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.

Defective secretion of saliva in transgenic mice lacking aquaporin-5 water channels. (1/171)

Aquaporin-5 (AQP5) is a water-selective transporting protein expressed in epithelial cells of serous acini in salivary gland. We generated AQP5 null mice by targeted gene disruption. The genotype distribution from intercross of founder AQP5 heterozygous mice was 70:69:29 wild-type:heterozygote:knockout, indicating impaired prenatal survival of the null mice. The knockout mice had grossly normal appearance, but grew approximately 20% slower than litter-matched wild-type mice when placed on solid food after weaning. Pilocarpine-stimulated saliva production was reduced by more than 60% in AQP5 knockout mice. Compared with the saliva from wild-type mice, the saliva from knockout mice was hypertonic (420 mosM) and dramatically more viscous. Amylase and protein secretion, functions of salivary mucous cells, were not affected by AQP5 deletion. Water channels AQP1 and AQP4 have also been localized to salivary gland; however, pilocarpine stimulation studies showed no defect in the volume or composition of saliva in AQP1 and AQP4 knockout mice. These results implicate a key role for AQP5 in saliva fluid secretion and provide direct evidence that high epithelial cell membrane water permeability is required for active, near-isosmolar fluid transport.  (+info)

Lung fluid transport in aquaporin-5 knockout mice. (2/171)

The mammalian lung expresses water channel aquaporin-1 (AQP1) in microvascular endothelia, AQP4 in airway epithelia, and AQP5 at the apical plasma membrane in type I cells of alveolar epithelia. We previously studied the role of AQP1 and AQP4 in lung fluid transport using knockout mice. Here, we examined the role of AQP5 using AQP5 knockout mice, which were recently shown to manifest defective saliva secretion. AQP5 deletion did not affect lung morphology at the light microscopic level, nor did it affect the distribution or expression of aquaporins 1, 3, or 4. Airspace-capillary osmotic water permeability (P(f)) was measured in isolated perfused lungs by pleural surface fluorescence and gravimetric methods. P(f) was reduced 10-fold by AQP5 deletion and was further reduced by 2- to 3-fold in AQP1/AQP5 double-knockout mice. Hydrostatic lung edema in response to acute increases in pulmonary artery pressure was not affected by AQP5 deletion. Active alveolar fluid absorption was measured in an in situ lung model from the increase in concentration of a volume marker in an isosmolar alveolar instillate. Interestingly, fluid absorption did not differ in litter-matched AQP5 knockout mice, nor was there an effect of AQP5 deletion when fluid absorption was maximally stimulated by pretreatment of mice with keratinocyte growth factor. These results indicate that AQP5 is responsible for the majority of water transport across the apical membrane of type I alveolar epithelial cells. The unimpaired alveolar fluid clearance in AQP5-null mice indicates that high alveolar water permeability is not required for active, near-isosmolar fluid transport.  (+info)

Hypertonic induction of aquaporin-5 expression through an ERK-dependent pathway. (3/171)

Aquaporin-5 (AQP5) is a water channel protein expressed in lung, salivary gland, and lacrimal gland epithelia. Each of these sites may experience fluctuations in surface liquid osmolarity; however, osmotic regulation of AQP5 expression has not been reported. This study demonstrates that AQP5 is induced by hypertonic stress and that induction requires activation of extracellular signal-regulated kinase (ERK). Incubation of mouse lung epithelial cells (MLE-15) in hypertonic medium produced a dose-dependent increase in AQP5 expression; AQP5 protein peaked by 24 h and returned to baseline levels within hours of returning cells to isotonic medium. AQP5 induction was observed only with relatively impermeable solutes, suggesting an osmotic pressure gradient is required for induction. ERK was selectively activated in MLE-15 cells by hypertonic stress, and inhibition of ERK activation with two distinct mitogen-activated extracellular regulated kinase kinase (MEK) inhibitors, U0126 and PD98059, blocked AQP5 induction. AQP5 induction was also observed in the lung, salivary, and lacrimal glands of hyperosmolar rats, suggesting potential physiologic relevance for osmotic regulation of AQP5 expression. This report provides the first example of hypertonic induction of an extrarenal aquaporin, as well as the first association between mitogen-activated protein kinase signaling and aquaporin expression.  (+info)

Conditional expression of fibroblast growth factor-7 in the developing and mature lung. (4/171)

