Aquaporin 1 forms a water-specific channel that is constitutively expressed at the PLASMA MEMBRANE of ERYTHROCYTES and KIDNEY TUBULES, PROXIMAL. It provides these cells with a high permeability to WATER. In humans polymorphisms of this protein result in the Colton blood group antigen.
Aquaporin 5 is a water-specific channel protein that is expressed primarily in alveolar, tracheal, and upper bronchial EPITHELIUM. It plays an important role in maintaining water HOMEOSTASIS in the LUNGS and may also regulate release of SALIVA and TEARS in the SALIVARY GLANDS and the LACRIMAL GLAND.
Aquaporin 3 is an aquaglyceroporin that is expressed in the KIDNEY COLLECTING DUCTS and is constitutively localized at the basolateral MEMBRANE.
Aquaporin 4 is the major water-selective channel in the CENTRAL NERVOUS SYSTEM of mammals.
A class of porins that allow the passage of WATER and other small molecules across CELL MEMBRANES.
Aquaporin 2 is a water-specific channel protein that is expressed in KIDNEY COLLECTING DUCTS. The translocation of aquaporin 2 to the apical PLASMA MEMBRANE is regulated by VASOPRESSIN, and MUTATIONS in AQP2 have been implicated in a variety of kidney disorders including DIABETES INSIPIDUS.
Aquaporin 6 is an aquaglyceroporin that is found primarily in KIDNEY COLLECTING DUCTS. AQP6 protein functions as an anion-selective channel.
A clear, odorless, tasteless liquid that is essential for most animal and plant life and is an excellent solvent for many substances. The chemical formula is hydrogen oxide (H2O). (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Mercury chloride (HgCl2). A highly toxic compound that volatizes slightly at ordinary temperature and appreciably at 100 degrees C. It is corrosive to mucous membranes and used as a topical antiseptic and disinfectant.
Tendency of fluids (e.g., water) to move from the less concentrated to the more concentrated side of a semipermeable membrane.
A subgroup of aquaporins that transport WATER; GLYCEROL; and other small solutes across CELL MEMBRANES.
Sets of cell surface antigens located on BLOOD CELLS. They are usually membrane GLYCOPROTEINS or GLYCOLIPIDS that are antigenically distinguished by their carbohydrate moieties.
The balance of fluid in the BODY FLUID COMPARTMENTS; total BODY WATER; BLOOD VOLUME; EXTRACELLULAR SPACE; INTRACELLULAR SPACE, maintained by processes in the body that regulate the intake and excretion of WATER and ELECTROLYTES, particularly SODIUM and POTASSIUM.
A trihydroxy sugar alcohol that is an intermediate in carbohydrate and lipid metabolism. It is used as a solvent, emollient, pharmaceutical agent, and sweetening agent.
Property of membranes and other structures to permit passage of light, heat, gases, liquids, metabolites, and mineral ions.
A quality of cell membranes which permits the passage of solvents and solutes into and out of cells.
The loss of water vapor by plants to the atmosphere. It occurs mainly from the leaves through pores (stomata) whose primary function is gas exchange. The water is replaced by a continuous column of water moving upwards from the roots within the xylem vessels. (Concise Dictionary of Biology, 1990)
Straight tubes commencing in the radiate part of the kidney cortex where they receive the curved ends of the distal convoluted tubules. In the medulla the collecting tubules of each pyramid converge to join a central tube (duct of Bellini) which opens on the summit of the papilla.
The ability of the kidney to excrete in the urine high concentrations of solutes from the blood plasma.
A genetic or acquired polyuric disorder characterized by persistent hypotonic urine and HYPOKALEMIA. This condition is due to renal tubular insensitivity to VASOPRESSIN and failure to reduce urine volume. It may be the result of mutations of genes encoding VASOPRESSIN RECEPTORS or AQUAPORIN-2; KIDNEY DISEASES; adverse drug effects; or complications from PREGNANCY.
Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.
Gated, ion-selective glycoproteins that traverse membranes. The stimulus for ION CHANNEL GATING can be due to a variety of stimuli such as LIGANDS, a TRANSMEMBRANE POTENTIAL DIFFERENCE, mechanical deformation or through INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS.
A syndrome characterized by acute OPTIC NEURITIS; MYELITIS, TRANSVERSE; demyelinating and/or necrotizing lesions in the OPTIC NERVES and SPINAL CORD; and presence of specific autoantibodies to AQUAPORIN 4.
Urination of a large volume of urine with an increase in urinary frequency, commonly seen in diabetes (DIABETES MELLITUS; DIABETES INSIPIDUS).
The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.
The commonest and widest ranging species of the clawed "frog" (Xenopus) in Africa. This species is used extensively in research. There is now a significant population in California derived from escaped laboratory animals.
The pressure required to prevent the passage of solvent through a semipermeable membrane that separates a pure solvent from a solution of the solvent and solute or that separates different concentrations of a solution. It is proportional to the osmolality of the solution.
Female germ cells derived from OOGONIA and termed OOCYTES when they enter MEIOSIS. The primary oocytes begin meiosis but are arrested at the diplotene state until OVULATION at PUBERTY to give rise to haploid secondary oocytes or ova (OVUM).
Agents that reduce the excretion of URINE, most notably the octapeptide VASOPRESSINS.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
A plant genus of the family LILIACEAE. Members contain tuliposides and tulipalins and have been associated with allergic contact dermatitis in florists.
The contribution to barometric PRESSURE of gaseous substance in equilibrium with its solid or liquid phase.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
A plant family of the order Violales, subclass Dilleniidae, class Magnoliopsida. The common name of rock rose is used with several plants of this family.
The usually underground portions of a plant that serve as support, store food, and through which water and mineral nutrients enter the plant. (From American Heritage Dictionary, 1982; Concise Dictionary of Biology, 1990)
Increased intracellular or extracellular fluid in brain tissue. Cytotoxic brain edema (swelling due to increased intracellular fluid) is indicative of a disturbance in cell metabolism, and is commonly associated with hypoxic or ischemic injuries (see HYPOXIA, BRAIN). An increase in extracellular fluid may be caused by increased brain capillary permeability (vasogenic edema), an osmotic gradient, local blockages in interstitial fluid pathways, or by obstruction of CSF flow (e.g., obstructive HYDROCEPHALUS). (From Childs Nerv Syst 1992 Sep; 8(6):301-6)
Inorganic compounds that contain mercury as an integral part of the molecule.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
A transparent, biconvex structure of the EYE, enclosed in a capsule and situated behind the IRIS and in front of the vitreous humor (VITREOUS BODY). It is slightly overlapped at its margin by the ciliary processes. Adaptation by the CILIARY BODY is crucial for OCULAR ACCOMMODATION.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in plants.
Fluids composed mainly of water found within the body.
Drugs used for their effects on the kidneys' regulation of body fluid composition and volume. The most commonly used are the diuretics. Also included are drugs used for their antidiuretic and uricosuric actions, for their effects on the kidneys' clearance of other drugs, and for diagnosis of renal function.
The concentration of osmotically active particles in solution expressed in terms of osmoles of solute per liter of solution. Osmolality is expressed in terms of osmoles of solute per kilogram of solvent.
Antidiuretic hormones released by the NEUROHYPOPHYSIS of all vertebrates (structure varies with species) to regulate water balance and OSMOLARITY. In general, vasopressin is a nonapeptide consisting of a six-amino-acid ring with a cysteine 1 to cysteine 6 disulfide bridge or an octapeptide containing a CYSTINE. All mammals have arginine vasopressin except the pig with a lysine at position 8. Vasopressin, a vasoconstrictor, acts on the KIDNEY COLLECTING DUCTS to increase water reabsorption, increase blood volume and blood pressure.
Histochemical localization of immunoreactive substances using labeled antibodies as reagents.
The condition that results from excessive loss of water from a living organism.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
A phylum of fungi that are mutualistic symbionts and form ARBUSCULAR MYCORRHIZAE with PLANT ROOTS.
A type of TRANSMISSION ELECTRON MICROSCOPY in which the object is examined directly by an extremely narrow electron beam scanning the specimen point-by-point and using the reactions of the electrons that are transmitted through the specimen to create the image. It should not be confused with SCANNING ELECTRON MICROSCOPY.
Glands that secrete SALIVA in the MOUTH. There are three pairs of salivary glands (PAROTID GLAND; SUBLINGUAL GLAND; SUBMANDIBULAR GLAND).
The body of a fungus which is made up of HYPHAE.
A synthetic analog of the pituitary hormone, ARGININE VASOPRESSIN. Its action is mediated by the VASOPRESSIN receptor V2. It has prolonged antidiuretic activity, but little pressor effects. It also modulates levels of circulating FACTOR VIII and VON WILLEBRAND FACTOR.
A clear, colorless, viscous organic solvent and diluent used in pharmaceutical preparations.
Large and highly vacuolated cells possessing many chloroplasts occuring in the interior cross-section of leaves, juxtaposed between the epidermal layers.
A plant genus of the family AIZOACEAE. It is a native of Africa and widely planted for erosion control to stabilize soil along roadsides and beaches.
The internal portion of the kidney, consisting of striated conical masses, the renal pyramids, whose bases are adjacent to the cortex and whose apices form prominent papillae projecting into the lumen of the minor calyces.
Body organ that filters blood for the secretion of URINE and that regulates ion concentrations.
One of two salivary glands in the neck, located in the space bound by the two bellies of the digastric muscle and the angle of the mandible. It discharges through the submandibular duct. The secretory units are predominantly serous although a few mucous alveoli, some with serous demilunes, occur. (Stedman, 25th ed)
Specific molecular sites or proteins on or in cells to which VASOPRESSINS bind or interact in order to modify the function of the cells. Two types of vasopressin receptor exist, the V1 receptor in the vascular smooth muscle and the V2 receptor in the kidneys. The V1 receptor can be subdivided into V1a and V1b (formerly V3) receptors.
Prolonged dry periods in natural climate cycle. They are slow-onset phenomena caused by rainfall deficit combined with other predisposing factors.
A class of large neuroglial (macroglial) cells in the central nervous system - the largest and most numerous neuroglial cells in the brain and spinal cord. Astrocytes (from "star" cells) are irregularly shaped with many long processes, including those with "end feet" which form the glial (limiting) membrane and directly and indirectly contribute to the BLOOD-BRAIN BARRIER. They regulate the extracellular ionic and chemical environment, and "reactive astrocytes" (along with MICROGLIA) respond to injury.
A variation of the PCR technique in which cDNA is made from RNA via reverse transcription. The resultant cDNA is then amplified using standard PCR protocols.
An aquatic genus of the family, Pipidae, occurring in Africa and distinguished by having black horny claws on three inner hind toes.
A silver metallic element that exists as a liquid at room temperature. It has the atomic symbol Hg (from hydrargyrum, liquid silver), atomic number 80, and atomic weight 200.59. Mercury is used in many industrial applications and its salts have been employed therapeutically as purgatives, antisyphilitics, disinfectants, and astringents. It can be absorbed through the skin and mucous membranes which leads to MERCURY POISONING. Because of its toxicity, the clinical use of mercury and mercurials is diminishing.
The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.
A strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company.
A widely cultivated plant, native to Asia, having succulent, edible leaves eaten as a vegetable. (From American Heritage Dictionary, 1982)
An enzyme that catalyzes the formation of glycerol 3-phosphate from ATP and glycerol. Dihydroxyacetone and L-glyceraldehyde can also act as acceptors; UTP and, in the case of the yeast enzyme, ITP and GTP can act as donors. It provides a way for glycerol derived from fats or glycerides to enter the glycolytic pathway. EC 2.7.1.30.
The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.
Yeast-like ascomycetous fungi of the family Saccharomycetaceae, order SACCHAROMYCETALES isolated from exuded tree sap.
A plant genus of the family ROSACEAE known for the edible fruit.
A mutant strain of Rattus norvegicus used in research on renal function and hypertension and as a disease model for diabetes insipidus.
Closable openings in the epidermis of plants on the underside of leaves. They allow the exchange of gases between the internal tissues of the plant and the outside atmosphere.
Protein-lipid combinations abundant in brain tissue, but also present in a wide variety of animal and plant tissues. In contrast to lipoproteins, they are insoluble in water, but soluble in a chloroform-methanol mixture. The protein moiety has a high content of hydrophobic amino acids. The associated lipids consist of a mixture of GLYCEROPHOSPHATES; CEREBROSIDES; and SULFOGLYCOSPHINGOLIPIDS; while lipoproteins contain PHOSPHOLIPIDS; CHOLESTEROL; and TRIGLYCERIDES.
Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.
Hypertonic sodium chloride solution. A solution having an osmotic pressure greater than that of physiologic salt solution (0.9 g NaCl in 100 ml purified water).
A schistosomicide possibly useful against other parasites. It has irritant emetic properties and may cause lethal cardiac toxicity among other adverse effects.
Expanded structures, usually green, of vascular plants, characteristically consisting of a bladelike expansion attached to a stem, and functioning as the principal organ of photosynthesis and transpiration. (American Heritage Dictionary, 2d ed)
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Slender tubular or hairlike excretory structures found in insects. They emerge from the alimentary canal between the mesenteron (midgut) and the proctodeum (hindgut).
