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. ...
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
Aquaporins (AQPs) are membrane proteins that enable water transport across cellular plasma membranes in response to osmotic gradients. Phenotypic analyses have revealed important physiological roles for AQPs, and the potential for AQP water channel modulators in various disease states has been proposed. For example, AQP1 is overexpressed in tumor microvessels, and this correlates with higher metastatic potential and aggressiveness of the malignancy. Chemical modulators would help in identifying the precise contribution of water channel activity in these disease states. These inhibitors would also be important therapeutically, e.g., in anti-cancer treatment. This perceived importance contrasts with the lack of success of high-throughput screens (HTS) to identify effective and specific inhibitors of aquaporins. In this paper, we have screened a library of 1500
Aquaporin 8 (AQP8) is a water channel protein. Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). Aquaporin 8 mRNA is found in pancreas and colon but not other tissues. [provided by RefSeq, Jul 2008 ...
Purpose: : To demonstrate in the conjunctiva the presence of aquaporin type 5 (AQP5), a water channel homologue found in the apical membrane of several tissues including the cornea. Presently, there are no reports indicating as to which AQP might be expressed apically in the conjunctiva; only AQP3 has been identified in the lateral membranes of rat and human conjunctival epithelia. Because we had data from gene-expression microarray assays (Turner; ARVO 2004) indicating message for AQP5 in the human conjunctiva, tissue samples from human, as well as from rats and rabbits (given the ease of their procurement), were analyzed to confirm that the AQP5 protein was indeed expressed in mammalian conjunctivae. Methods: : Goat polyclonal IgG against AQP5 was purchased commercially and used in immunoblotting and immunohistochemical techniques to identify and localize the water channel in rat, rabbit and human epithelia. Results: : Immunoblot analysis of rabbit bulbar-plus-palpebral plasma membrane ...
Aquaporin A/S is a global cleantech company located in Kongens Lyngby, Denmark. Aquaporin is dedicated to revolutionizing water purification through the use of industrial biotechn
Peptides , Phosphopeptides , Aquaporin-2 (254-267), pSER261, human; This peptide is a fragment of the human aquaporin-2 (AQP2) phosphorylated at Ser261. Protein phosphorylation plays a key role in vasopressin signaling in renal-collecting duct. Phosphorylation at several AQP2 residues including Ser256 and Ser261, is altered in response to vasopressin. It is possible that both sites are involved in vasopressin-dependent AQP2 trafficking.; RQSVELH-pS-PQSLPR; H-Arg-Gln-Ser-Val-Glu-Leu-His-pSer-Pro-Gln- Ser-Leu-Pro-Arg-OH
The researchers showed that this technique was successful in monitoring gene expression in a brain tumor in mice. After implanting the tumor, they gave the mice a drug to trigger the tumor cells to express the aquaporin reporter gene, which made the tumor look darker in MRI images.. Overexpression of aquaporin has no negative impact on cells because it is exclusive to water and simply allows the molecules to go back and forth across the cell membrane, Shapiro says. Under normal physiological conditions the number of water molecules entering and exiting an aquaporin-expressing cell is the same, so that the total amount of water in each cell does not change. Aquaporin is a very convenient way to genetically change the way that cells look under MRI.. Though the work was done in mice, it has the potential for clinical translation, according to Shapiro. Aquaporin is a naturally occurring gene and will not cause an immune reaction. Previously developed reporter genes for MRI have been much more ...
C. elegans AQP-4 protein; contains similarity to Pfam domain PF00230 (Major intrinsic protein)contains similarity to Interpro domains IPR000425 (Major intrinsic protein), IPR012269 (Aquaporin ...
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 ...
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.. ...
Using PLIF to analyse water channel simulations of turbulent diffusion in the atmospheric boundary layer A. Butet METEO-FRANCE CNRM/GMEI/SPEA,...
Polyclonal antibody for AQUAPORIN 3/AQP3 detection. Host: Rabbit.Size: 100μg/vial. Tested applications: IHC-P. Reactive species: Human. AQUAPORIN 3/AQP3 information: Molecular Weight: 31544 MW; Subcellular Localization: Basolateral cell membrane; Multi-pa
Aquaporin 10 antibody, C-term (aquaporin 10) for WB. Anti-Aquaporin 10 pAb (GTX45889) is tested in Human samples. 100% Ab-Assurance.
Looking for online definition of Aquaporin1 or what Aquaporin1 stands for? Aquaporin1 is listed in the Worlds largest and most authoritative dictionary database of abbreviations and acronyms
Structural data on AQPs, together with mutagenesis and molecular dynamics simulations, have indicated that single-file transport occurs through a narrow pore in each monomer, where water selectivity is conferred by electrostatic and steric factors (Hub et al., 2009; Khalali-Araghi et al., 2009). Glycerol-transporting AQPs, called aquaglyceroporins, have a less-constricted pore compared with that of water-selective AQPs (diameter of 3.4 Å compared with 2.8 Å, respectively), with relatively more hydrophobic residues lining the pore.. Many mammalian AQPs, including AQP1, AQP2, AQP4, AQP5 and AQP8, function primarily as bidirectional water-selective transporters. Cells expressing AQPs on their plasma membrane have an ~5- to 50-fold higher osmotic water permeability than membranes that do not (Verkman and Mitra, 2000). Water transport through single-file pores poses a biophysical limitation on the efficiency with which AQPs can transport water, so that AQPs must be present in the membrane at a high ...