Effects of fibroblast growth factor-7 (FGF-7) on lung morphogenesis, respiratory epithelial cell differentiation, and proliferation were assessed in transgenic mice in which the human FGF-7 cDNA was controlled by a conditional promoter under the direction of regulatory elements from either the human surfactant protein-C (SP-C) or rat Clara cell secretory protein (ccsp) genes. Expression of FGF-7 was induced in respiratory epithelial cells of the fetal lung by administration of doxycycline to the dam. Prenatally, doxycycline induced FGF-7 mRNA in respiratory epithelial cells in both Sp-c and Ccsp transgenic lines, increasing lung size and causing cystadenomatoid malformation. Postnatally, mice bearing both Ccsp-rtta and (Teto)(7)-cmv-fgf-7 transgenes survived, and lung morphology was normal. Induction of FGF-7 expression by doxycycline in the Ccsp-rtta x (Teto)(7)-cmv-fgf-7 mice caused marked epithelial cell proliferation, adenomatous hyperplasia, and pulmonary infiltration with mononuclear cells. Epithelial cell hyperplasia caused by FGF-7 was largely resolved after removal of doxycycline. Surfactant proteins, TTF-1, and aquaporin 5 expression were conditionally induced by doxycycline. The Sp-c-rtta and Ccsp-rtta activator mice provide models in which expression is conditionally controlled in respiratory epithelial cells in the developing and mature lung, altering lung morphogenesis, differentiation, and proliferation.  (+info)

Differential regulation of rat aquaporin-5 promoter/enhancer activities in lung and salivary epithelial cells. (5/171)

Aquaporin-5 (AQP5) is a water channel protein that is selectively expressed in respiratory, salivary, and lacrimal tissues. In order to establish the tissue-specific transcriptional programs that underlie its lung- and salivary-specific expression, a 4.5-kilobase pair DNA fragment encompassing the 5'-flanking region of the rat AQP5 gene has been characterized in detail. A major transcription start site utilized in lung and salivary glands has been localized downstream of a TATAA-like motif. Transient transfection assays of -4.3- and -1.7-AQP5-luciferase constructs in AQP5-expressing lung (MLE-15) and salivary (Pa-4) cells and nonexpressing fibroblast (NIH3T3) and epithelial (HeLa) cells demonstrate preferential transcriptional enhancement of reporter activities in MLE-15 and Pa-4 cells. Transient transfection assays of a series of 5' --> 3' deletion constructs of -4.3-AQP5-luciferase suggest that a common salivary and lung enhancer is located between nucleotides -274 and -139, and a lung-specific enhancer is located between nucleotides -894 and -710. There is one putative lung-specific repressor located in the region of nucleotides -1003/-894 and a common lung and salivary repressor located at nucleotides -503/-385. Moreover, 3' --> 5' deletions up to -171 and -127 base pairs almost abolish transcriptional activation in salivary and lung cells, respectively. Together, our findings indicate that the combination of enhancer/repressor elements within the proximal 5'-flanking region of rat AQP5 gene dictates its restricted expression in both lung and salivary cells.  (+info)

Role of aquaporins in alveolar fluid clearance in neonatal and adult lung, and in oedema formation following acute lung injury: studies in transgenic aquaporin null mice. (6/171)

Aquaporin (AQP) water channels provide a major pathway for osmotically driven water movement across epithelial and microvascular barriers in the lung. We used mice deficient in each of the three principal lung aquaporins, AQP1, AQP4 and AQP5, to test the hypothesis that aquaporins are important in neonatal lung fluid balance, adult lung fluid clearance and formation of lung oedema after acute lung injury. Wet-to-dry weight ratios (W/D) in lungs from wild-type mice decreased from 7.9 to 5.7 over the first hour after spontaneous delivery. AQP deletion did not significantly affect W/D at 45 min after birth. Alveolar fluid clearance was measured in living ventilated mice in which 0.5 ml saline containing radiolabelled albumin was instilled into the airspaces. Fluid clearance was 17.4 % in 15 min and inhibited >90 % by amiloride, but clearance was not affected by AQP deletion. W/D was measured in established models of acute lung injury - acid aspiration and thiourea administration. Two hours after intratracheal administration of HCl, W/D increased from 3.7 to 7.5 but was not affected by AQP deletion. Three hours after intraperitoneal infusion of thiourea, W/D increased to 5.5 and marked pleural effusions appeared, but there were no differences in wild-type and AQP knockout mice. Hyperoxic subacute lung injury was induced by 95 % oxygen. Neither mean survival (143 h) nor W/D at 65 h (5.1) were significantly affected by AQP deletion. Despite their role in osmotically driven lung water transport, aquaporins are not required for the physiological clearance of lung water in the neonatal or adult lung, or for the accumulation of extravascular lung water in the injured lung.  (+info)