An intermediate filament protein found only in glial cells or cells of glial origin. MW 51,000.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Synthetic transcripts of a specific DNA molecule or fragment, made by an in vitro transcription system. This cRNA can be labeled with radioactive uracil and then used as a probe. (King & Stansfield, A Dictionary of Genetics, 4th ed)
Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies.
Microscopy in which the samples are first stained immunocytochemically and then examined using an electron microscope. Immunoelectron microscopy is used extensively in diagnostic virology as part of very sensitive immunoassays.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Liquids transforming into solids by the removal of heat.
Na-K-Cl transporter in the ASCENDING LIMB OF LOOP OF HENLE. It mediates active reabsorption of sodium chloride and is inhibited by LOOP DIURETICS such as FUROSEMIDE; and BUMETANIDE. Mutations in the gene encoding SLC12A1 are associated with a BARTTER SYNDROME.
A cytotoxic sulfhydryl reagent that inhibits several subcellular metabolic systems and is used as a tool in cellular physiology.
Strains of mice in which certain GENES of their GENOMES have been disrupted, or "knocked-out". To produce knockouts, using RECOMBINANT DNA technology, the normal DNA sequence of the gene being studied is altered to prevent synthesis of a normal gene product. Cloned cells in which this DNA alteration is successful are then injected into mouse EMBRYOS to produce chimeric mice. The chimeric mice are then bred to yield a strain in which all the cells of the mouse contain the disrupted gene. Knockout mice are used as EXPERIMENTAL ANIMAL MODELS for diseases (DISEASE MODELS, ANIMAL) and to clarify the functions of the genes.
Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.
A compound formed in the liver from ammonia produced by the deamination of amino acids. It is the principal end product of protein catabolism and constitutes about one half of the total urinary solids.
Solutions that have a greater osmotic pressure than a reference solution such as blood, plasma, or interstitial fluid.
A plant genus of the family BRASSICACEAE that contains ARABIDOPSIS PROTEINS and MADS DOMAIN PROTEINS. The species A. thaliana is used for experiments in classical plant genetics as well as molecular genetic studies in plant physiology, biochemistry, and development.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.
The quantity of volume or surface area of CELLS.
An early embryo that is a compact mass of about 16 BLASTOMERES. It resembles a cluster of mulberries with two types of cells, outer cells and inner cells. Morula is the stage before BLASTULA in non-mammalian animals or a BLASTOCYST in mammals.
A subclass of symporters that specifically transport SODIUM CHLORIDE and/or POTASSIUM CHLORIDE across cellular membranes in a tightly coupled process.
Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.
Cells that line the inner and outer surfaces of the body by forming cellular layers (EPITHELIUM) or masses. Epithelial cells lining the SKIN; the MOUTH; the NOSE; and the ANAL CANAL derive from ectoderm; those lining the RESPIRATORY SYSTEM and the DIGESTIVE SYSTEM derive from endoderm; others (CARDIOVASCULAR SYSTEM and LYMPHATIC SYSTEM) derive from mesoderm. Epithelial cells can be classified mainly by cell shape and function into squamous, glandular and transitional epithelial cells.
A plant genus of the family FAGACEAE that is a source of TANNINS. Do not confuse with Holly (ILEX).
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
A plant species of the family POACEAE. It is a tall grass grown for its EDIBLE GRAIN, corn, used as food and animal FODDER.
A computer simulation developed to study the motion of molecules over a period of time.
Adaptation to a new environment or to a change in the old.
The relationships of groups of organisms as reflected by their genetic makeup.
Starches that have been chemically modified so that a percentage of OH groups are substituted with 2-hydroxyethyl ether groups.
A ubiquitous sodium salt that is commonly used to season food.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

AQP2 is found in the apical cell membranes of the kidneys collecting duct principal cells and in intracellular vesicles located throughout the cell. It is the only aquaporin regulated by vasopressin. The basic job of aquaporin 2 is to reabsorb water from the urine while its being removed from the blood by the kidney. Aquaporin 2 is in kidney epithelial cells and usually lies dormant in intracellular vesicle membranes. When it is needed, vasopressin binds to the cell surface vasopressin receptor thereby activating a signaling pathway that causes the aquaporin 2 containing vesicles to fuse with the plasma membrane, so the aquaporin 2 can be used by the cell. This aquaporin is regulated in two ways by the peptide hormone vasopressin: short-term regulation (minutes) through trafficking of AQP2 vesicles to the apical region where they fuse with the apical plasma membrane long-term regulation (days) through an increase in AQP2 gene expression. This aquaporin is also regulated by food intake. Fasting ...
Vasopressin is the key regulator of water homeostasis in vertebrates. Central to its antidiuretic action in mammals is the redistribution of the water channel aquaporin 2 (AQP2) from intracellular vesicles to the apical membrane of kidney epithelial cells, an event initiated by an increase in cAMP and activation of protein kinase A. The subsequent steps of the signaling cascade are not known. To identify proteins involved in the AQP2 shuttle we exploited a recently developed cell line (CD8) derived from the rabbit cortical collecting duct and stably transfected with rat AQP2 cDNA. Treatment of CD8 cells with pertussis toxin (PTX) inhibited both the vasopressin-induced increase in water permeability and the redistribution of AQP2 from an intracellular compartment to the apical membrane. ADP-ribosylation studies revealed the presence of at least two major PTX substrates. Correspondingly, two alpha subunits of PTX-sensitive G proteins, Galphai2 and Galphai3, were identified by Western blotting.
With Aquaporin Inside™ Reverse Osmosis membranes, water treatment can be done with lower energy consumption compared to conventional membrane technology. The benefit comes from the aquaporin proteins which are very efficient in transporting water. This enables the water treatment plant to increase the capacity of treated wastewater without increasing the energy consumption, or remaining at the same capacity level while lowering the energy consumption. At the same time, Aquaporin membranes has the potential to remove also small, neutral compounds such as micro pollutants/trace organics, improving re-use water quality.. Aquaporin Inside™ Forward Osmosis ...
Plasma Membrane Abundance of Human Aquaporin 5 Is Dynamically Regulated by Multiple Pathways. . Biblioteca virtual para leer y descargar libros, documentos, trabajos y tesis universitarias en PDF. Material universiario, documentación y tareas realizadas por universitarios en nuestra biblioteca. Para descargar gratis y para leer online.
TY - JOUR. T1 - Role of Aquaporin 0 in lens biomechanics. AU - Sindhu Kumari, S.. AU - Gupta, Neha. AU - Shiels, Alan. AU - FitzGerald, Paul G. AU - Menon, Anil G.. AU - Mathias, Richard T.. AU - Varadaraj, Kulandaiappan. PY - 2015/4/19. Y1 - 2015/4/19. N2 - Abstract Maintenance of proper biomechanics of the eye lens is important for its structural integrity and for the process of accommodation to focus near and far objects. Several studies have shown that specialized cytoskeletal systems such as the beaded filament (BF) and spectrin-actin networks contribute to mammalian lens biomechanics; mutations or deletion in these proteins alters lens biomechanics. Aquaporin 0 (AQP0), which constitutes ∼45% of the total membrane proteins of lens fiber cells, has been shown to function as a water channel and a structural cell-to-cell adhesion (CTCA) protein. Our recent ex vivo study on AQP0 knockout (AQP0 KO) mouse lenses showed the CTCA function of AQP0 could be crucial for establishing the refractive ...
Aquaporin 1: Aquaporin 1 forms a water-specific channel that is constitutively expressed at the PLASMA MEMBRANE of ERYTHROCYTES and KIDNEY TUBULES, PROXIMAL. It provides these cells with a high permeability to WATER. In humans polymorphisms of this protein result in the Colton blood group antigen.
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Aquaporin 4 is found in the basolateral cell membrane of principal collecting duct cells and provide a pathway for water to exit these cells. AQP4 is constitutively expressed. AQP4 is expressed in astrocytes and are upregulated by direct insult to the central nervous system. ...
Description: FLRT3 produced in Sf9 insect cells is a single, glycosylated polypeptide chain containing 508 amino acids (29-528a.a.) and having a molecular mass of 57.6kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).;FLRT3 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques ...
Hypertrophic cardiac myocytes, which are larger than normal, have more cytoplasm and larger nuclei than normal cells. The enlarged nuclei contain more DNA and RNA than their normal counterparts and generate more messenger RNA. The cytoplasm of hypertrophic myocytes contains more myofilaments and mitochondria, but the number of other cytoplasmic organelles is not increased. Water influx, which is typical of hydropic swelling, is not found in hypertrophy. ...
Aqp4 - Aqp4 (untagged) - Mouse aquaporin 4 (cDNA clone MGC:37514 IMAGE:4985265), (10ug) available for purchase from OriGene - Your Gene Company.
TY - JOUR. T1 - Aquaporin water channels - From atomic structure to clinical medicine. AU - Agre, Peter. AU - King, Landon S.. AU - Yasui, Masato. AU - Guggino, Wm B.. AU - Ottersen, Ole Petter. AU - Fujiyoshi, Yoshinori. AU - Engel, Andreas. AU - Nielsen, Søren. PY - 2002/7/1. Y1 - 2002/7/1. N2 - The water permeability of biological membranes has been a longstanding problem in physiology, but the proteins responsible for this remained unknown until discovery of the aquaporin 1 (AQP1) water channel protein. AQP1 is selectively permeated by water driven by osmotic gradients. The atomic structure of human AQP1 has recently been defined. Each subunit of the tetramer contains an individual aqueous pore that permits single-file passage of water molecules but interrupts the hydrogen bonding needed for passage of protons. At least 10 mammalian aquaporins have been identified, and these are selectively permeated by water (aquaporins) or water plus glycerol (aquaglyceroporins). The sites of expression ...
TY - JOUR. T1 - Expression and subcellular localization of aquaporin water channels in the polarized hepatocyte cell line, WIF-B. AU - Gradilone, Sergio A.. AU - Tietz, Pamela S.. AU - Splinter, Patrick L.. AU - Marinelli, Raúl A.. AU - LaRusso, Nicholas F.. PY - 2005/8/18. Y1 - 2005/8/18. N2 - Background: Recent data suggest that canalicular bile secretion involves selective expression and coordinated regulation of aquaporins (AQPs), a family of water channels proteins. In order to further characterize the role of AQPs in this process, an in vitro cell system with retained polarity and expression of AQPs and relevant solute transporters involved in bile formation is highly desirable. The WIF-B cell line is a highly differentiated and polarized rat hepatoma/human fibroblast hybrid, which forms abundant bile canalicular structures. This cell line has been reported to be a good in vitro model for studying hepatocyte polarity. Results: Using RT-PCR, immunoblotting and confocal immunofluorescence, ...
Purpose: The expression of aquaporin water channel genes are shown to be affected in several pathological conditions of retina, such as in diabetic retinopathy, retinal ischemia and in autoimmune uveitis. Human native retinal pigment epithelial (RPE) cells and immortalized human RPEs are formerly shown to express aquaporins, still the expression of aquaporins in stem cell derived RPE have not been previously elucidated. The objective of this study was to determine the expression of several aquaporin genes (aquaporin1,- 3, -4, -5, -6, -7, -10, -11 and -12) and assess the localization of aquaporin 1 water channel protein in human embryonic (hESCs) and induced pluripotent stem cells (hiPSCs) derived RPE cells.. Methods: hESC- and hiPSC derived RPE cells were grown as monolayer in serum-free media. The expression of aquaporin genes was determined with qRT-PCR. The localization of AQP1-protein was studied with confocal microscopy. Finally, the functionality of aquaporins was assessed with dye ...
Aquaporin-5 is a protein that in humans is encoded by the AQP5 gene. Aquaporin 5 (AQP5) is a water channel protein. Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). Aquaporin 5 plays a role in the generation of saliva, tears and pulmonary secretions. AQP0, AQP2, AQP5, and AQP6 are closely related and all map to 12q13. Aquaporin GRCh38: Ensembl release 89: ENSG00000161798 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000044217 - Ensembl, May 2017 Human PubMed Reference:. Mouse PubMed Reference:. Lee MD, Bhakta KY, Raina S, Yonescu R, Griffin CA, Copeland NG, Gilbert DJ, Jenkins NA, Preston GM, Agre P (Jun 1996). The human Aquaporin-5 gene. Molecular characterization and chromosomal localization. J Biol Chem. 271 (15): 8599-604. doi:10.1074/jbc.271.15.8599. PMID 8621489. Entrez Gene: AQP5 aquaporin 5. Verkman AS (2003). Role of aquaporin water channels in eye function. Exp. Eye Res. 76 (2): 137-43. ...
