ensembl, May 2017 Human PubMed Reference:. Mouse PubMed Reference:. Lee MD, Bhakta KY, Raina S, Yonescu R, Griffin CA, Copeland NG, Gilbert DJ, Jenkins NA, Preston GM, Agre P (Jun 1996). The human Aquaporin-5 gene. Molecular characterization and chromosomal localization. J Biol Chem. 271 (15): 8599-604. doi:10.1074/jbc.271.15.8599. PMID 8621489. Entrez Gene: AQP5 aquaporin 5. Verkman AS (2003). Role of aquaporin water channels in eye function. Exp. Eye Res. 76 (2): 137-43. ...
With Aquaporin Inside™ Reverse Osmosis membranes, water treatment can be done with lower energy consumption compared to conventional membrane technology. The benefit comes from the aquaporin proteins which are very efficient in transporting water. This enables the water treatment plant to increase the capacity of treated wastewater without increasing the energy consumption, or remaining at the same capacity level while lowering the energy consumption. At the same time, Aquaporin membranes has the potential to remove also small, neutral compounds such as micro pollutants/trace organics, improving re-use water quality.. Aquaporin Inside™ Forward Osmosis ...
Looking for online definition of Aquaporin1 or what Aquaporin1 stands for? Aquaporin1 is listed in the Worlds largest and most authoritative dictionary database of abbreviations and acronyms
In starvation, glycerol is released from adipose tissue and serves as an important precursor for hepatic gluconeogenesis. By unknown gender-specific mechanisms, women suppress the endogenous glucose production better than men and respond to metabolic stress with higher plasma glycerol levels. Hepatic glycerol uptake is facilitated by aquaporin-9 (AQP9), a broad-selectivity neutral solute channel, and represents an insulin-regulated step in supplying gluconeogenesis with glycerol. In the current study, hepatic AQP9 abundance was increased 2.6-fold in starved male rats as assessed by immunoblotting and immunohistochemistry. By contrast, starvation had no significant effect on hepatic AQP9 expression in female rats. Coordinately, plasma glycerol levels remained unchanged upon starvation in male rats whereas it was increased in female rats. The different responses to starvation were paralleled by higher glycerol permeability in basolateral hepatocyte membranes from starved male rats as compared to ...
Aquaporin membrane protein, molecular model. Computer illustration showing the structure of a molecule of the human aquaporin 1 protein (blue, and white ribbon). Aquaporins are membrane proteins that form channels (centre) that help water molecules (red and white spheres) pass in and out of cells. Unlike ion channels, aquaporins help prevent ions and other dissolved substances carrying electrical charge from entering the cell, as they only allow lone water molecules or certain uncharged solutes to pass through. This helps maintain the electrochemical potential of the cell membrane. - Stock Image C035/5236
Müller glial cells are important regulators of physiological function of retina. In a model disease of retinal inflammation and spontaneous recurrent uveitis in horses (ERU), we could show that retinal Müller glial cells significantly change potassium and water channel protein expression during autoimmune pathogenesis. The most significantly changed channel protein in neuroinflammatory ERU was aquaporin 11 (AQP11). Aquaporins (AQP, 13 members) are important regulators of water and small solute transport through membranes. AQP11 is an unorthodox member of this family and was assigned to a third group of AQPs because of its difference in amino acid sequence (conserved sequence is only 11 %) and especially its largely unknown function. In order to gain insight into the distribution, localization, and function of AQP11 in the retina, we first developed a novel monoclonal antibody for AQP11 enabling quantification, localization, and functional studies. In the horse retina, AQP11 was exclusively expressed
Transmembrane glycerol transport is an ancient biophysical property that evolved in selected subfamilies of water channel (aquaporin) proteins. Here, we conducted broad level genome (,550) and transcriptome (,300) analyses ...
I think it will be found that aquaporin 3 will be the item of interest (1).. Aquaporin 3 is found in normal skeletal myofibres (2).. I suspect it will be found that the problem is not a mutation, but something interfering with the normal proper function of the aqp3 channels.. Aquaporin 3 is, in addition to being a water channel, also an arsenic transporter.. Arsenic has been implicated in Alzheimers in at least a few instances. For example, this statement appears in Reference 3 below:. Arsenic can induce apoptosis in cortical neurons of rats. This process is based on the activation of JNK3 and p38 MAPK by arsenic...[which] can activate p38 MAPK and JNK3..... And the title of the last paper speaks for itself: Arsenic exposure may be a risk factor for Alzheimers disease.. ...
Kit contents: 1. MICROTITER PLATE * 1 2. ENZYME CONJUGATE*1 vial 3. STANDARD A*1 vial 4. STANDARD B*1 vial 5. STANDARD C*1 vial 6. STANDARD D*1 vial 7. STANDARD E*1 vial 8. STANDARD F*1 vial 9. SUBSTRATE A*1 vial 10. SUBSTRATE B*1 vial 11. STOP ...
Kit contents: 1. MICROTITER PLATE * 1 2. ENZYME CONJUGATE*1 vial 3. STANDARD A*1 vial 4. STANDARD B*1 vial 5. STANDARD C*1 vial 6. STANDARD D*1 vial 7. STANDARD E*1 vial 8. STANDARD F*1 vial 9. SUBSTRATE A*1 vial 10. SUBSTRATE B*1 vial 11. STOP ...
Polyclonal antibody for AQUAPORIN 3/AQP3 detection. Host: Rabbit.Size: 100μg/vial. Tested applications: IHC-P. Reactive species: Human. AQUAPORIN 3/AQP3 information: Molecular Weight: 31544 MW; Subcellular Localization: Basolateral cell membrane; Multi-pa
Aquaporin 10 antibody, C-term (aquaporin 10) for WB. Anti-Aquaporin 10 pAb (GTX45889) is tested in Human samples. 100% Ab-Assurance.
Purpose: The expression of aquaporin water channel genes are shown to be affected in several pathological conditions of retina, such as in diabetic retinopathy, retinal ischemia and in autoimmune uveitis. Human native retinal pigment epithelial (RPE) cells and immortalized human RPEs are formerly shown to express aquaporins, still the expression of aquaporins in stem cell derived RPE have not been previously elucidated. The objective of this study was to determine the expression of several aquaporin genes (aquaporin1,- 3, -4, -5, -6, -7, -10, -11 and -12) and assess the localization of aquaporin 1 water channel protein in human embryonic (hESCs) and induced pluripotent stem cells (hiPSCs) derived RPE cells.. Methods: hESC- and hiPSC derived RPE cells were grown as monolayer in serum-free media. The expression of aquaporin genes was determined with qRT-PCR. The localization of AQP1-protein was studied with confocal microscopy. Finally, the functionality of aquaporins was assessed with dye ...
Plant cells contain proteins that are members of the major intrinsic protein (MIP) family, an ancient family of membrane channel proteins characterized by six membrane-spanning domains and two asparagine-proline-alanine (NPA) amino acid motifs in the two halves of the protein. We recently demonstrated that [gamma]-TIP, one of the MIP homologs found in the vacuolar membrane of plant cells, is an aquaporin or water channel protein (C. Maurel, J. Reizer, J.I. Schroeder, M.J. Chrispeels [1993] EMBO J 12: 2241-2247). RD28, another MIP homolog in Arabidopsis thaliana, was first identified as being encoded by a turgor-responsive transcript. To find out if RD28 is a water channel protein, rd28 cRNA was injected into Xenopus laevis oocytes. Expression of RD28 caused a 10- to 15-fold increase in the osmotic water permeability of the oocytes, indicating that the protein creates water channels in the plasma membrane of the oocytes and is an aquaporin just like its homolog [gamma]-TIP. Although RD28 has ...
TY - JOUR. T1 - Aquaporin-3 facilitates epidermal cell migration and proliferation during wound healing. AU - Hara-Chikuma, Mariko. AU - Verkman, A. S.. PY - 2008/2/1. Y1 - 2008/2/1. N2 - Healing of skin wounds is a multi-step process involving the migration and proliferation of basal keratinocytes in epidermis, which strongly express the water/glycerol-transporting protein aquaporin-3 (AQP3). In this study, we show impaired skin wound healing in AQP3-deficient mice, which results from distinct defects in epidermal cell migration and proliferation. In vivo wound healing was ∼80% complete in wild-type mice at 5 days vs ∼50% complete in AQP3 null mice, with remarkably fewer proliferating, BrdU-positive keratinocytes. After AQP3 knock-down in keratinocyte cell cultures, which reduced cell membrane water and glycerol permeabilities, cell migration was slowed by more than twofold, with reduced lamellipodia formation at the leading edge of migrating cells. Proliferation of AQP3 knock-down ...