Persistent increase in the amount of aquaporin-5 in the apical plasma membrane of rat parotid acinar cells induced by a muscarinic agonist SNI-2011. (7/171)

SNI-2011 induces the long-lasting increase in the amount of aquaporin-5 (AQP5) in apical plasma membranes (APMs) of rat parotid acini in a concentration-dependent manner. This induction was inhibited by p-F-HHSiD, U73122, TMB-8, or dantrolene but not by bisindolmaleimide or H-7, indicating that SNI-2011 acting at M(3) muscarinic receptors induced translocation of AQP5 via [Ca(2+)](i) elevation but not via the activation of protein kinase C. In contrast, acetylcholine induced a transient translocation of AQP5 to APMs. SNI-2011 induces long-lasting oscillations of [Ca(2+)](i) in the presence of extracellular Ca(2+). Thus, SNI-2011 induces a long-lasting translocation of AQP5 to APMs coupled with persistent [Ca(2+)](i) oscillations.  (+info)

Aquaporin water channel in salivary glands. (8/171)

Water secretion from salivary glands, which are innervated by parasympathetic and sympathetic nerves, occurs in response to the stimulation by neurotransmitters. In general, parasympathetic or sympathetic stimulation produces a high flow of saliva as a result of the activation of M3 muscarinic or alpha1-adrenergic receptors, respectively. The secretory mechanisms of fluid secretion were osmotically regulated in response to a transepithelial ion gradient generated by ion transport systems that were located in the apical or basolateral membranes of the acinar cells. Recently, the identification of water-specific channels, or aquaporins (AQPs), in many mammalian tissue and cell types has provided insight into the molecular basis of water movement across biological membranes. It has been reported that several AQPs are expressed in salivary glands and especially AQP5 plays an important role in fluid secretion. This review will focus on the role of AQP5 in the movement of water across the apical plasma membrane in relation to the physiology and pathophysiology of salivary glands.  (+info)

