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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

AQP2 is found in the apical cell membranes of the kidneys collecting duct principal cells and in intracellular vesicles located throughout the cell. It is the only aquaporin regulated by vasopressin. The basic job of aquaporin 2 is to reabsorb water from the urine while its being removed from the blood by the kidney. Aquaporin 2 is in kidney epithelial cells and usually lies dormant in intracellular vesicle membranes. When it is needed, vasopressin binds to the cell surface vasopressin receptor thereby activating a signaling pathway that causes the aquaporin 2 containing vesicles to fuse with the plasma membrane, so the aquaporin 2 can be used by the cell. This aquaporin is regulated in two ways by the peptide hormone vasopressin: short-term regulation (minutes) through trafficking of AQP2 vesicles to the apical region where they fuse with the apical plasma membrane long-term regulation (days) through an increase in AQP2 gene expression. This aquaporin is also regulated by food intake. Fasting ...
Vasopressin is the key regulator of water homeostasis in vertebrates. Central to its antidiuretic action in mammals is the redistribution of the water channel aquaporin 2 (AQP2) from intracellular vesicles to the apical membrane of kidney epithelial cells, an event initiated by an increase in cAMP and activation of protein kinase A. The subsequent steps of the signaling cascade are not known. To identify proteins involved in the AQP2 shuttle we exploited a recently developed cell line (CD8) derived from the rabbit cortical collecting duct and stably transfected with rat AQP2 cDNA. Treatment of CD8 cells with pertussis toxin (PTX) inhibited both the vasopressin-induced increase in water permeability and the redistribution of AQP2 from an intracellular compartment to the apical membrane. ADP-ribosylation studies revealed the presence of at least two major PTX substrates. Correspondingly, two alpha subunits of PTX-sensitive G proteins, Galphai2 and Galphai3, were identified by Western blotting.
With Aquaporin Inside™ Reverse Osmosis membranes, water treatment can be done with lower energy consumption compared to conventional membrane technology. The benefit comes from the aquaporin proteins which are very efficient in transporting water. This enables the water treatment plant to increase the capacity of treated wastewater without increasing the energy consumption, or remaining at the same capacity level while lowering the energy consumption. At the same time, Aquaporin membranes has the potential to remove also small, neutral compounds such as micro pollutants/trace organics, improving re-use water quality.. Aquaporin Inside™ Forward Osmosis ...
Plasma Membrane Abundance of Human Aquaporin 5 Is Dynamically Regulated by Multiple Pathways. . Biblioteca virtual para leer y descargar libros, documentos, trabajos y tesis universitarias en PDF. Material universiario, documentación y tareas realizadas por universitarios en nuestra biblioteca. Para descargar gratis y para leer online.
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 ...
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.
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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. ...
Description: FLRT3 produced in Sf9 insect cells is a single, glycosylated polypeptide chain containing 508 amino acids (29-528a.a.) and having a molecular mass of 57.6kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).;FLRT3 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques ...
Hypertrophic cardiac myocytes, which are larger than normal, have more cytoplasm and larger nuclei than normal cells. The enlarged nuclei contain more DNA and RNA than their normal counterparts and generate more messenger RNA. The cytoplasm of hypertrophic myocytes contains more myofilaments and mitochondria, but the number of other cytoplasmic organelles is not increased. Water influx, which is typical of hydropic swelling, is not found in hypertrophy. ...
Aqp4 - Aqp4 (untagged) - Mouse aquaporin 4 (cDNA clone MGC:37514 IMAGE:4985265), (10ug) available for purchase from OriGene - Your Gene Company.
TY - JOUR. T1 - 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, ...
Purpose: The expression of aquaporin water channel genes are shown to be affected in several pathological conditions of retina, such as in diabetic retinopathy, retinal ischemia and in autoimmune uveitis. Human native retinal pigment epithelial (RPE) cells and immortalized human RPEs are formerly shown to express aquaporins, still the expression of aquaporins in stem cell derived RPE have not been previously elucidated. The objective of this study was to determine the expression of several aquaporin genes (aquaporin1,- 3, -4, -5, -6, -7, -10, -11 and -12) and assess the localization of aquaporin 1 water channel protein in human embryonic (hESCs) and induced pluripotent stem cells (hiPSCs) derived RPE cells.. Methods: hESC- and hiPSC derived RPE cells were grown as monolayer in serum-free media. The expression of aquaporin genes was determined with qRT-PCR. The localization of AQP1-protein was studied with confocal microscopy. Finally, the functionality of aquaporins was assessed with dye ...
Aquaporin-5 is a protein that in humans is encoded by the AQP5 gene. Aquaporin 5 (AQP5) is a water channel protein. Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). Aquaporin 5 plays a role in the generation of saliva, tears and pulmonary secretions. AQP0, AQP2, AQP5, and AQP6 are closely related and all map to 12q13. Aquaporin GRCh38: Ensembl release 89: ENSG00000161798 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000044217 - Ensembl, May 2017 Human PubMed Reference:. Mouse PubMed Reference:. Lee MD, Bhakta KY, Raina S, Yonescu R, Griffin CA, Copeland NG, Gilbert DJ, Jenkins NA, Preston GM, Agre P (Jun 1996). The human Aquaporin-5 gene. Molecular characterization and chromosomal localization. J Biol Chem. 271 (15): 8599-604. doi:10.1074/jbc.271.15.8599. PMID 8621489. Entrez Gene: AQP5 aquaporin 5. Verkman AS (2003). Role of aquaporin water channels in eye function. Exp. Eye Res. 76 (2): 137-43. ...
Abstract Background and Aims Diarrhoea is a common, debilitating symptom of gastrointestinal disorders. Pathomechanisms probably involve defects in trans-epithelial water transport, but the role of aquaporin [AQP] family water channels in diarrhoea-predominant diseases is unknown. We investigated the involvement of AQPs in the pathobiology of collagenous colitis [CC], which features chronic, watery diarrhoea despite overtly normal intestinal epithelial cells [IECs]. Methods We assessed the expression of all AQP family members in mucosal samples of CC patients before and during treatment with the corticosteroid drug budesonide, steroid-refractory CC patients and healthy controls. Samples were analysed by genome-wide mRNA sequencing [RNA-seq] and quantitative real-time PCR [qPCR]. In some patients, we performed tissue microdissection followed by RNA-seq to explore the IEC-specific CC transcriptome. We determined changes in the protein levels of the lead candidates
Plant cells contain proteins that are members of the major intrinsic protein (MIP) family, an ancient family of membrane channel proteins characterized by six membrane-spanning domains and two asparagine-proline-alanine (NPA) amino acid motifs in the two halves of the protein. We recently demonstrated that [gamma]-TIP, one of the MIP homologs found in the vacuolar membrane of plant cells, is an aquaporin or water channel protein (C. Maurel, J. Reizer, J.I. Schroeder, M.J. Chrispeels [1993] EMBO J 12: 2241-2247). RD28, another MIP homolog in Arabidopsis thaliana, was first identified as being encoded by a turgor-responsive transcript. To find out if RD28 is a water channel protein, rd28 cRNA was injected into Xenopus laevis oocytes. Expression of RD28 caused a 10- to 15-fold increase in the osmotic water permeability of the oocytes, indicating that the protein creates water channels in the plasma membrane of the oocytes and is an aquaporin just like its homolog [gamma]-TIP. Although RD28 has ...
The pre-ovulatory hydration of the oocyte of marine teleosts, a unique process among vertebrates that occurs concomitantly with meiosis resumption (oocyte maturation), is a critical process for the correct development and survival of the embryo. Increasing information is available on the molecular mechanisms that control oocyte maturation in fish, but the identification of the cellular processes involved in oocyte hydration has remained long ignored. During the past few years, a number of studies have identified the major inorganic and organic osmolytes that create a transient intra-oocytic osmotic potential for hydrating the oocytes, whereas water influx was believed to occur passively. Recent work, however, has uncovered the role of a novel molecular water channel (aquaporin), designated aquaporin-1b (Aqp1b), which facilitates water permeation and resultant swelling of the oocyte. The Aqp1b belongs to a teleost-specific subfamily of water-selective aquaporins, similar to mammalian aquaporin-1 ...
Semantic Scholar extracted view of Aquaporin water channels in liver: their significance in bile formation. by Raúl Alberto Marinelli et al.
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
Author(s): Chen, Qi; Peng, Hongying; Lei, Li; Zhang, Ying; Kuang, Haibin; Cao, Yujing; Shi, Qi-Xian; Ma, Tonghui; Duan, Enkui | Abstract: In the journey from the male to female reproductive tract, mammalian sperm experience a natural osmotic decrease (e.g., in mouse, from ~415 mOsm in the cauda epididymis to ~310 mOsm in the uterine cavity). Sperm have evolved to utilize this hypotonic exposure for motility activation, meanwhile efficiently silence the negative impact of hypotonic cell swelling. Previous physiological and pharmacological studies have shown that ion channel-controlled water influx/efflux is actively involved in the process of sperm volume regulation; however, no specific sperm proteins have been found responsible for this rapid osmoadaptation. Here, we report that aquaporin3 (AQP3) is a sperm water channel in mice and humans. Aqp3-deficient sperm show normal motility activation in response to hypotonicity but display increased vulnerability to hypotonic cell swelling, characterized by
TY - JOUR. T1 - Identification of a novel aquaporin, AQP12, expressed in pancreatic acinar cells. AU - Itoh, Tomohiro. AU - Rai, Tatemitsu. AU - Kuwahara, Michio. AU - Ko, Shigeru B.H.. AU - Uchida, Shinichi. AU - Sasaki, Sei. AU - Ishibashi, Kenichi. N1 - Funding Information: We thank N. Ozaki (Nagoya university, Japan) for his skillful technical assistance in isolation of pancreatic islet. This work was supported by grants from the Ministry of Education, Culture, Sports, Science and Technology of Japan.. PY - 2005/5/13. Y1 - 2005/5/13. N2 - Members of the aquaporin (AQP) water channel family are widely distributed in various tissues and contribute to the water permeability of epithelial and endothelial cells. Currently 11 members of the AQP family (AQP0-10) have been reported in mammals. Here we report the identification of AQP12, which we found by performing a BLAST program search. Northern blot analysis revealed that AQP12 was specifically expressed in the pancreas. Further analysis by in ...
Aquaporins (AQPs) are membrane proteins that enable water transport across cellular plasma membranes in response to osmotic gradients. Phenotypic analyses have revealed important physiological roles for AQPs, and the potential for AQP water channel modulators in various disease states has been proposed. For example, AQP1 is overexpressed in tumor microvessels, and this correlates with higher metastatic potential and aggressiveness of the malignancy. Chemical modulators would help in identifying the precise contribution of water channel activity in these disease states. These inhibitors would also be important therapeutically, e.g., in anti-cancer treatment. This perceived importance contrasts with the lack of success of high-throughput screens (HTS) to identify effective and specific inhibitors of aquaporins. In this paper, we have screened a library of 1500
Aquaporin (AQP) 6 belongs to the aquaporin water channel family. Unlike other aquaporins, AQP6 functions not as a water channel but as an anion-selective channel. Single-channel analyses have shown AQP6 to flicker rapidly ...
Aquaporin (AQP) 6 belongs to the aquaporin water channel family. Unlike other aquaporins, AQP6 functions not as a water channel but as an anion-selective channel. Single-channel analyses have shown AQP6 to flicker rapidly ...
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
Aquaporin 8 (AQP8) is a water channel protein. Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). Aquaporin 8 mRNA is found in pancreas and colon but not other tissues. [provided by RefSeq, Jul 2008 ...
Purpose: : To demonstrate in the conjunctiva the presence of aquaporin type 5 (AQP5), a water channel homologue found in the apical membrane of several tissues including the cornea. Presently, there are no reports indicating as to which AQP might be expressed apically in the conjunctiva; only AQP3 has been identified in the lateral membranes of rat and human conjunctival epithelia. Because we had data from gene-expression microarray assays (Turner; ARVO 2004) indicating message for AQP5 in the human conjunctiva, tissue samples from human, as well as from rats and rabbits (given the ease of their procurement), were analyzed to confirm that the AQP5 protein was indeed expressed in mammalian conjunctivae. Methods: : Goat polyclonal IgG against AQP5 was purchased commercially and used in immunoblotting and immunohistochemical techniques to identify and localize the water channel in rat, rabbit and human epithelia. Results: : Immunoblot analysis of rabbit bulbar-plus-palpebral plasma membrane ...
Aquaporin A/S is a global cleantech company located in Kongens Lyngby, Denmark. Aquaporin is dedicated to revolutionizing water purification through the use of industrial biotechn
Peptides , Phosphopeptides , Aquaporin-2 (254-267), pSER261, human; This peptide is a fragment of the human aquaporin-2 (AQP2) phosphorylated at Ser261. Protein phosphorylation plays a key role in vasopressin signaling in renal-collecting duct. Phosphorylation at several AQP2 residues including Ser256 and Ser261, is altered in response to vasopressin. It is possible that both sites are involved in vasopressin-dependent AQP2 trafficking.; RQSVELH-pS-PQSLPR; H-Arg-Gln-Ser-Val-Glu-Leu-His-pSer-Pro-Gln- Ser-Leu-Pro-Arg-OH
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 ...
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 ...
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 ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
collections, groups of modules structured into books or course notes, or for other uses. Our open license allows for free use and reuse of all our content. ...