This paper strongly supports the conclusion that AQP0 has a high permeability mode and a low permeability mode. How do these two modes differ? Available structural data on the nature of the water-filled pore through AQP1 and the glycerol facilitator suggest a possible answer. For both, water and glycerol must move through the pore by single-file diffusion. The crystal structure and molecular dynamic simulations suggest that there are multiple water molecules in the pore. There are ∼6 waters seen in the narrow constriction of the pore in the X-ray structure (Sui et al., 2001), and molecular dynamic simulations suggest that there are ∼7 or 8 water molecules moving in concert in the single-file portion of the pore (Tajkhorshid et al., 2002; Zhu et al., 2004). The lack of passage of ionic current through AQP0 and AQP1 is explained by electrostatic considerations that strongly inhibit the movement of protons into the NPA region or hydroxyls into regions flanking either side of the NPA region (de ...
Purpose: : To demonstrate in the conjunctiva the presence of aquaporin type 5 (AQP5), a water channel homologue found in the apical membrane of several tissues including the cornea. Presently, there are no reports indicating as to which AQP might be expressed apically in the conjunctiva; only AQP3 has been identified in the lateral membranes of rat and human conjunctival epithelia. Because we had data from gene-expression microarray assays (Turner; ARVO 2004) indicating message for AQP5 in the human conjunctiva, tissue samples from human, as well as from rats and rabbits (given the ease of their procurement), were analyzed to confirm that the AQP5 protein was indeed expressed in mammalian conjunctivae. Methods: : Goat polyclonal IgG against AQP5 was purchased commercially and used in immunoblotting and immunohistochemical techniques to identify and localize the water channel in rat, rabbit and human epithelia. Results: : Immunoblot analysis of rabbit bulbar-plus-palpebral plasma membrane ...
Aquaporin 3 (AQP3) is an aquaglyceroporin that transports water and glycerol and is expressed in the epidermis, among other epithelial tissues. We have recently shown that there is an association between this glycerol channel and phospholipase D2 (PLD2) in caveolin-rich membrane microdomains. While …
Stahl, Katja; Rahmani, Soulmaz; Prydz, Agnete; Skauli, Nadia; MacAulay, Nanna; Mylonakou, Maria-Niki; Torp, Reidun; Skare, Øivind; Berg, Torill; Leergaard, Trygve Brauns; Paulsen, Ragnhild Elisabeth; Ottersen, Ole Petter & Amiry-Moghaddam, Mahmood (2018). Targeted deletion of the aquaglyceroporin AQP9 is protective in a mouse model of Parkinsons disease. PLOS ONE. ISSN 1932-6203. 13(3) . doi: 10.1371/journal.pone.0194896 Fulltekst i vitenarkiv. Vis sammendrag More than 90% of the cases of Parkinsons disease have unknown etiology. Gradual loss of dopaminergic neurons of substantia nigra is the main cause of morbidity in this disease. External factors such as environmental toxins are believed to play a role in the cell loss, although the cause of the selective vulnerability of dopaminergic neurons remains unknown. We have previously shown that aquaglyceroporin AQP9 is expressed in dopaminergic neurons and astrocytes of rodent brain. AQP9 is permeable to a broad spectrum of substrates including ...
Objective: It is well known that VEGFR expression is correlated with peritumoral brain edema in meningiomas. Also Aquaporin4 seems to induce the perifocal edema. In our study we analyzed the correlation of VEGFR1, VEGFR2 and Aquaporin4 to the brain edema. Additionally a potential correlation between[for full text, please go to the a.m. URL ...
Hi, Bit more than a month ago my mom developed burning sensation on her back and stomach, she went to a doc but he said its nothing lifetreatening and she waited for for her turn for the tests, it was like this for a week or two. Few weeks ago the burning sensation became too much to bear and my mom went to a hospital. They took her in and the next day she had issues walking and day later she couldnt walk on her own at all. After a few days they put her on some steroid IV thing for
Hi, Bit more than a month ago my mom developed burning sensation on her back and stomach, she went to a doc but he said its nothing lifetreatening and she waited for for her turn for the tests, it was like this for a week or two. Few weeks ago the burning sensation became too much to bear and my mom went to a hospital. They took her in and the next day she had issues walking and day later she couldnt walk on her own at all. After a few days they put her on some steroid IV thing for
PDB 2B6O, EMDB 2973 - 1.9Å resolutuion electron crystallography structure of the water channel Aquaporin-0 in its closed state. ...
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 ...
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 ... 73 (3): 792-9. doi:10.1182/blood.V73.3.792.bloodjournal733792. PMID 2537119. Cesarman E, Chang Y, Moore PS, Said JW, Knowles DM ... It has carried a median survival time of ~5 months, with overall survival rates at 1, 3, and 5 year of only 30, 18, and 17%, ...
... and aquaporin-1 in human erythrocyte membrane domains". Biochimica et Biophysica Acta (BBA) - Biomembranes. 1828 (3): 956-66. ... 34 (2-3): 121-38. doi:10.1016/j.mam.2012.07.001. PMC 4104978. PMID 23506862. Zong NC, Li H, Li H, Lam MP, Jimenez RC, Kim CS, ... 16 (3): 224-31. doi:10.1002/1098-1004(200009)16:3. 3.0.CO;2-P. PMID 10980529. Online Mendelian Inheritance in Man, OMIM®. Johns ... 18 (3): 183-93. doi:10.1080/09687680110072140. PMID 11681785. Baumann MU, Deborde S, Illsley NP (October 2002). "Placental ...
Zheng X, Bollinger Bollag W (December 2003). "Aquaporin 3 colocates with phospholipase d2 in caveolin-rich membrane ... 467 (2-3): 326-32. doi:10.1016/s0014-5793(00)01174-1. PMID 10675563. S2CID 21891748. Kim JH, Lee S, Park JB, Lee SD, Kim JH, Ha ... N-(2-(1-(3-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]decan-8-yl)ethyl)-2-naphthamide: 75-fold selective versus PLD1, IC50 = 20 ... 467 (2-3): 326-32. doi:10.1016/S0014-5793(00)01174-1. PMID 10675563. S2CID 21891748. Lee C, Kim SR, Chung JK, Frohman MA, ...
Zheng X, Bollinger Bollag W (December 2003). "Aquaporin 3 colocates with phospholipase d2 in caveolin-rich membrane ... 467 (2-3): 326-32. doi:10.1016/S0014-5793(00)01174-1. PMID 10675563. S2CID 21891748. Vargas L, Nore BF, Berglof A, Heinonen JE ... 56 (3): 355-6. doi:10.1006/geno.1998.5723. PMID 10087206. "Entrez Gene: CAV1 caveolin 1, caveolae protein, 22kDa". Li S, ...
Two types of aquaporins are expressed in the CNS: aquaporin-1, which is expressed by specialized epithelial cells of the ... Aquaporins are membrane-bound channels that play critical roles in regulating the flux of water into and out of cells. Relative ... Aquaporin-4 expression in astrocytes is highly polarized to the endfoot processes ensheathing the cerebral vasculature. Up to ... Verkman AS, Binder DK, Bloch O, Auguste K, Papadopoulos MC (August 2006). "Three distinct roles of aquaporin-4 in brain ...
Аквапорин-1, AQP1 (англ. Aquaporin 1 (Colton blood group)) - білок, який кодується геном AQP1, розташованим у людей на ... de Groot B.L., Engel A., Grubmueller H. (2001). A refined structure of human aquaporin-1.. FEBS Lett. 504: 206 - 211. PubMed ... AQP1, AQP-CHIP, CHIP28, CO, aquaporin 1 (Colton blood group). Зовнішні ІД. OMIM: 107776 MGI: 103201 HomoloGene: 68051 GeneCards ... Сполуки, які фізично взаємодіють з Aquaporin 1 переглянути/редагувати посилання на ВікіДаних. ...
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 ...
... and the Aquaporin 4 channel.[47] Focal lactic acidosis also causes secondary oedema, oxidative stress, inflammation and white ... 50 (3): 329-33. doi:10.1590/S0004-282X1992000300012. PMID 1308411.. *^ a b Xin, Y.; Wan, D. H.; Chu, Q.; Li, A. M.; Gao, X. J ... WE is more likely to occur in males than females.[35] Among the minority who are diagnosed, mortality can reach 17%.[3] The ... When it occurs simultaneously with alcoholic Korsakoff syndrome it is known as Wernicke-Korsakoff syndrome.[2][3] ...