Abstract Background and Aims Diarrhoea is a common, debilitating symptom of gastrointestinal disorders. Pathomechanisms probably involve defects in trans-epithelial water transport, but the role of aquaporin [AQP] family water channels in diarrhoea-predominant diseases is unknown. We investigated the involvement of AQPs in the pathobiology of collagenous colitis [CC], which features chronic, watery diarrhoea despite overtly normal intestinal epithelial cells [IECs]. Methods We assessed the expression of all AQP family members in mucosal samples of CC patients before and during treatment with the corticosteroid drug budesonide, steroid-refractory CC patients and healthy controls. Samples were analysed by genome-wide mRNA sequencing [RNA-seq] and quantitative real-time PCR [qPCR]. In some patients, we performed tissue microdissection followed by RNA-seq to explore the IEC-specific CC transcriptome. We determined changes in the protein levels of the lead candidates
Plant cells contain proteins that are members of the major intrinsic protein (MIP) family, an ancient family of membrane channel proteins characterized by six membrane-spanning domains and two asparagine-proline-alanine (NPA) amino acid motifs in the two halves of the protein. We recently demonstrated that [gamma]-TIP, one of the MIP homologs found in the vacuolar membrane of plant cells, is an aquaporin or water channel protein (C. Maurel, J. Reizer, J.I. Schroeder, M.J. Chrispeels [1993] EMBO J 12: 2241-2247). RD28, another MIP homolog in Arabidopsis thaliana, was first identified as being encoded by a turgor-responsive transcript. To find out if RD28 is a water channel protein, rd28 cRNA was injected into Xenopus laevis oocytes. Expression of RD28 caused a 10- to 15-fold increase in the osmotic water permeability of the oocytes, indicating that the protein creates water channels in the plasma membrane of the oocytes and is an aquaporin just like its homolog [gamma]-TIP. Although RD28 has ...
The pre-ovulatory hydration of the oocyte of marine teleosts, a unique process among vertebrates that occurs concomitantly with meiosis resumption (oocyte maturation), is a critical process for the correct development and survival of the embryo. Increasing information is available on the molecular mechanisms that control oocyte maturation in fish, but the identification of the cellular processes involved in oocyte hydration has remained long ignored. During the past few years, a number of studies have identified the major inorganic and organic osmolytes that create a transient intra-oocytic osmotic potential for hydrating the oocytes, whereas water influx was believed to occur passively. Recent work, however, has uncovered the role of a novel molecular water channel (aquaporin), designated aquaporin-1b (Aqp1b), which facilitates water permeation and resultant swelling of the oocyte. The Aqp1b belongs to a teleost-specific subfamily of water-selective aquaporins, similar to mammalian aquaporin-1 ...
Semantic Scholar extracted view of Aquaporin water channels in liver: their significance in bile formation. by Raúl Alberto Marinelli et al.
Aquaporin membrane protein, molecular model. Computer illustration showing the structure of a molecule of the human aquaporin 1 protein (blue, and white ribbon). Aquaporins are membrane proteins that form channels (centre) that help water molecules (red and white spheres) pass in and out of cells. Unlike ion channels, aquaporins help prevent ions and other dissolved substances carrying electrical charge from entering the cell, as they only allow lone water molecules or certain uncharged solutes to pass through. This helps maintain the electrochemical potential of the cell membrane. - Stock Image C035/5236
Author(s): Chen, Qi; Peng, Hongying; Lei, Li; Zhang, Ying; Kuang, Haibin; Cao, Yujing; Shi, Qi-Xian; Ma, Tonghui; Duan, Enkui | Abstract: In the journey from the male to female reproductive tract, mammalian sperm experience a natural osmotic decrease (e.g., in mouse, from ~415 mOsm in the cauda epididymis to ~310 mOsm in the uterine cavity). Sperm have evolved to utilize this hypotonic exposure for motility activation, meanwhile efficiently silence the negative impact of hypotonic cell swelling. Previous physiological and pharmacological studies have shown that ion channel-controlled water influx/efflux is actively involved in the process of sperm volume regulation; however, no specific sperm proteins have been found responsible for this rapid osmoadaptation. Here, we report that aquaporin3 (AQP3) is a sperm water channel in mice and humans. Aqp3-deficient sperm show normal motility activation in response to hypotonicity but display increased vulnerability to hypotonic cell swelling, characterized by
TY - JOUR. T1 - Identification of a novel aquaporin, AQP12, expressed in pancreatic acinar cells. AU - Itoh, Tomohiro. AU - Rai, Tatemitsu. AU - Kuwahara, Michio. AU - Ko, Shigeru B.H.. AU - Uchida, Shinichi. AU - Sasaki, Sei. AU - Ishibashi, Kenichi. N1 - Funding Information: We thank N. Ozaki (Nagoya university, Japan) for his skillful technical assistance in isolation of pancreatic islet. This work was supported by grants from the Ministry of Education, Culture, Sports, Science and Technology of Japan.. PY - 2005/5/13. Y1 - 2005/5/13. N2 - Members of the aquaporin (AQP) water channel family are widely distributed in various tissues and contribute to the water permeability of epithelial and endothelial cells. Currently 11 members of the AQP family (AQP0-10) have been reported in mammals. Here we report the identification of AQP12, which we found by performing a BLAST program search. Northern blot analysis revealed that AQP12 was specifically expressed in the pancreas. Further analysis by in ...
Aquaporins (AQPs) are membrane proteins that enable water transport across cellular plasma membranes in response to osmotic gradients. Phenotypic analyses have revealed important physiological roles for AQPs, and the potential for AQP water channel modulators in various disease states has been proposed. For example, AQP1 is overexpressed in tumor microvessels, and this correlates with higher metastatic potential and aggressiveness of the malignancy. Chemical modulators would help in identifying the precise contribution of water channel activity in these disease states. These inhibitors would also be important therapeutically, e.g., in anti-cancer treatment. This perceived importance contrasts with the lack of success of high-throughput screens (HTS) to identify effective and specific inhibitors of aquaporins. In this paper, we have screened a library of 1500
Aquaporin (AQP) 6 belongs to the aquaporin water channel family. Unlike other aquaporins, AQP6 functions not as a water channel but as an anion-selective channel. Single-channel analyses have shown AQP6 to flicker rapidly ...
Aquaporins facilitate the diffusion of water across cell membranes. We previously showed that acid pH or low Ca2+ increase the water permeability of bovine AQP0
Aquaporin 8 (AQP8) is a water channel protein. Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). Aquaporin 8 mRNA is found in pancreas and colon but not other tissues. [provided by RefSeq, Jul 2008 ...
Purpose: : To demonstrate in the conjunctiva the presence of aquaporin type 5 (AQP5), a water channel homologue found in the apical membrane of several tissues including the cornea. Presently, there are no reports indicating as to which AQP might be expressed apically in the conjunctiva; only AQP3 has been identified in the lateral membranes of rat and human conjunctival epithelia. Because we had data from gene-expression microarray assays (Turner; ARVO 2004) indicating message for AQP5 in the human conjunctiva, tissue samples from human, as well as from rats and rabbits (given the ease of their procurement), were analyzed to confirm that the AQP5 protein was indeed expressed in mammalian conjunctivae. Methods: : Goat polyclonal IgG against AQP5 was purchased commercially and used in immunoblotting and immunohistochemical techniques to identify and localize the water channel in rat, rabbit and human epithelia. Results: : Immunoblot analysis of rabbit bulbar-plus-palpebral plasma membrane ...
Aquaporin A/S is a global cleantech company located in Kongens Lyngby, Denmark. Aquaporin is dedicated to revolutionizing water purification through the use of industrial biotechn
Peptides , Phosphopeptides , Aquaporin-2 (254-267), pSER261, human; This peptide is a fragment of the human aquaporin-2 (AQP2) phosphorylated at Ser261. Protein phosphorylation plays a key role in vasopressin signaling in renal-collecting duct. Phosphorylation at several AQP2 residues including Ser256 and Ser261, is altered in response to vasopressin. It is possible that both sites are involved in vasopressin-dependent AQP2 trafficking.; RQSVELH-pS-PQSLPR; H-Arg-Gln-Ser-Val-Glu-Leu-His-pSer-Pro-Gln- Ser-Leu-Pro-Arg-OH
The researchers showed that this technique was successful in monitoring gene expression in a brain tumor in mice. After implanting the tumor, they gave the mice a drug to trigger the tumor cells to express the aquaporin reporter gene, which made the tumor look darker in MRI images.. Overexpression of aquaporin has no negative impact on cells because it is exclusive to water and simply allows the molecules to go back and forth across the cell membrane, Shapiro says. Under normal physiological conditions the number of water molecules entering and exiting an aquaporin-expressing cell is the same, so that the total amount of water in each cell does not change. Aquaporin is a very convenient way to genetically change the way that cells look under MRI.. Though the work was done in mice, it has the potential for clinical translation, according to Shapiro. Aquaporin is a naturally occurring gene and will not cause an immune reaction. Previously developed reporter genes for MRI have been much more ...
Kit contents: 1. MICROTITER PLATE * 1 2. ENZYME CONJUGATE*1 vial 3. STANDARD A*1 vial 4. STANDARD B*1 vial 5. STANDARD C*1 vial 6. STANDARD D*1 vial 7. STANDARD E*1 vial 8. STANDARD F*1 vial 9. SUBSTRATE A*1 vial 10. SUBSTRATE B*1 vial 11. STOP ...
C. elegans AQP-4 protein; contains similarity to Pfam domain PF00230 (Major intrinsic protein)contains similarity to Interpro domains IPR000425 (Major intrinsic protein), IPR012269 (Aquaporin ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
collections, groups of modules structured into books or course notes, or for other uses. Our open license allows for free use and reuse of all our content. ...
Significant progress in the understanding of imaging conditions and the interpretation of topographs recorded with the AFM has allowed the surface topography of bacteriorhodopsin to be correlated with the helixconnecting loops to a lateral resolution of 5 Å (Müller et al., 1999b). Here we have used this technology to study the surface of AqpZ, the first bacterial water channel identified (Calamita et al., 1995). Its overexpression, isolation and 2D crystallization have recently been described (Borgnia et al., 1999; Ringler et al., 1999).. 2D crystals adsorbed firmly and without folds or wrinkles to freshly cleaved mica in a high ionic strength buffer (Müller et al., 1997). Subsequent change to a buffer adjusted to compensate for van der Waals interactions allowed their height to be measured accurately (Müller and Engel, 1997). The result, 57 ± 4 Å, compares favorably with the height previously reported for AQP1, 58 ± 3 Å (Walz et al., 1996).. The p4212 crystals of AqpZ with unit cell ...
Marinelli RA, Pham L, Agre P, La Russo NF. Secretin promotes osmotic water transport in rat cholangiocytes by incresing aquaporin-1 water channels in plasma membrane. Evidence for a secretin-induced vesicular translocation of aquaporin-1. J Biol Chem 1997; 272: 12984-12988 ...
Aquaporins are a family of water channel proteins that provide a major pathway for osmotically driven water transport through cell membranes. So far, 13 aquaporin isoforms (AQP0-AQP12) have been identified in mammalian species (Verkman, 2005). AQP4, the predominant isoform in adult brain, is primarily expressed at the border between brain parenchyma and major fluid compartments, including astrocyte foot processes and glia limitans, as well as ependymal cells and subependymal astrocytes (Venero et al., 2001). The bidirectional water channel AQP4 has an important role in water homeostasis in the brain. It probably helps in the redistribution and absorption of edema fluid, because disruption of AQP4 is found to contribute to the pathophysiology of brain edema (Zador et al., 2007). AQP4 knockout markedly reduced brain swelling in mouse models of cytotoxic brain edema, whereas it significantly worsened outcome in mouse models of vasogenic brain edema (Papadopoulos and Verkman, 2007). Thus, AQP4 ...
Aquaporins are transmembrane water channel proteins present in biological plasma membranes that aid in biological water filtration processes by transporting water molecules through at high speeds, while selectively blocking out other kinds of solutes. Aquaporin Z incorporated biomimetic membranes are envisaged to overcome the problem of high pressure needed, and holds great potential for use in water purification processes, giving high flux while keeping energy consumption low. The functionality of aquaporin Z in terms of osmotic permeability might be regulated by factors such as pH, temperature, crosslinking and hydrophobic thickness of the reconstituted bilayers. Hence, we reconstituted aquaporin Z into vesicles that are made from a series of amphiphilic block copolymers PMOXA-PDMS-PMOXAs with various hydrophobic molecular weights. The osmotic permeability of aquaporin Z in these vesicles was determined through a stopped-flow spectroscopy. In addition, the temperature and pH value of the vesicle
This paper strongly supports the conclusion that AQP0 has a high permeability mode and a low permeability mode. How do these two modes differ? Available structural data on the nature of the water-filled pore through AQP1 and the glycerol facilitator suggest a possible answer. For both, water and glycerol must move through the pore by single-file diffusion. The crystal structure and molecular dynamic simulations suggest that there are multiple water molecules in the pore. There are ∼6 waters seen in the narrow constriction of the pore in the X-ray structure (Sui et al., 2001), and molecular dynamic simulations suggest that there are ∼7 or 8 water molecules moving in concert in the single-file portion of the pore (Tajkhorshid et al., 2002; Zhu et al., 2004). The lack of passage of ionic current through AQP0 and AQP1 is explained by electrostatic considerations that strongly inhibit the movement of protons into the NPA region or hydroxyls into regions flanking either side of the NPA region (de ...