Significant progress in the understanding of imaging conditions and the interpretation of topographs recorded with the AFM has allowed the surface topography of bacteriorhodopsin to be correlated with the helixconnecting loops to a lateral resolution of 5 Å (Müller et al., 1999b). Here we have used this technology to study the surface of AqpZ, the first bacterial water channel identified (Calamita et al., 1995). Its overexpression, isolation and 2D crystallization have recently been described (Borgnia et al., 1999; Ringler et al., 1999).. 2D crystals adsorbed firmly and without folds or wrinkles to freshly cleaved mica in a high ionic strength buffer (Müller et al., 1997). Subsequent change to a buffer adjusted to compensate for van der Waals interactions allowed their height to be measured accurately (Müller and Engel, 1997). The result, 57 ± 4 Å, compares favorably with the height previously reported for AQP1, 58 ± 3 Å (Walz et al., 1996).. The p4212 crystals of AqpZ with unit cell ...
Marinelli RA, Pham L, Agre P, La Russo NF. Secretin promotes osmotic water transport in rat cholangiocytes by incresing aquaporin-1 water channels in plasma membrane. Evidence for a secretin-induced vesicular translocation of aquaporin-1. J Biol Chem 1997; 272: 12984-12988 ...
Aquaporins are a family of water channel proteins that provide a major pathway for osmotically driven water transport through cell membranes. So far, 13 aquaporin isoforms (AQP0-AQP12) have been identified in mammalian species (Verkman, 2005). AQP4, the predominant isoform in adult brain, is primarily expressed at the border between brain parenchyma and major fluid compartments, including astrocyte foot processes and glia limitans, as well as ependymal cells and subependymal astrocytes (Venero et al., 2001). The bidirectional water channel AQP4 has an important role in water homeostasis in the brain. It probably helps in the redistribution and absorption of edema fluid, because disruption of AQP4 is found to contribute to the pathophysiology of brain edema (Zador et al., 2007). AQP4 knockout markedly reduced brain swelling in mouse models of cytotoxic brain edema, whereas it significantly worsened outcome in mouse models of vasogenic brain edema (Papadopoulos and Verkman, 2007). Thus, AQP4 ...
Aquaporins are transmembrane water channel proteins present in biological plasma membranes that aid in biological water filtration processes by transporting water molecules through at high speeds, while selectively blocking out other kinds of solutes. Aquaporin Z incorporated biomimetic membranes are envisaged to overcome the problem of high pressure needed, and holds great potential for use in water purification processes, giving high flux while keeping energy consumption low. The functionality of aquaporin Z in terms of osmotic permeability might be regulated by factors such as pH, temperature, crosslinking and hydrophobic thickness of the reconstituted bilayers. Hence, we reconstituted aquaporin Z into vesicles that are made from a series of amphiphilic block copolymers PMOXA-PDMS-PMOXAs with various hydrophobic molecular weights. The osmotic permeability of aquaporin Z in these vesicles was determined through a stopped-flow spectroscopy. In addition, the temperature and pH value of the vesicle
This paper strongly supports the conclusion that AQP0 has a high permeability mode and a low permeability mode. How do these two modes differ? Available structural data on the nature of the water-filled pore through AQP1 and the glycerol facilitator suggest a possible answer. For both, water and glycerol must move through the pore by single-file diffusion. The crystal structure and molecular dynamic simulations suggest that there are multiple water molecules in the pore. There are ∼6 waters seen in the narrow constriction of the pore in the X-ray structure (Sui et al., 2001), and molecular dynamic simulations suggest that there are ∼7 or 8 water molecules moving in concert in the single-file portion of the pore (Tajkhorshid et al., 2002; Zhu et al., 2004). The lack of passage of ionic current through AQP0 and AQP1 is explained by electrostatic considerations that strongly inhibit the movement of protons into the NPA region or hydroxyls into regions flanking either side of the NPA region (de ...
Proteins that selectively transport water across the membranes of cells are recognized as important in the normal functioning of the body systems of vertebrates. There are 13 known mammalian aquaporins (AQP0 to AQP12), some of which have been shown to have unexpected cellular roles beyond transmembrane water transport. The availability of non-mammalian vertebrate animal models has the potential to provide insight into the emergence of diverse function in the aquaporins. The domesticated chicken (Gallus gallus) is the premier avian model for biological research; however, only a limited number of studies have compared chicken and mammalian aquaporins. The identification of aquaporins that share functional motifs or are expressed in the same tissues in human and chicken could allow the further functional analyses of homologous aquaporins in both species. We hypothesize that integrative analyses of protein sequences and body site expression of human, mouse, rat and chicken aquaporins has the potential to
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 ...
Aquaporins play a direct role in plant water relation under salt stress, but the effects of 5-aminolevulinic acid (ALA) on aquaporin gene expression in salt-treated plants remain unknown. This study investigated the potential effects of exogenous ALA (50 mg/dm3) on aquaporin expression levels under salt stress (75 mM NaCl) in the salt-sensitive (Jinchun No.4) and the relatively salt-tolerant cucumber (Jinyou No.1) seedlings.
We investigated the in vivo ramifications of a book aquaporin 4 (AQP4) inhibitor 2-(nicotinamide)-1,3,4-thiadiazole, TGN-020, inside a mouse style of focal cerebral ischemia using 7. research convincingly exhibited that pretreatment using the AQP4 inhibitor TGN-020 considerably reduced the quantity of mind edema connected with ischemic damage. Ischemic edema is usually thought to be initiated by influx of Na+ connected with energy failing. Higher osmolarity circumstances create the generating force for drinking water influx into cells, leading to ionic edema [17]. This early edema stage, so-called cytotoxic edema, is certainly thought to last a long time before mass leakage of drinking water into the human brain ensues, making so-called vasogenic edema [18]. AQP4 is certainly thought to play a substantial function in the real drinking water flux in both procedures. Flux through AQP4 is certainly buy 154992-24-2 bidirectional and solely reliant on osmolarity distinctions between your two spaces ...
Müller glial cells are important regulators of physiological function of retina. In a model disease of retinal inflammation and spontaneous recurrent uveitis in horses (ERU), we could show that retinal Müller glial cells significantly change potassium and water channel protein expression during autoimmune pathogenesis. The most significantly changed channel protein in neuroinflammatory ERU was aquaporin 11 (AQP11). Aquaporins (AQP, 13 members) are important regulators of water and small solute transport through membranes. AQP11 is an unorthodox member of this family and was assigned to a third group of AQPs because of its difference in amino acid sequence (conserved sequence is only 11 %) and especially its largely unknown function. In order to gain insight into the distribution, localization, and function of AQP11 in the retina, we first developed a novel monoclonal antibody for AQP11 enabling quantification, localization, and functional studies. In the horse retina, AQP11 was exclusively expressed
Background: Aquaporins are integral membrane proteins that facilitate the transport of water and small solutes across cell membranes. These proteins are vital for maintaining water homeostasis in living organisms. In mammals, thirteen aquaporins (AQP0-12) have been characterized, but in lower vertebrates, such as fish, the diversity, structure and substrate specificity of these membrane channel proteins are largely unknown. Results: The screening and isolation of transcripts from the zebrafish (Danio rerio) genome revealed eighteen sequences structurally related to the four subfamilies of tetrapod aquaporins, i.e., aquaporins (AQP0, -1 and -4), water and glycerol transporters or aquaglyceroporins (Glps; AQP3 and AQP7-10), a water and urea transporter (AQP8), and two unorthodox aquaporins (AQP11 and -12). Phylogenetic analyses of nucleotide and deduced amino acid sequences demonstrated dual paralogy between teleost and human aquaporins. Three of the duplicated zebrafish isoforms have unlinked ...
After producing a recombinant form of AqpZ in E. coli, the proteins were crystallized--capturing five water molecules inside--and then analyzed by state-of-the-art high-resolution X-ray diffraction techniques. The architecture of aquaporin Z is typical of aquaporins, with a spiral of eight oxygens providing water-binding sites inside the channel. The outer membrane and cytoplasmic ends of the channel are wider than the interior, which is long and narrow. This structure demonstrates that aquaporin selectivity arises in part from erecting a physical barrier: small molecules, like water, can easily pass, but larger ones simply cant fit. And the strategic positioning of amino acid residues with hydrophilic or hydrophobic properties along the channel helps police the influx of molecules based on their affinity for water. While it seems two amino acid chains located in the middle of the channel also provide a water-friendly surface, Stroud et al. say they play a more intriguing role. Noting that the ...
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 ...
Aquaporin (AQP) proteins comprise a group of membrane intrinsic proteins (MIPs) that are responsible for transporting water and other small molecules, which is crucial for plant survival under stress conditions including salt stress. Despite the vital role of AQPs, little is known about them in cucumber (Cucumis sativus L.). In this study, we identified 39 aquaporin-encoding genes in cucumber that were separated by phylogenetic analysis into five sub-families (PIP, TIP, NIP, SIP, and XIP). Their substrate specificity was then assessed based on key amino acid residues such as the aromatic/Arginine (ar/R) selectivity filter, Frogers positions, and specificity-determining positions. The putative cis-regulatory motifs available in the promoter region of each AQP gene were analyzed and results revealed that their promoter regions contain many abiotic related cis-regulatory elements. Furthermore, analysis of previously released RNA-seq data revealed tissue- and treatment-specific expression patterns of
I think it will be found that aquaporin 3 will be the item of interest (1).. Aquaporin 3 is found in normal skeletal myofibres (2).. I suspect it will be found that the problem is not a mutation, but something interfering with the normal proper function of the aqp3 channels.. Aquaporin 3 is, in addition to being a water channel, also an arsenic transporter.. Arsenic has been implicated in Alzheimers in at least a few instances. For example, this statement appears in Reference 3 below:. Arsenic can induce apoptosis in cortical neurons of rats. This process is based on the activation of JNK3 and p38 MAPK by arsenic...[which] can activate p38 MAPK and JNK3..... And the title of the last paper speaks for itself: Arsenic exposure may be a risk factor for Alzheimers disease.. ...
TY - JOUR. T1 - An experimental study on water transport through the membrane of a PEFC operating in the dead-end mode. AU - Lee, Yongtaek. AU - Kim, Bosung. AU - Kim, Yongchan. N1 - Funding Information: This work was supported by a grant (No. R01-2006-000-11014-0) from the Basic Research Program of the Korea Science & Engineering Foundation. PY - 2009/9. Y1 - 2009/9. N2 - Water transport through the membrane of a polymer electrolyte fuel cell (PEFC) was investigated by not only measuring the voltage variation but also visualizing the accumulation of water at the anode for various values of operating parameters, such as the humidity, current density, stoichiometry, location of humidification, and membrane properties. The PEFC was operated in the dead-end mode to prevent the discharge of water from the anode. The water transport in the PEFC was characterized by the elapsed time for the voltage to reach its limit. Anode visualization showed water transport under various conditions. In addition, ...
S6 - Northeastern. This pod is released every hour at past 20 and 50. It travels a very big distance and it is a really long trip. It goes very far in East, close to Linden Village. It exits Snowlands very fast. It goes North, through Tethis sim, where is located the highest mountain of Sansara (see Altitude for details). There are a few other very high mountains in this sim and nearby places. Then, it follows the tundra to East, close to the border with endless snow-coverd land. Then, close to Clarksberg, it changes route to North-East. This road connects a group of long islands. Water channels are to left and to rignt. Altitude is not too high, but land is never complete flat. It is up to your imagination to decide if these channels are rivers or straights of salt, oceanic water. The high number of bridges is to be noted. Then, the pod makes a small stop at Waterhead infohub. This is a good place to meet people, since it is one of the most active of all infohubs, but also a very good place to ...
Using PLIF to analyse water channel simulations of turbulent diffusion in the atmospheric boundary layer A. Butet METEO-FRANCE CNRM/GMEI/SPEA,...
Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
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.
Free ground shippingShips directly from Da-Lite within 4-5 business days Whats Included? 1 Da-Lite UTB Contour Fixed-Frame Projection Screen 58x136.5 viewable area - 148 Diag / 2.35:1 Cinemascope format Extruded aluminum frame with 0.25 wide bezel Black, acid etch finish on frame and bezel Wall hanging bracket(s)
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 ...
E. M. Müller, J. S. Hub, H. Grubmüller, and B. L. de Groot (2008). "Is TEA an inhibitor for human Aquaporin-1?" Pflügers Arch. ... It has also been reported that TEA inhibits aquaporin (APQ) channels, but this still seems to be a disputed issue. A partial ... doi:10.1002/9780470132470.ch36 G. W. Parshall "Tetraethylammonium Trichlorogermanate(1−) and Trichlorostannate(1−)" Inorganic ...
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 ...
Defines the Diego Blood Group; Aquaporin 1 - water transporter, defines the Colton Blood Group; Glut1 - glucose and L- ... 6-1 Uptake and Delivery of the Respiratory Gasses". In Brobeck, John R., PhD, M.D. (ed.). Best & Taylor's Physiological basis ... Kesava, Shobana (1 September 2007). "Red blood cells do more than just carry oxygen; New findings by NUS team show they ... 135 (1-3): 14-8. doi:10.1016/j.bpc.2008.02.015. PMID 18394774.CS1 maint: uses authors parameter (link) Hempelmann E, Götze O ( ...
Evidence for a secretin-induced vesicular translocation of aquaporin-1". The Journal of Biological Chemistry. 272 (20): 12984-8 ... translocation of aquaporin 2, or both are found. It has been suggested that "Secretin as a neurosecretory hormone from the ... "Secretin promotes osmotic water transport in rat cholangiocytes by increasing aquaporin-1 water channels in plasma membrane. ... 127 (1): 43-54. doi:10.1002/ijc.25028. PMID 19904746. S2CID 2789418. Lee LT, Tan-Un KC, Pang RT, Lam DT, Chow BK (2004). " ...