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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 ...
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.
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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. ...
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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, ...
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. ...
Semantic Scholar extracted view of Aquaporin water channels in liver: their significance in bile formation. by Raúl Alberto Marinelli et al.
RATIONALE: Cevimeline may be effective in treating dry mouth that is caused by radiation therapy for head and neck cancer. It is not yet known if cevimeline is more effective than no therapy in treating dry mouth caused by radiation therapy.. PURPOSE: Randomized phase III trial to determine the effectiveness of cevimeline in treating patients who have dryness of the mouth caused by radiation therapy for head and neck cancer. ...
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
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.
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
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 ...
Photo: Dr. Alison Bauer]. In addition to decreased overall tumor burden, mice lacking Ereg also showed reduced inflammation and, in cell studies, both human and mouse lung epithelial cells treated with Ereg had significant increases in wound healing.. Because Ereg is under-studied - as compared to its cousin, EGF - much of the science surrounding this growth factor is still poorly understood. Despite challenges, researchers believe Ereg to contain exciting opportunities as a promising biomarker.. Full story here.. ...
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. ...
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 ...
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
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 ...
After producing a recombinant form of AqpZ in E. coli, the proteins were crystallized--capturing five water molecules inside--and then analyzed by state-of-the-art high-resolution X-ray diffraction techniques. The architecture of aquaporin Z is typical of aquaporins, with a spiral of eight oxygens providing water-binding sites inside the channel. The outer membrane and cytoplasmic ends of the channel are wider than the interior, which is long and narrow. This structure demonstrates that aquaporin selectivity arises in part from erecting a physical barrier: small molecules, like water, can easily pass, but larger ones simply cant fit. And the strategic positioning of amino acid residues with hydrophilic or hydrophobic properties along the channel helps police the influx of molecules based on their affinity for water. While it seems two amino acid chains located in the middle of the channel also provide a water-friendly surface, Stroud et al. say they play a more intriguing role. Noting that the ...
Aquaporins facilitate the diffusion of water across cell membranes. We previously showed that acid pH or low Ca2+ increase the water permeability of bovine AQP0
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.. ...
Polyclonal antibody for AQUAPORIN 3/AQP3 detection. Host: Rabbit.Size: 100μg/vial. Tested applications: IHC-P. Reactive species: Human. AQUAPORIN 3/AQP3 information: Molecular Weight: 31544 MW; Subcellular Localization: Basolateral cell membrane; Multi-pa
Aquaporin 10 antibody, C-term (aquaporin 10) for WB. Anti-Aquaporin 10 pAb (GTX45889) is tested in Human samples. 100% Ab-Assurance.
Purpose: The expression of aquaporin water channel genes are shown to be affected in several pathological conditions of retina, such as in diabetic retinopathy, retinal ischemia and in autoimmune uveitis. Human native retinal pigment epithelial (RPE) cells and immortalized human RPEs are formerly shown to express aquaporins, still the expression of aquaporins in stem cell derived RPE have not been previously elucidated. The objective of this study was to determine the expression of several aquaporin genes (aquaporin1,- 3, -4, -5, -6, -7, -10, -11 and -12) and assess the localization of aquaporin 1 water channel protein in human embryonic (hESCs) and induced pluripotent stem cells (hiPSCs) derived RPE cells.. Methods: hESC- and hiPSC derived RPE cells were grown as monolayer in serum-free media. The expression of aquaporin genes was determined with qRT-PCR. The localization of AQP1-protein was studied with confocal microscopy. Finally, the functionality of aquaporins was assessed with dye ...
With Aquaporin Inside™ Reverse Osmosis membranes, water treatment can be done with lower energy consumption compared to conventional membrane technology. The benefit comes from the aquaporin proteins which are very efficient in transporting water. This enables the water treatment plant to increase the capacity of treated wastewater without increasing the energy consumption, or remaining at the same capacity level while lowering the energy consumption. At the same time, Aquaporin membranes has the potential to remove also small, neutral compounds such as micro pollutants/trace organics, improving re-use water quality.. Aquaporin Inside™ Forward Osmosis ...