Proteins that selectively transport water across the membranes of cells are recognized as important in the normal functioning of the body systems of vertebrates. There are 13 known mammalian aquaporins (AQP0 to AQP12), some of which have been shown to have unexpected cellular roles beyond transmembrane water transport. The availability of non-mammalian vertebrate animal models has the potential to provide insight into the emergence of diverse function in the aquaporins. The domesticated chicken (Gallus gallus) is the premier avian model for biological research; however, only a limited number of studies have compared chicken and mammalian aquaporins. The identification of aquaporins that share functional motifs or are expressed in the same tissues in human and chicken could allow the further functional analyses of homologous aquaporins in both species. We hypothesize that integrative analyses of protein sequences and body site expression of human, mouse, rat and chicken aquaporins has the potential to
We recently demonstrated that the aquaglyceroporins (AQGPs) could act as potent transporters for orthosilicic acid (H4SiO4). Although interesting, this finding raised the question of whether water and H4SiO4, the transportable form of Si, permeate AQGPs by interacting with the same region of the pore, especially in view of the difference in molecular radius between the two substrates. Here, our goal was to identify residues that endow the AQGPs with the ability to facilitate Si diffusion by examining the transport characteristics of mutants in which residues were interchanged between a water-permeable but Si-impermeable channel (aquaporin 1 [AQP1]) and a Si-permeable but water-impermeable channel (AQP10). Our results indicate that the composition of the arginine filter (XX/R), known to include three residues that play an important role in water transport, may also be involved in Si selectivity. Interchanging the identities of the nonarginine residues within this filter causes Si transport to ...
Aquaporins play a direct role in plant water relation under salt stress, but the effects of 5-aminolevulinic acid (ALA) on aquaporin gene expression in salt-treated plants remain unknown. This study investigated the potential effects of exogenous ALA (50 mg/dm3) on aquaporin expression levels under salt stress (75 mM NaCl) in the salt-sensitive (Jinchun No.4) and the relatively salt-tolerant cucumber (Jinyou No.1) seedlings.
We investigated the in vivo ramifications of a book aquaporin 4 (AQP4) inhibitor 2-(nicotinamide)-1,3,4-thiadiazole, TGN-020, inside a mouse style of focal cerebral ischemia using 7. research convincingly exhibited that pretreatment using the AQP4 inhibitor TGN-020 considerably reduced the quantity of mind edema connected with ischemic damage. Ischemic edema is usually thought to be initiated by influx of Na+ connected with energy failing. Higher osmolarity circumstances create the generating force for drinking water influx into cells, leading to ionic edema [17]. This early edema stage, so-called cytotoxic edema, is certainly thought to last a long time before mass leakage of drinking water into the human brain ensues, making so-called vasogenic edema [18]. AQP4 is certainly thought to play a substantial function in the real drinking water flux in both procedures. Flux through AQP4 is certainly buy 154992-24-2 bidirectional and solely reliant on osmolarity distinctions between your two spaces ...
Müller glial cells are important regulators of physiological function of retina. In a model disease of retinal inflammation and spontaneous recurrent uveitis in horses (ERU), we could show that retinal Müller glial cells significantly change potassium and water channel protein expression during autoimmune pathogenesis. The most significantly changed channel protein in neuroinflammatory ERU was aquaporin 11 (AQP11). Aquaporins (AQP, 13 members) are important regulators of water and small solute transport through membranes. AQP11 is an unorthodox member of this family and was assigned to a third group of AQPs because of its difference in amino acid sequence (conserved sequence is only 11 %) and especially its largely unknown function. In order to gain insight into the distribution, localization, and function of AQP11 in the retina, we first developed a novel monoclonal antibody for AQP11 enabling quantification, localization, and functional studies. In the horse retina, AQP11 was exclusively expressed
Background: Aquaporins are integral membrane proteins that facilitate the transport of water and small solutes across cell membranes. These proteins are vital for maintaining water homeostasis in living organisms. In mammals, thirteen aquaporins (AQP0-12) have been characterized, but in lower vertebrates, such as fish, the diversity, structure and substrate specificity of these membrane channel proteins are largely unknown. Results: The screening and isolation of transcripts from the zebrafish (Danio rerio) genome revealed eighteen sequences structurally related to the four subfamilies of tetrapod aquaporins, i.e., aquaporins (AQP0, -1 and -4), water and glycerol transporters or aquaglyceroporins (Glps; AQP3 and AQP7-10), a water and urea transporter (AQP8), and two unorthodox aquaporins (AQP11 and -12). Phylogenetic analyses of nucleotide and deduced amino acid sequences demonstrated dual paralogy between teleost and human aquaporins. Three of the duplicated zebrafish isoforms have unlinked ...
After producing a recombinant form of AqpZ in E. coli, the proteins were crystallized--capturing five water molecules inside--and then analyzed by state-of-the-art high-resolution X-ray diffraction techniques. The architecture of aquaporin Z is typical of aquaporins, with a spiral of eight oxygens providing water-binding sites inside the channel. The outer membrane and cytoplasmic ends of the channel are wider than the interior, which is long and narrow. This structure demonstrates that aquaporin selectivity arises in part from erecting a physical barrier: small molecules, like water, can easily pass, but larger ones simply cant fit. And the strategic positioning of amino acid residues with hydrophilic or hydrophobic properties along the channel helps police the influx of molecules based on their affinity for water. While it seems two amino acid chains located in the middle of the channel also provide a water-friendly surface, Stroud et al. say they play a more intriguing role. Noting that the ...
Transmembrane glycerol transport is an ancient biophysical property that evolved in selected subfamilies of water channel (aquaporin) proteins. Here, we conducted broad level genome (,550) and transcriptome (,300) analyses ...
Aquaporin (AQP) proteins comprise a group of membrane intrinsic proteins (MIPs) that are responsible for transporting water and other small molecules, which is crucial for plant survival under stress conditions including salt stress. Despite the vital role of AQPs, little is known about them in cucumber (Cucumis sativus L.). In this study, we identified 39 aquaporin-encoding genes in cucumber that were separated by phylogenetic analysis into five sub-families (PIP, TIP, NIP, SIP, and XIP). Their substrate specificity was then assessed based on key amino acid residues such as the aromatic/Arginine (ar/R) selectivity filter, Frogers positions, and specificity-determining positions. The putative cis-regulatory motifs available in the promoter region of each AQP gene were analyzed and results revealed that their promoter regions contain many abiotic related cis-regulatory elements. Furthermore, analysis of previously released RNA-seq data revealed tissue- and treatment-specific expression patterns of
I think it will be found that aquaporin 3 will be the item of interest (1).. Aquaporin 3 is found in normal skeletal myofibres (2).. I suspect it will be found that the problem is not a mutation, but something interfering with the normal proper function of the aqp3 channels.. Aquaporin 3 is, in addition to being a water channel, also an arsenic transporter.. Arsenic has been implicated in Alzheimers in at least a few instances. For example, this statement appears in Reference 3 below:. Arsenic can induce apoptosis in cortical neurons of rats. This process is based on the activation of JNK3 and p38 MAPK by arsenic...[which] can activate p38 MAPK and JNK3..... And the title of the last paper speaks for itself: Arsenic exposure may be a risk factor for Alzheimers disease.. ...
TY - JOUR. T1 - An experimental study on water transport through the membrane of a PEFC operating in the dead-end mode. AU - Lee, Yongtaek. AU - Kim, Bosung. AU - Kim, Yongchan. N1 - Funding Information: This work was supported by a grant (No. R01-2006-000-11014-0) from the Basic Research Program of the Korea Science & Engineering Foundation. PY - 2009/9. Y1 - 2009/9. N2 - Water transport through the membrane of a polymer electrolyte fuel cell (PEFC) was investigated by not only measuring the voltage variation but also visualizing the accumulation of water at the anode for various values of operating parameters, such as the humidity, current density, stoichiometry, location of humidification, and membrane properties. The PEFC was operated in the dead-end mode to prevent the discharge of water from the anode. The water transport in the PEFC was characterized by the elapsed time for the voltage to reach its limit. Anode visualization showed water transport under various conditions. In addition, ...
S6 - Northeastern. This pod is released every hour at past 20 and 50. It travels a very big distance and it is a really long trip. It goes very far in East, close to Linden Village. It exits Snowlands very fast. It goes North, through Tethis sim, where is located the highest mountain of Sansara (see Altitude for details). There are a few other very high mountains in this sim and nearby places. Then, it follows the tundra to East, close to the border with endless snow-coverd land. Then, close to Clarksberg, it changes route to North-East. This road connects a group of long islands. Water channels are to left and to rignt. Altitude is not too high, but land is never complete flat. It is up to your imagination to decide if these channels are rivers or straights of salt, oceanic water. The high number of bridges is to be noted. Then, the pod makes a small stop at Waterhead infohub. This is a good place to meet people, since it is one of the most active of all infohubs, but also a very good place to ...
Using PLIF to analyse water channel simulations of turbulent diffusion in the atmospheric boundary layer A. Butet METEO-FRANCE CNRM/GMEI/SPEA,...
Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
Polyclonal antibody for AQUAPORIN 3/AQP3 detection. Host: Rabbit.Size: 100μg/vial. Tested applications: IHC-P. Reactive species: Human. AQUAPORIN 3/AQP3 information: Molecular Weight: 31544 MW; Subcellular Localization: Basolateral cell membrane; Multi-pa
Aquaporin 10 antibody, C-term (aquaporin 10) for WB. Anti-Aquaporin 10 pAb (GTX45889) is tested in Human samples. 100% Ab-Assurance.
Free ground shippingShips directly from Da-Lite within 4-5 business days Whats Included? 1 Da-Lite UTB Contour Fixed-Frame Projection Screen 58x136.5 viewable area - 148 Diag / 2.35:1 Cinemascope format Extruded aluminum frame with 0.25 wide bezel Black, acid etch finish on frame and bezel Wall hanging bracket(s)
摘要(Abstract): 目的探讨头孢曲松钠在水通道蛋白4(AQP4)抗体诱导的星形胶质细胞损伤中的作用以及机制。方法常规体外培养新生SD大鼠大脑皮质细胞,将培养的细胞分为4组,分别加入健康人血清(对照组)、AQP4抗体阳性患者血清、头孢曲松钠+AQP4抗体阳性血清以及单纯头孢曲松钠。细胞培养24h后采用免疫组织化荧光染色观察不同组星形胶质细胞数目的变化,采用比色法测定上清液谷氨酸浓度以及免疫印迹分析谷氨酸转运体-1(GLT-1)蛋白表达水平。结果和对照组比较,AQP4抗体阳性血清组星形胶质细胞数目和谷氨酸转运体-1(GLT-1)蛋白表达明显减少,上清液谷氨酸浓度明显增高(均 ...
The gene encoding this aquaporin is a possible candidate for disorders involving imbalance in ocular fluid movement. Aquaporin ... Aquaporin 1 (AQP-1) is a protein that in humans is encoded by the AQP1 gene. AQP-1 is a widely expressed water channel, whose ... Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). This gene ... Aquaporin and Blood Brain Barrier, Current Neuropharmacology from U.S. National Library of Medicine, 2010. Rauen K, Pop V, ...
This results in aquaporin-2 containing vesicles to increase water uptake and return to circulation. Mutation of the aquaporin 2 ... The gating of an aquaporin is carried out by an interaction between a gating mechanism and the aquaporin, which causes a 3D ... It was not until 1992 that the first aquaporin, 'aquaporin-1' (originally known as CHIP 28), was reported by Peter Agre, of ... There have been two clear examples of diseases identified as resulting from mutations in aquaporins: Mutations in the aquaporin ...
Aquaporin 3 is expressed more in atopic eczema. Recent studies indicate that aquaporin 3 is overexpressed in many types of ... Sasaki S, Ishibashi K, Marumo F (1998). "Aquaporin-2 and -3: representatives of two subgroups of the aquaporin family ... Aquaporin 3 (AQP-3) is the protein product of the human AQP3 gene. It is found in the basolateral cell membrane of principal ... 2005). "Roles of aquaporin-3 water channels in volume-regulatory water flow in a human epithelial cell line". J. Membr. Biol. ...
E. M. Müller, J. S. Hub, H. Grubmüller, and B. L. de Groot (2008). "Is TEA an inhibitor for human Aquaporin-1?" Pflügers Arch. ... It has also been reported that TEA inhibits aquaporin (APQ) channels, but this still seems to be a disputed issue. A partial ... 131-137 doi:10.1002/9780470132470.ch36 G. W. Parshall "Tetraethylammonium Trichlorogermanate(1−) and Trichlorostannate(1−)" ...
The MIP superfamily includes three subfamilies: aquaporins, aquaglyceroporins and S-aquaporins. The aquaporins (AQPs) are water ... Aquaporin-1 (Aqp1) from the human red blood cell has been solved by electron crystallography to 3.8 Å resolution (PDB: 1FQY​). ... Aquaporins generally have the NPA motif in both halves, the glycerol facilitators generally have an NPA motif in the first ... Roles of aquaporins in human cancer have been reviewed as have their folding pathways. AQPs may act as transmembrane ...
Defines the Diego Blood Group; Aquaporin 1 - water transporter, defines the Colton Blood Group; Glut1 - glucose and L- ... 6-1 Uptake and Delivery of the Respiratory Gasses". In Brobeck, John R., PhD, M.D. (ed.). Best & Taylor's Physiological basis ... Kesava, Shobana (1 September 2007). "Red blood cells do more than just carry oxygen; New findings by NUS team show they ... 35 (1): 43-57. doi:10.1016/j.cll.2014.10.002. PMC 4717490. PMID 25676371. Lang F, Lang E, Föller M (2012). "Physiology and ...