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 ...
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". Retrieved 2015- ... 542 (1): 3-16. doi:10.1113/jphysiol.2002.020818. PMC 2290382. PMID 12096044. "Structure of the rhodopsin dimer: a working model ...
... some aquaporins, some AMPA receptors, as well as some enzymes. Ion-exchange chromatography is useful for isolating specific ... "Heterotetrameric Composition of Aquaporin-4 Water Channels". Biochemistry. 38 (34): 11156-63. doi:10.1021/bi990941s. PMID ... 426 (1): 199-214. doi:10.1016/j.jmb.2013.09.016. PMC 4047826. PMID 24056174. Howarth, Mark; Chinnapen, Daniel J-F; Gerrow, ... Warren, M. A.; Kucharski, L. M.; Veenstra, A.; Shi, L.; Grulich, P. F.; Maguire, M. E. (1 July 2004). "The CorA Mg2+ ...
"Aquaporin-1 promotes angiogenesis, fibrosis, and portal hypertension through mechanisms dependent on osmotically sensitive ... 70 (1): 36-45. doi:10.1158/0008-5472.CAN-09-3153. PMID 20028859. Schotte D, Chau JC, Sylvester G, Liu G, Chen C, van der Velden ... miR-708 is located on chromosome 11q14.1 and is endcoded in intron 1 of the ODZ4 gene. It is most highly expressed in the brain ...
... and aquaporin-1 in human erythrocyte membrane domains". Biochimica et Biophysica Acta (BBA) - Biomembranes. 1828 (3): 956-66. ... GLUT 1 of humans and mice have 98% identity at the amino acid level. GLUT 1 is encoded by the SLC2 gene and is one of a family ... The SLC2A1 gene is located on the p arm of chromosome 1 in position 34.2 and has 10 exons spanning 33,802 base pairs. The gene ... Glucose transporter 1 (or GLUT1), also known as solute carrier family 2, facilitated glucose transporter member 1 (SLC2A1), is ...
Horng, J.L.; Chao, P.L.; Chen, P.Y.; Shih, T.H.; Lin, L.Y. (2015). "Aquaporin 1 Is Involved in Acid Secretion by Ionocytes of ... Li, S.; Liu, J.; An, Y.; Cao, Y.; Liu, Y.; Zhang, J.; Geng, J.; Hu, T.; Yang, P. (2019). "MsPIP2;2, a novel aquaporin gene from ... 19 (1): 89. doi:10.1186/s12870-019-1674-5. PMC 6394093. PMID 30819104. Zhang, Z.Y.; Wang, W.J.; Pan, L.J.; Xu, Y.; Zhang, Z.M ... ISBN 1-58603-083-3. Yang, C.; Fang, S.; Chen, D.; Wang, J.; Liu, F.; Xia, C. (2015). "The possible role of bacterial signal ...
Shanahan, CM (1999). "Aquaporin-1 is expressed by vascular smooth muscle cells and mediates rapid water transport across ... 1999 Aquaporin-1 is expressed by vascular smooth muscle cells and mediates rapid water transport across vascular cell membranes ... doi:10.1385/1-59259-240-6:201. ISBN 1-59259-240-6. PMID 11968489. "AstraZeneca to buy CAT for £702m". May 15, ... Retrieved 1 August 2019. CS1 maint: discouraged parameter (link) Osbourn, J. K.; Watts, J. W.; Beachy, R. N.; Wilson, T. M. ( ...
Proteins found in the tonoplast (aquaporins) control the flow of water into and out of the vacuole through active transport, ... "Acceleration of vacuolar regeneration and cell growth by overexpression of an aquaporin NtTIP1;1 in tobacco BY-2 cells". Plant ... 1. pp. 295-298. doi:10.1007/3-540-33774-1_10. ISBN 978-3-540-26205-3. Brooker RJ, Widmaier EP, Graham LE, Stiling PD (2007). ... 1. World Scientific Publishing Co Pte Ltd. Thomas Boller Archived 2013-12-06 at the Wayback Machine. ...
The Co antigen is found on a protein called aquaporin-1 which is responsible for water homeostasis and urine concentration. The ... Agre P.Defective urinary-concentrating ability due to a complete deficiency of aquaporin-1. N Engl J Med. 2001 Jul 19;345(3): ... Uehlein, N., & Kaldenhoff, R. (2007). Aquaporins and Plant Leaf Movements. Annals ... ISBN 978-0-12-614445-1 Galston, A. W. (1974). Plant Photobiology in the Last Half-Century. PLANT PHYSIOLOGY, 54(4), 427-436. ... 1-4. Sage, L. C. (1992). Pigment of the Imagination: A History of Phytochrome Research. ...
Evidence for a secretin-induced vesicular translocation of aquaporin-1". The Journal of Biological Chemistry. 272 (20): 12984-8 ... translocation of aquaporin 2, or both are found.[9] It has been suggested that "Secretin as a neurosecretory hormone from the ... 90 (1-2): 47-52. doi:10.1159/000015658. PMID 11060443.. *^ 1947-, Costanzo, Linda S., (2006). Physiology (3rd ed.). ... "Secretin promotes osmotic water transport in rat cholangiocytes by increasing aquaporin-1 water channels in plasma membrane. ...
Evidence for a secretin-induced vesicular translocation of aquaporin-1" (PDF). J. Biol. Chem. 272 (20): 12984-12988. PMID ... "Secretin promotes osmotic water transport in rat cholangiocytes by increasing aquaporin-1 water channels in plasma membrane. ... 1] *↑ 3,0 3,1 Kopin AS, Wheeler MB, Leiter AB (1990). "Secretin: structure of the precursor and tissue distribution of the mRNA ... 6,0 6,1 6,2 6,3 Chu JY, Lee LT, Lai CH, Vaudry H, Chan YS, Yung WH, Chow BK (2009). "Secretin as a neurohypophysial factor ...
Aquaporin 4 in Müller cell in rats transports water to the vitreous body. The vitreous has many anatomical landmarks, including ... "Aquaporin-4 water channel protein in the rat retina and optic nerve: polarized expression in Müller cells and fibrous ... Nagelhus, EA; Veruki, ML; Torp, R; Haug, FM; Laake, JH; Nielsen, S; Agre, P; Ottersen, OP (1 April 1998). " ... 1 March 2016. Velpandian, Thirumurthy (29 February 2016). Pharmacology of Ocular Therapeutics. Springer. ISBN 9783319254982 - ...
"In vivo requirement of the alpha-syntrophin PDZ domain for the sarcolemmal localization of nNOS and aquaporin-4". J. Cell Biol ... and Aquaporin 4. GRCh38: Ensembl release 89: ENSG00000101400 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000027488 ... "Syntrophin-dependent expression and localization of Aquaporin-4 water channel protein". Proc. Natl. Acad. Sci. U.S.A. 98 (24): ... "Syntrophin-dependent expression and localization of Aquaporin-4 water channel protein". Proc. Natl. Acad. Sci. U.S.A. 98 (24): ...
Yang B, Verkman AS (September 2002). "Analysis of double knockout mice lacking aquaporin-1 and urea transporter UT-B. Evidence ... UT-1 is activated by ADH, but is a passive transporter. It reabsorbs up to 70% of the original filtered load of urea. Urea ...
Agre was recognized for his discovery of aquaporin water channels. Aquaporins are water-channel proteins that move water ... Aquaporins are "the plumbing system for cells," said Agre. Every cell is primarily water. "But the water doesn't just sit in ... Aquaporin Roderick MacKinnon Gheorghe Benga "The Nobel Prize in Chemistry 2003". Retrieved March 21, 2018. ... The 28 kDa protein is now known as aquaporin-1 (abbreviated AQP1), the archetypal member of a large family of water channel ...
Around active NMO lesions AQP4 may selectively be lost in the absence of aquaporin 1 (AQP1) loss or other structural damage ( ... 28 (1): 84-94. doi:10.1055/s-2007-1019130. PMID 18256989. Misu T, Höftberger R, Fujihara K, Wimmer I, Takai Y, Nishiyama S, ... 255 (1): 1-10. doi:10.1007/s00415-007-0754-x. PMID 18004634. S2CID 1411872. Garrido C, Levy-Gomes A, Teixeira J, Temudo T (2004 ... 183 (1-2): 168-74. doi:10.1016/j.jneuroim.2006.09.008. PMID 17084910. S2CID 41262535. Jilek S, Schluep M, Rossetti AO, et al. ( ...
Lindsay, L. A., & Murphy, C. R. (2006). Redistribution of aquaporins 1 and 5 in the rat uterus is dependent on progesterone: a ... Lindsay, L. A., & Murphy, C. R. (2004). Redistribution of aquaporins in uterine epithelial cells at the time of implantation in ... Cell Physiology, 283(1), C142-C147. Enders, A. C., & Nelson, D. M. (1973). Pinocytotic activity of the uterus of the rat. ... The Journal of membrane biology, 206(1), 17-28. Tsang, L. L., Chan, L. N., Wang, X. F., So, S. C., Yuen, J. P., Fiscus, R. R ...
Zheng X, Bollinger Bollag W (December 2003). "Aquaporin 3 colocates with phospholipase d2 in caveolin-rich membrane ... Caveolin-1 is a protein that in humans is encoded by the CAV1 gene. The scaffolding protein encoded by this gene is the main ... Caveolin 1 has been shown to interact with heterotrimeric G proteins, Src tyrosine kinases (Src, Lyn) and H-Ras,cholesterol,TGF ... 271 (1): 568-73. doi:10.1074/jbc.271.1.568. PMID 8550621. Razani B, Zhang XL, Bitzer M, von Gersdorff G, Böttinger EP, Lisanti ...
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. ... Volkov, Alexander G; Foster, Justin C; Markin, Vladislav S (1 July 2010). "Molecular electronics in pinnae of Mimosa pudica". ...
Syntrophin-dependent expression and localization of Aquaporin-4 water channel protein. vol. 98 no. 24. John D. Neely, 14108- ... 128-137 Delayed K+ clearance associated with aquaporin-4 mislocalization: Phenotypic defects in brains of α-syntrophin-null ...
The thick ascending limb of the loop of Henle is the only part of the nephron lacking in aquaporin-a common transporter protein ... The ascending limb is impermeable to water (because of a lack of aquaporin, a common transporter protein for water channels in ... due to the presence of aquaporin 1 in its tubular wall. Thus, water moves across the tubular wall into the medullary space, ...
"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. ...
To help conserve water they produce very concentrated urine, via a process apparently associated with expression of aquaporin 1 ... 117 (1): 211-213. doi:10.2307/2425723. JSTOR 2425723. Patton, J.L. (2005). "Family Heteromyidae". In Wilson, D.E.; Reeder, D.M ... 353 (353): 1-10. doi:10.2307/3504290. JSTOR 3504290. Reynolds, H. G. (February 1958). "The Ecology of the Merriam Kangaroo Rat ... Offspring remain in the mound for 1-6 more months in the maternal caches. Family Heteromyidae Subfamily Dipodomyinae Dipodomys ...
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145 (1): 426-36. doi:10.1210/en.2003-0319. PMID 14525906.. *^ Cahalan MD (Oct 2010). "Cell biology. How to STIMulate calcium ... 22 (1): 77-87. doi:10.1006/geno.1994.1347. PMID 7959794.. *. Tang S, Mikala G, Bahinski A, Yatani A, Varadi G, Schwartz A (Jun ... Click on genes, proteins and metabolites below to link to respective Wikipedia articles. [§ 1] ... 236 (1): 107-13. doi:10.1006/abio.1996.0138. PMID 8619474.. *. Soldatov NM, Zühlke RD, Bouron A, Reuter H (Feb 1997). " ...
Competitive vasopressin antagonism leads to decreased number of aquaporin channels in the apical membrane of the renal ... 1. Arginine vasopressin. receptor 2 antagonists amphotericin B, lithium[13][14]. Inhibits vasopressin's action 5. collecting ... 21 (1): 163-70. doi:10.1359/JBMR.051003. PMID 16355285.. *^ Du, Xiaoping. Diuretics Archived April 7, 2006, at the Wayback ... 978-94-009-0449-1. .. *^ Schrier, Robert W.; Gross, Peter; Gheorghiade, Mihai; Berl, Tomas; Verbalis, Joseph G.; Czerwiec, ...
Aquaporin 1 - water transporter, defines the Colton Blood Group;. *Glut1 - glucose and L-dehydroascorbic acid transporter; ... Red blood cells, also known as RBCs, red cells,[1] red blood corpuscles, haematids, erythroid cells or erythrocytes (from Greek ... R.Lipowsky and E.Sackmann, vol.1, Elsevier, 1995 *^ a b J. A. Blom (15 December 2003). Monitoring of Respiration and ... p. 1. ISBN 978-0-07-144035-6. .. *^ D'Alessandro, Angelo (2017). "Red blood cell proteomics update: is there more to discover?" ...