... via activation of aquaporins, the site of the ADH receptors - back into the circulation. This has two consequences. First, in ... aquaporin 2), and their insertion into the cells' luminal membranes. Excessive ADH causes an inappropriate increase in the ... "Physiology and pathophysiology of renal aquaporins". Seminars in Nephrology. 21 (3): 231-8. doi:10.1053/snep.2001.21647. PMID ... ISBN 978-3-540-79565-0. Zietse, R.; van der Lubbe, N.; Hoorn, E. J. (2009). "Current and future treatment options in SIADH". ...
... aquaporin 6 MeSH D12.776.157.530.400.500.040.374 - aquaporin 1 MeSH D12.776.157.530.400.500.040.437 - aquaporin 2 MeSH D12.776. ... 157.530.400.500.040.468 - aquaporin 4 MeSH D12.776.157.530.400.500.040.484 - aquaporin 5 MeSH D12.776.157.530.400.500.520 - ... aquaporins MeSH D12.776.157.530.400.500.040.249 - aquaglyceroporins MeSH D12.776.157.530.400.500.040.249.500 - aquaporin 3 MeSH ... glucose transporter type 3 MeSH D12.776.157.530.500.500.937 - glucose transporter type 4 MeSH D12.776.157.530.500.500.968 - ...
Mershin Andrew Huxley Animal locomotion Animal locomotion on the water surface Anita Goel Antiporter Aquaporin 2 Aquaporin 3 ... Aquaporin 4 Archibald Hill Ariel Fernandez Arthropod exoskeleton Arthropod leg Avery Gilbert BEST2 BK channel Bacterial outer ... alpha 3 Cyclic nucleotide-gated channel alpha 4 Cyclic nucleotide-gated ion channel Cyclic nucleotide gated channel beta 3 Cys- ... Aggregate modulus Aharon Katzir Alan Lloyd Hodgkin Alexander Rich Alexander van Oudenaarden Allan McLeod Cormack Alpha-3 beta-4 ...
... aquaporin 6 MeSH D12.776.543.550.425.730.040.374 - aquaporin 1 MeSH D12.776.543.550.425.730.040.437 - aquaporin 2 MeSH D12.776. ... aquaporin 6 MeSH D12.776.543.585.400.730.040.436 - aquaporin 1 MeSH D12.776.543.585.400.730.040.530 - aquaporin 2 MeSH D12.776. ... 543.550.425.730.040.468 - aquaporin 4 MeSH D12.776.543.550.425.730.040.484 - aquaporin 5 MeSH D12.776.543.550.425.730.520 - ... 543.585.400.730.040.577 - aquaporin 4 MeSH D12.776.543.585.400.730.040.600 - aquaporin 5 MeSH D12.776.543.585.400.730.520 - ...
... occurs in one of two ways: either the osmoreceptor-aquaporin feedback loop is overwhelmed, or it is interrupted. ... 163 (3): ITC1-19. doi:10.7326/aitc201508040. PMID 26237763.. *^ a b c d e f g h i j k l m n o Lee, JJ; Kilonzo, K; Nistico, A; ... ISBN 978-3-540-79565-0.. *^ a b c Rondon-Berrios, Helbert; Berl, Tomas (2017). "Vasopressin Receptor Antagonists in ... "Physiology and pathophysiology of renal aquaporins". Seminars in nephrology. 21 (3): 231-8. doi:10.1053/snep.2001.21647. PMID ...
Around active NMO lesions AQP4 may selectively be lost in the absence of aquaporin 1 (AQP1) loss or other structural damage ( ... 246 (3): 880-6. doi:10.1148/radiol.2463070486. PMID 18195384. Calabrese M, Filippi M, Rovaris M, Mattisi I, Bernardi V, Atzori ... 72 (3): 385-94. doi:10.1002/ana.23621. PMID 23034911. Lucchinetti C. F.; et al. (2008). "Clinical and radiographic spectrum of ... 2 (3): 295-301. doi:10.1002/acn3.164. PMC 4369279 . PMID 25815356. Young NP, Weinshenker BG, Parisi JE, Scheithauer B, Giannini ...
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 ...
An upregulation of aquaporin and H+ - ATPase allows for the rapid flux of water out of these motor cells. Water flux out of the ... Aquaporins on the vacuole membrane of pulvini allow for the efflux of water that contributes to the change in turgor pressure. ... "Increased Expression of Vacuolar Aquaporin and H+-ATPase Related to Motor Cell Function in Mimosa pudica L". Plant Physiology. ... 114 (3): 827-834. doi:10.1104/pp.114.3.827. ISSN 0032-0889. PMC 158368. PMID 12223745. Volkov, Alexander G.; Foster, Justin C ...
... is the protein product of the human AQP3 gene. It is found in the basolateral cell membrane of principal collecting ... 2005). "Roles of aquaporin-3 water channels in volume-regulatory water flow in a human epithelial cell line". J. Membr. Biol. ... Aquaporin 3 is expressed more in atopic eczema. Recent studies indicate that aquaporin 3 is overexpressed in many types of ... Aquaporin 3 is also permeable to glycerol, ammonia, urea, and hydrogen peroxide. It is expressed in various tissues including ...
It is the only aquaporin regulated by vasopressin. The basic job of aquaporin 2 is to reabsorb water from the urine while its ... This aquaporin is also regulated by food intake. Fasting reduces expression of this aquaporin independently of vasopressin. ... so the aquaporin 2 can be used by the cell. This aquaporin is regulated in two ways by the peptide hormone vasopressin: short- ... Aquaporin 2 is in kidney epithelial cells and usually lies dormant in intracellular vesicle membranes. When it is needed, ...
The expression of aquaporin 4 is reliant on the disease stage of TBI. In an acute stage of TBI, the lack of aquaporin 4 causes ... Aquaporin-4, also known as AQP4, is a water channel protein encoded by the AQP4 gene in humans. AQP4 belongs to the aquaporin ... Aquaporin-4 is 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 ...
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 is a protein that in humans is encoded by the AQP1 gene. AQP1 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 ... "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 ... Wang W, Hart PS, Piesco NP, Lu X, Gorry MC, Hart TC (Mar 2003). "Aquaporin expression in developing human teeth and selected ...
Agre, P.; King, L. S.; Yasui, M.; Guggino, W. B.; Ottersen, O. P.; Fujiyoshi, Y.; Engel, A.; Nielsen, S. (2002). "Aquaporin ... Fujiyoshi and Engel solved the structure of Aquaporin-1 in collaboration with Agre. Together with Palczewski Engel's team ... 177 (1): 3-13. doi:10.1016/j.jsb.2011.11.013. PMID 22115996. "Farewell Symposium for Andreas Engel". unibas.ch. Retrieved 2015- ... 542 (1): 3-16. doi:10.1113/jphysiol.2002.020818. PMC 2290382. PMID 12096044. "Structure of the rhodopsin dimer: a working model ...
... or Aquaporin, cytoskeletal structural proteins, paired-like homeodomain transcription factor 3 (PITX3), avian ... Any central opacity or surrounding cortical distortion greater than 3 mm can be assumed to be visually significant. Laboratory ...
Water has been shown in at least some species to enter the CV through aquaporins. Acidocalcisomes have been implied to work ... Although it is known that several proteins decorate the CV membrane (V−H+−ATPases, aquaporins), a complete list is missing. The ... "Presence of aquaporin and V-ATPase on the contractile vacuole of Amoeba proteus". Biol Cell. 100 (3): 179-188. doi:10.1042/ ...
Aquaporin-8 is a protein that in humans is encoded by the AQP8 gene. Aquaporin 8 (AQP8) is a water channel protein. Aquaporins ... "Entrez Gene: AQP8 aquaporin 8". Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of ... 2007). "Aquaporin-8 expression is reduced in ileum and induced in colon of patients with ulcerative colitis". World J. ... Wang S, Chen J, Au KT, Ross MG (2003). "Expression of aquaporin 8 and its up-regulation by cyclic adenosine monophosphate in ...
In 2005 they identified the aquaporin 4 protein as the target of the disease, and developed first in-house test to aid in the ... 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 ...
Zador, Zsolt; Stiver, Shirley; Wang, Vincent; Manley, Geoffrey T. (2009). "Role of Aquaporin-4 in Cerebral Edema and Stroke". ... In Beitz, Eric (ed.). Aquaporins. Handbook of Experimental Pharmacology. 190. pp. 159-70. doi:10.1007/978-3-540-79885-9_7. ISBN ... 28 (3): 138-45. doi:10.1016/j.it.2007.01.005. PMID 17276138. John, Gareth R.; Lee, Sunhee C.; Song, Xianyuan; Rivieccio, Mark; ... 60 (3): 430-40. doi:10.1016/j.neuron.2008.10.013. PMID 18995817. Sofroniew, M. V. (2005). "Reactive Astrocytes in Neural Repair ...