Looking for online definition of Aquaporin1 or what Aquaporin1 stands for? Aquaporin1 is listed in the Worlds largest and most authoritative dictionary database of abbreviations and acronyms
Background Aquaporins (Aqps) are integral membrane proteins that facilitate the transport of water and small solutes across cell membranes. Among vertebrate species, Aqps are highly conserved in both gene structure and amino acid sequence. These proteins are vital for maintaining water homeostasis in living organisms, especially for aquatic animals such as teleost fish. Studies on teleost Aqps are mainly limited to several model species with diploid genomes. Common carp, which has a tetraploidized genome, is one of the most common aquaculture species being adapted to a wide range of aquatic environments. The complete common carp genome has recently been released, providing us the possibility for gene evolution of aqp gene family after whole genome duplication. Results In this study, we identified a total of 37 aqp genes from common carp genome. Phylogenetic analysis revealed that most of aqps are highly conserved. Comparative analysis was performed across five typical vertebrate genomes. We found that
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.
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
An important thing in our body is the saliva. It keeps our mouth hydrated always without our knowledge. What will happen to our mouth and body if there is no saliva?. The work of saliva is to help us digest the food and it also controls the bacteria and fungi in our body.. Bacteria will increase if the saliva secretion in our mouth reduces. Tongue dryness, gum crack might occur if there is less saliva in the mouth. Let us now understand the truth behind saliva secretion and the reason for less secretion.. Do you want white teeth…? Eat this!!! ...
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 ...
Cevimeline is a parasympathomimetic and muscarinic agonist, with particular effect on M3 receptors. It is indicated by the Food and Drug Administration for the treatment of dry mouth associated with Sjögrens syndrome.
Youll soon see a new drug for severe dry mouth called Evoxac (EE-vo-zak, cevimeline). ... Learn more with Pharmacists Letter.
Get the latest reverse osmosis membranes (water and wastewater) news , the worlds largest environmental industry marketplace and information resource.
Kit contents: 1. MICROTITER PLATE * 1 2. ENZYME CONJUGATE*1 vial 3. STANDARD A*1 vial 4. STANDARD B*1 vial 5. STANDARD C*1 vial 6. STANDARD D*1 vial 7. STANDARD E*1 vial 8. STANDARD F*1 vial 9. SUBSTRATE A*1 vial 10. SUBSTRATE B*1 vial 11. STOP ...
Kit contents: 1. MICROTITER PLATE * 1 2. ENZYME CONJUGATE*1 vial 3. STANDARD A*1 vial 4. STANDARD B*1 vial 5. STANDARD C*1 vial 6. STANDARD D*1 vial 7. STANDARD E*1 vial 8. STANDARD F*1 vial 9. SUBSTRATE A*1 vial 10. SUBSTRATE B*1 vial 11. STOP ...
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 main role of salivary glands (SG) is the production and secretion of saliva, in which aquaporins (AQPs) play a key role by ensuring water flow. The AQPs are transmembrane channel proteins permeable to water to allow water transport across cell membranes according to osmotic gradient. This review gives an insight into SG AQPs. Indeed, it gives a summary of the expression and localization of AQPs in adult human, rat and mouse SG, as well as of their physiological role in SG function. Furthermore, the review provides a comprehensive view of the involvement of AQPs in pathological conditions affecting SG, including Sjögren’s syndrome, diabetes, agedness, head and neck cancer radiotherapy and SG cancer. These conditions are characterized by salivary hypofunction resulting in xerostomia. A specific focus is given on current and future therapeutic strategies aiming at AQPs to treat xerostomia. A deeper understanding of the AQPs involvement in molecular mechanisms of saliva secretion and diseases
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 ...
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
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 ...
Bronchopulmonary dysplasia (BPD) remains a major respiratory illness in extremely premature infants. The biological mechanisms leading to BPD are not fully understood, although an arrest in lung development has been implicated. The current study aimed to investigate the occurrence of autophagy in the developing mouse lung and its regulatory role in airway branching and terminal sacculi formation. We found 2 windows of epithelial autophagy activation in the developing mouse lung, both resulting from AMPK activation. Inhibition of AMPK-mediated autophagy led to reduced lung branching in vitro. Conditional deletion of beclin 1 (Becn1) in mouse lung epithelial cells (Becn1Epi-KO), either at early (E10.5) or late (E16.5) gestation, resulted in lethal respiratory distress at birth or shortly after. E10.5 Becn1Epi-KO lungs displayed reduced airway branching and sacculi formation accompanied by impaired vascularization, excessive epithelial cell death, reduced mesenchymal thinning of the interstitial ...