June 1999). "Urinary excretion of aquaporin-2 water channel differentiates psychogenic polydipsia from central diabetes ... 22 (1): 54-60. ISSN 0090-838X. PMID 15706734. Taivainen, H.; Laitinen, K.; Tähtelä, R.; Kilanmaa, K.; Välimäki, M. J. (1995-06- ... 35 (1): 65-68. doi:10.1046/j.1440-1614.2001.00847.x. ISSN 0004-8674. PMID 11270459. (subscription required) Goh, Kian Peng. " ... 2015: 1-3. doi:10.1155/2015/846459. ISSN 2090-682X. PMC 4320790 . PMID 25688318. de Leon, Jose; Verghese, Cherian; Tracy, ...
Aquaporins are protein channel pores permeable to H2O water. Reverse osmosisEdit. This section does not cite any sources. ... See Tfd›[1], ‹See Tfd›Sidney, Loeb & Sourirajan Srinivasa, "High flow porous membranes for separating water from saline ... Sidney Loeb and Srinivasa Sourirajan invented the first practical synthetic semi-permeable membrane.[1] Membranes used in ...
... it acts on proteins called aquaporins and more specifically aquaporin 2 in the following cascade. When released, ADH binds to ... Nephrogenic DI results from lack of aquaporin channels in the distal collecting duct (decreased surface expression and ... stimulating translocation of the aquaporin 2 channel stored in the cytoplasm of the distal convoluted tubules and collecting ... doi:10.1007/s11102-007-0006-1. PMID 17308961.. *^ Fujiwara TM, Bichet DG (2005). "Molecular Biology of Hereditary Diabetes ...
inositol 1,4,5 trisphosphate binding. • ion channel activity. • protein binding. • actin binding. • calcium channel activity. • ...
inositol 1,4,5-trisphosphate receptor, type 1[1]. Crystal structure of the ligand binding suppressor domain of type 1 inositol ... InsP3R-1 is the most widely expressed of these three and is found in all tissue types and all developmental stages of life. It ... December 2002). "Structure of the inositol 1,4,5-trisphosphate receptor binding core in complex with its ligand". Nature. 420 ( ... structure of the ligand binding suppressor domain of type 1 inositol 1,4,5-trisphosphate receptor 6181 Crystal structure of the ...
... highest resolution protein structure solved by electron crystallography of 2D crystals is that of the water channel aquaporin-0 ... 59 (Pt 1): 18-21. doi:10.1107/S0108767302018275. PMID 12496457.. *^ Weirich, TE (2004). "First-principles calculations as a ... 56 (Pt 1): 29-35. doi:10.1107/S0108767399009605. PMID 10874414.. *^ Zandbergen, H. W. (1997). "Structure Determination of ... ISBN 978-1-4020-3919-5. External links[edit]. *Interview with Aaron Klug Nobel Laureate for work on crystallograph electron ...
2004). „Antidiuretic action of oxytocin is associated with increased urinary excretion of aquaporin-2". Nephrology, Dialysis, ... 1]. [2]. Antidiuretski hormon (ADH) ili vazopresin je ljudski hormon, izlučevina zadnjeg režnja hipofize, zapravo nervnog ... NK1. Agonisti: Supstanca P. Antagonisti: Aprepitant • Befetupitant • Kasopitant • CI-1021 • CP-96,345 • CP-99,994 • CP-122,721 ... MCH1. Agonisti: Melanin-koncentrirajući hormon. Antagonisti: ATC-0175 • GW-803,430 • NGD-4715 • SNAP-7941 • SNAP-94847 ...
Competitive vasopressin antagonism leads to decreased number of aquaporin channels in the apical membrane of the renal ... 1. Arginine vasopressin. receptor 2 antagonists amphotericin B, lithium[12][13] Inhibits vasopressin's action 5. collecting ... 21 (1): 163-70. doi:10.1359/JBMR.051003. PMID 16355285.. *^ Du, Xiaoping. Diuretics Archived April 7, 2006, at the Wayback ... ISBN 0-7817-4118-1.. *^ Rejnmark L, Vestergaard P, Pedersen AR, Heickendorff L, Andreasen F, Mosekilde L (January 2003). "Dose- ...
However, when plasma blood volume is low and ADH is released the aquaporins that are opened are also permeable to urea. This ... ADH binds to principal cells in the collecting duct that translocate aquaporins to the membrane, allowing water to leave the ... ADH acts on the V2 receptor and inserts aquaporins on the luminal side ... ISBN 978-1-58829-081-6.. *^ a b Post TW, Rose BD, auths and Curhan GC, Sheridan AM, eds. Diagnostic Approach to the Patient ...
Such molecules can diffuse passively through protein channels such as aquaporins in facilitated diffusion or are pumped across ... 1-18, Academic Press, San Diego, [3]. *^ Mast, S. O. (1924). "Structure and locomotion in Amoeba proteus". Anat. Rec. 29 (2): ... The Physiology of Plants, [1] Archived 2018-06-02 at the Wayback Machine.. Translated by A. J. Ewart from the 2nd German ed. of ... 1. Passive osmosis and diffusion: Some substances (small molecules, ions) such as carbon dioxide (CO2) and oxygen (O2), can ...
There are seven subfamilies of Kir channels, denoted as Kir1 - Kir7.[1] Each subfamily has multiple members (i.e. Kir2.1, Kir ... Figure 1. Whole-cell current recordings of Kir2 inwardly-rectifying potassium channels expressed in an HEK293 cell. (This is a ... To date, seven subfamilies have been identified in various mammalian cell types,[1] plants,[2] and bacteria.[3] They are the ... "1.A.2 Inward Rectifier K Channel (IRK-C) Family". TCDB. Retrieved 2016-04-09.. ...
aquaporin 5, calmodulin, pacsin 3 2 TRPV5 calcium-selective TRP channel intestine, kidney, placenta 100:1 TRPV6 annexin II / ... 1 TRPV1 vanilloid (capsaicin) receptor and noxious thermosensor (43 °C) CNS and PNS 9:1 TRPV2, TRPV3 calmodulin, PI3 kinase ... 14 (1): 18-31. doi:10.2174/138161208783330763. PMID 18220815.. *^ Cheng W, Yang F, Takanishi CL, Zheng J (March 2007). " ... PIP2 signaling ligands are represented by space-filling models (carbon = white, oxygen = red, phosphorus = orange).[1] ...
Yeum CH, Kim SW, Kim NH, Choi KC, Lee J (July 2002). "Increased expression of aquaporin water channels in hypothyroid rat ... வளர்சிதை மாற்றக் குறியீட்டைச் சிதைத்தல் (தொகுதி 2 இல் 1) - ஜேம்ஸ் பி. லாவெல்லே R.Ph. C.C.N. N.D, ISBN 1442950390, பக்கம் 100 ... தைராய்டு சுரப்புக் குறை என்பது பொதுவான மக்கள் தொகையில் மூன்று சதவீதம் இருக்கின்றது.[1] அயோடின் குறைபாடு அல்லது அயோடின்-131 (I- ... 1] முதல்நிலை தைராய்டு சுரப்புக் குறையில், TSH அளவுகள் அதிகமாகவும் T4 மற்றும் T3 அளவுகள் குறைவாகவும் உள்ளன. வழக்கமாக T4
exocytosis of aquaporin 2 to apical membrane.[12]. *synthesis of aquaporin 2[12] ... ISBN 978-1-4160-2328-9.. *^ a b c d Boron WF, Boulpaep EL (2005). Medical Physiology: A Cellular And Molecular Approach ( ... ISBN 978-1-4160-2328-9.. *^ Boron WF, Boulpaep EL (2005). Medical Physiology: A Cellular And Molecular Approach (Updated ed.). ... ISBN 978-1-4160-2328-9.. *^ Boron WF, Boulpaep EL (2005). Medical Physiology: A Cellular And Molecular Approaoch (Updated ed ...
126 (Pt 1): 134-51. doi:10.1093/brain/awg012. PMID 12477701.. *. Sato H, Hagiwara H, Ohde Y, Senba H, Virgona N, Yano T (March ... Gap junction beta-1 protein (GJB1), also known as connexin 32 (Cx32) is a transmembrane protein that in humans is encoded by ... "Entrez Gene: GJB1 gap junction protein, beta 1, 32kDa".. *^ Hoek KS, Schlegel NC, Eichhoff OM, Widmer DS, Praetorius C, ... ISBN 978-1-934115-46-6.. *. Latour P, Fabreguette A, Ressot C, Blanquet-Grossard F, Antoine JC, Calvas P, Chapon F, Corbillon E ...
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. ... Aquaporin 1 (Colton blood group)) - білок, який кодується геном AQP1, розташованим у людей на короткому плечі 7-ї хромосоми.[4] ...
Aquaporins are membrane proteins that selectively conduct water molecules while preventing the passage of ions and other ... ADH affects the function of aquaporins, resulting in the reabsorption of water molecules as it passes through the collecting ... The nephron is the functional unit of the kidney.[1] Each nephron is composed of a renal corpuscle, the initial filtering ... Fig.1) Schematic diagram of the nephron (yellow), relevant circulation (red/blue), and the four methods of altering the ...
... water permeability of the kidney's collecting duct and distal convoluted tubule by inducing translocation of aquaporin-CD water ... 1. Human urinary system: 2. Kidney, 3. Renal pelvis, 4. Ureter, 5. Urinary bladder, 6. Urethra. (Left side with frontal section ... ISBN 0-13-981176-1.. *^ Caldwell HK, Young WS III, Lajtha A, Lim R (2006). "Oxytocin and Vasopressin: Genetics and Behavioral ... The urinary tract is the body's drainage system for the eventual removal of urine.[1] The kidneys have an extensive blood ...
... occurs in one of two ways: either the osmoreceptor-aquaporin feedback loop is overwhelmed, or it is interrupted. ... "Physiology and pathophysiology of renal aquaporins". Seminars in nephrology. 21 (3): 231-8. doi:10.1053/snep.2001.21647. PMID ... 2 (1): 151-61. doi:10.2215/CJN.02730806. PMID 17699400.. *^ "High incidence of mild hyponatraemia in females using ecstasy at a ... Accessed 1 August 2016.. *^ Simon, Eric E. (2014). Hyponatremia: Evaluation and Treatment. Springer Science & Business Media. p ...
Aquaporin 1. *Arachidonate 5-lipoxygenase. *Atrophin 1. *BH3 interacting-domain death agonist ... 13:54, 1 August 2017. 453 × 200 (10.31 MB). Was a bee. {{Information ,Description={{en,1=Ideogram of house mouse (''Mus ...
Nielsen, J.; Kwon, T.H.; Christensen, B.M.; Frokiaer, J.; Nielsen, S. (May 2008). "Dysregulation of renal aquaporins and ... Retrieved 1 December 2015.. *^ a b Sneader, Walter (2005). Drug discovery : a history (Rev. and updated ed.). Chichester: Wiley ... Retrieved 1 November 2014.. *^ a b c Finley, PR (February 1996). "Lithium and angiotensin-converting enzyme inhibitors: ... 978-1-60913-713-7. .. *^ Boyer, EW. "Serotonin syndrome". UpToDate. Wolters Kluwer. Archived from the original on 16 December ...
Aquaporins. *Chloride channels. *Outer membrane auxiliary proteins (polysaccharide transporter) - α-helical transmembrane ... Schematic representation of transmembrane proteins: 1) a single transmembrane α-helix (bitopic membrane protein). 2) a ... 1] Depending on the number of transmembrane segments, transmembrane proteins can be classified as single-span (or bitopic) or ...
Such molecules can diffuse passively through protein channels such as aquaporins in facilitated diffusion or are pumped across ... 1-18, Academic Press, San Diego, [3]. *^ Mast SO (1924). "Structure and locomotion in Amoeba proteus". Anat. Rec. 29 (2): 88. ... 40 (1): 97-111. doi:10.1002/jlb.40.1.97. PMID 3011937.. *^ Jesse Gray; Shana Groeschler; Tony Le; Zara Gonzalez (2002). " ... The Physiology of Plants, [1] Archived 2018-06-02 at the Wayback Machine. Translated by A. J. Ewart from the 2nd German ed. of ...
The gene encoding this aquaporin is a possible candidate for disorders involving imbalance in ocular fluid movement. Aquaporin ... Aquaporin 1 is a protein that in humans is encoded by the AQP1 gene. AQP1 is a widely expressed water channel, whose ... Aquaporin and Blood Brain Barrier, Current Neuropharmacology from U.S. National Library of Medicine, 2010. Boassa D, Yool AJ ( ... Aquaporin+1 at the US National Library of Medicine Medical Subject Headings (MeSH) Gallery of Aquaporin Simulations Human AQP1 ...
... to identify effective and specific inhibitors of aquaporins. In this paper, we have screened a library of 1500 ... Aquaporins (AQPs) are membrane proteins that enable water transport across cellular plasma membranes in response to osmotic ... This article belongs to the Special Issue Aquaporin) View Full-Text , Download PDF [9881 KB, uploaded 25 March 2016] , Browse ... Aquaporins (AQPs) are membrane proteins that enable water transport across cellular plasma membranes in response to osmotic ...
Anti-Aquaporin 1 antibody (ab15080) has been cited in 22 publications. References for Human, Mouse, Rat, Shp, Cow in ICC, ICC/ ... Sánchez Gomar I et al. Comparative Analysis for the Presence of IgG Anti-Aquaporin-1 in Patients with NMO-Spectrum Disorders. ... Biçakçi H et al. Investigation of the effects of aging on the expression of aquaporin 1 and aquaporin 4 protein in heart tissue ... Wang Y et al. Investigation of aquaporins and apparent diffusion coefficient from ultra-high b-values in a rat model of ...