"Increased aquaporin 1 expression in the tunica albuginea of Peyronie's disease patients: an in vivo pilot study. ". Histol ... "Overexpression of Aquaporin 1 on cysts of patients with polycystic liver disease.". Rev Esp Enferm Dig. 2016. PMID 26838488. ... "Overexpression of Aquaporin-1 is a Prognostic Factor for Biochemical Recurrence in Prostate Adenocarcinoma. ". Pathol Oncol Res ... "Red blood cell aquaporin-1 expression is decreased in hereditary spherocytosis. ". Ann Hematol. 2016. PMID 27465156. ...
Aquaporin 3 is the protein product of the human AQP3 gene. It is found in the basolateral cell membrane of principal collecting ... 2005). "Roles of aquaporin-3 water channels in volume-regulatory water flow in a human epithelial cell line". J. Membr. Biol. ... Aquaporin 3 is expressed more in atopic eczema. Recent studies indicate that aquaporin 3 is overexpressed in many types of ... Aquaporin 3 is also permeable to glycerol, ammonia, urea, and hydrogen peroxide. It is expressed in various tissues including ...
Rabbit polyclonal Aquaporin 3 antibody. Validated in WB, ELISA, IHC and tested in Rat. Cited in 1 publication(s). Independently ... Primary - Rabbit Anti-Aquaporin 3 antibody (ab15117) WB, ELISA, IHC-Fr Secondary - Goat Anti-Rabbit IgG H&L (HRP) (ab205718) ... Anti-Aquaporin 3 antibody (ab15117). Rabbit polyclonal Aquaporin 3 antibody. Validated in WB, ELISA, IHC and tested in Rat. ... Hi, I would like to know if antibody aquaporin 3 cat#ab15117 is an extracellular antibody and can it be used for FACS? Thanks ...
Rabbit polyclonal Aquaporin 3 antibody. Validated in WB, ELISA, IHC and tested in Rat. Cited in 1 publication(s). Independently ... Hi, I would like to know if antibody aquaporin 3 cat#ab15117 is an extracellular antibody and can it be used for FACS? Thanks ... Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the ... Predicted molecular weight: 32 kDa.Can be blocked with Aquaporin 3 peptide (ab80550). ...
Two previous articles in this series on aquaporins have discussed their history, mechanism and stimulation. The current article ... Aquaporins (AQPs) are integral membrane proteins that form pores in the membrane of biological cells. At least 13 mammalian ... 4. M Hara-Chikuma and AS Verkman, Roles of Aquaporin-3 in the epidermis, (In press at J Invest Derm) ... For this explanation and for the role that an aquaporin plays, we turn to cell physiologist Wendy B. Bollag, PhD, of the ...
Aquaporin-3 water channel localization and regulation in rat kidney.. [C A Ecelbarger, J Terris, G Frindt, M Echevarria, D ... Anti-Water Channel Aquaporin 3 antibody produced in rabbit, affinity isolated antibody pricing ... The aquaporins are a family of water channels expressed in several water-transporting tissues, including the kidney. We have ... affinity-purified polyclonal antibody to aquaporin-3 (AQP-3) to investigate its localization and regulation in the kidney. ...
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Aquaporins (Aqps) are a superfamily of integral membrane proteins which generally facilitate the permeation of water through ... Aquaporins (Aqps) are a superfamily of integral membrane proteins which generally facilitate the permeation of water through ... Figure 5. The gene expression of (A) aquaporin 1 (aqp1) and (B) aquaporin 3 (aqp3) in various tissues/organs of Protopterus ... Table 1. Primers used for PCR, RACE, and qPCR of aquaporin 1 (aqp1) and aquaporin 3 (aqp3) from the gills of Protopterus ...
Immunolocalisation of aquaporin 3 in the gill and the gastrointestinal tract of the European eel Anguilla anguilla (L.) LIGNOT ... Glycosylation is not essential for vasopressin-dependent routing of aquaporin 2 in transfected Madin-Darby canine kidney cells ... Aquaporin-3 expressed in the basolateral membrane of gill chloride cells in Mozambique tilapia Oreochromis mossambicus adapted ... Evidence for stabilization of aquaporin 2 folding mutants by N-linked glycosylation in endoplasmic reticulum BUCK TM ...
Abstract Aquaporin (AQP) 3 expression is altered in inflammatory bowel diseases, although the exact mechanisms regulating AQP ... Zhao G, Li J, Wang J, Shen X, Sun J (2014) Aquaporin 3 and 8 are down-regulated in TNBS-induced rat colitis. Biochem Biophys ... Zhang W, Xu Y, Chen Z, Xu Z, Xu H (2011) Knockdown of aquaporin 3 is involved in intestinal barrier integrity impairment. FEBS ... Aquaporin (AQP) 3 expression is altered in inflammatory bowel diseases, although the exact mechanisms regulating AQP abundance ...
2007). Structural basis of aquaporin inhibition by mercury. J. Mol. Biol. 368, 607-617. doi:10.1016/j.jmb.2007.02.070. ... 2000). Aquaporin 3 cloned from Xenopus laevis is regulated by the cystic fibrosis transmembrane conductance regulator. FEBS ... Water transport is associated with an aquaporin, AQP3. The above data with genistein and MBP-91 indicated that Cl− and water ... et al.(2008). Role of NHERF1, cystic fibrosis transmembrane conductance regulator, and cAMP in the regulation of aquaporin 9. J ...
Relationship of aquaporins 3 (AQP3), 7 (AQP7), and 11 (AQP11) with boar sperm resilience to withstand freeze-thawing procedures ... In this context, the hypothesis of this study was that aquaporins AQP3, AQP7, and AQP11 could be linked to boar sperm ...
Aquaporin 3 antibody LS-C3804 is an unconjugated rabbit polyclonal antibody to rat Aquaporin 3 (AQP3). Validated for ELISA, IF ... Aquaporin 3 antibody LS-C3804 is an unconjugated rabbit polyclonal antibody to rat Aquaporin 3 (AQP3). Validated for ELISA, IF ... Aquaporin 3 antibody LS-C3804 is an unconjugated rabbit polyclonal antibody to rat Aquaporin 3 (AQP3). Validated for ELISA, IF ...
The circadian fluctuations in aquaporin transcript abundance suggest that aquaporin water channels play a role in these ... 2002). Plasma membrane aquaporins in the motor cells of Samanea saman: Diurnal and circadian regulation. Plant Cell 14: 727-739 ... Oscillating Aquaporin Phosphorylation and 14-3-3 Proteins Mediate the Circadian Regulation of Leaf Hydraulics. Karine Prado, ... 2014). Aquaporins: Highly regulated channels controlling plant water relations. Plant Physiol. 164: 1600-1618. ...
Aquaporin 3 antibody LS-C3802 is an unconjugated rabbit polyclonal antibody to rat Aquaporin 3 (AQP3). Validated for ELISA, IHC ... Aquaporin 3 antibody LS-C3802 is an unconjugated rabbit polyclonal antibody to rat Aquaporin 3 (AQP3). Validated for ELISA, IHC ... Aquaporin 3 antibody LS-C3802 is an unconjugated rabbit polyclonal antibody to rat Aquaporin 3 (AQP3). Validated for ELISA, IHC ... Recognizes rat Aquaporin 3 (AQP3/GLIP). Species sequence homology: mouse 92%, human 85%. ...
aquaporin-3; GA, glycolic acid; IL, interleukin; MAPK, mitogen-activated protein kinase; MCP-1, monocyte chemoattractant ... GA reverted and dose-dependently increased the level of aquaporin-3 (AQP3), the expression of which was down-regulated by UVB. ... Glycolic acid attenuates UVB-induced aquaporin-3, matrix metalloproteinase-9 expression, and collagen degradation in ... Glycolic acid attenuates UVB-induced aquaporin-3, matrix metalloproteinase-9 expression, and collagen degradation in ...
Does aquaporin 3 (AQP3) affect the migration and invasion of human extravillous trophoblast (HTR8/Svneo) cells?Method of Study ... Problem: Does aquaporin 3 (AQP3) affect the migration and invasion of human extravillous trophoblast (HTR8/Svneo) cells? ... Expression of AQP3 lasts from zygophase to the blastula stage[20], and is the most abundant aquaporin expressed in villi during ... Problem: Does aquaporin 3 (AQP3) affect the migration and invasion of human extravillous trophoblast (HTR8/Svneo) cells? ...