TY - JOUR. T1 - Urine-concentrating mechanism in the inner medulla. T2 - Function of the thin limbs of the loops of henle. AU - Dantzler, William H.. AU - Layton, Anita T.. AU - Layton, Harold E.. AU - Pannabecker, Thomas L.. PY - 2014. Y1 - 2014. N2 - The ability of mammals to produce urine hyperosmotic to plasma requires the generation of a gradient of increasing osmolality along the medulla from the corticomedullary junction to the papilla tip. Countercurrent multiplication apparently establishes this gradient in the outer medulla, where there is substantial transepithelial reabsorption of NaCl from the water-impermeable thick ascending limbs of the loops of Henle. However, this process does not establish the much steeper osmotic gradient in the inner medulla, where there are no thick ascending limbs of the loops of Henle and the water-impermeable ascending thin limbs lack active transepithelial transport of NaCl or any other solute. The mechanism generating the osmotic gradient in the inner ...
plasma membrane intrinsic protein 2-7, PIP2;7, plasma membrane intrinsic protein 3, salt stress-induced major intrinsic protein, P93004, Q9ATM4 Plasma membrane aquaporin, PIP2;7 is water channel protein required for water transport across cell membrane
Brain. 2019 Jun 1;142(6):1598-1615. doi: 10.1093/brain/awz106.. Cotzomi E1,2, Stathopoulos P1,2, Lee CS1,2, Ritchie AM3, Soltys JN3, Delmotte FR2, Oe T2, Sng J2, Jiang R2, Ma AK4, Vander Heiden JA1, Kleinstein SH2,4,5, Levy M6, Bennett JL3, Meffre E2, OConnor KC1,2.. Neuromyelitis optica spectrum disorders (NMOSD) constitute rare autoimmune disorders of the CNS that are primarily characterized by severe inflammation of the spinal cord and optic nerve. Approximately 75% of NMOSD patients harbour circulating pathogenic autoantibodies targeting the aquaporin-4 water channel (AQP4). The source of these autoantibodies remains unclear, but parallels between NMOSD and other autoantibody-mediated diseases posit compromised B cell tolerance checkpoints as common underlying and contributing factors. Using a well established assay, we assessed tolerance fidelity by creating recombinant antibodies from B cell populations directly downstream of each checkpoint and testing them for polyreactivity and ...
INTERNET-DRAFT DTLS as a Transport Layer for RADIUS 9 October 2013 The above paragraph can be rephrased more generically. A session MUST be deleted when non-RADIUS traffic is received over it. This specification is for RADIUS, and there is no reason to allow non- RADIUS traffic over a RADIUS/DTLS connection. A session MUST be deleted when RADIUS traffic fails to pass security checks. There is no reason to permit insecure networks. A session SHOULD NOT be deleted when a well-formed, but unexpected RADIUS packet is received over it. Future specifications may extend RADIUS/DTLS, and we do not want to forbid those specifications. Once a DTLS session is established, a RADIUS/DTLS server SHOULD use DTLS Heartbeats [RFC6520] to determine connectivity between the two servers. A server SHOULD also use watchdog packets from the client to determine that the connection is still active. As UDP does not guarantee delivery of messages, RADIUS/DTLS servers which do not implement an application-layer watchdog ...
TY - JOUR. T1 - Involvement of aquaporin in thromboxane A2 receptor-mediated, G12/13/RhoA/NHE-sensitive cell swelling in 1321N1 human astrocytoma cells. AU - Saito, Masaki. AU - Tanaka, Hiroyuki. AU - Sasaki, Masako. AU - Kurose, Hitoshi. AU - Nakahata, Norimichi. PY - 2010/1/1. Y1 - 2010/1/1. N2 - The physiological role of the thromboxane A2 (TXA2) receptor expressed on glial cells remains unclear. We previously reported that 1321N1 human astrocytoma cells pretreated with dibutyryl cyclic AMP (dbcAMP) became swollen in response to U46619, a TXA2 analogue. In the present study, we examined the detailed mechanisms of TXA2 receptor-mediated cell swelling in 1321N1 cells. The cell swelling caused by U46619 was suppressed by expression of p115-RGS, an inhibitory peptide of Gα12/13 pathway and C3 toxin, an inhibitory protein for RhoA. The swelling was also inhibited by treatment with Y27632, a Rho kinase inhibitor and 5-(ethyl-N-isopropyl)amiloride (EIPA), a Na+/H+-exchanger inhibitor. Furthermore, ...
The collecting duct principle cells (PC) play a major role for concentration of urine and regulation of K+ homeostasis. Two water channels, AQP3 and AQP4, are expressed in the PC basolateral membrane (BLM). Here we present evidence that AQP4 participates in regulation of renal K+ transport. K+ enters the cell via Na+,K+-ATPase mediated transport in BLM. The presence of K+ channels in BLM, which is deeply infolded, thus providing a diffusion limited space, permits K+ recirculation, considered important for maintenance of membrane potential. Here we show with co-immunoprecipitation and GST pulldown assays, that in rat renal papilla, AQP4, but not AQP3, assembles with Na+,K+-ATPase and the K+ channel Kir7.1. This led us to hypothesize that AQP4, Na+,K+-ATPase and Kir7.1 form a K+ transporting microdomain, where AQP4 water transport maintains a favorable gradient for K+ efflux and stabilizes membrane potential. A mathematical model of K+ transport across an epithelial cells with a deeply infolded ...
Industrys need to predict the lifetime of adhesively bonded joints has been met by the development of a wide variety of techniques. One particular approach utilises the fact that adhesives and the joints they form can be susceptible to moisture attack. The ingress of moisture into, and through, an adhesive or polymer is termed water permeation. Such a phenomenon can be measured extremely accurately (e.g. through mass change, dielectric permittivity, etc) and it has been shown that for particular systems and environments, a good correlation can be made between the accelerated ageing protocol and in-service failure. This approach has been studied extensively for application within the electronics sector where adhesive/polymeric systems are used both to retain components and coat them. ...