Evidence for a secretin-induced vesicular translocation of aquaporin-1". The Journal of Biological Chemistry. 272 (20): 12984-8 ... translocation of aquaporin 2, or both are found. It has been suggested that "Secretin as a neurosecretory hormone from the ... "Secretin promotes osmotic water transport in rat cholangiocytes by increasing aquaporin-1 water channels in plasma membrane. ... 127 (1): 43-54. doi:10.1002/ijc.25028. PMID 19904746. S2CID 2789418. Lee LT, Tan-Un KC, Pang RT, Lam DT, Chow BK (2004). " ...
... is a protein that in humans is encoded by the AQP8 gene. Aquaporin-8 (AQP-8) is a water channel protein. Aquaporins ... "Entrez Gene: AQP8 aquaporin 8". Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of ... 2007). "Aquaporin-8 expression is reduced in ileum and induced in colon of patients with ulcerative colitis". World J. ... Wang S, Chen J, Au KT, Ross MG (2003). "Expression of aquaporin 8 and its up-regulation by cyclic adenosine monophosphate in ...
July 2009). "Aquaporin-4 autoimmune syndrome and anti-aquaporin-4 antibody-negative opticospinal multiple sclerosis in Japanese ... The presence of anti-MOG autoantibodies has been associated with the following conditions Some cases of aquaporin-4- ... Vojdani A, Mukherjee PS, Berookhim J, Kharrazian D (2015). "Detection of Antibodies against Human and Plant Aquaporins in ... Tzartos JS, Stergiou C, Kilidireas K, Zisimopoulou P, Thomaidis T, Tzartos SJ (2013). "Anti-aquaporin-1 autoantibodies in ...
In 2005 they identified the aquaporin 4 protein as the target of the disease, and developed the first in-house test to aid in ... In more than 80% of cases, IgG autoantibodies against aquaporin-4 (anti-AQP4+) are the cause, and in 10-40% of the remaining ... In more than 80% of cases, NMO is caused by immunoglobulin G autoantibodies to aquaporin 4 (anti-AQP4), the most abundant water ... Some authors propose to use the name "autoimmune aquaporin-4 channelopathy" for these diseases, while others prefer a more ...
... and AQP3 are at the same chromosomal location suggesting that 9p13 may be a site of an aquaporin cluster. Aquaporin ... Aquaporin-7 (AQP-7) is a protein that in humans is encoded by the AQP7 gene. Aquaporins/major intrinsic proteins (MIP) are a ... "Entrez Gene: AQP7 aquaporin 7". Dibas AI, Mia AJ, Yorio T (1998). "Aquaporins (water channels): role in vasopressin-activated ... Aquaporin-7 has greater sequence similarity with AQP3 and AQP9 and they may be a subfamily. ...
... (AQP-9) is a protein that in humans is encoded by the AQP9 gene. The aquaporins/major intrinsic protein are a ... Aquaporin-9 has greater sequence similarity with AQP3 and AQP7 and they may be a subfamily. Aquaporin-9 allows passage of a ... "Entrez Gene: AQP9 aquaporin 9". Ishibashi K, Kuwahara M, Gu Y, et al. (1998). "Cloning and functional expression of a new ... 2003). "Aquaporin-9 is expressed in a mucus-secreting goblet cell subset in the small intestine". FEBS Lett. 540 (1-3): 157-62 ...
... (AQP-5) is a protein that in humans is encoded by the AQP5 gene. Aquaporin-5 (AQP-5) is a water channel protein. ... Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). Aquaporin-5 ... "Entrez Gene: AQP5 aquaporin 5". Verkman AS (2003). "Role of aquaporin water channels in eye function". Exp. Eye Res. 76 (2): ... 2003). "Distribution of aquaporin water channels AQP1 and AQP5 in the ductal system of the human pancreas". Gut. 52 (7): 1008- ...
The expression of aquaporin 4 is reliant on the disease stage of TBI. In an acute stage of TBI, the lack of aquaporin 4 causes ... Aquaporin-4, also known as AQP-4, is a water channel protein encoded by the AQP4 gene in humans. AQP-4 belongs to the aquaporin ... Aquaporin-4 is the most common aquaporin in the brain, spinal cord, and optic nerve. It is highly expressed in the human body ... Aquaporin-4 is essential in the formation of memory as well as synaptic plasticity. Other performances that aquaporin-4 is ...
It is the only aquaporin regulated by vasopressin. The basic job of aquaporin 2 is to reabsorb water from the urine while its ... This aquaporin is also regulated by food intake. Fasting reduces expression of this aquaporin independently of vasopressin. ... so the aquaporin 2 can be used by the cell. This aquaporin is regulated in two ways by the peptide hormone vasopressin: short- ... Aquaporin-2 (AQP-2) is found in the apical cell membranes of the kidney's collecting duct principal cells and in intracellular ...
Agre, P.; King, L. S.; Yasui, M.; Guggino, W. B.; Ottersen, O. P.; Fujiyoshi, Y.; Engel, A.; Nielsen, S. (2002). "Aquaporin ... Fujiyoshi and Engel solved the structure of Aquaporin-1 in collaboration with Agre. Together with Palczewski Engel's team ... 177 (1): 3-13. doi:10.1016/j.jsb.2011.11.013. PMID 22115996. "Farewell Symposium for Andreas Engel". unibas.ch. Archived from ... 542 (1): 3-16. doi:10.1113/jphysiol.2002.020818. PMC 2290382. PMID 12096044. "Structure of the rhodopsin dimer: a working model ...
"Aquaporin-1 promotes angiogenesis, fibrosis, and portal hypertension through mechanisms dependent on osmotically sensitive ... 70 (1): 36-45. doi:10.1158/0008-5472.CAN-09-3153. PMID 20028859. Schotte D, Chau JC, Sylvester G, Liu G, Chen C, van der Velden ... miR-708 is located on chromosome 11q14.1 and is endcoded in intron 1 of the ODZ4 gene. It is most highly expressed in the brain ...
... and aquaporin-1 in human erythrocyte membrane domains". Biochimica et Biophysica Acta (BBA) - Biomembranes. 1828 (3): 956-66. ... GLUT 1 of humans and mice have 98% identity at the amino acid level. GLUT 1 is encoded by the SLC2 gene and is one of a family ... The SLC2A1 gene is located on the p arm of chromosome 1 in position 34.2 and has 10 exons spanning 33,802 base pairs. The gene ... Glucose transporter 1 (or GLUT1), also known as solute carrier family 2, facilitated glucose transporter member 1 (SLC2A1), is ...
Horng, J.L.; Chao, P.L.; Chen, P.Y.; Shih, T.H.; Lin, L.Y. (2015). "Aquaporin 1 Is Involved in Acid Secretion by Ionocytes of ... Li, S.; Liu, J.; An, Y.; Cao, Y.; Liu, Y.; Zhang, J.; Geng, J.; Hu, T.; Yang, P. (2019). "MsPIP2;2, a novel aquaporin gene from ... 19 (1): 89. doi:10.1186/s12870-019-1674-5. PMC 6394093. PMID 30819104. Zhang, Z.Y.; Wang, W.J.; Pan, L.J.; Xu, Y.; Zhang, Z.M ... ISBN 1-58603-083-3. Yang, C.; Fang, S.; Chen, D.; Wang, J.; Liu, F.; Xia, C. (2015). "The possible role of bacterial signal ...
Shanahan, CM (1999). "Aquaporin-1 is expressed by vascular smooth muscle cells and mediates rapid water transport across ... 1999 Aquaporin-1 is expressed by vascular smooth muscle cells and mediates rapid water transport across vascular cell membranes ... doi:10.1385/1-59259-240-6:201. ISBN 1-59259-240-6. PMID 11968489. "AstraZeneca to buy CAT for £702m". News.bbc.co.uk. 15 May ... Retrieved 1 August 2019. "The Record 1988". Issuu.com. Retrieved 1 August 2019. Osbourn, J. K.; Watts, J. W.; Beachy, R. N.; ...
"In vivo requirement of the alpha-syntrophin PDZ domain for the sarcolemmal localization of nNOS and aquaporin-4". J. Cell Biol ... and Aquaporin 4. GRCh38: Ensembl release 89: ENSG00000101400 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000027488 ... "Syntrophin-dependent expression and localization of Aquaporin-4 water channel protein". Proc. Natl. Acad. Sci. U.S.A. 98 (24): ... "Syntrophin-dependent expression and localization of Aquaporin-4 water channel protein". Proc. Natl. Acad. Sci. U.S.A. 98 (24): ...
Proteins found in the tonoplast (aquaporins) control the flow of water into and out of the vacuole through active transport, ... "Acceleration of vacuolar regeneration and cell growth by overexpression of an aquaporin NtTIP1;1 in tobacco BY-2 cells". Plant ... 1. pp. 295-298. doi:10.1007/3-540-33774-1_10. ISBN 978-3-540-26205-3. Brooker RJ, Widmaier EP, Graham LE, Stiling PD (2007). ... 1. World Scientific Publishing Co Pte Ltd. Thomas Boller Archived 2013-12-06 at the Wayback Machine. Plantbiology.unibas.ch. ...
The Co antigen is found on a protein called aquaporin-1 which is responsible for water homeostasis and urine concentration. The ... Agre P.Defective urinary-concentrating ability due to a complete deficiency of aquaporin-1. N Engl J Med. 2001 Jul 19;345(3): ...
https://doi.org/10.1016/j.febslet.2007.04.002 Uehlein, N., & Kaldenhoff, R. (2007). Aquaporins and Plant Leaf Movements. Annals ... ISBN 978-0-12-614445-1 Galston, A. W. (1974). Plant Photobiology in the Last Half-Century. PLANT PHYSIOLOGY, 54(4), 427-436. ... 1-4. https://doi.org/10.1093/aob/mcm278 Sage, L. C. (1992). Pigment of the Imagination: A History of Phytochrome Research. ...
Aquaporin 4 in Müller cells in rats transports water to the vitreous body. The vitreous has many anatomical landmarks, ... "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 - ...
Yang B, Verkman AS (September 2002). "Analysis of double knockout mice lacking aquaporin-1 and urea transporter UT-B. Evidence ... UT-1 is activated by ADH, but is a passive transporter. It reabsorbs up to 70% of the original filtered load of urea. Urea ...
Agre was recognized for his discovery of aquaporin water channels. Aquaporins are water-channel proteins that move water ... Aquaporins are "the plumbing system for cells," said Agre. Every cell is primarily water. "But the water doesn't just sit in ... The 28 kDa protein is now known as aquaporin-1 (abbreviated AQP1), the archetypal member of a large family of water channel ... Permeated by water, aquaporins are required for generation of cerebrospinal fluid, aqueous humour, tears, sweat, saliva, ...
Around active NMO lesions AQP4 may selectively be lost in the absence of aquaporin 1 (AQP1) loss or other structural damage ( ... 28 (1): 84-94. doi:10.1055/s-2007-1019130. PMID 18256989. Misu T, Höftberger R, Fujihara K, Wimmer I, Takai Y, Nishiyama S, ... 255 (1): 1-10. doi:10.1007/s00415-007-0754-x. PMID 18004634. S2CID 1411872. Garrido C, Levy-Gomes A, Teixeira J, Temudo T (2004 ... 183 (1-2): 168-74. doi:10.1016/j.jneuroim.2006.09.008. PMID 17084910. S2CID 41262535. Jilek S, Schluep M, Rossetti AO, et al. ( ...
Lindsay, L. A., & Murphy, C. R. (2006). Redistribution of aquaporins 1 and 5 in the rat uterus is dependent on progesterone: a ... Lindsay, L. A., & Murphy, C. R. (2004). Redistribution of aquaporins in uterine epithelial cells at the time of implantation in ... Cell Physiology, 283(1), C142-C147. Enders, A. C., & Nelson, D. M. (1973). Pinocytotic activity of the uterus of the rat. ... The Journal of membrane biology, 206(1), 17-28. Tsang, L. L., Chan, L. N., Wang, X. F., So, S. C., Yuen, J. P., Fiscus, R. R ...
Zheng X, Bollinger Bollag W (December 2003). "Aquaporin 3 colocates with phospholipase d2 in caveolin-rich membrane ... Caveolin-1 is a protein that in humans is encoded by the CAV1 gene. The scaffolding protein encoded by this gene is the main ... Caveolin 1 has been shown to interact with heterotrimeric G proteins, Src tyrosine kinases (Src, Lyn) and H-Ras,cholesterol,TGF ... 271 (1): 568-73. doi:10.1074/jbc.271.1.568. PMID 8550621. Razani B, Zhang XL, Bitzer M, von Gersdorff G, Böttinger EP, Lisanti ...
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 ... ISBN 978-1-4160-2328-9. Mitchell B, Sharma R (2009). Embriology (2nd ed.). Churchill Livingstone Elsevier. Kuro-O M (January ... A healthy adult has 1 to 1.5 million nephrons in each kidney.: 22 Blood is filtered as it passes through three layers: the ...