Aquaporin 3 (AQP3) is an aquaglyceroporin that transports water and glycerol and is expressed in the epidermis, among other ... Aquaporin-3 in Keratinocytes and Skin: Its Role and Interaction With Phospholipase D2 Arch Biochem Biophys. 2011 Apr 15;508(2): ... Aquaporin 3 (AQP3) is an aquaglyceroporin that transports water and glycerol and is expressed in the epidermis, among other ...
Rabbit pAb Anti-Aquaporin 3 (275-292), rabbit polyclonal, recognizes the ~40 and ~29 kDa forms of aquaporin-3 in rat kidney ... Anti-Aquaporin 3 (275-292) Rabbit pAb MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other ... Anti-Aquaporin 3 (275-292), rabbit polyclonal, recognizes the ~40 and ~29 kDa forms of aquaporin-3 in rat kidney membrane. It ... Detection of rat aquaporin 3 by immunoblotting. Sample: Extract from rat kidney membranes left untreated (lane 1) and treated ...
Potential role of aquaporin 3 in gastric intestinal metaplasia. Haijian Zhao _, Xiaojun Yang, Yangchun Zhou, Weiming Zhang, Yao ... Keywords: gastric intestinal metaplasia, aquaporin 3, gastric cancer, pathology. Received: June 25, 2015 Accepted: August 30, ... Aquaporin 3 (AQP3) has been found to be expressed in goblet cells rather than mucus-secreting glands. To investigate the ... Haijian Zhao1,2, Xiaojun Yang3, Yangchun Zhou1,4, Weiming Zhang5, Yao Wang1, Jianfei Wen1, Zhihong Zhang5, Lizong Shen1 ...
AQUAPORIN 3/AQP3 information: Molecular Weight: 31544 MW; Subcellular Localization: Basolateral cell membrane; Multi-pa ... Polyclonal antibody for AQUAPORIN 3/AQP3 detection. Host: Rabbit.Size: 100μg/vial. Tested applications: IHC-P. Reactive species ... also known as aquaporin 0. Aquaporin 3 is localized at the basal lateral membranes of collecting duct cells in the kidney. In ... Aquaporin-3;AQP-3;Aquaglyceroporin-3;AQP3;. Research Areas. ,signal transduction,metabolism,plasma membrane,channels, ...
This study investigated the role of aquaporin 1 and aquaporin 3 in the pathobiology of skin cancers. Might they have potential ... Expression Pattern of Aquaporin 1 and Aquaporin 3 in Melanocytic and Nonmelanocytic Skin Tumors ... Expression Pattern of Aquaporin 1 and Aquaporin 3 in Melanocytic and Nonmelanocytic Skin Tumors. ... Giovana Osorio, MD, PhD1,2, Teresa Zulueta-Dorado, MD, PhD3, Patricia González-Rodríguez, PhD1, José Bernabéu-Wittel, MD, PhD2 ...
This type of aquaporin transports not only water but also neutral solutes, including cell-permeating cryoprotectants. PMID: ... Aquaporin-1,3 were widely expressed in the cochlea and endolymphatic sac of guinea pig. PMID: 16494013 ... Aquaporin-3 is expressed in developmental zebrafish embryos (Danio rerio). PMID: 15533783 ... By using immunohistochemical techniques applied to confocal microscopy, the presence of aquaporin 3 water channel in the ...
Aquaporins (AQPs) are important in controlling water permeability. As AQP1 is known as a serum-responsive gene, we hypothesized ... By reverse transcriptase-polymerase chain reaction analysis, expression of AQPs 1, 3, and 5 was found in seven colon and ... Aquaporins 1, 3 and 5 in Different Tumors, their Expression, Prognosis Value and Role as New Therapeutic Targets *Mahdieh-Sadat ... Moon, C., Soria, JC., Jang, S. et al. Involvement of aquaporins in colorectal carcinogenesis. Oncogene 22, 6699-6703 (2003). ...
Aquaporin-3,Mouse,Mus musculus \ U0581m for more molecular products just contact us ... Aquaporin-3,Mouse,Mus musculus mus musculus murine CLIA Aqp3,AQP-3,Aquaglyceroporin-3,Aquaporin-3,Mouse,Mus musculus detects ... Aquaporin-3,Mouse,Mus musculus / Product Detail : U0581m CLIA Aqp3,AQP-3,Aquaglyceroporin-3,Aquaporin-3,Mouse,Mus musculus. ... Aquaporin-3,Mouse,Mus musculus. Related products : CLIA Aqp3,AQP-3,Aquaglyceroporin-3,Aquaporin-3,Mouse,Mus musculus ...
Here, we examined whether up-regulation of aquaporin 3 (AQP3) mRNA in cancer cells treated with 5′-DFUR represents a collateral ... trigger a transcriptomic response that involves the aquaglyceroporin aquaporin 3 along with other p53-dependent genes. ... Aquaporin 3 (AQP3) participates in the cytotoxic response to nucleoside-derived drugs. Access & Citations. * 4165 Article ...
Plasmids expressing aquaporin homologs rAQP9, AtNIP5;1, Atnip5;1Δ2-67, AtNIP6;1, Atnip6;1Δ2-29, Atnip6;1Δ2-69, AtNIP7;1 or ... Expression of Arabidopsis aquaporin homologs improves yeast growth in the presence of arsenate (As(V)). Δfps1 Δacr3 Δycf1 ... N-terminal truncation is required for functional expression in yeast of specific Lotus japonicus aquaporin homologs. Δfps1 Δ ... Yeast expressing specific Arabidopsis aquaporin homologs display sensitivity to arsenite (As(III)) and antimonite (Sb(III)). Δ ...
Hwang SM, Lee RH, Song JM, Yoon S, Kim YS, Lee SJ, Kang SK, Jung JS (2002) Expression of aquaporin-5 and its regulation in ... Krane CM, Fortner CN, Hand AR, McGraw DW, Lorenz JN, Wert SE, Towne JE, Paul RJ, Whitsett JA, Menon AG (2001) Aquaporin 5- ... Leitch V, Agre P, King LS (2001) Altered ubiquitination and stability of aquaporin-1 in hypertonic stress. Proc Natl Acad Sci U ... Verkman AS, Matthay MA, Song Y (2000) Aquaporin water channels and lung physiology. Am J Physiol Lung Cell Mol Physiol 278(5): ...
Purchase Recombinant Zea mays Aquaporin NIP2-3(NIP2-3). It is produced in in vitro E.coli expression system. High purity. Good ... Recombinant Zea mays Aquaporin NIP2-3(NIP2-3),partial ( Yeast-CSB-YP861006ZAX1 E.coli-CSB-EP861006ZAX1 Baculovirus-CSB- ... Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.. ... MIP/aquaporin (TC 1.A.8) family, NIP (TC 1.A.8.12) subfamily. ... Recombinant Zea mays Aquaporin NIP2-3(NIP2-3). *in vitro E.coli ...