Aquaporins are channel proteins that facilitate the transport of water across cells. The discovery of aquaporins in 1992, for which researcher Peter Agre received the Nobel Prize in Chemistry, opened the door to a new therapeutic approach for treating many health conditions. On one particular start-ups journey in finding applicable aquaporin modulators, the student has become the master. Water is one of the substances that are essential for life on Earth and for the survival of all plants and animals. Although ...
Aquaporin 1 (CO2-, O2- and nitrous oxide-permeable and water-selective) (Zwiazek et al. 2017). Aquaporin-1 tunes pain perception by interacting with Na(v)1.8 Na+ channels in dorsal root ganglion neurons (Zhang and Verkman, 2010). It is upregulated in skeletal muscle in muscular dystrophy (Au et al. 2008). AQP1 has been reported to first insert as a four-helical intermediate, where helices 2 and 4 are not inserted into the membrane. In a second step this intermediate is folded into a six-helical topology. During this process, the orientation of the third helix is inverted, and it can shift out the membrane core (Virkki et al. 2014). Its synthesis is regluated by Kruppel-like factor 2 (KLF2; Q9Y5W3) which also interacts directly with Aqp1 (Fontijn et al. 2015). A nanoscale ion pump has been derived artificially from Aqp1 (Decker et al. 2017 ...
EGFR-mediated expression of aquaporin-3 is involved in human skin fibroblast migration: AQP3 (aquaporin-3), known as an integral membrane channel in epidermal k
Sigma-Aldrich offers abstracts and full-text articles by [C A Ecelbarger, J Terris, G Frindt, M Echevarria, D Marples, S Nielsen, M A Knepper].
I just got a new Betta. He is in a 15 gallon Column tank. (Tall) it came with a filter but after reading a little bit about Bettas I am wondering if I should leave it on there. Is it true that Bettas need very little water movement? Will the HOB filter cause too much water disturbance for him?
PhD Project - Permeable Pavement Engineering for Water Movement in Road Structures and Drainage Effects at University of Greenwich, listed on
Objective: It is well known that VEGFR expression is correlated with peritumoral brain edema in meningiomas. Also Aquaporin4 seems to induce the perifocal edema. In our study we analyzed the correlation of VEGFR1, VEGFR2 and Aquaporin4 to the brain edema. Additionally a potential correlation between[for full text, please go to the a.m. URL ...
Hi, Bit more than a month ago my mom developed burning sensation on her back and stomach, she went to a doc but he said its nothing lifetreatening and she waited for for her turn for the tests, it was like this for a week or two. Few weeks ago the burning sensation became too much to bear and my mom went to a hospital. They took her in and the next day she had issues walking and day later she couldnt walk on her own at all. After a few days they put her on some steroid IV thing for
Hi, Bit more than a month ago my mom developed burning sensation on her back and stomach, she went to a doc but he said its nothing lifetreatening and she waited for for her turn for the tests, it was like this for a week or two. Few weeks ago the burning sensation became too much to bear and my mom went to a hospital. They took her in and the next day she had issues walking and day later she couldnt walk on her own at all. After a few days they put her on some steroid IV thing for
Purchase Molecular Mechanisms of Water Transport Across Biological Membranes, Volume 215 - 1st Edition. Print Book & E-Book. ISBN 9780123646194, 9780080918846
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The Corps of Engineers, Pittsburgh District has been forced to close several recreation areas due to high water following recent rainfall.
Two previous articles in this series on aquaporins have discussed their history, mechanism and stimulation. The current article describes the role of AQP3 in regulating skin cell growth.
The relation between the expressed amounts and conferred water permeabilities of AQP2-S256D-F. Of oocytes, injected with 0.1, 0.2, 0.3, or 0.4 ng of AQP2-S256D-
Please Note, The ebooks are not always PDF format, you might receive epub/kindle formats after purchase. This is Digital Version of (Ebook) 978-3
High-Solids Filtration from DW&PS allows customers to consistently filter high and variable solids while achieving high water recovery.
A new case report about a woman with a UTI who became ill from high water intake raises questions about doctors advice to drink plenty of fluids ...
... 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 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 - ...
... and aquaporin-1 in human erythrocyte membrane domains". Biochimica et Biophysica Acta. 1828 (3): 956-66. doi:10.1016/j.bbamem. ... ISBN 978-0-7167-7108-1.. [page needed] *^ Montel-Hagen A, Kinet S, Manel N, Mongellaz C, Prohaska R, Battini JL, Delaunay J, ... Glucose transporter 1 (or GLUT1), also known as solute carrier family 2, facilitated glucose transporter member 1 (SLC2A1), is ... GLUT 1 is highly conserved.[5] GLUT 1 of humans and mice have 98% identity at the amino acid level. GLUT 1 is encoded by the ...
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 ...
NMOSD can be associated with antibodies that bind to a protein called aquaporin-4 (AQP4). Binding of the anti-AQP4 antibody ... people who are anti-aquaporin-4 or AQP4 antibody-positive. NMOSD is a rare autoimmune disease of the central nervous system ... of 116 participants with NMOSD who were anti-aquaporin-4 (AQP4) antibody positive. The trials were conducted at 62 sites in the ... including the formation of pathological autoantibodies against aquaporin-4 (AQP4), and the permeability of the blood-brain ...