Bronchopulmonary dysplasia (BPD) remains a major respiratory illness in extremely premature infants. The biological mechanisms leading to BPD are not fully understood, although an arrest in lung development has been implicated. The current study aimed to investigate the occurrence of autophagy in the developing mouse lung and its regulatory role in airway branching and terminal sacculi formation. We found 2 windows of epithelial autophagy activation in the developing mouse lung, both resulting from AMPK activation. Inhibition of AMPK-mediated autophagy led to reduced lung branching in vitro. Conditional deletion of beclin 1 (Becn1) in mouse lung epithelial cells (Becn1Epi-KO), either at early (E10.5) or late (E16.5) gestation, resulted in lethal respiratory distress at birth or shortly after. E10.5 Becn1Epi-KO lungs displayed reduced airway branching and sacculi formation accompanied by impaired vascularization, excessive epithelial cell death, reduced mesenchymal thinning of the interstitial ...
Objective: It is well known that VEGFR expression is correlated with peritumoral brain edema in meningiomas. Also Aquaporin4 seems to induce the perifocal edema. In our study we analyzed the correlation of VEGFR1, VEGFR2 and Aquaporin4 to the brain edema. Additionally a potential correlation between[for full text, please go to the a.m. URL ...
Hi, Bit more than a month ago my mom developed burning sensation on her back and stomach, she went to a doc but he said its nothing lifetreatening and she waited for for her turn for the tests, it was like this for a week or two. Few weeks ago the burning sensation became too much to bear and my mom went to a hospital. They took her in and the next day she had issues walking and day later she couldnt walk on her own at all. After a few days they put her on some steroid IV thing for
Hi, Bit more than a month ago my mom developed burning sensation on her back and stomach, she went to a doc but he said its nothing lifetreatening and she waited for for her turn for the tests, it was like this for a week or two. Few weeks ago the burning sensation became too much to bear and my mom went to a hospital. They took her in and the next day she had issues walking and day later she couldnt walk on her own at all. After a few days they put her on some steroid IV thing for
Pringle S, Maimets M, van der Zwaag M, Stokman MA, van Gosliga D, Zwart E, Witjes MJ, de Haan G, van Os R, Coppes RP. (2016) Human Salivary Gland Stem Cells Functionally Restore Radiation Damaged Salivary Glands. Stem Cells.. Back to previous page ...
Immunohistochemistry: STK39 Antibody [NBP2-49347] - Staining of human salivary gland shows strong cytoplasmic and nuclear positivity in glandular cells ...
Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). Aquaporin 5 ... Aquaporin-5 is a protein that in humans is encoded by the AQP5 gene. Aquaporin 5 (AQP5) is a water channel protein. ... "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- ...
24 (4): 1001-5. doi:10.1042/bst0241001. PMID 8968500. Mitchell CA, Brown S, Campbell JK, Munday AD, Speed CJ (Nov 1996). " ... The inositol 5-phosphatase skip localizes to the endoplasmic reticulum and translocates to membrane ruffles following epidermal ... This gene encodes a protein with 5-phosphatase activity toward polyphosphate inositol. The protein localizes to the cytosol in ... 275 (15): 10870-5. doi:10.1074/jbc.275.15.10870. PMID 10753883. v t e. ...
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 ...
Agre was recognized for his discovery of aquaporin water channels. Aquaporins are water-channel proteins that move water ... Aquaporins are "the plumbing system for cells," said Agre. Every cell is primarily water. "But the water doesn't just sit in ... Aquaporin Roderick MacKinnon Gheorghe Benga "The Nobel Prize in Chemistry 2003". www.nobelprize.org. Retrieved March 21, 2018. ... The 28 kDa protein is now known as aquaporin-1 (abbreviated AQP1), the archetypal member of a large family of water channel ...
... also indicated in proper lung development by controlling the late differentiation stages of alveolar epithelium and aquaporin-5 ... 275 (33): 25330-5. doi:10.1074/jbc.M000828200. PMID 10851229. Crawford SE, Qi C, Misra P, Stellmach V, Rao MS, Engel JD, Zhu Y ... 277 (5): 3585-92. doi:10.1074/jbc.M107995200. PMID 11724781. Liu C, Glasser SW, Wan H, Whitsett JA (2002). "GATA-6 and thyroid ... "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1-2): 149-56. doi: ...
... a novel cornea-expressed gene and the absence of transcripts for aquaporin 5" (PDF). Invest. Ophthalmol. Vis. Sci. 46 (4): 1239 ...
Based on previous research using mice and rats, researchers looked towards the role of aquaporin 5 (AQP5), a water channel ... Gresz, V.; Kwon, T; Gong, H; Agre, P.; Steward, M; King, L; Nielsen, S. (2004). "Immunolocalization of AQP-5 in rat parotid and ...