Upon transfection of salivary glands, adenovirus encoding human aquaporin-1 (AdhAQP1) directs human aquaporin-1 (hAQP1) ... recombinant adenovirus encoding human aquaporin-1 with potential membrane water channel activity. ... adenovirus encoding human aquaporin-1 A replication-deficient, recombinant adenovirus encoding human aquaporin-1 with potential ... Upon transfection of salivary glands, adenovirus encoding human aquaporin-1 (AdhAQP1) directs human aquaporin-1 (hAQP1) ...
Aquaporins Aquaporin-1 (AQP1) was first discovered in human red blood cell membranes by Gheorghe Bengas research group in 1986 ... Water selective aquaporins are AQP1, -2, -4, -5, -6, -8, -12, and -0. A subgroup of aquaporins called aquaglycerporins allow ... Aquaporins are integral membrane proteins that specialize in the regulation of cellular water flow across the cell membrane.[3] ... Aquaporin-1 Structure Aquaporin-1 is an integral membrane protein that is considered to have an "open" structure. Despite being ...
Aquaporin 1 splice variant 2Imported. ,p>Information which has been imported from another database using automatic procedures ... Belongs to the MIP/aquaporin (TC 1.A.8) family. [View classification]SAAS annotation. Automatic assertion according to rulesi ... tr,Q6JSD8,Q6JSD8_HUMAN Aquaporin 1 splice variant 2 (Fragment) OS=Homo sapiens OX=9606 GN=AQP1 PE=2 SV=1 ... 1.20.1080.10, 1 hit. InterProi. View protein in InterPro. IPR023271 Aquaporin-like. IPR034294 Aquaporin_transptr. IPR000425 ...
IPR023271, Aquaporin-like. IPR034294, Aquaporin_transptr. IPR000425, MIP. IPR022357, MIP_CS. PANTHERi. PTHR45665, ... IPR023271, Aquaporin-like. IPR034294, Aquaporin_transptr. IPR000425, MIP. IPR022357, MIP_CS. The PANTHER Classification ... "Aquaporins constitute a large and highly divergent protein family in maize.". Chaumont F., Barrieu F., Wojcik E., Chrispeels M. ... Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the ...
Aquaporin 1 forms a water-specific channel that is constitutively expressed at the PLASMA MEMBRANE of ERYTHROCYTES and KIDNEY ... Aquaporin-CHIP; CHIP28 Protein; Channel-Forming Integral Membrane Protein Of 28 kDa; AQP CHIP Protein; Aquaporin CHIP; Channel ... Aquaporin 1. Subscribe to New Research on Aquaporin 1 Aquaporin 1 forms a water-specific channel that is constitutively ... 01/01/2012 - "In this study, we were going to elucidate the involvement of aquaporin 1 and 4 (AQP1,4) in the metastasis of lung ...
2008) Aquaporin 1 is important for maintaining secretory granule biogenesis in endocrine cells. Mol Endocrinol 22:1924-1934. ... 1994) Requirement of human renal water channel aquaporin-2 for vasopressin-dependent concentration of urine. Science 264:92-95. ... 2007) Nephrogenic diabetes insipidus in mice caused by deleting COOH-terminal tail of aquaporin-2. Am J Physiol Renal Physiol ... The persistent high urine volume after AVP administration was traced to a reduction in aquaporin-1 expression in the kidney of ...
Normal mesothelium expresses aquaporin 1 (AQP1) and retained expression has been associated with improved survival in MM. AQP1 ... The Effect of Aquaporin 1-Inhibition on Vasculogenic Mimicry in Malignant Mesothelioma by Emily Pulford ... "The Effect of Aquaporin 1-Inhibition on Vasculogenic Mimicry in Malignant Mesothelioma" Int. J. Mol. Sci. 18, no. 11: 2293. ... Normal mesothelium expresses aquaporin 1 (AQP1) and retained expression has been associated with improved survival in MM. AQP1 ...
The structure of the aquaporin-1 water channel: a comparison between cryo-electron microscopy and X-ray crystallography. de ... Regulation of water channel activity of aquaporin 1 by arginine vasopressin and atrial natriuretic peptide. Patil, R.V., Han, Z ... Immunocytochemical localization of aquaporin-1 in bovine corneal endothelial cells and keratocytes. Wen, Q., Diecke, F.P., ... Phosphorylation regulates the water channel activity of the seed-specific aquaporin alpha-TIP. Maurel, C., Kado, R.T., Guern, J ...
A) The aquaporin PIP2;1 was identified as a βCA4-interacting protein by screening a split ubiquitin yeast two-hybrid library. ... Wang C1, Hu H2, Qin X3, Zeise B3, Xu D4, Rappel WJ5, Boron WF3, Schroeder JI6. ... PIP2;1 alone served as a negative control.. (C) PIP2;1-G103W impaired the CO2 permeability of PIP2;1 as measured by changes in ... B) and (C) Split YFP (B) and reversible split luciferase complementation assays (C) showed that βCA4 interacts with PIP2;1 at ...
Anti-Aquaporin 1 mAb (GTX11025) is tested in Human, Mouse, Rat samples. 100% Ab-Assurance. ... Aquaporin 1 antibody [7D11] (aquaporin 1) for ELISA, FACS, IHC-P, WB. ... aquaporin 1. Background. integral membrane protein that is a major water transport molecule in the kidney proximal tubule and ... Aqp1 Antibody , CHIP28 Antibody , aquaporin 1 Antibody. Specificity. This antibody recognizes an epitope within an ...
Aquaporins (AQPs) facilitate the transepithelial water flow involved in epithelial fluid secretion in numerous tissues; however ... Aquaporins (AQPs) facilitate the transepithelial water flow involved in epithelial fluid secretion in numerous tissues; however ... in Capan-1 cells. The presence of AQP1 and CFTR in the mice and human pancreas were investigated by immunohistochemistry. ... in Capan-1 cells. The presence of AQP1 and CFTR in the mice and human pancreas were investigated by immunohistochemistry. ...
1996 Jan;270(1 Pt 2):H416-22. Comparative Study; Research Support, Non-U.S. Govt; Research Support, U.S. Govt, P.H.S. ... Aquaporin-1 in plasma membrane and caveolae provides mercury-sensitive water channels across lung endothelium.. Schnitzer JE1, ... Immunoblotting of these fractions showed that the transmembrane water channel protein aquaporin-1 was amply expressed on the ... Just like certain epithelia, endothelia might express physiologically relevant amounts of aquaporin-1 on their cell surface to ...
Safety of a Single Administration of AAV2hAQP1, an Adeno-Associated Viral Vector Encoding Human Aquaporin-1 to One Parotid ... Early responses to adenoviral-mediated transfer of the aquaporin-1 cDNA for radiation-induced salivary hypofunction. Proc Natl ... Increased fluid secretion after adenoviral-mediated transfer of the aquaporin-1 cDNA to irradiated rat salivary glands. Proc ... AAV2-mediated transfer of the human aquaporin-1 cDNA restores fluid secretion from irradiated miniature pig parotid glands. ...
Aquaporin 1 Antibody, Affinity purified polyclonal antibody validated in WB (AG1048-025), Abgent ... home , Products , Primary Antibodies , Signal Transduction , Aquaporin 1 Antibody Aquaporin 1 Antibody. Affinity purified ... Aquaporin 1 (AQP-1) belongs to a family of membrane proteins that allow passage of water and certain other solutes through ... Aquaporin-1, AQP-1, Aquaporin-CHIP, Urine water channel, Water channel protein for red blood cells and kidney proximal tubule, ...
aquaporin-1 DEFINITION: Also known as CHIP-28, aquaporin-1 is the major water channel of the red blood cells. In the kidneys, ... aquaporin-1 DEFINITION: Also known as CHIP-28, aquaporin-1 is the major water channel of the red blood cells. In the kidneys, ... Mice that do not have the aquaporin-1 (AQP1) gene are unable to concentrate urine. Brooks, et al., examined mice lacking AQP1 ... Renal medullary gene expression in aquaporin-1 null mice Authors: Brooks, Heddwen L.; McReynolds, Matthew R.; Garcia-Taylor, ...
Purpose:: Aquaporins are a family of water channel proteins that facilitates water transport across the plasma membrane. ... R. Patil, S. Xu, A. Rusinko, N. A. Sharif, M. B. Wax, R. T. Mathias, K. Varadaraj; Inhibition of Human Aquaporin-1 Water ... Inhibition of Human Aquaporin-1 Water Channel Activity by Carbonic Anhydrase Inhibitors ... Inhibition of Human Aquaporin-1 Water Channel Activity by Carbonic Anhydrase Inhibitors ...
Aquaporins (Aqps) are a superfamily of integral membrane proteins which generally facilitate the permeation of water through ... Aquaporins (Aqps) are a superfamily of integral membrane proteins which generally facilitate the permeation of water through ... Figure 5. The gene expression of (A) aquaporin 1 (aqp1) and (B) aquaporin 3 (aqp3) in various tissues/organs of Protopterus ... Figure 2. A multiple amino acid alignment of aquaporin 3 (Aqp3) from Protopterus annectens with Danio rerio Aqp3a (AAH44188.1 ...
aquaporin-1. (. AQP1. ) has two asparagine-proline-alanine (NPA) repeats on loops B and E. From recent structural information, ... Mercurial sensitivity of aquaporin 1 endofacial loop B residues. Kuang K , Haller JF , Shi G , Kang F , Cheung M , Iserovich P ...
Arabidopsis thaliana, Aquaporin, Nodulin26-like intrinsic proteins, AtNIP1;1. Alternative keywords:. Alternative keywords. ... For many Aquaporins the water conductivity exhibits mercury sensitivity. For AtNIP1;1 it was not possible to inhibit the water ... The plant aquaporin family of the Nodulin26-like intrinsic proteins was named because of the high structural and functional ... Charakterisierung des Arabidopsis thaliana Aquaporins AtNIP1;1.. Darmstadt, Technische Universität, [Ph.D. Thesis]. Preview ...
2 aquaporin displays CO2 permeability in yeast (Heckwolf et al., 2011). Four barley PIP2 aquaporins were recently shown to ... It has been widely demonstrated that CO2 is transported across membranes via aquaporins: The AQP1 aquaporin from tobacco ... A) The aquaporin PIP2;1 was identified as a βCA4-interacting protein by screening a split ubiquitin yeast two-hybrid library. ... The aquaporins Nt-AQP1 from tobacco, PIP1;2 from Arabidopsis, and four PIP2 proteins in barley (Hordeum vulgare) have been ...
We stained the sections with N-cadherin and keratin 15 (Limbal basal epithelial layer), aquaporin 1 (AQP1; subepithelial cells ... Aquaporin 1 Positive Mesenchymal Cell Imply Existence Of Cornea Limbal Niche Cells ... Aquaporin 1 Positive Mesenchymal Cell Imply Existence Of Cornea Limbal Niche Cells ... Kazunari Higa, Naoko Kato, Satoru Yoshida, Yoko Ogawa, Jun Shimazaki, Kazuo Tsubota, Shigeto Shimmura; Aquaporin 1 Positive ...
... ... The aquaporins (AQPs) are a family of water channel proteins with at least 13 mammalian members (AQPs 0-12) expressed in ... Aquaporin expression in the peripheral nervous system is poorly studied. Here we report that the AQP1 water channel is ...
Assessing the selectivity, regulation and physiological relevance of aquaporin membrane channels (AQPs) requires structural and ... PIP1;1 was produced as a histidine-tagged form, 10His-OsPIP1;1, in an Escherichia coli-based expression system. The recombinant ... PIP1;1 proteoliposomes and control empty liposomes had good size homogeneity as seen by quasi-elastic light scattering and ... Write a short (1 or 2 sentence) testimonial describing your experience with GenScript products or services. If your testimonial ...
Aquaporins serve as pores for water thus allowing enhanced water permeability in biological membranes (Preston, et al., 1992). ... REGULATION OF AQUAPORIN-1 ION CHANNEL FUNCTION BY INTRACELLULAR SIGNALING PATHWAYS. by Birdsell, Dawn Nice. ... A subset of Aquaporin proteins behave as ion channels regulated by intracellular signaling pathways (Anthony, et al., 2000; ... The Carboxyl (C) -terminus of Aqp1 encodes a PSD-95/DLG/ZO- 1 (PDZ) ligand binding domain and a number of putative regulatory ...
Aquaporin 1 It is a Custom assay which can detect AQP1 / Aquaporin 1 ... Aquaporin 1 ELISA Kit LS-F14830 is a 96-Well enzyme-linked immunosorbent assay for the Quantitative detection of Bovine AQP1 / ... LS-F14830 is a 96-well enzyme-linked immunosorbent assay (ELISA) for the Quantitative detection of Bovine AQP1 / Aquaporin 1. ...
Aquaporin-1 (AQP1) water channels are present in the apical and basolateral plasma membrane domains of bile duct epithelial ... Expression and immunolocalization of aquaporin water channels in rat exocrine pancreas.. *P. T. Hurley, C. Ferguson, +5 authors ... Aquaporin-1 (AQP1) water channels are present in the apical and basolateral plasma membrane domains of bile duct epithelial ... Aquaporin 2 is a vasopressin-independent, constitutive apical membrane protein in rat vas deferens. ...
Aquaporin 1 (AQP1) is a cell membrane channel involved in water transport, cell motility, and proliferation. A blocker and an ... Cohort 1 consisted of 80 consecutive patients who underwent radical surgery (extrapleural pneumonectomy [EPP]). Cohort 2 ... Aquaporin 1 (AQP1) is a cell membrane channel involved in water transport, cell motility, and proliferation. A blocker and an ... Aquaporin 1 is an independent prognostic factor in pleural malignant mesothelioma.. Abstract. BACKGROUND: Malignant ...