  • Aquaporin 3 is the protein product of the human AQP3 gene. (wikipedia.org)
  • Indeed, the protein abundance of Aqp1 recovered partially, with complete recovery of mRNA expression level and protein abundance of Aqp3, in the gills of P. annectens after 3 days of arousal. (frontiersin.org)
  • IFNγ decreased AQP3 mRNA expression in HT-29 cells in a time- and concentration-dependent manner and reduced functional AQP3 protein expression (decreased 3 H-labelled glycerol uptake). (springer.com)
  • Finally, using a specific small-interfering RNA against the endogenous aquaporin AQP3, the water transport accompanying CFTR activity decreased. (biologists.org)
  • Relationship of aquaporins 3 (AQP3), 7 (AQP7), and 11 (AQP11) with boar sperm resilience to withstand freeze-thawing procedures. (sigmaaldrich.com)
  • In this context, the hypothesis of this study was that aquaporins AQP3, AQP7, and AQP11 could be linked to boar sperm cryotolerance. (sigmaaldrich.com)
  • Aquaporin 3 antibody LS-C3804 is an unconjugated rabbit polyclonal antibody to rat Aquaporin 3 (AQP3). (lsbio.com)
  • GA reverted and dose-dependently increased the level of aquaporin-3 (AQP3), the expression of which was down-regulated by UVB. (biochemj.org)
  • Does aquaporin 3 (AQP3) affect the migration and invasion of human extravillous trophoblast (HTR8/Svneo) cells? (researchsquare.com)
  • Aquaporin 3 (AQP3) is an aquaglyceroporin that transports water and glycerol and is expressed in the epidermis, among other epithelial tissues. (nih.gov)
  • Aquaporin 3 (AQP3) has been found to be expressed in goblet cells rather than mucus-secreting glands. (oncotarget.com)
  • Rabbit IgG polyclonal antibody for Aquaporin-3(AQP3) detection. (bosterbio.com)
  • AQP3 (aquaporin-3), known as an integral membrane channel in epidermal keratinocytes, facilitates water and glycerol movement into and out of the skin. (mysciencework.com)
  • MEK [MAPK (mitogen-activated protein kinase)/ERK (extracellular-signal-regulated kinase) kinase]/ERK inhibitor U0126 and PI3K (phosphoinositide 3-kinase) inhibitor LY294002 also inhibited EGF-induced AQP3 expression and cell migration. (mysciencework.com)
  • NIH3T3 cells transfected with AQP1 and AQP3 expression constructs were used as positive controls for the Western blots of AQPs 1 and 3, respectively. (nature.com)
  • Accumulating evidence in the literature indicates that the water-, glycerol-, and hydrogen peroxide-transporting channel aquaporin-3 (AQP3) plays a key role in various processes involved in keratinocyte function, and abnormalities in this channel have been observed in several human skin diseases. (elsevier.com)
  • Healing of skin wounds is a multi-step process involving the migration and proliferation of basal keratinocytes in epidermis, which strongly express the water/glycerol-transporting protein aquaporin-3 (AQP3). (elsevier.com)
  • Aquaporin-3 (AQP3) is a small transmembrane water/glycerol channel that may facilitate the membrane uptake of hydrogen peroxide (H 2 O 2 ). (elsevier.com)
  • In this regard, this study aimed to investigate the immunohistochemical expression and prognostic impact of aquaporin-3 (AQP3) and certain markers associated with epithelial-mesenchymal transition concerning invasive breast carcinoma of no special type. (ac.ir)
  • Aquaporin 7 has greater sequence similarity with AQP3 and AQP9 and they may be a subfamily. (novusbio.com)
  • Aquaporin 7 and AQP3 are at the same chromosomal location suggesting that 9p13 may be a site of an aquaporin cluster. (novusbio.com)
  • Estudiamos la expresión de AQP2, AQP3 y AQP4 en la médula renal del camello bactriano ( Camelus bactrianus ) usando tinción inmunohistoquímica en secciones de parafina . (bvsalud.org)
  • Se observó una fuerte expresión de AQP3 en la membrana plasmática basolateral del CCMI del camello. (bvsalud.org)
  • Concluimos que la expresión de AQP2, AQP3 y AQP4 en el riñón de camello mostró algunas diferencias con el bovino en el transporte trans-epitelial de agua renal. (bvsalud.org)
  • Ishibashi K, Sasaki S, Fushimi K, Uchida S, Kuwahara M, Saito H, Furukawa T, Nakajima K, Yamaguchi Y, Gojobori T et al (1994) Molecular cloning and expression of a member of the aquaporin family with permeability to glycerol and urea in addition to water expressed at the basolateral membrane of kidney collecting duct cells. (springer.com)
  • Aquaporins (AQPs) are important in controlling water permeability. (nature.com)
  • 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)
  • Aquaporin-3 function is to promote glycerol permeability across cell membrane. (proteopedia.org)
  • The diffusive nature of single-file transport ( 2 ) and the unaltered fluidity of confined water ( 3 ) suggest that the unitary osmotic water channel permeability p f may only vary within the narrow limits that are set by the small length deviations of the single-file region. (sciencemag.org)
  • Copper inhibits the water and glycerol permeability of aquaporin-3. (semanticscholar.org)
  • Immunoblotting studies revealed that thirsting of rats for 48 h approximately doubled the amount of AQP-3 protein in the inner medulla. (sigmaaldrich.com)
  • Ramirez-Lorca R, Vizuete ML, Venero JL, Revuelta M, Cano J, Ilundain AA, Echevarria M (1999) Localization of aquaporin-3 mRNA and protein along the gastrointestinal tract of Wistar rats. (springer.com)
  • As an example, in epithelial cells it was proposed that the movement of water could be directly linked to cystic fibrosis transmembrane conductance regulator (CFTR) protein activity through a cAMP-stimulated aqueous pore, or be dependent on aquaporin. (biologists.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)
  • Individual knockout plants for five 14-3-3 protein isoforms expressed in rosettes lacked circadian activation of K ros . (plantcell.org)
  • Further dilutions should be made in a physiological buffer containing a carrier protein such as 1-3% BSA. (emdmillipore.com)
  • Arima H, Yamamoto N, Sobue K, Umenishi F, Tada T, Katsuya H, Asai K (2003) Hyperosmolar mannitol simulates expression of aquaporins 4 and 9 through a p38 mitogen-activated protein kinase-dependent pathway in rat astrocytes. (springer.com)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Fibronectin Leucine Rich Transmembrane Protein 3 (FLRT3) in Tissue homogenates, cell lysates and other biological fluids. (aquaporins.org)
  • Known also as Fibronectin Leucine Rich Transmembrane Protein 3 elisa. (aquaporins.org)
  • show that transport of water in leaves (hydraulic conductivity) also follows circadian patterns, and that these patterns are in part driven by post-translational modifications of the aquaporin channel protein AtPIP2;1. (plantae.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)
  • The purpose of this study was to examine protein expression of renal sodium chloride and urea transporters and aquaporins in hypothyroid rats (HT) with diminished urinary concentration as compared with euthyroid controls (CTL) and hypothyroid rats replaced with L-thyroxine (HT+T). Hypothyroidism was induced by aminotriazole administration. (asnjournals.org)
  • Aquaporin 5 (AQP5) is a water channel protein. (genecards.org)
  • Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). (genecards.org)
  • AQP5 (Aquaporin 5) is a Protein Coding gene. (genecards.org)
  • GeNorm identified transferrin receptor ( Tfrc ) and microglobulin beta-2 ( B2m ) the most stable genes followed by ribosomal protein L19 ( Rpl19 ) whereas β-actin ( ActB ) and glyceraldehyde-3-phosphate-dehydrogenase ( Gapdh ) the most fluctuated ones in these neurons. (frontiersin.org)
  • [3] The gene produces a 54.1 kDa protein composed of 492 amino acids . (wikipedia.org)
  • We found no differences in A 2A R expression, 3′,5′-cyclic adenosine monophosphate abundance, or protein kinase A type 1 activity between HNSCC and HD CD8 + T cells. (sciencemag.org)
  • Aquaporin-11: a channel protein lacking apparent transport function expressed in brain. (ebi.ac.uk)
  • This includes the production of a harmful antibody that targets a protein called aquaporin-4 (AQP4). (roche.com)
  • Rabbit polyclonal Aquaporin 3 antibody. (abcam.com)
  • We have used a peptide-derived, affinity-purified polyclonal antibody to aquaporin-3 (AQP-3) to investigate its localization and regulation in the kidney. (sigmaaldrich.com)
  • Primary antibody: Anti-Aquaporin 3 (275-292) Rabbit pAb (Cat. (emdmillipore.com)
  • Reconstituted antibody contains phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.05% NaN 3 . (alomone.com)
  • 1. Anti-Aquaporin 3 Antibody (#AQP-003), (1:200). (alomone.com)
  • 2. Anti-Aquaporin 3 Antibody, preincubated with the negative control antigen. (alomone.com)
  • Diluted antibody solution can be used 2 to 3 times within one month if it contains 0.1 % sodium azide as preservative and is stored at -20ºC to -80ºC. (agrisera.com)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Myosin Heavy Chain 3, Skeletal Muscle, Embryonic (MYH3) in Tissue homogenates and other biological fluids. (aquaporins.org)