Around active NMO lesions AQP4 may selectively be lost in the absence of aquaporin 1 (AQP1) loss or other structural damage ( ... 28 (1): 84-94. doi:10.1055/s-2007-1019130. Misu T, Höftberger R, Fujihara K, Wimmer I, Takai Y, Nishiyama S, Nakashima I, Konno ... 255 (1): 1-10. doi:10.1007/s00415-007-0754-x. Garrido C, Levy-Gomes A, Teixeira J, Temudo T (2004). "[Schilder's disease: two ... 1][permanent dead link]list of CCSVI publications Dawson J.W. (1916). "The histology of disseminated sclerosis". Trans Roy Soc ...
"Increased aquaporin 1 expression in the tunica albuginea of Peyronie's disease patients: an in vivo pilot study. ". Histol ... "Overexpression of Aquaporin 1 on cysts of patients with polycystic liver disease.". Rev Esp Enferm Dig. 2016. PMID 26838488. ... "Overexpression of Aquaporin-1 is a Prognostic Factor for Biochemical Recurrence in Prostate Adenocarcinoma. ". Pathol Oncol Res ... "Red blood cell aquaporin-1 expression is decreased in hereditary spherocytosis. ". Ann Hematol. 2016. PMID 27465156. ...
"Aquaporin-4 water channel protein in the rat retina and optic nerve: polarized expression in Müller cells and fibrous ... இதன் அளவு மொத்த கண்ணின் அளவில் ஐந்தில் நான்கு பங்கு அளவு கொண்டதாகும்.[1] இதன் மைய பகுதிக்கு அருகாமையில் திரவ நிலையிலும், ... Nagelhus, EA; Veruki, ML; Torp, R; Haug, FM; Laake, JH; Nielsen, S; Agre, P; Ottersen, OP (1 April 1998). " ...
Clinical relevance of serum aquaporin-4 antibody levels in neuromyelitis optica. Neurochem Res. 2013;38(5):997-1001. doi: ... Riordan-Eva, P. (1 January 2004). "Clinical assessment of optic nerve disorders". Eye. 18 (11): 1161-1168. doi:10.1038/sj.eye. ... 91 (1): jnnp-2019-321653. doi:10.1136/jnnp-2019-321653. PMC 6952848. PMID 31740484. Rodriguez M, Siva A, Cross SA, O'Brien PC, ...
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
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] ...
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 ...
Evidence for an aquaporin-mediated water absorption. BBA − General Subjects 1810, 713 (2011). ... Gene, 395(1-2), pp.62-71. Otzen D. (2012). The role of proteins in biosilicification ... PLoS ONE 6, 1 (2011). X. Wang et al., Silicateins, silicatein interactors and ... Bullis, Kevin (1 November 2006). "Silicon and Sun". MIT Technology Review. Retrieved 6 ...
Marples D, Frøkiaer J, Dørup J, Knepper MA, Nielsen S (April 1996). "Hypokalemia-induced downregulation of aquaporin-2 water ... 366 (1): 11-7. doi:10.1007/BF02486556. PMID 185584. S2CID 29761514. Christensen S, Kusano E, Yusufi AN, Murayama N, Dousa TP ( ...
Congenital nephrogenic diabetes insipidus (NDI) may result from V2R or aquaporin-2 (AQP2) mutations. Exogenously administered ... 119 (7 Suppl 1): S87-92. doi:10.1016/j.amjmed.2006.05.014. PMID 16843091. Serradeil-Le Gal, C; Wagnon, J; Valette, G; Garcia, G ... ISBN 978-94-009-0449-1. Greenberg A, Verbalis JG (2006). "Vasopressin receptor antagonists". Kidney Int. 69 (12): 2124-30. doi: ...
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?" ...
... aquaporin, KV1.1, rhodopsin, beta2-adrenergic receptor, and PSD-95. The protein palmitoylation is ... 26 (1): 5-13. doi:10.1080/09687680802683839. PMC 2635919. PMID 19152182. Creaser, S. P.; Peterson, B. R. (2002). "Sensitive and ...
Lee's research also showed that the astrocytic volume change through aquaporin-4 water channel is critical for synaptic ... 231 (1-2): 78-85. doi:10.1016/j.jneuroim.2010.09.020. PMID 20943275. Xu, H.; Zhang, S. L.; Tan, G. W.; Zhu, H. W.; Huang, C. Q ... 151 (1): 25-40. doi:10.1016/j.cell.2012.09.005. PMID 23021213. Yoon, Bo‐Eun; Woo, Junsung; Chun, Ye‐Eun; Chun, Heejung; Jo, ... His team went on to discover two models of glutamate release; a fast mode through TREK-1 in the K2P channel and a slow mode ...
Aquaporins Chloride channels Outer membrane auxiliary proteins (polysaccharide transporter) - α-helical transmembrane proteins ... 1 (1): 21-35. CiteSeerX PMID 15130854. Hopf, Thomas A.; Colwell, Lucy J.; Sheridan, Robert; Rost, Burkhard; ... 76 (1): 125-140. CiteSeerX doi:10.1146/annurev.biochem.76.052705.163539. PMID 17579561. Chen, Chien Peter; ... Sodium/proton antiporter 1 NhaA) Neurotransmitter sodium symporter Ammonia transporters Drug/Metabolite Transporter (small ...
May 2007). "Pattern-specific loss of aquaporin-4 immunoreactivity distinguishes neuromyelitis optica from multiple sclerosis". ... is characterized by neuromyelitis optica IgG antibodies which selectively bind to aquaporin-4. Optic neuritis is associated ... HSV-1 commonly resides in cranial nerve ganglia, particularly the trigeminal ganglia, and may cause painful neuralgias during ... 16 (1): 5-11. doi:10.1080/14787210.2018.1417836. PMID 29278020. Sharma NC, Efstratiou A, Mokrousov I, Mutreja A, Das B, ...