  • Aquaporin 1 is a protein that in humans is encoded by the AQP1 gene. (
  • Aquaporin-1 (AQP1) was first discovered in human red blood cell membranes by Gheorghe Benga's research group in 1986. (
  • Vasculogenic mimicry (VM) is a newly described phenomenon associated with increased aggressiveness in other malignancies, and has been characterized in MM. Normal mesothelium expresses aquaporin 1 (AQP1) and retained expression has been associated with improved survival in MM. AQP1 is expressed by normal vascular endothelium and is involved in mediating MM cell motility and proliferation. (
  • As a proof of concept that AQP1 would restore saliva flow in a human population, we recently completed a phase 1 clinical trial (06-D-0206) using an Adenovirus-based vector encoding AQP1 to a single previously irradiated parotid gland in eleven patients using an open label, single dose, dose-escalation design. (
  • Mice that lack the aquaporin-1 gene ( AQP1 ) lack a functional countercurrent multiplier mechanism , fail to concentrate the inner medullary (IM) interstitium and present with a urinary concentrating defect . (
  • Mice that do not have the aquaporin-1 ( AQP1 ) gene are unable to concentrate urine . (
  • My dissertation work has focused on identifying regulatory mechanisms that govern Cyclic Guanosine Monophosphate (cGMP)-activation of Aquaprorin-1 (Aqp1) ion channels. (
  • The Carboxyl (C) -terminus of Aqp1 encodes a PSD-95/DLG/ZO- 1 (PDZ) ligand binding domain and a number of putative regulatory domains. (
  • LS-F14830 is a 96-well enzyme-linked immunosorbent assay (ELISA) for the Quantitative detection of Bovine AQP1 / Aquaporin 1. (
  • Aquaporin-1 (AQP1) water channels are present in the apical and basolateral plasma membrane domains of bile duct epithelial cells, or cholangiocytes, and mediate the transport of water in these cells. (
  • Aquaporin 1 (AQP1) is a cell membrane channel involved in water transport, cell motility, and proliferation. (
  • Here, we have investigated the functional properties and cellular localization in the intestine of two gilthead seabream (Sparus aurata) homologs of mammalian aquaporin-1 (AQP1), named SaAqp1a and SaAqp1b. (
  • Aquaporin-1 (AQP1) passively transports water across the plasma membrane according to the osmotic gradient. (
  • The marine teleost gilthead sea bream ( Sparus aurata ) has a mammalian aquaporin-1 (AQP1)-related channel, termed AQP1o, with a specialized physiological role in mediating egg hydration. (
  • Aquaporin-1 (AQP1) is a candidate oncogene that is epigenetically modified in adenoid cystic carcinoma (ACC). (
  • We sought to (1) assess AQP1 promoter methylation and expression in an ACC cohort, (2) identify correlations between AQP1 and clinical outcomes, and (3) explore the role of AQP1 in tumor progression in vitro. (
  • You need info about Human Aquaporin 1 (AQP1) ELISA Kit or any other Gentaur produtct? (
  • In this study, we performed immunohistochemical analysis of AQP1 and AQP3 expression on tissue sections of biopsy specimens from 70 patients with various skin tumors, as shown in Table 1 . (
  • We hypothesized that seronegative NMOsd patients might have autoantibodies against aquaporin-1 (AQP1), another water channel in CNS astrocytes. (
  • Aquaporin-1 (AQP1) functions as an osmotic water channel and a gated cation channel. (
  • For example, AQP1 expressed in Xenopus oocytes exhibited water-to-ion channel ratios ranging from 1:30,000 to 1:180,000, depending on the batch of oocytes (Boassa and Yool, unpublished observations). (
  • CONCLUSION: Biphasic AQP1 expression in the CP with increased AQPs 1 and 4 at the brain-fluid interfaces may indicate compensatory mechanisms to regulate choroidal cerebrospinal fluid secretion and increase parenchymal fluid absorption in the high-pressure hydrocephalic condition. (
  • The aim of this study was to investigate the genes encoding the brain aquaporins (AQPs) AQP1 and AQP9 in SIDS. (
  • Aquaporin-1 (AQP1) facilitates the osmotic transport of water across the capillary endothelium, among other cell types, and thereby has a substantial role in ultrafiltration during peritoneal dialysis. (
  • The imprinting state, expression, and function of aquaporin-1 (Aqp1) were explored in knockout mice by imprinting analysis, real-time PCR, and immunohistochemistry. (
  • Objective To explore the expression and the significance of aquaporin 1 (AQP1) in breast carcinoma tissues . (
  • Real-time PCR showed that AQP1 mRNA in bleomycin 1 w, 2 w, and 3 w groups increased by 377%, 880% and 823% respectively compared to that in the control group (p (
  • Western blotting showed that the expression of AQP1 protein in bleomycin 1 w, 2 w, and 3 w groups increased by 53%, 144%, and 141%, respectively (p (
  • However, for some proteins, including Aquaporin 1 (AQP1), the folding appears to follow a more complicated path. (
  • OBJECTIVE To evaluate trends in urine aquaporin-1 (AQP1) and perilipin 2 (PLIN2) concentrations in sufferers with very clear cell and papillary renal cell carcinoma (RCC) this analysis determined the partnership between your urine concentration of the biomarkers and tumor size, stage and grade. (
  • The aim of this study was to investigate if aquaporin 1 (AQP1) genetic polymorphisms influence the risk of MM and the response to cisplatin based MM treatment. (
  • AQP1 expression did not co-localize with CD31, podoplanin, MART-1 positive cells, but were observed in vimentin positive stromal cells. (
  • Aquaporins (AQPs) are membrane proteins that enable water transport across cellular plasma membranes in response to osmotic gradients. (
  • Expression and localization of AQPs were investigated by real-time PCR and immunocytochemistry, whereas osmotic transmembrane water permeability was estimated by the dye dilution technique, in Capan-1 cells. (
  • Aquaporins (Aqps) are a superfamily of integral membrane proteins which generally facilitate the permeation of water through plasma membranes. (
  • Assessing the selectivity, regulation and physiological relevance of aquaporin membrane channels (AQPs) requires structural and functional studies of wild type and modified proteins. (
  • These results provide a valuable contribution in fully elucidating the regulation and water-conducting property of PIP1;1, an AQP that needs to hetero-multimerize with AQPs of the PIP2 subgroup to reach the native plasma membrane and play its role. (
  • Contents Aquaporins (AQPs) are essential membrane protein channels for the transport of water across membranes. (
  • These results indicate that AQPs 1 and 9 have reversed locations and roles in rams, suggesting activity variations related with fluid and solute absorption throughout the epididymis. (
  • Aquaporin (AQP)-mediated intestinal water absorption may play a major osmoregulatory role in euryhaline teleosts, although the molecular identity and anatomical distribution of AQPs in the fish gastrointestinal tract is poorly known. (
  • Investigating the evolution of aquaporins (AQPs) in these vertebrates should help to elucidate how mechanisms for water homeostasis evolved. (
  • Rapid membrane water transport is mediated by a family of molecular water channels, called aquaporins (AQPs), which have been identified in the epithelial and endothelial cells of higher vertebrates. (
  • We report the immunolocalization of aquaporins (AQPs) 1, 4, and 6 in the human auditory and vestibular endorgans. (
  • BACKGROUND: Hydrocephalus occurs because of an imbalance of bulk fluid flow in the brain, and aquaporins (AQPs) play pivotal roles in cerebral water movement as essential mediators during edema and fluid accumulation. (
  • METHODS: We evaluated differential expression of AQPs 1 and 4 in the congenital hydrocephalus Texas rat at postnatal days 5, 10, and 26 in isolated CP and cortex by enzyme-linked immunosorbent assay, Western blot, quantitative reverse transcriptase polymerase chain reaction, and immunohistochemistry. (
  • Aquaporins (AQPs) are integral membrane water channels, recognized for their importance in epithelial secretion and absorption. (
  • Transmembrane fluxes of water via specialized water channels, called aquaporins (AQPs), facilitate the changes of volume and shape, which additionally require a complex interplay between the plasma membrane and the cytoskeleton. (
  • Aquaporins (AQPs) are membrane proteins that form water channels, allowing rapid movement of water across cell membranes. (
  • Aquaporins (AQPs) play pivotal roles in lung fluid transport. (
  • Aquaporins (AQPs) are known to facilitate water transport across cell membranes, but the role of a single AQP in regulating plant water transport, particularly in plants other than Arabidopsis remains largely unexplored. (
  • Aquaporins (AQPs) are trans-membrane proteins that facilitate rapid and passive water transport across cell membranes. (
  • It is well-known that the rapid now of water into and out of cells is controlled by membrane proteins called aquaporins (AQPs). (
  • Aquaporins (AQPs) are an ancient family of channel proteins that transport water and neutral solutes through a pore and are found in all eukaryotes and most prokaryotes. (
  • Aquaporins (AQPs) are an ancient family of channel proteins that transport water and certain neutral metabolites across biological membranes. (
  • 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 ]. (
  • Aquaporins 11 and 12 are classified as members of a new AQP subfamily: the subcellular AQPs [ PMID: 17178102 ]. (
  • The eye contains numerous water channel proteins and the roles of AQPs (aquaporins) in the retina are blurred, especially under disease conditions. (
  • AQPs (aquaporins) are hydrophobic membrane proteins and the narrowest diameter of the pore of AQPs is 2.8 Å (1 Å=0.1 nm) [ 16 ]. (
  • Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). (
  • This gene encodes an aquaporin which functions as both a molecular water channel protein and as a non-selective cation channel gated by cyclic guanosine monophosphate (cGMP). (
  • Investigation of the effects of aging on the expression of aquaporin 1 and aquaporin 4 protein in heart tissue. (
  • Mice with targeted disruption of the acyl-CoA binding protein display attenuated urine concentrating ability and diminished renal aquaporin-3 abundance. (
  • [1] However, it was only known to be a novel protein and its function was unknown. (
  • Aquaporin-1 is an integral membrane protein that is considered to have an "open" structure. (
  • Protein Kinase C (PKC) has been documented as a common signal transducer among the aquaporins. (
  • Benga G. The first discovered water channel protein, later called aquaporin 1: molecular characteristics, functions and medical implications. (
  • These findings identify the CO2-permeable PIP2;1 as key interactor of βCA4 and demonstrate functional reconstitution of extracellular CO2 signaling to ion channel regulation upon coexpression of PIP2;1, βCA4, SLAC1, and protein kinases. (
  • Immunoblotting of these fractions showed that the transmembrane water channel protein aquaporin-1 was amply expressed on the endothelial cell surface at levels comparable to rat erythrocyte plasma membranes. (
  • By stopped-flow light scattering, indicating correct protein folding of the incorporated protein, the osmotic water permeability exhibited by the PIP1;1 proteoliposomes was markedly higher than empty liposomes. (
  • Aquaporin 2 is a vasopressin-independent, constitutive apical membrane protein in rat vas deferens. (
  • Antibodies anti-glial fibrillary acid protein (GFAP), aquaporin-4 (AQP4), hypoxia induced factor-1α (HIF-1α), macrophage/phagocytic activation (CD68), ionized calcium-binding adapter molecule-1 (IBA-1), and neutrophils (CD15) were used. (
  • The aquaporin AtPIP2;1 is an abundant plasma membrane intrinsic protein in Arabidopsis thaliana implicated in stomatal closure, but is also highly expressed in plasma membranes of root epidermal cells. (
  • We have previously shown that in cos 1 cells in vitro, both adenylyl cyclase activity and cAMP production can be regulated by VACM-1, a cul 5 gene that forms complexes involved in protein ubiquitination and subsequent degradation. (
  • To extend these observations further, the effects of changes in hydration state on the expression of VACM-1 at the mRNA and the protein level were examined in rats deprived of water (WD) for 24 hrs. (
  • In the kidney of WD rats Western blot analyses of kidney tissue showed that the decrease in VACM-1 protein concentration was correlated with the increase in the AQP2 protein level. (
  • To determine the possible consequences of the WD dependent decrease in VACM-1/cul5, we next examined the effects of VACM-1 expression on AQP2 protein in vitro. (
  • Immunocytochemistry and Western blot analyses data indicate that VACM-1/cul5 expression in MDCK line stably expressing AQP2 gene and in cos 1 cells co-transfected with the AQP2 and VACM-1/cul5 cDNAs decreased AQP2 protein concentration when compared to the vector transfected control groups. (
  • In summary, our data demonstrate that VACM-1 is involved in the regulation of AQP2 protein concentration and may play a role in regulating water balance. (
  • Epigenetic control of aquaporin 1 expression by the amyloid precursor protein. (
  • Here, we propose a molecular mechanism where the AQP7 mobility in adipocytes is dependent on perilipin 1 and protein kinase A. Biochemical analyses combined with ex vivo studies in human primary adipocytes, demonstrate that perilipin 1 binds to AQP7, and that catecholamine activated protein kinase A phosphorylates the N-terminus of AQP7, thereby reducing complex formation. (
  • The expression of several plant plasma membrane aquaporins in yeast, including PIP2;1 from Arabidopsis (where PIP is plasma membrane intrinsic protein), enhanced the toxicity of H 2 O 2 and increased the fluorescence of dye-loaded yeast when exposed to H 2 O 2 . (
  • Aquaporins constitute a large and highly divergent protein family in maize. (
  • Hypertonic shock induces the activation of mitogen-activated protein kinases and the expression of a defined set of genes, including aquaporins. (
  • Transient expression of MaPIP1;1-GFP fusion protein indicated its localization at plasma membrane. (