Potassium absorption has a positive correlation with aquaporins and the uptake of water in plant cells via cell membrane ... ISBN 978-1-319-38147-9. OCLC 1333920083. Weinberg ED (February 1996). "The role of iron in cancer". European Journal of Cancer ... 1055: 1-20. doi:10.1007/978-3-319-90143-5_1. ISBN 978-3-319-90143-5. PMID 29884959. S2CID 46997332. Banci L, ed. (2013). ... 5 (1): 19-36. JSTOR 45074238. PMID 8664805. Lippard SJ (1994). "Metals in Medicine". Bioinorganic Chemistry (PDF). pp. 505-83. ...
Subsequent research by Nedergaard and colleagues has revealed that the aquaporin-4 water channel protein plays a crucial role ... doi:10.1016/S1474-4422(18)30318-1. PMC 6261373. PMID 30353860. "Nedergaard Lab". University of Rochester Medical Center. ...
... aquaporin - archaea - arginine - argipressin - aromatic amine - aromatic compound - arrestin - Arrhenius equation - aryl ... IGF type 1 receptor - IGF type 2 receptor - IgG - IgM - immediate-early protein - immune cell - immune system - immunoglobulin ... alpha-1 adrenergic receptor - alpha-2 adrenergic receptor - alpha-beta T-cell antigen receptor - alpha-fetoprotein - alpha- ... endothelin-1 - energy decomposition cycles - energy level - enhancer - enkephalin - enthalpy - entomology - entropy - env gene ...
Marlar S, Jensen HH, Login FH, Nejsum LN (October 2017). "Aquaporin-3 in Cancer". International Journal of Molecular Sciences. ... aquaporin 3, is a water channel that when overexpressed is thought to promote the progression and spread of various types of ... Overall median and 1 year survival rates in a series of 28 patients treated with chemotherapy for PEL were 6.2 months and 39.3 ... 35 (1): 94-6. doi:10.1093/ageing/afj009. PMID 16364944. Kubota T, Sasaki Y, Shiozawa E, Takimoto M, Hishima T, Chong JM ( ...
To help conserve water they produce very concentrated urine, via a process apparently associated with expression of aquaporin 1 ... 117 (1): 211-213. doi:10.2307/2425723. JSTOR 2425723. Patton, J.L. (2005). "Family Heteromyidae". In Wilson, D.E.; Reeder, D.M ... Offspring remain in the mound for 1-6 more months in the maternal caches. Family Heteromyidae Subfamily Dipodomyinae Dipodomys ... Garrison, T.E.; Best, T.L. (April 1990). "Dipodomys ordii". Mammalian Species (353): 1-10. doi:10.2307/3504290. JSTOR 3504290. ...
... for Aquaporin Membrane water purification and desalination technology). He was named a Bill & Melinda Gates Grand Challenge ... Xi, Jianzhong; Schmidt, Jacob J.; Montemagno, Carlo D. (1 February 2005). "Self-assembled microdevices driven by muscle". ...
... possible role in aquaporin-2 trafficking". The Journal of Clinical Investigation. 98 (4): 906-13. doi:10.1172/JCI118873. PMC ... 138 (1-2): 171-4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. Jagadish MN, Fernandez CS, Hewish DR, Macaulay SL, Gough KH, ... 200 (1-2): 149-56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. Weir ML, Klip A, Trimble WS (Jul 1998). "Identification of ... 254 (1): 21-6. doi:10.1006/bbrc.1998.9876. PMID 9920726. Valdez AC, Cabaniols JP, Brown MJ, Roche PA (Mar 1999). "Syntaxin 11 ...
Aquaporin tetramer composition modifies the function of tobacco aquaporins. Journal of Biological Chemistry, 2010. 285(41): p. ... He is known for his work on the aquaporin protein class, where he detected facilitated diffusion of CO2 in plant tissue and ... Kaldenhoff was one of the first scientists to describe plant aquaporins. He initially accomplished to analyse the function and ... For the first time, Kaldenhoff could provide evidence that an aquaporin molecule could conduct CO₂. Kaldenhoff also worked on ...
Congenital nephrogenic diabetes insipidus (NDI) may result from V2R or aquaporin-2 (AQP2) mutations. Exogenously administered ... 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: ... 1-8. doi:10.1042/CS20030062. PMID 12639215. (Vasopressin receptor antagonists, World Anti-Doping Agency prohibited substances) ...
... aquaporins or Na/K-ATPase. In sweat glands, CFTR is responsible for the reabsorption of chloride in the sweat duct. Sodium ions ... 252 (1): 208-13. doi:10.1006/bbrc.1998.9625. PMID 9813171. Shekdar K, Langer J, Venkatachalan S, Schmid L, Anobile J, Shah P, ... 23 (4 Pt 1): 763-6. doi:10.1016/0190-9622(90)70285-p. PMID 2229513. Hanukoglu I (February 2017). "ASIC and ENaC type sodium ... Jasti J, Furukawa H, Gonzales EB, Gouaux E (September 2007). "Structure of acid-sensing ion channel 1 at 1.9 A resolution and ...
The presence of anti-MOG autoantibodies has been associated with the following conditions Most cases of aquaporin-4- ... 259 (1-2): 21-6. doi:10.1016/j.jns.2006.05.070. PMID 17367811. S2CID 23257594. Boyle LH, Traherne JA, Plotnek G, Ward R, ... 12 (1): 46. doi:10.1186/s12974-015-0256-1. PMC 4359547. PMID 25889963. CYNTHIA MCKELVEY, Press Report, What's the Role of ... Ichiro Nakashima, Anti-myelin oligodendrocyte glycoprotein antibody in demyelinating diseases [1] Kezuka T, Usui Y, Yamakawa N ...
... colocalization with aquaporin-2 in collecting duct vesicles". The American Journal of Physiology. 275 (5 Pt 2): F752-60. doi: ... 234 (1): 257-62. doi:10.1006/bbrc.1997.6560. PMID 9168999. Steegmaier M, Yang B, Yoo JS, Huang B, Shen M, Yu S, Luo Y, Scheller ... 234 (1): 257-62. doi:10.1006/bbrc.1997.6560. PMID 9168999. Tang BL, Tan AE, Lim LK, Lee SS, Low DY, Hong W (Mar 1998). " ...
NMOSD can be associated with antibodies that bind to a protein called aquaporin-4 (AQP4). Binding of the anti-AQP4 antibody ... who are anti-aquaporin 4 immunoglobulin G (AQP4-IgG) seropositive. The applicant for this medicinal product is Viela Bio. ... patients who are anti-aquaporin-4 or AQP4 antibody positive). NMOSD is a rare autoimmune disorder in which immune system cells ... 30 (1). hdl:10665/331046. License: CC BY-NC-SA 3.0 IGO. "Inebilizumab" (PDF). USAN. Cree BA, Bennett JL, Kim HJ, Weinshenker BG ...
June 1999). "Urinary excretion of aquaporin-2 water channel differentiates psychogenic polydipsia from central diabetes ... 22 (1): 54-60. ISSN 0090-838X. PMC 6761819. PMID 15706734. Taivainen, H.; Laitinen, K.; Tähtelä, R.; Kilanmaa, K.; Välimäki, M ... 21 (1): 53-61. doi:10.1016/0005-7916(90)90049-q. ISSN 0005-7916. PMID 2373769.(subscription required) Costanzo, Erin S.; Antes ... 35 (1): 65-68. doi:10.1046/j.1440-1614.2001.00847.x. ISSN 0004-8674. PMID 11270459. S2CID 13168153.(subscription required) Goh ...
"IgG marker of optic-spinal multiple sclerosis binds to the aquaporin-4 water channel". Journal of Experimental Medicine. 202 (4 ... "Neuromyelitis optica brain lesions localized at sites of high aquaporin 4 expression". Archives of Neurology. 63 (7): 964-968. ... ISBN 978-1-4160-2973-1. 8th edition. Toro JR, Finlay D, Dou X, Zheng SC, LeBoit PE, Connoly KM (2000). "Detection of Type 1 ... 26 (1 Suppl 48): S12-7. PMID 18570749. Faé KC, da Silva DD, Oshiro SE, Tanaka AC, Pomerantzeff PM, Douay C, Charron D, Toubert ...
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 ...
... although the membrane contains aquaporins that are believed to be conduits for regulated water transport. Mitochondrial matrix ... Mitochondrial DNA is 1% of total DNA of a cell. It is rich in guanine and cytosine content. Mitochondria of mammals have 55s ... 203 (Pt 1): 51-59. doi:10.1242/jeb.203.1.51. ISSN 0022-0949. PMID 10600673. Karmen, A.; Wroblewski, F.; Ladue, J. S. (1955-01- ... Dimroth, P.; Kaim, G.; Matthey, U. (2000-01-01). "Crucial role of the membrane potential for ATP synthesis by F(1)F(o) ATP ...
... or Aquaporin, cytoskeletal structural proteins, paired-like homeodomain transcription factor 3 (PITX3), avian ... with an estimated prevalence of 1 to 6 cases per 10,000 live births. Basic and clinical science course (2011-2012). Pediatric ... galactose 1-phosphate uridyltransferase, galactokinase, amino acids - Infectious diseases: TORCH and varicella titers, VDRL - ... in a darkened room and involves shining a bright direct ophthalmoscope into both eyes simultaneously from a distance of 1- 2 ft ...
"A water-specific aquaporin involved in aphid osmoregulation". Insect Biochemistry and Molecular Biology. 39 (1): 1-10. doi: ... ISBN 978-1-118-84615-5. Hales, Dinah F.; Wilson, Alex C. C.; Sloane, Mathew A.; Simon, Jean-Christophe; Legallic, Jean-François ... ISBN 978-1-4443-5784-4. van Emden, Helmut F.; Harrington, Richard (2017). Aphids as Crop Pests. CABI. pp. 229-230. ISBN 978-1- ... ISBN 978-1-78064-709-8. Archived from the original on 2021-06-24. Retrieved 2018-04-29. Von Dohlen, Carol; Moran, Nancy A. ( ...
... enters the cells though aquaporins 7 and 9, which is a type of aquaglyceroporin. Arsenic (V) compounds use phosphate ... The anhydride 1-arsenato-3-phospho-D-glycerate generated readily hydrolyzes due to the longer bond length of As-O compared to P ... 533 (1-2): 37-65. doi:10.1016/j.mrfmmm.2003.07.009. PMID 14643412. Pierce, B.L; Kibriya, M.G (2012). "Genome-wide association ... 715 (1-2): 32-41. doi:10.1016/j.mrfmmm.2011.07.004. PMID 21782832. Sykora, P; Snow, E.T (2008). "Modulation of DNA polymerase ...
... aquaporins) or other solutes to passively pass through the membrane down their electrochemical gradient. They are studied using ... 1828 (1): 79-93. doi:10.1016/j.bbamem.2012.01.002. PMID 22266266. Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P ( ...
... of their apt location in the cell membranes of root caps as well as their interactions and effect on a type of aquaporin water ... This mechanism is supported strongly by the observation of growth patterns of the Arabidopsis abscisic acid mutants (aba1-1 and ... abi2-1) and no hydrotropic response mutant (nhr1). Abscisic acid mutants were unable to produce abscisic acid, and haphazardly ...
This creates osmotic pressure and draws water into CSF, facilitated by aquaporins. Chloride, with a negative charge, moves with ... and specific antibodies such as aquaporin-4 may be tested for to assist in the diagnosis of autoimmune conditions. A lumbar ... ISBN 978-1-58829-040-3. Iliff JJ, Wang M, Liao Y, Plogg BA, Peng W, Gundersen GA, et al. (August 2012). "A paravascular pathway ... 15 (4): 1 p following ECP4. doi:10.3171/foc.2003.15.6.8. PMID 15376362. Seehusen DA, Reeves MM, Fomin DA (September 2003). " ...
Only mature blood cells contain the membrane proteins, such as aquaporin and glycophorin, that are required to attach to and ... Poulton, T B; Murphy, W D; Duerk, J L; Chapek, C C; Feiglin, D H (1 December 1993). "Bone marrow reconversion in adults who are ... 2016 (7): 1-24. doi:10.1155/2016/6940283. PMC 4969512. PMID 27516776.{{cite journal}}: CS1 maint: uses authors parameter (link ... Chan, Brian Y.; Gill, Kara G.; Rebsamen, Susan L.; Nguyen, Jie C. (1 October 2016). "MR Imaging of Pediatric Bone Marrow". ...
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. S2CID 22534091. Sharma NC, Efstratiou A, Mokrousov I, Mutreja A ...
The erythrocyte water channel aquaporin 1 (AQP1) is expressed in multiple absorptive and secretory epithelia including the ... Microvessel overexpression of aquaporin 1 parallels bone marrow angiogenesis in patients with active multiple myeloma Br J ... The erythrocyte water channel aquaporin 1 (AQP1) is expressed in multiple absorptive and secretory epithelia including the ... A Vacca 1 , A Frigeri, D Ribatti, G P Nicchia, B Nico, R Ria, M Svelto, F Dammacco ...
keywords = "Aquaporins, Bile secretion, Biliary epithelia",. author = "Marinelli, {Ra{\u}l A.} and Tietz, {Pamela S.} and Pham ... Aquaporin-1 (AQP1) water channels are present in the apical and basolateral plasma membrane domains of bile duct epithelial ... abstract = "Aquaporin-1 (AQP1) water channels are present in the apical and basolateral plasma membrane domains of bile duct ... N2 - Aquaporin-1 (AQP1) water channels are present in the apical and basolateral plasma membrane domains of bile duct ...