... 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 ...
... via activation of aquaporins, the site of the ADH receptors - back into the circulation. This has two consequences. First, in ... aquaporin 2), and their insertion into the cells' luminal membranes. Excessive ADH causes an inappropriate increase in the ... "Physiology and pathophysiology of renal aquaporins". Seminars in Nephrology. 21 (3): 231-8. doi:10.1053/snep.2001.21647. PMID ... 1%; 7) a fractional urea excretion >55%; 8) an abnormal water load test; and 9) an elevated plasma AVP. Antidiuretic hormone ( ...
Boron's group has extended its interest to understanding mechanisms of gas movement through aquaporins and Rh proteins, and the ... 1st Edition (2002) [1] Medical Physiology Walter F. Boron, Emile L. Boulpaep. 2nd Edition (2008) [2] Medical Physiology Walter ... 259 (5540): 240-1. Bibcode:1976Natur.259..240B. doi:10.1038/259240a0. PMID 2874. S2CID 4276509. Boron, Walter F. (2006). "Acid- ...
The presence of these aquaporin channels in the distal nephron causes increasing water reabsorption from the urine, which ... which signal for the translocation of aquaporin channels via cytosolic vesicles to the apical membrane of the collecting duct. ... Desmopressin (1-deamino-8-D-arginine vasopressin) is a man-made form of the normal human hormone arginine vasopressin (the ... Desmopressin (DDAVP) is usually the first line treatment for mild to moderate type 1 von Willebrand disease. It is not ...
"Demeclocycline attenuates hyponatremia by reducing aquaporin-2 expression in the renal inner medulla". Am. J. Physiol. Renal ... doi:10.1007/978-1-4684-4214-4_15. ISBN 978-1-4684-4216-8. Mørk, A.; Geisler, A. (1995). "A comparative study on the effects of ... 4 (1). Archived from the original on June 6, 2013. Cox, Malcolm (1982). "Tetracycline Nephrotoxicity". In Porter, George A. (ed ... 356-. ISBN 978-1-4757-2085-3. DailyMed. "Demeclocycline Hydrochloride - demeclocycline tablet". Drug label information. ...
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] ...
They contain a variety of aquaporin water channels and appear to be involved in ion transport. They also play a role in sealing ... The oval window has only approximately 1/18 the area of the tympanic membrane and thus produces a higher pressure. The cochlea ... ISBN 1-56053-561-X. Retrieved 2011-05-14. Schacter, Daniel (2012). Psychology. New York, NY: Worth Publishers. ISBN 978- ... 1 (1): 73-81. PMID 4619861. Retrieved 2009-03-11. Ruckenstein, M. J. (2004). "Autoimmune Inner Ear Disease". Current Opinion in ...
Another extremely important factor in dealing with drought stress and regulating the uptake and export of water is aquaporins ( ... "Aquaporins as potential drought tolerance inducing proteins: Towards instigating stress tolerance". Journal of Proteomics. 169 ... 206 (1): 57-73. doi:10.1111/nph.13209. PMID 25580769. Sasidharan, R; Hartman, S; Liu, Z; Martopawiro, S; Sajeev, N; van Veen, H ... ISBN 978-1-78985-317-9. Martinez-Beltran J, Manzur CL. (2005). Overview of salinity problems in the world and FAO strategies to ...
Aquaporins are protein channel pores permeable to H2O water. The diffusion of water through a selectively permeable membrane is ... Koros, W. J.; Ma, Y. H.; Shimidzu, T. (1 January 1996). "Terminology for membranes and membrane processes (IUPAC ... 1], Sidney, Loeb & Sourirajan Srinivasa, "High flow porous membranes for separating water from saline solutions" Friedl, Sarah ...
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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, ...
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.. ...
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 ...
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 ...
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 ...
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 ...
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 ...
Aquaporin 4, FITC conjugates \ AQP4-FITC for more molecular products just contact us ... AQP7 AQP7L AQP9] Aquaporin-7 (AQP-7) (Aquaglyceroporin-7) (Aquaporin adipose) (AQPap) (Aquaporin-7-like). [AQP2] Aquaporin-2 ( ... Aqp7] Aquaporin-7 (AQP-7) (Aquaglyceroporin-7). [AQP6 AQP2L] Aquaporin-6 (AQP-6) (Aquaporin-2-like) (Kidney-specific aquaporin ... Aqp3] Aquaporin-3 (AQP-3) (Aquaglyceroporin-3). [Aqp5] Aquaporin-5 (AQP-5). [AQP9 SSC1] Aquaporin-9 (AQP-9) (Aquaglyceroporin-9 ...
Aquaporin 4 is found in the basolateral cell membrane of principal collecting duct cells and provide a pathway for water to ... TRPA - TRPC (TRPC6) - TRPM (TRPM6) - TRPML (Mucolipin-1) - TRPP - TRPV (TRPV1, TRPV6) ... Retrieved from "" ...
Mouse aquaporin 4 (cDNA clone MGC:37514 IMAGE:4985265), (10ug) available for purchase from OriGene - Your Gene Company. ... Aqp4 (untagged) - Mouse aquaporin 4 (cDNA clone MGC:37514 IMAGE:4985265), (10ug), BC024526, 10ug. $670. 2 weeks. ... Lenti ORF particles, AQP4 (mGFP-tagged) - Human aquaporin 4 (AQP4), transcript variant a, 200ul, >10^7 TU/mL. $960. 3 weeks. ... Lenti ORF particles, AQP4 (mGFP-tagged) - Human aquaporin 4 (AQP4), transcript variant b, 200ul, >10^7 TU/mL. $960. 9 weeks. ...