  • Positional cloning revealed that tls1 encodes a protein in the aquaporin family co-orthologous to known B channel proteins in other species. (
  • Aquaporin-11: a channel protein lacking apparent transport function expressed in brain. (
  • However, it remains a mystery how aquaporin-2 (an integral membrane protein) and other apical transporters are delivered to the urine. (
  • 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. (
  • AIM: To study effects of acetazolamide on aquaporin-1 (AQP(1)) protein expression and angiogenesis. (
  • Acetazolamide inhibits aquaporin-1 protein expression and angiogenesis[J]. ACTA PHARMACOLOGICA SINICA,2004,25(6):812-816. (
  • 2004).Acetazolamide inhibits aquaporin-1 protein expression and angiogenesis. (
  • Aquaporins are integral membrane proteins that specialize in the regulation of cellular water flow across the cell membrane. (
  • Aquaporins are a family of water channel proteins that facilitates water transport across the plasma membrane. (
  • The plant aquaporin family of the Nodulin26-like intrinsic proteins was named because of the high structural and functional similarity to soybean Nodulin 26. (
  • 1992). A subset of Aquaporin proteins behave as ion channels regulated by intracellular signaling pathways (Anthony, et al. (
  • Aquaporins are integral membrane proteins , which function as specialized water channels to facilitate the passage of water through the cell membrane . (
  • What follows in this process is not entirely clear, but it leads to water-transporting proteins called aquaporin-2 ( AQP2 proteins ) traveling from their holding place inside the CD cell to the apical membrane of the cell . (
  • Here we define the cellular and subcellular sites of aquaporin (AQP) water transport proteins in human and rat eyes by immunoblotting, high-resolution immunocytochemistry, and immunoelectron microscopy. (
  • Aquaporins, also called water channels, are channel proteins from a larger family of major intrinsic proteins that form pores in the membrane of biological cells, mainly facilitating transport of water between cells. (
  • Also known as water channels, aquaporins are integral membrane pore proteins. (
  • Aquaporin membrane proteins enable the transport of water across membranes in various organisms. (
  • For simplicity, we will designate the proteins of this family, which are also called major intrinsic proteins, as aquaporins throughout the present paper, despite the ability of several homologues to conduct other solutes. (
  • Aquaporins are channel producing proteins which regulate the flow of water across the cell membrane. (
  • Plasma membrane intrinsic proteins from maize cluster in two sequence subgroups with differential aquaporin activity. (
  • Aquaporins (AQP) are water channel proteins that enable fluid fluxes across cell membranes, important for homeostasis of the tissue environment and for cell migration. (
  • Mammalian aquaporins are a family of 13 classes of intrinsic membrane proteins that assemble as tetramers (~30 kDa per subunit) and are known for their role in fluid homeostasis and trans-membrane transport of water and other small solutes [ 6 , 7 ]. (
  • Aquaporin (AQP) proteins function in transporting water and other small molecules through the biological membranes, which is crucial for plants to survive in drought or salt stress conditions. (
  • AQP11 is functionally distinct from other proteins of the aquaporin superfamily and could represent a new aquaporin subfamily [ PMID: 16650285 ]. (
  • 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. (
  • Cytoprotective effect of aquaporin 1 against lipopolysaccharide-induced apoptosis and inflammation of renal epithelial HK-2 cells. (
  • Because of its importance for normal water homeostasis and its involvement in many water balance disorders , aquaporin-2 , the predominant vasopressin - regulated water channel of the renal collecting duct , is discussed in detail. (
  • In the renal collecting duct, vasopressin regulates water permeability by a process that involves stimulation of adenylyl cyclase activity, cAMP production and subsequent translocation of water channel aquaporin-2 (AQP2) into the apical plasma membrane. (
  • The immunostaining data suggested that VACM-1/cul5 may be decreased in renal collecting duct but increases in the vasculature of the inner medullary region in response to WD. (
  • Recently, mutations in the autosomal gene coding for water-channel aquaporin 2 (AQP2) of the renal collecting duct were reported in an NDI patient. (
  • Keywords: Kidney Tumor, Urine Biomarkers, Aquaporin-1, Perilipin 2 Launch Renal cell carcinoma (RCC) may be the most lethal urologic malignancy1 and buy SB-742457 there's been a reliable rise in its occurrence1C5. (
  • Long-term regulation of four renal aquaporins in rats. (
  • The gene encoding this aquaporin is a possible candidate for disorders involving imbalance in ocular fluid movement. (
  • Our research group has been developing an adeno-associated virus vector based on the hypothesis that this vector is capable of safely transferring the human aquaporin-1 (hAQP1) cDNA gene to parotid glands of adult patients with IR-induced salivary hypofunction, resulting in an elevated salivary output. (
  • An analysis of the promoter activity with an AtNIP1;1-Promoter-GUS-fusion lead to reporter gene activity in the root tip and in the vascular bundles of roots and leaves. (
  • The human aquaporin-CHIP gene. (
  • Aquaporin-2 levels in vitro and in vivo are regulated by VACM-1, a cul 5 gene. (
  • In the present study, missense mutations and a single nucleotide deletion in the aquaporin 2 gene of three NDI patients from consanguineous matings are described. (
  • However, when we expressed the Saccharomyces cerevisiae aquaporin-encoding gene AQY2-1 in S. pombe cells, we found that the relatively low freeze tolerance of S. pombe could be significantly enhanced. (
  • At the mRNA level, different PIP2;1 aquaporin gene expressions in roots of drought-tolerant and drought-sensitive maize genotypes with sufficient substrate moisture, as well as their distinct responses towards water deficit, are shown. (
  • An expression analysis of a gene family encoding plasma membrane aquaporins in response to abiotic stresses in Arabidopsis thaliana. (
  • Whole gene family expression and drought stress regulation of aquaporins. (
  • PIP2 - aquaporin gene expression of Sium latifolium L. under different water supply. (
  • Although the physiology of AQP-1 has been the subject of several publications, much less is known about the trans-acting factors involved in the control of AQP-1 gene expression. (
  • Here we report that TTF-1, a homeodomain-containing transcriptional regulator, is coexpressed with AQP-1 in the rat brain choroid plexus and enhances AQP-1 gene transcription by binding to conserved core TTF-1-binding motifs in the 5′-flanking region of the AQP-1 gene. (
  • In this study, we have identified a PIP1 subfamily AQP ( MaPIP1;1 ) gene from banana and characterized it by overexpression in transgenic Arabidopsis plants. (
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Uridine Phosphorylase 1 (UPP1) in Tissue homogenates, cell lysates and other biological fluids. (
  • In order to get hints about the function of AtNIP1;1 in planta, the expression pattern and the localization of AtNIP1;1 was investigated. (
  • An investigation of the subcellular localization of AtNIP1;1 revealed that it is localized in the plasma membrane. (
  • 2008). Tissue and cell-specific localization of rice aquaporins and their water transport activities- Plant Cell Physiol. (
  • AQP-1 expression and localization was examined in normal and cirrhotic liver tissues derived from human and mouse. (
  • RESULTS: Immunohistochemical localization of AQP(1) in mice tumor was labeled in capillaries, post capillary venules endothelial cells. (
  • Expression, localization, and regulation of aquaporin-1 to -3 in rat urothelia. (
  • We propose that ligand-dependent HER activation constitutes a generalized signaling principle in the mammalian hypertonic stress response relevant to aquaporin expression. (
  • AQP 11 and 12 appear to be more distantly related to the other mammalian aquaporins and aquaglyceroporins. (
  • In conclusion, this study adds further evidence to the involvement of brain aquaporins in SIDS, suggesting that specific variants of AQP genes constitute a genetic predisposition, making the infant vulnerable to sudden death together with external risk factors and probably other genetic factors. (
  • Identification of Key HIF-1α Target Genes that Regulate Adaptation to Hypoxic Conditions in Tibetan Chicken Embryos. (
  • Genetic defects involving aquaporin genes have been associated with several human diseases including nephrogenic diabetes insipidus and neuromyelitis optica. (
  • When we analyzed the freeze tolerance of Schizosaccharomyces pombe, an organism whose genome sequence has revealed no genes encoding a bona fide water channel, we found very low intrinsic freeze tolerance compared to other yeast species with aquaporin-encoding genes. (
  • Identification of 33 rice aquaporin genes and analysis of their expression and function. (
  • Expression analysis of sugarcane aquaporin genes under water deficit. (
  • We previously identified TIP5;1 and TIP1;3 as the only Arabidopsis aquaporin genes that are selectively and highly expressed in mature pollen, and showed that they can transport both water and urea when expressed in Xenopus oocytes. (
  • Finally, reduced expression of ABA-responsive genes in MaPIP1;1 -overexpressing plants reflects their improved physiological status. (
  • Im Rahmen dieser Arbeit sollte das zu dieser Familie gehörende Arabidopsis thaliana Aquaporin AtNIP1;1 funktionell charakterisiert werden. (
  • The aim of the thesis was the functional characterization of the Arabidopsis thaliana NIP-aquaporin AtNIP1;1. (
  • In the model plant Arabidopsis thaliana , 35 aquaporin homologues are encoded in the genome, and several of them conduct urea or ammonia in addition to water [ 4 , 5 ]. (
  • 1] "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana. (
  • 3] "From genome to function: the Arabidopsis aquaporins. (
  • TIP5;1 is an aquaporin specifically targeted to pollen mitochondria and is probably involved in nitrogen remobilization in Arabidopsis thaliana. (
  • Thus, we propose that TIP5;1 and TIP1;3 are involved in nitrogen recycling in pollen tubes of Arabidopsis thaliana. (
  • Overexpression of MaPIP1;1 in Arabidopsis resulted in an increased primary root elongation, root hair numbers and survival rates compared to WT under salt or drought conditions. (
  • Our results demonstrated that heterologous expression of banana MaPIP1;1 in Arabidopsis confers salt and drought stress tolerances by reducing membrane injury, improving ion distribution and maintaining osmotic balance. (
  • Because aquaporins are usually always open and are prevalent in just about every cell type, this leads to a misconception that water readily passes through the cell membrane down its concentration gradient. (
  • Aquaporin-3 function is to promote glycerol permeability across cell membrane. (
  • Aquaporins are specialized water transport channels in plasma membranes of water-permeable tissues. (
  • Water moves through cells in an organized way, most rapidly in tissues that have aquaporin water channels. (
  • Water channels, aquaporins, have been identified in most organisms, including plants, and have specific physiological functions related to water facilitation in many tissues [ 1 - 3 ]. (
  • PIP2;1 exhibited CO2 permeability. (
  • An inactive PIP2;1 point mutation was identified that abrogated water and CO2 permeability and extracellular CO2 regulation of SLAC1 activity. (
  • PIP2;1 exhibited CO 2 permeability. (
  • Aquaporins serve as pores for water thus allowing enhanced water permeability in biological membranes (Preston, et al. (
  • Vasopressin increases water permeability of kidney collecting duct by inducing translocation of aquaporin-CD water channels to plasma membrane. (
  • Using human red cell membranes, in which the osmotic flow is dominated by Aquaporin-1, we show here that compared to NaCl the reflexion coefficient of the channel for methylurea, when corrected for solute volume exchange and for the water permeability of the lipid membrane, is 0.54. (
  • A mutation in the water pore, G103W, prevented both the ionic conductance and water permeability of PIP2;1. (
  • Co-expression of AtPIP2;1 with AtPIP1;2 increased water permeability but abolished the ionic conductance. (
  • AtPIP2;2 (93% identical to AtPIP2;1) similarly increased water permeability but not ionic conductance. (
  • Establishing whether AtPIP2;1 has dual ion and water permeability in planta will be important in understanding the roles of this aquaporin, and if AtPIP2;1 is a candidate for a previously reported NSCC responsible for Ca²⁺ and pH sensitive Na⁺ entry into roots. (
  • In the oocyte expression system, only a small proportion of the population of aquaporin water channels appear active as ion channels, as determined by comparing the total water permeability and the total ion conductance values. (
  • AQP-1 levels were modulated in LEC using retroviral overexpression or small interfering RNA (siRNA) knockdown and functional effects on invasion, membrane blebbing dynamics, and osmotic water permeability were assayed. (
  • Additionally, AQP-1 localizes to plasma membrane blebs, where it increases osmotic water permeability and locally facilitates the rapid, trans-membrane flux of water. (
  • Conclusion: AQP-1 enhances osmotic water permeability and FGF-induced dynamic membrane blebbing in LEC and thereby drives invasion and pathological angiogenesis during cirrhosis. (
  • AVP increases the osmotic water permeability of the collecting duct cells through aquaporin-2 (AQP2) and aquaporin-3 (AQP3). (
  • In the brain, aquaporin-1 (AQP-1), a water channel for high osmotic water permeability, is mainly expressed in the apical membrane of the ventricular choroid plexus and regulates formation of cerebrospinal fluid (CSF). (
  • Functional reconstitution of OsPIP1;1 was further confirmed by the low Arrhenius activation energy (3.37 kcal/mol) and sensitivity to HgCl2, a known AQP blocker, of the PIP1;1-mediated osmotic water conductance. (