  • There are currently no images for Aquaporin-7 Antibody (NBP1-30862). (novusbio.com)
  • Aquaporins (AQPs) are integral membrane proteins that form pores in the membrane of biological cells. (cosmeticsandtoiletries.com)
  • AQPs 3, 7, 9 and 10, termed aquaglyceroporins, transport water as well as glycerol and possibly other small solutes. (cosmeticsandtoiletries.com)
  • Aquaporins (Aqps) are a superfamily of integral membrane proteins which generally facilitate the permeation of water through plasma membranes. (frontiersin.org)
  • By reverse transcriptase-polymerase chain reaction analysis, expression of AQPs 1, 3, and 5 was found in seven colon and colorectal cancer cell lines. (nature.com)
  • Of the five AQPs examined, AQPs 1, 3, and 5 were expressed in all the seven cell lines ( Figure 1a ). (nature.com)
  • Western blot analysis demonstrated that AQPs 1, 3, and 5 were expressed concurrently in all four of the tested cancer cell lines ( Figure 1b ), confirming our RT-PCR results. (nature.com)
  • Expression of AQPs 1, 3, and 5 in seven colon and colorectal cancer cell lines. (nature.com)
  • Aquaporins (AQPs) are members of the aquaporin water channel family that play an important role in reabsorption of water from the renal tubular fluid to concentrate urine . (bvsalud.org)
  • Aquaporins (AQPs) are integral membrane proteins that facilitate the transport of water across biological membranes along an osmotic gradient. (genecards.org)
  • The aquaporins (AQPs) are small integral membrane proteins that transport water and in some cases small solutes such as glycerol. (springer.com)
  • The aquaporins (AQPs) are a family of water-transporting channels that are expressed widely in mammalian fluid-transporting epithelia and endothelia. (arvojournals.org)
  • 1 2 3 4 5 6 Because of this expression pattern, it has been proposed that AQPs play a role in intraocular pressure regulation, corneal and lens transparency, and vision. (arvojournals.org)
  • 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)
  • STUDY HYPOTHESIS Are the placental aquaporins (AQPs) involved in the apoptosis of human trophoblast? (semanticscholar.org)
  • Suberoylanilide hydroxamic acid (SAHA) (a HDAC inhibitor) increases expression of aquaporin-3 in normal skin cells (keratinocytes). (wikipedia.org)
  • These studies are consistent with a role for AQP-3 in osmotically driven water absorption across the collecting duct epithelium and suggest that the expression of AQP-3 is regulated on a long-term basis. (sigmaaldrich.com)
  • Aquaporin (AQP) 3 expression is altered in inflammatory bowel diseases, although the exact mechanisms regulating AQP abundance are unclear. (springer.com)
  • 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)
  • EGFR-mediated expression of aquaporin-3 is involved in human s. (mysciencework.com)
  • Expression of aquaporin-5 (AQP5), studied by immunofluorescence and confocal microscopy, showed an increase in parallel with the increase in P f following hyperosmotic stress. (springer.com)
  • Bellemere G, Von Stetten O, Oddos T (2008) Retinoic acid increases aquaporin 3 expression in normal human skin. (springer.com)
  • Boury-Jamot M, Sougrat R, Tailhardat M, Le Varlet B, Bonte F, Dumas M, Verbavatz JM (2006) Expression and function of aquaporins in human skin: Is aquaporin-3 just a glycerol transporter? (springer.com)
  • A versatile aquaporin-2 cell system for quantitative temporal expression and live cell imaging. (nih.gov)
  • Systemic LPS induces toll-like receptor 3 (TLR3) expression and apoptosis in testicular mouse tissue. (nih.gov)
  • Gene expression is controlled by transcriptional regulatory proteins, which bind specific DNA sequences and recruit cofactors and the transcription apparatus to promoters ( 1 - 3 ). (sciencemag.org)
  • Expression, localization, and regulation of aquaporin-1 to -3 in rat urothelia. (findaphd.com)
  • Expression and localisation of aquaporin water channels in human urothelium in situ and in vitro. (findaphd.com)
  • Aberrant expression of aquaporin-3 in hereditary papulotranslucent acrokeratoderma and aquagenic palmoplantar keratoderma. (pubfacts.com)
  • Background: The immunohistochemical expression of aquaporin-1 (AQP1) in asbestos-related malignant pleural mesothelioma (MPM) is emerging as a useful prognostic indicator of improved survival. (mdpi.com)
  • Angelico G, Caltabiano R, Loreto C, Ieni A, Tuccari G, Ledda C, Rapisarda V. Immunohistochemical Expression of Aquaporin-1 in Fluoro-Edenite-Induced Malignant Mesothelioma: A Preliminary Report. (mdpi.com)
  • Immunocytochemistry showed strong aquaporin (AQP)-4 water channel expression in Müller cells in mouse retina and fibrous astrocytes in optic nerve. (arvojournals.org)
  • Reduced expression of Na⁺/H⁺ exchanger isoform 3 (NHE-3) in preeclamptic placentas. (semanticscholar.org)
  • Decreased aquaporin expression leads to increased resistance to apoptosis in hepatocellular carcinoma. (semanticscholar.org)
  • However, for some proteins, including Aquaporin 1 (AQP1), the folding appears to follow a more complicated path. (abo.fi)
  • For example, p f for human aquaporin-1 (AQP1) ranges from 1 × 10 −14 to 16 × 10 −14 cm 3 s −1 ( 5 ). (sciencemag.org)
  • We investigated the supporting role of 14-3-3 proteins, which are known to interact with and regulate phosphorylated proteins. (plantcell.org)
  • Below: Immunospecificity of anti.PIP1;3 antibodies to recombinant PIP proteins expressed in yeast cells. (agrisera.com)
  • Aquaporins are a family of membrane proteins that provide channels for the rapid movement of water molecules and some small solutes across the cellular membrane. (georgiasouthern.edu)
  • Benga G (2009) Water channel proteins (later called aquaporins) and relatives: past, present, and future. (springer.com)
  • These clock-driven cycles of phosphorylation / dephosphorylation may affect interactions with 14-3-3 proteins. (plantae.org)
  • Aquaporins are an ancient family of proteins that provide a route for water to rapidly move in and out of cells in response to the changing needs of the body. (findaphd.com)
  • Aquaporins are channel producing proteins which regulate the flow of water across the cell membrane. (proteopedia.org)
  • AQP11 is functionally distinct from other proteins of the aquaporin superfamily and could represent a new aquaporin subfamily [ PMID: 16650285 ]. (ebi.ac.uk)
  • Anti-Aquaporin 3 (275-292), rabbit polyclonal, recognizes the ~40 and ~29 kDa forms of aquaporin-3 in rat kidney membrane. (emdmillipore.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). (abcam.com)
  • AQP-2 and -3 circumferentially lined the epithelial cell membranes except for the apical membrane of the epithelial cells adjacent to the lumens of both ureter and bladder. (antibodybeyond.com)
  • PIP1;3 is a plasma membrane aquaporine which facilitates trasport of water across cell membrane. (agrisera.com)
  • Regulation of Plasma Membrane Nanodomains of the Water Channel Aquaporin-3 Revealed by Fixed and Live Photoactivated Localization Microscopy. (nih.gov)
  • Here, we propose a mechanism for how this reorientation could be initiated: first, helix 3 slides out from the membrane core resulting in that the preceding loop enters the membrane. (abo.fi)
  • The final conformation could then be formed as helix 2, 3, and 4 are inserted into the membrane and the reentrant regions come together. (abo.fi)
  • We find support for the first step in this process by showing that the loop preceding helix 3 can insert into the membrane. (abo.fi)
  • Further, hydrophobicity curves, experimentally measured insertion efficiencies and MD-simulations suggest that the barrier between these two hydrophobic regions is relatively low, supporting the idea that helix 3 can slide out of the membrane core, initiating the rearrangement process. (abo.fi)
  • We obtained high-precision p f values by (i) having measured the abundance of the reconstituted aquaporins in the vesicular membrane via fluorescence correlation spectroscopy and via high-speed atomic force microscopy, and (ii) having acquired the vesicular water efflux from scattered light intensities via our new adaptation of the Rayleigh-Gans-Debye equation. (sciencemag.org)
  • Plasma membrane aquaporin activity can affect the rate of apoptosis but is inhibited after apoptotic volume decrease. (semanticscholar.org)
  • AQP 11 and 12 appear to be more distantly related to the other mammalian aquaporins and aquaglyceroporins. (ebi.ac.uk)
  • One year later, a Chesebrough-Ponds patent 6 disclosing cosmetic compositions containing phytovitamin D 3 contained a discussion of keratinocytes, which constitute 75-80% of the total number of cells in the human epidermis. (cosmeticsandtoiletries.com)
  • Aquaporin-3 water channel localization and regulation in rat kidney. (sigmaaldrich.com)
  • 2008). Tissue and cell-specific localization of rice aquaporins and their water transport activities- Plant Cell Physiol. (agrisera.com)