... 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 ...
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 ...
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 ...
The immunohistochemical expression of aquaporin-1 (AQP1) in asbestos-related malignant pleural mesothelioma (MPM) is emerging ... Immunohistochemical Expression of Aquaporin-1 in Fluoro-Edenite-Induced Malignant Mesothelioma: A Preliminary Report. Giuseppe ... "Immunohistochemical Expression of Aquaporin-1 in Fluoro-Edenite-Induced Malignant Mesothelioma: A Preliminary Report." Int. J. ... The Aquaporin 1 Inhibitor Bacopaside II Reduces Endothelial Cell Migration and Tubulogenesis and Induces Apoptosis ...
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 ...
Localization of aquaporin-1 water channel in glial cells of the human peripheral nervous system. ... The aquaporins (AQPs) are a family of water channel proteins with at least 13 mammalian members (AQPs 0-12) expressed in ... Aquaporin expression in the peripheral nervous system is poorly studied. Here we report that the AQP1 water channel is ...
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. ...
ContentsAquaporins (AQPs) are essential membrane protein channels for the transport of water across membranes. Fluid movement ... Immunolocalization of Aquaporins 1 and 9 in the Ram Efferent Ducts and Epididymis ... 1Department of Anatomy, Biosciences Institute of Botucatu, UNESP - Universidade Estadual Paulista, Botucatu, São Paulo, Brazil2 ... These results indicate that AQPs 1 and 9 have reversed locations and roles in rams, suggesting activity variations related with ...
Differential localization and regulation of two aquaporin-1 homologs in the intestinal epithelia of the marine teleost Sparus ... Differential localization and regulation of two aquaporin-1 homologs in the intestinal epithelia of the marine teleost Sparus ... First published January 2, 2008; doi:10.1152/ajpregu.00695.2007.-Aquaporin (AQP)-mediated intestinal water absorption may play ... homologs of mammalian aquaporin-1 (AQP1), named SaAqp1a and SaAqp1b. Heterologous expression in Xenopus laevis oocytes showed ...
Aquaporin 4 antibody Rabbit Polyclonal from Proteintech validated in Western Blot (WB), Immunoprecipitation (IP), ... Aquaporins are specialized water transport channels in plasma membranes of water-permeable tissues. Aquaporin-4 (AQP4) is the ... Aquaporin 4 Antibody 14 Publications. Rabbit Polyclonal, Catalog number: 16473-1-AP Featured Product KD/KO validated ... Aquaporin-4 exists as two isoforms, a long (M1) isoform with translation initiation at Met-1, and a shorter (M23) isoform with ...
AQP-1 is weakly expressed in neurons and gray matter astrocytes, and more so in white matter astrocytes in uninjured spinal ... Delayed AQP-1 increases were also found in cervical and lumbar segments, suggesting the spreading of AQP-1 changes over time ... Based on our results we propose possible novel roles for AQP-1 in the injured spinal cords: (i) in neuronal and astrocytic ... Interestingly; AQP-1 levels were not affected by long-lasting hypertonicity that significantly increased astrocytic AQP-4, ...
  • 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. (
  • 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. (
  • 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 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 (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. (
  • Aquaporins (AQPs) are membrane protein channels that allow the rapid movement of water through epithelium . (
  • 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) facilitate the rapid and selective movement of small neutral molecules, such as water and glycerol, across cell membranes. (
  • To gain insight into the mechanisms underlying this estrogen-stimulated water transport, we have explored the expression profile and functionality of water channels termed aquaporins (AQPs) in the ovariectomized mouse uterus treated with ovarian steroid hormones. (
  • Aquaporins (AQPs) are integral membrane proteins that form pores in the membrane of biological cells. (
  • 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 . (
  • Aquaporins are channel producing proteins which regulate the flow of water across the cell membrane. (
  • 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. (
  • Positional cloning revealed that tls1 encodes a protein in the aquaporin family co-orthologous to known B channel proteins in other species. (
  • AQP11 is functionally distinct from other proteins of the aquaporin superfamily and could represent a new aquaporin subfamily [ PMID: 16650285 ]. (
  • 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. (
  • Kang, Hunseung 2007-05-24 00:00:00 Despite the high isoform multiplicity of aquaporins in plants, with 35 homologues including 13 plasma membrane intrinsic proteins (PIPs) in Arabidosis thaliana, the individual and integrated functions of aquaporins under various physiological conditions remain unclear. (
  • Benga G (2009) Water channel proteins (later called aquaporins) and relatives: past, present, and future. (
  • 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. (
  • Aquaporins are membrane proteins that form channels (centre) that help water molecules (red and white spheres) pass in and out of cells. (
  • Aquaporins, channel proteins that facilitate the transfer of water across cell membranes, play a central role in maintaining the plant water status. (
  • Aquaporins are a class of proteins that form membrane channels in cell walls and allow for water movement between a cell and its surroundings. (
  • 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. (
  • 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. (
  • 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. (
  • Aquaporin-11: a channel protein lacking apparent transport function expressed in brain. (
  • 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. (
  • 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 . (
  • 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. (
  • However, it remains a mystery how aquaporin-2 (an integral membrane protein) and other apical transporters are delivered to the urine. (
  • Computer illustration showing the structure of a molecule of the human aquaporin 1 protein (blue, and white ribbon). (
  • 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. (
  • 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 ]. (