  • Additionally, the improved drought tolerance conferred by MaPIP1;1 is associated with decreased membrane injury and improved osmotic adjustment. (
  • and ( iv ) polydipsic, induced primarily by high water intake with consequent suppression of vasopressin release ( 1 ). (
  • The researchers also observed that mice lacking AQP -1 did not express vasopressin -2 ( V2R ) in the kidney medullae. (
  • The aim is to investigate the physiological role of aquaporins and vasopressin receptors in porcine and rat urinary bladders. (
  • The functional role of these water channels in transport was examined in rat lungs perfused in situ with tritiated water by testing known inhibitors of aquaporin-1-mediated transmembrane water transport. (
  • Plant aquaporins: multi functional water and solute channels with expanding roles. (
  • Aquaporin-4 (AQP4) is the most abundant water channel in the human central nervous system and is important to fluid movements in brain. (
  • In this study, we retrospectively examined brain samples in 145 cases of death after different survival times following TBI, to investigate aquaporin-4 (AQP4) expression and correlation with hypoxia, and neuroinflammation in human TBI. (
  • There were further increases in AQP4 immunopositivity in groups 4 (seven-day survival), 5 (14-dayssurvival), and 6 (30-day survival), suggesting an upregulation of AQP4 at 7 to 30 days compared to group 1. (
  • Autoantibodies against aquaporin-4 (AQP4), a water channel in CNS astrocytes, are detected in ∼50-80% of patients with neuromyelitis optica spectrum disorders (NMOsd), characterized by longitudinally extensive transverse myelitis (LETM) and/or optic neuritis. (
  • Retinal Muller cells and astrocytes exhibit notable concentrations of AQP4, whereas neurons and retinal pigment epithelium do not display aquaporin immunolabeling. (
  • Aquaporin-4 (AQP4) is implicated in a number of physiopathological processes, particularly in the development of brain edema, and other functions such as the regulation of extracellular space volume, potassium buffering, waste clearance, and calcium signaling. (
  • methyl-D-aspartate NMDA receptor (NMDAR) and aquaporin 4 (AQP4) are involved in the molecular cascade of edema after traumatic brain injury (TBI) and are potential targets of studies in pharmacology and medicine. (
  • Furthermore, the regulation of NMDA receptor 1 by AQP4 was studied by injection of a viral vector targeting AQP4 by RNAi into the rat brain before TBI. (
  • Aquaporin channels may be subject to intense short term regulation via signal transduction. (
  • Reconstitution of CO2 Regulation of SLAC1 Anion Channel and Function of CO2-Permeable PIP2;1 Aquaporin as CARBONIC ANHYDRASE4 Interactor. (
  • Die Ergebnisse weisen auf eine Funktion von AtNIP1;1 in der Regulation des Wasser- und Stickstoffhaushaltes der Pflanze hin. (
  • Regulation of aquaporins in plants under stress. (
  • Aquaporin-1 Overexpression Lysate (Adult Normal). (
  • AQP-1 overexpression promotes fibroblast growth factor (FGF)-induced dynamic membrane blebbing in LEC, which is sufficient to augment invasion through extracellular matrix. (
  • Therefore, (i) the absence of a bona fide water channel in S. pombe might provide in part an explanation for its overall low freeze tolerance compared to other yeast species, and (ii) aquaporin overexpression might be a tool to improve cryopreservation of many other cell types as well, as has recently been shown for mouse oocytes and fish embryos. (
  • Aquaporins are tetramers and each subunit forms a pore. (
  • Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). (
  • Also known as CHIP-28, aquaporin-1 is the major water channel of the red blood cells. (
  • It was not until 1992 that the first aquaporin, 'aquaporin-1' (originally known as CHIP 28), was reported by Peter Agre, of Johns Hopkins University. (
  • Taken together, the results strongly suggest that plasma membrane aquaporin pores determine the efficiency of H 2 O 2 signalling between cells. (
  • The persistent high urine volume after AVP administration was traced to a reduction in aquaporin-1 expression in the kidney of LXRβ −/− mice. (
  • Diabetes insipidus (DI) is a clinical condition characterized by polyuria (an abnormally high excretion of diluted urine) and by polydipsia (increased thirst and fluid intake) ( 1 ). (
  • Aquaporin-2 function is to reabsorb water from urine in the kidney. (
  • The water channel aquaporin-2 (AQP2) is one biomarker that can be readily measured in urine ( 3 ) and that has been exploited in studies of various water-balance disorders ( 4 ). (
  • Aquaporins have been implicated in a variety of illnesses involving the transport of water and other molecules, such as brain swelling after stroke or trauma, obesity, urine production defects and dry skin conditions. (
  • Expression of aquaporins in bronchial tissue and lung parenchyma of patients with chronic obstructive pulmonary disease. (
  • Detection:16473-1-AP 1:300) with mouse heart tissue lysate 4000ug. (
  • All the rabbits were followed by slit lamp microscopy, Tonopen tonometer, and anterior segment optical coherent tomography (AS-OCT). The expressions of metalloproteinase MMP-2, aquaporin-1, and tissue inhibitors of metalloproteinase-2 in corneoscleral junctionwere evaluatedin both groups byimmunofluorescence, quantitative reverse-transcription polymerase chain reaction (qRT-PCR), and enzyme-linked immunosorbent assay (ELISA). (
  • Upon transfection of salivary glands, adenovirus encoding human aquaporin-1 (AdhAQP1) directs human aquaporin-1 (hAQP1) expression in the apical and basolateral plasma membranes of salivary secretory cells, which may result in increased saliva production. (
  • subepithelial cells), vimentin (mesenchymal cells), CD31 (vascular endothelial cells), podoplanin (lymphatic endothelial cells) and MART-1 (melanocytes). (
  • These AQP1+ cells were CD31, podoplanin, MART-1 negative and vimentin positive suggesting a mesenchymal lineage. (
  • As reported before, AQP-1 is also present in ependymal cells, but most abundantly in small diameter sensory fibers of the dorsal horn. (
  • The cell membranes of a variety of different bacteria, fungi, animal and plant cells contain aquaporins through which water can flow more rapidly into and out of the cell than by diffusing through the phospholipid bilayer. (
  • The AQP-1-positive cells mainly located in Schlemm's canal, the inner surface of trabecular meshwork (TM), and the surface of iris, which began to decline on 1 month after angle-closure. (
  • We investigated upstream components of the response to hypertonicity in lung epithelial cells and found that before extracellular signal-regulated kinase activation and aquaporin synthesis, the membrane-bound prohormone neuregulin 1-β is cleaved and binds to human epidermal growth factor receptor 3 (HER3). (
  • No aquaporin-1 was found on alveolar type I cells with immunogold transmission electron microscopy, but small amounts were present on some type II cells. (
  • Aquaporin 9 changes in pyramidal cells before and is expressed in astrocytes after delayed neuronal death in the ischemic hippocampal CA1 region of the gerbil. (
  • Glaucoma is a group of slow progressive vision disorders affecting the trabecular meshwork, the ONH (optic nerve head) and RGCs (retinal ganglion cells) [ 1 ]. (
  • Personalized oncology provides new hopes for reducing cancer mortality by selectively targeting anticancer drugs to malignant cells, at the level of the target-sites on the cell surface and within the tumor microenvironment [ 1 , 2 ]. (
  • The checkpoint regulators CTLA-4 and PD-1 expressed in immune cells were successfully targeted for immunotherapies: in metastatic melanoma patients the anti-CTLA-4 ipilimumab significantly extended the median OS to 10.1 m, in phase III, compared to 6.4 m for the control group, enabling an unprecedented durable tumor regression of 46,6% at 1 y. and 23,5% at 2 y. [ 8 ]. (
  • 2001), Mercurial sensitivity of aquaporin 1 endofacial. (
  • Pulford E, McEvoy J, Hocking A, Prabhakaran S, Griggs K, Klebe S. The Effect of Aquaporin 1-Inhibition on Vasculogenic Mimicry in Malignant Mesothelioma. (
  • The sensitivity of aquaporin-expressing yeast to H 2 O 2 was altered by mutations that alter gating and the selectivity of the aquaporins. (
  • The ar/R (aromatic/arginine) region and the highly conserved NPA (for asparagine, proline, alanine) region have been implicated in the selectivity of aquaporins. (
  • Humans have 13 different aquaporins that allow water to pass at different speeds and have different selectivity behaviour (e.g. for glycerol and urea). (
  • Aquaporin 1 forms a water-specific channel that is constitutively expressed at the PLASMA MEMBRANE of ERYTHROCYTES and KIDNEY TUBULES, PROXIMAL. (
  • In mammals six different aquaporins have been identified up to now, four of which ( aquaporin-1 to aquaporin-4 ) are expressed in the kidney . (
  • [3] This process is vital for any living organism to sustain proper physiological conditions and aquaporins are necessary to sustain this process (i.e. osmosis alone could not provide a sufficient flow of water). (
  • To find evidence for the physiological functions further investigations, for example with AtNIP1;1-T-DNA-insertion lines, should be performed. (
  • Aquaporins are present in most species and their capacity to facilitate the diffusion of H 2 O 2 may be of physiological significance in many organisms and particularly in communication between different species. (
  • Physiological indices demonstrated that the increased salt tolerance conferred by MaPIP1;1 is related to reduced membrane injury and high cytosolic K + /Na + ratio. (
  • 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). (
  • 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. (
  • This perceived importance contrasts with the lack of success of high-throughput screens (HTS) to identify effective and specific inhibitors of aquaporins. (
  • Applications of aquaporin inhibitors. (
  • Extensive research on the function of aquaporins have been implemented into many separate types of cell membranes. (
  • A subgroup of aquaporins called aquaglycerporins allow the passage of small solutes such as glycerol, urea, and ammonia. (
  • Many plant aquaporin homologues are believed to specifically conduct water, whereas several homologues also conduct other small neutral solutes, such as glycerol, and are, therefore, called aquaglyceroporins [ 1 - 3 ]. (
  • Comparative Analysis for the Presence of IgG Anti-Aquaporin-1 in Patients with NMO-Spectrum Disorders. (
  • 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). (
  • Recent evidence suggests that water transport between the pulmonary vasculature and air spaces can be inhibited by HgCl 2 , an agent that inhibits water channels (aquaporin-1 and -5) of cell membranes. (
  • Inhibition of HER activation interferes with the hypertonic induction of two different aquaporins in three distinct cell lines of mouse and human origin. (
  • 1. How do the different aquaporins have different rates of water transport? (
  • PDF] Secretin induces the apical insertion of aquaporin-1 water channels in rat cholangiocytes. (
  • In this paper, we have screened a library of 1500 "fragments", i.e. , smaller than molecules used in HTS, against human aquaporin (hAQP1) using a thermal shift assay and surface plasmon resonance. (
  • To J, Torres J. Fragment Screening of Human Aquaporin 1. (
  • A replication-deficient, recombinant adenovirus encoding human aquaporin-1 with potential membrane water channel activity. (
  • The three-dimensional structure of human erythrocyte aquaporin CHIP. (
  • Human red cell aquaporin CHIP. (
  • Home Research Outputs Perilipin 1 binds to aquaporin 7 in human adipocytes and con. (
  • Agre P, Kozono D. Aquaporin water channels: molecular mechanisms for human diseases. (
  • King, Landon S. / Role of proneuregulin 1 cleavage and human epidermal growth factor receptor activation in hypertonic aquaporin induction . (
  • Expression and localisation of aquaporin water channels in human urothelium in situ and in vitro. (
  • Hydrogen-rich solution against myocardial injury and aquaporin expression via the PI3K/Akt signaling pathway during cardiopulmonary bypass in rats. (
  • Expression and immunolocalization of aquaporin water channels in rat exocrine pancreas. (
  • Hyperosmotic pretreatment (increase from 300 up to 600 mOsm·l −1 ) caused a time- and osmolarity-dependent increase (up to ∼1.5 times) in epithelial P f which was of similar magnitude in cystic fibrosis (CF) and non-CF spheroids. (
  • Split-ubiquitin screening identified the PIP2;1 aquaporin as an interactor of the βCA4 carbonic anhydrase, which was confirmed in split luciferase, bimolecular fluorescence complementation, and coimmunoprecipitation experiments. (
  • Mutation of PIP2;1 in planta alone was insufficient to impair CO2- and abscisic acid-induced stomatal closing, likely due to redundancy. (
  • Interestingly, coexpression of βCA4 and PIP2;1 with OST1-SLAC1 or CPK6/23-SLAC1 in oocytes enabled extracellular CO2 enhancement of SLAC1 anion channel activity. (
  • An analysis of the obtained data allow us to consider PIP2;1 expression as a possible molecular marker in maize breeding for drought tolerance. (
  • Aquaporin-5 is implicated in the forming of saliva, tears and pulmonary secretions. (
  • Water transport and the distribution of aquaporin-1 in pulmonary air s" by Richard M. Effros, C. Darin et al. (
  • Confocal laser scanning microscopy demonstrated that aquaporin-1 is on mouse pulmonary endothelium. (
  • Differential upregulation of aquaporin-4 mRNA expression in reactive astrocytes after brain injury: potential role in brain edema. (
  • Plant aquaporins: roles in plant physiology. (
  • This is supported by the fact that the bladder urothelium expresses the transmembrane water channels (aquaporins). (
  • Host water homeostasis and aquaporins (AQP) are essential during pathological conditions since they interfere with the cell cytoskeleton and signaling, and hereby affect cell morphology and functions. (
  • 13. Zhang C, Chen J, Lu H. Expression of aquaporin-4 and pathological characteristics of brain injury in a rat model of traumatic brain injury. (