Keywords: irritable bowel syndrome, aquaporins, NF-κB. Received: November 04, 2016 Accepted: April 18, 2017 Published: May 02, ... Objective: Our research was to detect the expression of aquaporins. NF-κB in Irritable bowel syndrome (IBS) rat models colon ... Aquaporins 1, 3 and 8 expression in irritable bowel syndrome rats colon via NF-κB pathway. ... Guanqun Chao1 and Shuo Zhang2. 1Department of Family Medicine, Sir Run Run Shaw Hospital, Zhejiang University, Hangzhou, China ...
Crystallization and Preliminary Crystallographic Analysis of Human Aquaporin 1 at a Resolution of 3.28 A.. ...
Red blood cell aquaporin-1 expression is decreased in hereditary spherocytosis. Ann Hematol. 2016 Oct. 95 (10):1595-601. [QxMD ... Aquaporin-1. In addition to abnormal levels of proteins affected by mutations, patients with HS may demonstrate aberrant ... Crisp et al found reduced expression of the water channel protein aquaporin-1 (AQP1) in the membranes of erythrocytes from ... 1, 2] It is also one of the most common causes of hemolytic anemia due to membrane defect. The morphologic hallmark of HS is ...
Living cells regulate the movement of water via pores in the cell membrane called aquaporins. In a study of plant aquaporin, ... Here we report the X-ray structure of the spinach plasma membrane aquaporin SoPIP2;1 in its closed conformation at 2.1 Å ... These results reveal a molecular gating mechanism which appears conserved throughout all plant plasma membrane aquaporins. ... Plants counteract fluctuations in water supply by regulating all aquaporins in the cell plasma membrane. Channel closure ...
To explore the expression of aquaporin 1 (AQP1) in bladder uroepithelium cell carcinoma (BUCC)and its relevance to recurrence. ... "Expression of Aquaporin 1 in Bladder Uroepithelial Cell Carcinoma and its Relevance to Recurrence". Asian Pacific Journal of ... Expression of Aquaporin 1 in Bladder Uroepithelial Cell Carcinoma and its Relevance to Recurrence. Asian Pacific Journal of ... 2015). Expression of Aquaporin 1 in Bladder Uroepithelial Cell Carcinoma and its Relevance to Recurrence. Asian Pacific Journal ...
Enhancement of Proton Conductance by Mutations of the Selectivity Filter of Aquaporin-1. Title. Enhancement of Proton ...
Aquaporins (AQPs) are a family of channel proteins that facilitate water transportation across cell membranes. Kidney AQPs play ... Aquaporins (AQPs) are a family of channel proteins that facilitate water transportation across cell membranes. Kidney AQPs play ... 2000). Nephrogenic diabetes insipidus in mice lacking aquaporin-3 water channels. Proc. Natl. Acad. Sci. U.S.A. 97, 4386-4391. ... 2001). Immunolocalization of aquaporin-8 in rat kidney, gastrointestinal tract, testis, and airways. Am. J. Physiol. Renal. ...
Normal mesothelium expresses aquaporin 1 (AQP1) and retained expression has been associated with improved survival in MM. AQP1 ... The Effect of Aquaporin 1-Inhibition on Vasculogenic Mimicry in Malignant Mesothelioma November 11, 2017 ...
Anaemia stimulates aquaporin 1 expression in the fetal sheep heart. / Jonker, S. S.; Davis, L. E.; van der Bilt, J. D.W. et al. ... Anaemia stimulates aquaporin 1 expression in the fetal sheep heart. S. S. Jonker, L. E. Davis, J. D.W. van der Bilt, B. Hadder ... Anaemia stimulates aquaporin 1 expression in the fetal sheep heart. In: Experimental physiology. 2003 ; Vol. 88, No. 6. pp. 691 ... Anaemia stimulates aquaporin 1 expression in the fetal sheep heart. Experimental physiology. 2003 Nov;88(6):691-698. doi: ...
Aquaporin 1 (AQP1), a transmembrane protein that forms water channels, has previously been shown to facilitate growth and ... Down-regulation of Aquaporin-1 mediates a microglial phenotype switch affecting glioma growth ... Down-regulation of Aquaporin-1 mediates a microglial phenotype switch affecting glioma growth. ...
Classification and Gene Structure of Aquaporins.. Xu, Long; Guo, Xiangdong; Wang, Weidong; Li, Chunling. Adv Exp Med Biol; 1398 ... A pair of NPA boxes forming a pore is highly conserved among all aquaporins and is also key residues for the classification of ... Aquaporins (AQPs) are a family of membrane water channels that basically function as regulators of intracellular and ...
Aquaporin-mediated dysregulation of cell migration in disease states. Cell Mol Life Sci 2023;80:48. [PMID: 36682037 DOI: ... Aquaporins: New Targets for Cancer Therapy. Technol Cancer Res Treat 2016;15:821-8. [PMID: 26438607 DOI: 10.1177/ ... Aquaporins 1, 3 and 5 in Different Tumors, their Expression, Prognosis Value and Role as New Therapeutic Targets. Pathol Oncol ... Dutta A, Das M. Deciphering the Role of Aquaporins in Metabolic Diseases: A Mini Review. The American Journal of the Medical ...
To mimic phosphorylation, residues implicated in the opening and closing of this gated aquaporin were mutated and their X-ray ... Our findings show that aquaporins, even though similar in size and fold, give very diverse protein yields. Factors influencing ... Increased structural and functional knowledge of aquaporins will aid in understanding how the flux of water through these pores ... Observations regarding the influence of the aquaporin construct on crystal packing are also discussed. Regulatory mechanisms of ...
A full-length cDNA sequence of aquaporin (GenBank JQ970426) was isolated from the hypodermis of the blue crab, C. sapidus, ... Callinectes larvae differed in their capacity to molt in hyposalinity, as those at earlier stages from Zoea (Z) 1 to Z4 had ... CasAQP-1 expression differed with ontogeny during larval development, with significantly higher expression at Z1-2, compared to ... However, it remains to be determined if the increase in CasAQP-1 expression at later larval stages may have a role in ...
Expression of aquaporin-4 water channels in rat cholangiocytes. Raúl A. Marinelli, Linh D. Pham, Pamela S. Tietz, Nicholas F. ... Expression of aquaporin-4 water channels in rat cholangiocytes. / Marinelli, Raúl A.; Pham, Linh D.; Tietz, Pamela S. et al. ... Expression of aquaporin-4 water channels in rat cholangiocytes. In: Hepatology. 2000 ; Vol. 31, No. 6. pp. 1313-1317. ... Marinelli, R. A., Pham, L. D., Tietz, P. S., & LaRusso, N. F. (2000). Expression of aquaporin-4 water channels in rat ...
Impairment of angiogenesis and cell migration by targeted aquaporin-1 gene disruption p.786 doi: 10.1038/nature03460 ...
aquaporins are basically proteins that are embedded in the cell membranes that perform the function of regulation of the water. ... Water Dynamics In Plants; Water In Plant Life, Aquaporins, Properties Of Water, An Excellent Solvent. Semester-1 Applied ... particularly it can pass more easily through aquaporin that are the low resistance pores. ... Seed Structure And Seed Germination; Seed Dormancy, Seed Viability, BS Applied biosciences, Semester-1, Plant Physiology ...
Aquaporin-1 and aquaporin-2 urinary excretion in cirrhosis: Relationship with ascites and hepatorenal syndrome. Hepatology. ... 10] Stage 1 AKI would be classified as an increase in serum creatinine level by 0.3 mg/dL or a 50% increase, whereas stages 2 ... 1] and, occasionally, fulminant hepatitis, who have portal hypertension and ascites. Estimates indicate that at least 40% of ... Reversal of type 1 hepatorenal syndrome with the administration of midodrine and octreotide. Hepatology. 1999 Jun. 29(6):1690-7 ...
102000010637 Aquaporins Human genes 0.000 description 1 * 108010063290 Aquaporins Proteins 0.000 description 1 ... CN (1) CN207340514U (en) Cited By (1). * Cited by examiner, † Cited by third party. Publication number. Priority date. ... Priority Applications (1). Application Number. Priority Date. Filing Date. Title. CN201721292603.9U CN207340514U (en) 2017-10- ... Applications Claiming Priority (1). Application Number. Priority Date. Filing Date. Title. CN201721292603.9U CN207340514U (en) ...
AquaPorin Hydrating Cream - 1.7 oz. Home \ Retail Products \ Retail Hydrating/Moisturizing \ AquaPorin Hydrating Cream - 1.7 oz ... AquaPorin Hydrating Cream - 1.7 oz. Log in to see prices. Hydrate with natural oils to maintain and increase skin moisture. ... Boosts Aquaporin-3 which promotes inner hydration mechanisms and water movement from the basal layer of epidermis and to the ... Increases Aquaporins-3, 9, and 10 to hydrate skin, increases fibronectin, and envelope proteins to improve corneocyte cohesion ...
Aquaporin-1 Show on y-axis - References (HTP + LTP). References (LTP). References (HTP). ...
Aquaporin (1) Bactenecin (2) Bacterial signal peptidase (1) BAD (3) BAK (2) ...
Aquaporin-1 in the peritoneal membrane: Implications for water transport across capillaries and peritoneal dialysis.. *O. ... It is concluded that the quantitative role of aquaporins in overall fluid transport may vary substantially in normal patients ... The conclusion was that the mechanisms describing peritoneal bicarbonate and pH kinetics during PD must include 1) ...
Anti-Rat Aquaporin 3 , 15-AQP31-A Catalog#: AQP31-A Antigen: 15aa peptide of Rat AQP3 (Gene accession #P47862; Designated ( ... Anti-Rat Aquaporin 1 , 15-aqp11-a Company name: Alpha Diagnostics Product type: Antibody Product name: Rabbit Anti-Aquaporin-1 ... Goat Anti-Mouse PSD95 , 513-DPABH-27821 Goat anti-Mouse DLG4 (aa 1-100) polyclonal antibody for ICC/IF, WB, IHC-P Host Species ... Exosome FLOT1 Antibody , 322-EXOAB-FLOT1-1 Anti-FLOT1 Antibody (rabbit anti-human, mouse, rat) with goat anti-rabbit HRP ...
Anti-Rat Aquaporin 3 Catalog#: AQP31-A Antigen: 15aa peptide of Rat AQP3 (Gene accession #P47862; Designated (AQP31-P or ... Anti-Rat Aquaporin 1 Company name: Alpha Diagnostics Product type: Antibody Product name: Rabbit Anti-Aquaporin-1 Antibody, ... QualiCode™ HIV-1/2 Western Blot Kit * QualiCode™ HIV-1/2 Western Blot Kit ... Exosome HSP70 Antibody Product name: Hsp70 Catalog: Exoab-hsp70a-1 Clonality: Polyclonal Host: Rabbit Conjugate: Nonconjugated ...
Hydrocephalus and Aquaporins: The Role of Aquaporin-1. M. Y. S. Kalani, A. S. Filippidis, H. L. Rekate. 12. Hydrocephalus and ... Aquaporins: The Role of Aquaporin-4. A. S. Filippidis, M. Y. S. Kalani, H. L. Rekate. 13. Effect of Acetazolamide on Aquaporin- ... 1. Series. Acta Neurochirurgica Supplementum. Page amount. 12 pages. Category. Medicine, Health Care, Mode. Format. Ebook. ... 1. Fifth International Hydrocephalus Workshop, Crete, Greece, May 20-23, 2010: Themes and Highlights. Harold L. Rekate, Gunes A ...
Journal Article] Expression of Aquaporin 1 in Primary Renal Tumors : A Prognostic Indicator for Clear-Cell Renal Cell Carcinoma ... 1. 腎癌及び膀胱癌細胞株においてHypoxia Inducible Factor (HIF) 1α& 2αそれぞれを強制発現または発現抑制させたクローンを作製しました。. 2. HIFαを強制発現させると、低酸素環境下でも増殖が抑制されにくい傾向が認め ... Presentation] Effect of binding proteins to Hypoxia-
Aquaporins and small neutral solute transporters [TC:1.A.8]. Aquaporins. 343 (AQP8). ... Ontology (2) KEGG BRITE (2) Pathway (1) KEGG PATHWAY (1) Disease (1) OMIM (1) Genome (1) KEGG GENOME (1) Gene (12) KEGG ... 1) HGNC (1) Ensembl (1) RIKEN BRC-DNA (1) OC (1) PHAROS (1) Protein sequence (5) UniProt (1) SWISS-PROT (1) RefSeq(pep) (3) DNA ... sequence (15) RefSeq(nuc) (3) GenBank (6) EMBL (6) Protein domain (1) Pfam (1) All databases (38) Download RDF ...