  • To better understand aquaporin functions in plants under various stress conditions, we examined transgenic Arabidopsis and tobacco plants that constitutively overexpress Arabidopsis PIP1;4 or PIP2;5 under various abiotic stress conditions. (
  • The expression of several PIPs was noticeably affected by the overexpression of PIP1;4 or PIP2;5 in Arabidopsis under dehydration stress, suggesting that the expression of one aquaporin isoform influences the expression levels of other aquaporins under stress conditions. (
  • 1] "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana. (
  • 3] "From genome to function: the Arabidopsis aquaporins. (
  • An expression analysis of a gene family encoding plasma membrane aquaporins in response to abiotic stresses in Arabidopsis thaliana. (
  • TIP5;1 is an aquaporin specifically targeted to pollen mitochondria and is probably involved in nitrogen remobilization in Arabidopsis thaliana. (
  • 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. (
  • Thus, we propose that TIP5;1 and TIP1;3 are involved in nitrogen recycling in pollen tubes of Arabidopsis thaliana. (
  • In this study, we have identified a PIP1 subfamily AQP ( MaPIP1;1 ) gene from banana and characterized it by overexpression in transgenic Arabidopsis plants. (
  • 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. (
  • 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. (
  • Recently, mutations in the autosomal gene coding for water-channel aquaporin 2 (AQP2) of the renal collecting duct were reported in an NDI patient. (
  • 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. (
  • Aquaporin-2 levels in vitro and in vivo are regulated by VACM-1, a cul 5 gene. (
  • 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. (
  • 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. (
  • AQP 11 and 12 appear to be more distantly related to the other mammalian aquaporins and aquaglyceroporins. (
  • We propose that ligand-dependent HER activation constitutes a generalized signaling principle in the mammalian hypertonic stress response relevant to aquaporin expression. (
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human UDP-Glucose Glycoprotein Glucosyltransferase 1 (UGGT1) in Tissue homogenates, cell lysates and other biological fluids. (
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Mannosyl Alpha-1,6-Glycoprotein Beta-1,6-N-Acetylglucosaminyltransferase (MGAT5) in serum, plasma, tissue homogenates and other biological fluids. (
  • The microtiter plate provided in this kit has been pre-coated with an antibody specific to Mannosyl Alpha-1,6-Glycoprotein Beta-1,6-N-Acetylglucosaminyltransferase (MGAT5). (
  • WB analysis of Jurkat cells using GTX45889 AQP10 antibody at 0.2-1μg/ml. (
  • 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. (
  • Long-term regulation of four renal aquaporins in rats. (
  • 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. (
  • 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. (
  • Altered aquaporin 9 expression and localization in human hepatocellular carcinoma. (
  • Expression, localization, and regulation of aquaporin-1 to -3 in rat urothelia. (
  • RESULTS: Immunohistochemical localization of AQP(1) in mice tumor was labeled in capillaries, post capillary venules endothelial cells. (
  • Furthermore, the position of histidines in different members of the aquaporin family can "tune" the pH sensitivity toward alkaline or acid pH ranges. (
  • pH regulation was also found in two other members of the aquaporin family. (
  • Extensive research on the function of aquaporins have been implemented into many separate types of cell membranes. (
  • Boury-Jamot M, Sougrat R, Tailhardat M, Le Varlet B, Bonte F, Dumas M, Verbavatz JM (2006) Expression and function of aquaporins in human skin: Is aquaporin-3 just a glycerol transporter? (
  • The aim is to investigate the physiological role of aquaporins and vasopressin receptors in porcine and rat urinary bladders. (
  • Agren J, Zelenin S, Hakansson M, Eklof AC, Aperia A, Nejsum LN, Nielsen S, Sedin G (2003) Transepidermal water loss in developing rats: role of aquaporins in the immature skin. (
  • 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. (
  • 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. (
  • Aquaporin-3 function is to promote glycerol permeability across cell membrane. (
  • 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. (
  • Defective hepatocyte aquaporin-8 expression and reduced canalicular membrane water permeability in estrogen-induced cholestasis. (
  • 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). (
  • [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. (
  • 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. (
  • 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. (
  • 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 ]. (
  • Physiological indices demonstrated that the increased salt tolerance conferred by MaPIP1;1 is related to reduced membrane injury and high cytosolic K + /Na + ratio. (
  • The team combines molecular, physiological and genetic approaches and characterizes water transport at the level of cloned aquaporins, purified membranes, living cells or organs like excised roots or rosettes. (
  • 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. (
  • 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. (
  • 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. (
  • 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. (
  • Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). (
  • Aquaporins are tetramers and each subunit forms a pore. (
  • Large Pore Ion and Metabolite-Permeable Channel Regulation of Postnatal Ventricular Zone Neural Stem and Progenitor Cells: Interplay between Aquaporins, Connexins, and Pannexins? (
  • Here, we focus on the roles of three such large pore channels, aquaporin 4, connexin 43, and pannexin 1. (
  • with six transmembrane helices (1-6) and five connecting loops (A-E). Two highly conserved loops (B and E) each contain the signature motif present in every aquaporin, asparagine-proline-alanine (NPA), which forms one wall of the water pore. (
  • Taking advantage of the known crystal structure of aquaporin-1 and the power of molecular dynamics simulations, the researchers explored the central pore as a candidate pathway for conducting ions. (