  • RESUMEN Las acuaporinas (AQP) son miembros de las proteínas de transporte que desempeñan un papel importante en la reabsorción de agua del líquido tubular renal para concentrar la orina . (bvsalud.org)
  • Long-term regulation of four renal aquaporins in rats. (findaphd.com)
  • Body water homeostasis is tightly regulated through the coordinated function of aquaporin (Aqp) that is expressed in the renal tubular cells. (asm.org)
  • What are the 3 parts of the renal tubule? (brainscape.com)
  • Subcellular fractionation of membranes, using progressively higher centrifugation speeds, revealed that AQP-3 is present predominantly in the 4,000 and 17,000 g pellets and, in contrast to AQP-2, is virtually absent in the high-speed (200,000 g) pellet that contains small intracellular vesicles. (sigmaaldrich.com)
  • Aquaporins facilitate the transport of water and small neutral solutes across cell membranes. (cusabio.com)
  • Membranes were washed 5 times with TBS-T, each time in a fresh polystyrene box and probed with anti-PIPs1;3 antibodies (AS09 504, 1:1000 , 1h) and secondary anti-rabbit ( 1:2000, 1 h). (agrisera.com)
  • [3] One good source of GLUT1 is erythrocyte membranes. (wikipedia.org)
  • Skin dryness alters the ability of epithelial cells to migrate and cover the wound site and reduces the supply of white blood cells and nutrients, which are essentials to form new tissues and protect skin against infections [ 3 ]. (hindawi.com)
  • Hara-Chikuma, M & Verkman, AS 2008, ' Aquaporin-3 facilitates epidermal cell migration and proliferation during wound healing ', Journal of Molecular Medicine , vol. 86, no. 2, pp. 221-231. (elsevier.com)
  • Here, I will summarize our current knowledge of the involvement of aquaporin-formed pores and tight junctions in epidermal water homeostasis - as well as in other functions - and their putative roles in skin dryness. (springer.com)
  • Epidermal aquaporin-3 is increased in the cutaneous burn wound. (hopkinsmedicine.org)
  • [email protected]#To investigate the mechanism of cAMP-PKA signaling pathway mediated by Chinese medicine formula Shaoyao Gancao Decoction (, SGD) on the regulation of aquaporin 5 (AQP5) and muscarinic receptor 3 (M3R) levels in Sjögren's syndrome (SS). (bvsalud.org)
  • Aquaporin 7 facilitates water, glycerol and urea transport. (novusbio.com)
  • There are also roles for other water channels, including aquaporins 1, 3, and 4, and for urea transporters in urinary concentration. (asnjournals.org)
  • Humans have 13 different aquaporins that allow water to pass at different speeds and have different selectivity behaviour (e.g. for glycerol and urea). (findaphd.com)
  • Bollag WB, Xie D, Zheng X, Zhong X (2007) A potential role for the phospholipase D2-aquaporin-3 signaling module in early keratinocyte differentiation: production of a phosphatidylglycerol signaling lipid. (springer.com)
  • Vasopressin-Independent Regulation of Aquaporin-2 by Tamoxifen in Kidney Collecting Ducts. (nih.gov)
  • Regulation of aquaporin-2gene transcription by gate-3. (nii.ac.jp)
  • Avp is an antidiuretic hormone secreted from the hypothalamic neurons, and the primary target of the Avp signaling for urine volume regulation is Aqp2 ( 2 , 3 , 4 ). (asm.org)
  • Association of the Aquaporin 3 Gene Polymorphism (rs2231231) with Epstein-Barr Virus-Associated Cancers in China. (cdc.gov)
  • Da T, Verkman AS (2004) Aquaporin-4 gene disruption in mice protects against impaired retinal function and cell death after ischemia. (springer.com)
  • Predicted molecular weight: 32 kDa.Can be blocked with Aquaporin 3 peptide (ab80550) . (abcam.com)
  • 3. How are aquaporins regulated in the cell and by what molecular partners? (findaphd.com)
  • Agre P, Kozono D. Aquaporin water channels: molecular mechanisms for human diseases. (proteopedia.org)
  • J Dtsch Dermatol Ges 2018 Mar 30;16(3):360-363. (pubfacts.com)
  • A synthetic peptide corresponding to a sequence at the C-terminus of human Aquaporin 3(278-292aa EENVKLAHVKHKEQI), different from the related rat and mouse sequences by one amino acid. (bosterbio.com)
  • the predominant aquaporin in human skin. (antibodybeyond.com)
  • We have recently developed isolated whole bladder models which have proved to be valuable alternatives to human bladder for elucidating physiological functions (1 &3 see above). (findaphd.com)
  • 3. The method according to claim 1, wherein the mammal subject is a human. (freepatentsonline.com)
  • and (3) to utilize the validated human trophoblast markers to identify subgroups of human preeclampsia. (mcponline.org)
  • Agren J, Zelenin S, Hakansson M, Eklof AC, Aperia A, Nejsum LN, Nielsen S, Sedin G (2003) Transepidermal water loss in developing rats: role of aquaporins in the immature skin. (springer.com)
  • AQP-3 may play an important functional role in osmoregulation the teleostean gill but is unlikely to be responsible for the increases in intestinal water absorption that occur following SW acclimation. (antibodybeyond.com)
  • published ahead of print January 3, 2017. (pnas.org)
  • G Ital Dermatol Venereol 2017 06 15;152(3):317-318. (pubfacts.com)
  • The circadian fluctuations in aquaporin transcript abundance suggest that aquaporin water channels play a role in these processes. (plantcell.org)
  • These components during fluid deprivation include release of the antidiuretic hormone, arginine vasopressin (AVP), and upregulation of the abundance of aquaporin-2 (AQP2) water channels in the principal cells of the collecting duct. (asnjournals.org)
  • This is supported by the fact that the bladder urothelium expresses the transmembrane water channels (aquaporins). (findaphd.com)
  • Aquaporins are widely expressed in a variety of cancers and were found to play an important role in cell migration, angiogenesis, tumor formation, and tumor development. (cdc.gov)
  • tumor antigen TAL6, aquaporin 3 etc. (aacrjournals.org)
  • In many solid malignancies, including head and neck squamous cell carcinoma (HNSCC), an increased infiltration of cytotoxic CD8 + T cells into the tumor mass is often associated with good prognosis and response to therapy ( 1 - 3 ). (sciencemag.org)
  • Aquaporins differentially regulate cell-cell adhesion in MDCK cells. (nih.gov)
  • Immunolocalisation of aquaporin 3 in the gill and the gastrointestinal tract of the European eel Anguilla anguilla (L. (nii.ac.jp)
  • Aquaporin 3 is, in addition to being a water channel, also an arsenic transporter. (alzforum.org)
  • These findings demonstrate a decrease in the medullary osmotic gradient secondary to impaired countercurrent multiplication and downregulation of aquaporins 2, 3, and 4 as contributors to the urinary concentrating defect in the hypothyroid rat. (asnjournals.org)
  • Aquaporin 5 plays a role in the generation of saliva, tears and pulmonary secretions. (genecards.org)
  • The aim is to investigate the physiological role of aquaporins and vasopressin receptors in porcine and rat urinary bladders. (findaphd.com)
  • 3 Studies of brain edema in AQP4-null mice implied an important role for AQP4 in fluid balance, 20 supporting the possibility that AQP4 may participate in the maintenance of retinal water balance during synaptic transmission and retinal edema. (arvojournals.org)
  • Placental programmed cell death: insights into the role of aquaporins. (semanticscholar.org)
  • Water movement during apoptosis: a role for aquaporins in the apoptotic volume decrease (AVD). (semanticscholar.org)
  • Among its related pathways are Aquaporin-mediated transport and Nanog in Mammalian ESC Pluripotency . (genecards.org)
  • This type of aquaporin transports not only water but also neutral solutes, including cell-permeating cryoprotectants. (antibodybeyond.com)
  • Bai C, Fukuda N, Song Y, Ma T, Matthay MA, Verkman AS (1999) Lung fluid transport in aquaporin-1 and aquaporin-4 knockout mice. (springer.com)
  • Belongs to the MIP/aquaporin (TC 1.A.8) family. (abcam.com)
  • The aquaporins are a family of water channels expressed in several water-transporting tissues, including the kidney. (sigmaaldrich.com)
  • This study will allow us to better understand the bladder function under physiological and pathological conditions and to validate aquaporins as targets for the treatment of UI and nocturia. (findaphd.com)
  • Understanding the basic mechanisms controlling how aquaporins function could lead to new medicine for many problems including the devastating effects of brain swelling and a number of other disorders. (findaphd.com)
  • Aquaporin-2 function is to reabsorb water from urine in the kidney. (proteopedia.org)
  • Mutations in HNF1α and HNF4α are the causes of the type 3 and type 1 forms of maturity-onset diabetes of the young (MODY3 and MODY1), a genetic disorder of the insulin-secreting pancreatic beta cells characterized by the onset of diabetes mellitus before 25 years of age and an autosomal dominant pattern of inheritance ( 19 ). (sciencemag.org)
  • Mutations in aquaporin-2 cause diabitis insipidus. (proteopedia.org)
  • Mutations in aquaporin-0 in mice cause congenital cataracts. (proteopedia.org)