  • The erythrocyte water channel aquaporin 1 (AQP1) is expressed in multiple absorptive and secretory epithelia including the capillary endothelia. (nih.gov)
  • Aquaporin-1 (AQP1) water channels are present in the apical and basolateral plasma membrane domains of bile duct epithelial cells, or cholangiocytes, and mediate the transport of water in these cells. (elsevier.com)
  • Vasculogenic mimicry (VM) is a newly described phenomenon associated with increased aggressiveness in other malignancies, and has been characterized in MM. Normal mesothelium expresses aquaporin 1 (AQP1) and retained expression has been associated with improved survival in MM. AQP1 is expressed by normal vascular endothelium and is involved in mediating MM cell motility and proliferation. (mesothelioma-line.com)
  • Therefore, the goal of our study was to determine the level of expression of the water channel aquaporin 1 (AQP1) during cardiac development and in the anaemic fetal sheep heart. (elsevier.com)
  • Aquaporin 1 (AQP1), a transmembrane protein that forms water channels, has previously been shown to facilitate growth and progression of many types of tumors by modulating tumor cell migration, proliferation and angiogenesis. (mdc-berlin.de)
  • We recently reported that secretin induces the exocytic insertion of functional aquaporin-1 water channels (AQP1) into the apical membrane of cholangiocytes and proposed that this was a key process in ductal bile secretion. (elsevier.com)
  • Our results indicate that: (1) cholangiocytes express AQP4 messenger RNA (mRNA) and protein and (2) in contrast to AQP1, which is targeted to the apical cholangiocyte membrane by secretin, AQP4 is constitutively expressed on the basolateral cholangiocyte membrane and is secretin unresponsive. (elsevier.com)
  • Our findings show that aquaporins, even though similar in size and fold, give very diverse protein yields. (chalmers.se)
  • Factors influencing the level of protein production are discussed, and one construct of human aquaporin 1 resulted in an exceptionally high yield. (chalmers.se)
  • The AQP2 gene provides instructions for making a protein called aquaporin 2. (medlineplus.gov)
  • Most of the known AQP2 gene mutations cause the aquaporin 2 protein to be misfolded into an incorrect 3-dimensional shape. (medlineplus.gov)
  • Aquaporin 6 is a protein in humans that is encoded by the AQP6 gene. (nsjbio.com)
  • In order to maintain water homeostasis, the rapid and specific regulation of cellular water flow is mediated by the aquaporin (AQP) family of membrane protein water channels. (shu.ac.uk)
  • Western blot analysis detected expression of alpha amylase and aquaporin 5 protein, suggesting that primary cells were acinar in origin. (cdc.gov)
  • Cells strongly expressed the tight junction protein ZO-1 at points of cell-cell contact. (cdc.gov)
  • 1/22 reacts on the intracellular C-terminal AQPl epitope of aquaporins which are members of the Major Intrinsic Protein family. (immbio.hu)
  • expressed in middle/late meiosis,IV" YDR525W 1 5 7 YDR525W "Ydr525wp,IV" YDR526C 1 5 8 YDR526C "Ydr526cp,IV" YER187W 1 5 9 YER187W "similar to killer toxin,V" YER188W 1 5 10 YER188W "Yer188wp,V" YER190W 1 5 11 YER190W "Yrf1-2p,V" YFL002C 1 5 12 YFL002C "ATP-dependent RNA helicase,VI" YFL002W-B 1 5 13 YFL002W-B "TyA gag protein. (davidson.edu)
  • contains a zinc finger,XV" YOL091W 1 15 16 YOL091W "involved in sporulation,XV" YOL103W-B 1 15 17 YOL103W-B "TyB Gag-Pol protein. (davidson.edu)
  • XV" YOL105C 1 15 18 YOL105C "Putative integral membrane protein containing novel cysteine motif. (davidson.edu)
  • Our research was to detect the expression of aquaporins. (oncotarget.com)
  • 2015). 'Expression of Aquaporin 1 in Bladder Uroepithelial Cell Carcinoma and its Relevance to Recurrence', Asian Pacific Journal of Cancer Prevention , 16(9), pp. 3973-3976. (waocp.org)
  • Journal Article] Expression of Aquaporin 1 in Primary Renal Tumors : A Prognostic Indicator for Clear-Cell Renal Cell Carcinoma. (nii.ac.jp)
  • Finally, a high level of aquaporin 1 unexpectedly appeared at the apical surfaces of CLIC4-suppressed RPE cells, together with a concomitant loss of basal surface expression of monocarboxylate transporter MCT3. (elsevier.com)
  • Red blood cell aquaporin-1 expression is decreased in hereditary spherocytosis. (medscape.com)
  • Brain expression of the water channels aquaporin-1 and -4 in mice with acute liver injury, hyperammonemia and brain edema. (medscape.com)
  • Devic's neuromyelitis optica is a chronic inflammatory demyelinating disease of the central nervous system that mainly affects spinal cord, optic nerve and brain regions with high aquaporin 4 antigen expression. (bvsalud.org)
  • Association analysis of aquaporin 7 (AQP7) gene variants with semen qu" by TENGHE MA, JIFENG LIU et al. (tubitak.gov.tr)
  • Aquaporins (AQPs) are a family of channel proteins that facilitate water transportation across cell membranes. (frontiersin.org)
  • Aquaporins (AQPs) are a family of membrane water channels that basically function as regulators of intracellular and intercellular water flow . (bvsalud.org)
  • The aquaporins (AQPs) are a family of water-transporting proteins that facilitate osmotically driven water movement across cell plasma membranes. (nsjbio.com)
  • These findings provide further insight into the molecular gating mechanism previously suggested for this plant aquaporin. (chalmers.se)
  • Diagram illustrating the structural mechanism of aquaporin gating in plant plasma membranes. (nature.com)
  • Johansson, I., Larsson, C., Ek, B. & Kjellbom, P. The major integral proteins of spinach leaf plasma membranes are putative aquaporins and are phosphorylated in response to Ca 2+ and apoplastic water potential. (nature.com)
  • Aquaporins are water channel proteins embedded in the membranes of cells. (chalmers.se)
  • aquaporins are basically proteins that are embedded in the cell membranes that perform the function of regulation of the water. (niazitv.pk)
  • Classification and Gene Structure of Aquaporins. (bvsalud.org)
  • Aquaporin 7 (AQP7) gene as a candidate Antifreeze gene was investigated and associated with fresh and frozen semen quality traits in 45 Simmental and Charolais bulls. (tubitak.gov.tr)
  • Influence of aquaporin-1 gene polymorphism on water retention in liver cirrhosis. (cdc.gov)
  • Aquaporin 4 (AQP4) regulates water content in blood, brain, and cerebrospinal fluid. (smarttots.org)
  • Aquaporin-4 (AQP4)-IgG seropositive neuromyelitis optica spectrum disorders (AQP4-IgG seropositive NMOSD) and myelin oligodendrocyte glycoprotein (MOG)-IgG-associated disease (MOGAD) are inflammatory demyelinating disorders distinct from each other and from multiple sclerosis (MS).While anti-CD20 treatments can be used to treat MS and AQP4-IgG seropositive NMOSD, some MS medications are ineffective or could exacerbate AQP4-IgG seropositive NMOSD including beta-interferons, natalizumab, and fingolimod. (elsevier.com)
  • Rituximab, eculizumab, inebilizumab, and satralizumab all have class 1 evidence for use in AQP4-IgG seropositive NMOSD, and the latter three have been approved by the US Food and Drug Administration (FDA). (elsevier.com)
  • A pair of NPA boxes forming a pore is highly conserved among all aquaporins and is also key residues for the classification of AQP superfamily into four groups according to primary sequences. (bvsalud.org)
  • Morishita, Y., Sakube, Y., Sasaki, S. & Ishibashi, K. Molecular mechanisms and drug development in aquaporin water channel diseases: aquaporin superfamily (superaquaporins): expansion of aquaporins restricted to multicellular organisms. (nature.com)
  • Electron density at the sites of regulation by phosphorylation and pH for SoPIP2;1 in its closed conformation. (nature.com)
  • Regulation of the cytoplasmic entrance into the SoPIP2;1 channel. (nature.com)
  • Here we report the X-ray structure of the spinach plasma membrane aquaporin SoPIP2;1 in its closed conformation at 2.1 Å resolution and in its open conformation at 3.9 Å resolution, and molecular dynamics simulations of the initial events governing gating. (nature.com)
  • Structures of the closed and open conformations of SoPIP2;1. (nature.com)
  • Characterizing the SoPIP2;1 channel. (nature.com)
  • Regulatory mechanisms of the spinach aquaporin SoPIP2;1 were also investigated. (chalmers.se)
  • Aquaporin-1 promoter hypermethylation is associated with improved prognosis in salivary gland adenoid cystic carcinoma. (wjgnet.com)
  • D'Agostino C , Elkashty OA , Chivasso C , Perret J , Tran SD , Delporte C . Insight into Salivary Gland Aquaporins. (wjgnet.com)
  • Aquaporins in Salivary Gland - The Water Fa(u)cet of an Acini? (adejournal.com)
  • The present article reviews the basic histology of salivary gland, its ductal system and also physiology of secretion of saliva and highlights the role of Aquaporins in saliva formation. (adejournal.com)
  • Furthermore, serine 188 was identified as a putative phosphorylation site as its mutation to a glutamate increased the water flux through the aquaporin. (chalmers.se)
  • FAR-INFRARED RAY INDUCED DECATIONIZATION Restores water molecules ability to pass through your body's aquaporins to hydrate at the cellular level. (aquacoolers.com)
  • These antibodies are directed against the aquaporin-4 water channels in the astrocyte foot processes at the blood-brain barrier, pia, subpia, and Virchow-Robin spaces. (medscape.com)
  • As of January 1, 2022, Oncotarget has shifted to a continuous publishing model. (oncotarget.com)
  • Requirement of human renal water channel aquaporin-2 for vasopressin-dependent concentration of urine. (medlineplus.gov)
  • Increased structural and functional knowledge of aquaporins will aid in understanding how the flux of water through these pores is controlled and why certain physical disorders in humans connected to the aquaporins arise. (chalmers.se)
  • A few mutations result in the production of functional aquaporin 2 water channels, but these channels are misrouted within the cell and do not reach the cell membrane. (medlineplus.gov)
  • Liao S , Gan L , Lv L , Mei Z . The regulatory roles of aquaporins in the digestive system. (wjgnet.com)
  • These results reveal a molecular gating mechanism which appears conserved throughout all plant plasma membrane aquaporins. (nature.com)
  • All these ducts function to transport saliva secretion through the terminal excretory duct and into the oral cavity ( Figure 1 ). (adejournal.com)
  • This hormone triggers chemical reactions that ultimately insert aquaporin 2 water channels into the membrane of collecting duct cells. (medlineplus.gov)
  • Without signals from ADH, aquaporin 2 water channels are removed from the membrane of collecting duct cells. (medlineplus.gov)
  • If aquaporin 2 water channels are not inserted into the membrane of collecting duct cells, the kidneys are unable to respond to signals from ADH. (medlineplus.gov)
  • Loonen AJ, Knoers NV, van Os CH, Deen PM. Aquaporin 2 mutations in nephrogenic diabetes insipidus. (medlineplus.gov)
  • Detection of Aquaporin 1 in human kidney tissue (formalin-fixed and paraffin-embedded (FFPE): SNAP i.d.® 2.0 IHC System (sections 1-13) vs. Standard IHC protocol (section M1). (emdmillipore.com)
  • Aquaporin 1 forms a water-specific channel that is constitutively expressed at the PLASMA MEMBRANE of ERYTHROCYTES and KIDNEY TUBULES, PROXIMAL. (bvsalud.org)
  • To mimic phosphorylation, residues implicated in the opening and closing of this gated aquaporin were mutated and their X-ray structures elucidated. (chalmers.se)
  • Water transport activity of the plasma membrane aquaporin PM28A is regulated by phosphorylation. (nature.com)
  • Aquaporin-mediated dysregulation of cell migration in disease states. (wjgnet.com)
  • Heparinized bloodstream examples (1C4 ml) had been acquired 10- to 54-day time post-IVIG (sub-acute cohort, topics #1C10) and 1- to 2-season post-IVIG for five topics (#11C14, 16) and 10-season post-IVIG for just one subject matter (#15) (convalescent cohort). (forgetmenotinitiative.org)
  • Agre, P. & Kozono, D. Aquaporin water channels: molecular mechanisms for human diseases. (nature.com)
  • Dutta A , Das M. Deciphering the Role of Aquaporins in Metabolic Diseases: A Mini Review. (wjgnet.com)
  • It is concluded that the quantitative role of aquaporins in overall fluid transport may vary substantially in normal patients as well in patients with permanent ultrafiltration failure. (semanticscholar.org)
  • The aquaporin 2 water channel plays an essential role in maintaining the body's water balance. (medlineplus.gov)
  • Aquaporins are water channels expressed in acini of salivary glands and play an important role in formation of saliva. (adejournal.com)
  • The role of Aquaporin is to permit the water inflow which determines the viscosity and tonicity of the saliva secreted. (adejournal.com)
  • Type 1 HRS has a more rapid onset, often precipitated by bacterial infection, gastrointestinal hemorrhage, large-volume paracentesis without albumin administration, or excessive response to diuretics, alcohol, or drugs. (medscape.com)
  • Molecular Membrane Biology , 30 (1), 1-12. (shu.ac.uk)
  • This specific transporter is called aquaporin. (coursera.org)
  • Observations regarding the influence of the aquaporin construct on crystal packing are also discussed. (chalmers.se)