  • Gating of the central pore is controlled by cyclic guanosine monophosphate, a signaling nucleotide inside the cell, which induces a conformational change in one of the aquaporin loops (loop D). (
  • By modifying the pore-lining residue, or altering the length of loop D that gates the pore, we can shut down the ion conductivity completely, or engineer new aquaporins that can be opened more easily or have a higher ion conduction rate once open. (
  • 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. (
  • Secretin promotes osmotic water transport in rat cholangiocytes by incresing aquaporin-1 water channels in plasma membrane. (
  • Additionally, the improved drought tolerance conferred by MaPIP1;1 is associated with decreased membrane injury and improved osmotic adjustment. (
  • 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. (
  • 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. (
  • Taken together, the results strongly suggest that plasma membrane aquaporin pores determine the efficiency of H 2 O 2 signalling between cells. (
  • Description: A sandwich ELISA kit for detection of Mannosyl Alpha-1,6-Glycoprotein Beta-1,6-N-Acetylglucosaminyltransferase from Human in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (
  • Aquaporins are specialized water transport channels in plasma membranes of water-permeable tissues. (
  • 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. (
  • Aquaporins facilitate the diffusion of water across cell membranes. (
  • Mutations in aquaporin-2 cause diabitis insipidus. (
  • Mutations in aquaporin-0 in mice cause congenital cataracts. (
  • 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 Aquaporin team studies the various modes of water transport in plant tissues. (
  • Angelico G, Caltabiano R, Loreto C, Ieni A, Tuccari G, Ledda C, Rapisarda V. Immunohistochemical Expression of Aquaporin-1 in Fluoro-Edenite-Induced Malignant Mesothelioma: A Preliminary Report. (
  • Expression of aquaporin-5 (AQP5), studied by immunofluorescence and confocal microscopy, showed an increase in parallel with the increase in P f following hyperosmotic stress. (
  • 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. (
  • 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. (
  • Bellati J , Champeyroux C , Hem S , Rofidal V , Krouk G , Maurel C , Santoni V ✉ (2016) Novel aquaporin regulatory mechanisms revealed by interactomics . (
  • 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. (
  • 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). (
  • The ar/R (aromatic/arginine) region and the highly conserved NPA (for asparagine, proline, alanine) region have been implicated in the selectivity of aquaporins. (
  • Here, I will summarize our current knowledge of the involvement of aquaporin-formed pores and tight junctions in epidermal water homeostasis - as well as in other functions - and their putative roles in skin dryness. (
  • Comparative Analysis for the Presence of IgG Anti-Aquaporin-1 in Patients with NMO-Spectrum Disorders. (
  • 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? (
  • Plant aquaporins: membrane channels with multiple integrated functions. (
  • Plant aquaporins: roles in plant physiology. (
  • Analysis of the water transport activity of a mutant version of TIP5;1 (TIP5;1-H131A) and amino acid alignment with other plant aquaporins regulated by pH suggested that a conserved motif is involved in pH sensing. (
  • In the last few years, the team has uncovered novel functions and regulations of plant aquaporins. (
  • In the present study, immunohistochemistry was utilized to localize the expression of AQP 1, AQP2 in the testis and prostate of adult bactrian camel ( Camelus bactrianus ). (
  • 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. (
  • Reconstitution of CO2 Regulation of SLAC1 Anion Channel and Function of CO2-Permeable PIP2;1 Aquaporin as CARBONIC ANHYDRASE4 Interactor. (
  • 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. (
  • Differential upregulation of aquaporin-4 mRNA expression in reactive astrocytes after brain injury: potential role in brain edema. (
  • 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. (
  • Agre P, Kozono D. Aquaporin water channels: molecular mechanisms for human diseases. (
  • Home Research Outputs Perilipin 1 binds to aquaporin 7 in human adipocytes and con. (
  • Human aquaporins: regulators of transcellular water flow. (
  • Expression and localisation of aquaporin water channels in human urothelium in situ and in vitro. (
  • Bellemere G, Von Stetten O, Oddos T (2008) Retinoic acid increases aquaporin 3 expression in normal human skin. (
  • King, Landon S. / Role of proneuregulin 1 cleavage and human epidermal growth factor receptor activation in hypertonic aquaporin induction . (
  • The molecular and cellular bases of this process are addressed by studying the multiple facets of aquaporin regulation. (
  • Wudick MM , Li X, Valentini V , Geldner N, Chory J, Lin J, Maurel C ✉, Luu D-T ✉ (2015) Sub-cellular redistribution of root aquaporins induced by hydrogen peroxide . (
  • and ( iv ) polydipsic, induced primarily by high water intake with consequent suppression of vasopressin release ( 1 ). (
  • Aquaporin channels may be subject to intense short term regulation via signal transduction. (
  • Aquaporin-1 in plasma membrane and caveolae provides mercury-sensitive water channels across lung endothelium. (
  • Single Water Channels of Aquaporin-1 Do not Obey the Kedem-Katchalsky Equations Curry, M.R. (
  • Marinelli, R. A. and LaRusso, N. F. (1997), Aquaporin water channels in liver: Their significance in bile formation. (
  • For the transcellular route water channels, formed by so-called aquaporins, are of importance. (
  • Agre P (2006) The aquaporin water channels. (
  • 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. (
  • A number of aquaporins, including aquaporin-1, have been found to function as ion channels, as well. (
  • Your search returned 2091 Miscellaneous Antibodies across 1 supplier. (
  • 2001), Mercurial sensitivity of aquaporin 1 endofacial. (
  • Mercurial sensitivity of aquaporin 1 endofacial loop B residues. (
  • For many Aquaporins the water conductivity exhibits mercury sensitivity. (
  • For AtNIP1;1 it was not possible to inhibit the water conductivity with mercury but the ammonia conductivity showed mercury sensitivity. (
  • Fig. 1 B shows the sequence alignments of the critical regions that contribute to pH and Ca 2+ sensitivity, loop A, loop C, and the COOH terminus tail. (