... can sometimes come with abnormal aquaporin 5 in the sweat glands. Cystic fibrosis can be diagnosed by a sweat test, as the ... 5 (1): 35-36. doi:10.1111/j.1600-0560.1978.tb00935.x. ISSN 1600-0560. James, Berger & Elston 2011, p. 534. Rubin & Strayer 2011 ... 25 (5): 761-767. doi:10.1172/JCI101760. ISSN 0021-9738. PMC 435616. PMID 16695370. Caceci, Thomas. "Integument I: Skin". VM8054 ... 100 (5): 1692-1701. doi:10.1152/japplphysiol.01124.2005. ISSN 8750-7587. PMID 16614366. Sørensen, Vibeke W.; Prasad, Gaya (1973 ...
Balo-like lesions have been reported in aquaporin-4 seropositive and seronegative NMOSD, and also in children, as part of an ... Nov 2010). "Aquaporin-4 astrocytopathy in Baló's disease". Acta Neuropathologica. 120 (5): 651-660. doi:10.1007/S00401-010-0733 ... similar to the one found in aquaporin-seropositive neuromyelitis optica. Though no anti-NMO antibodies have been found, the ... 5 (8): 900-912. doi:10.1002/acn3.572. PMC 6093849. PMID 30128315. Article at mult-sclerosis.org Lucas M.Pessini, Tumefactive ...
Aquaporin-9 is a protein that in humans is encoded by the AQP9 gene. The aquaporins/major intrinsic protein are a family of ... 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 ...
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 ...
Aquaporins allow water to move down their osmotic gradient and out of the nephron, increasing the amount of water re-absorbed ... Vasopressin, acting through cAMP, also increases transcription of the aquaporin-2 gene, thus increasing the total number of ... This occurs through increased transcription and insertion of water channels (Aquaporin-2) into the apical membrane of ... Wilson JL, Miranda CA, Knepper MA (2013). "Vasopressin and the Regulation of Aquaporin-2". Clinical and Experimental Nephrology ...
Two types of aquaporins are expressed in the CNS: aquaporin-1, which is expressed by specialized epithelial cells of the ... Aquaporins are membrane-bound channels that play critical roles in regulating the flux of water into and out of cells. Relative ... Aquaporin-4 expression in astrocytes is highly polarized to the endfoot processes ensheathing the cerebral vasculature. Up to ... Verkman AS, Binder DK, Bloch O, Auguste K, Papadopoulos MC (August 2006). "Three distinct roles of aquaporin-4 in brain ...
... 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 is the protein product of the human AQP3 gene. It is found in the basolateral cell membrane of principal collecting ... 2005). "Roles of aquaporin-3 water channels in volume-regulatory water flow in a human epithelial cell line". J. Membr. Biol. ...
It is the only aquaporin regulated by vasopressin. The basic job of aquaporin 2 is to reabsorb water from the urine while its ... This aquaporin is also regulated by food intake. Fasting reduces expression of this aquaporin independently of vasopressin. ... so the aquaporin 2 can be used by the cell. This aquaporin is regulated in two ways by the peptide hormone vasopressin: short- ... Aquaporin 2 is in kidney epithelial cells and usually lies dormant in intracellular vesicle membranes. When it is needed, ...
The expression of aquaporin 4 is reliant on the disease stage of TBI. In an acute stage of TBI, the lack of aquaporin 4 causes ... Aquaporin-4, also known as AQP4, is a water channel protein encoded by the AQP4 gene in humans. AQP4 belongs to the aquaporin ... Aquaporin-4 is the most common aquaporin in the brain, spinal cord, and optic nerve. It is highly expressed in the human body ... Aquaporin-4 is essential in the formation of memory as well as synaptic plasticity. Other performances that aquaporin-4 is ...
Bellati, J; Champeyroux, C; Hem, S; Rofidal, V; Krouk, G; Maurel, C; Santoni (2016). "Novel aquaporin regulatory mechanisms ... Li, G; Santoni, V; Maurel, C (2014). "Plant aquaporins: roles in plant physiology". Biochimica et Biophysica Acta (BBA) - ... of their apt location in the cell membranes of root caps as well as their interactions and effect on a type of aquaporin water ... 27 (5): 430-432. doi:10.21273/HORTSCI.27.5.430. PMID 11537612. Cassab, Gladys I.; Eapen, Delfeena; Campos, María Eugenia ( ...
Clinical relevance of serum aquaporin-4 antibody levels in neuromyelitis optica. Neurochem Res. 2013;38(5):997-1001. doi: ... 49 (5): 1413-1418. doi:10.1212/WNL.49.5.1413. PMID 9371931. S2CID 33205877. Lana-Peixoto, MA; Andrade, GC (June 2001). "The ... The annual incidence is approximately 5/100,000, with a prevalence estimated to be 115/100,000. In Charles Dickens' Bleak House ... Optic neuropathy Visual snow (2007). .In: Sibell, David M. & Kirsch, Jeffrey R. (eds.) , 5 Minute Pain Management Consult, The ...
... s, are a group of diseases characterized by auto-antibodies against aquaporin 4. After the discovery of anti- ... Some authors propose to use the name "autoimmune aquaporin-4 channelopathy" for these diseases, while others prefer a more ... Clinical relevance of serum aquaporin-4 antibody levels in neuromyelitis optica. Neurochem Res. 2013;38(5):997-1001. doi: ... Pittock SJ, Lucchinetti CF (February 2016). "Neuromyelitis optica and the evolving spectrum of autoimmune aquaporin-4 ...
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 ...
... elegans by downregulating DAF-16/FOXO activity and aquaporin gene expression". Cell Metabolism. 10 (5): 379-91. doi:10.1016/j. ... 5 (1): 31-7. doi:10.1111/j.1474-9726.2006.00188.x. PMC 1413578. PMID 16441841. Dorman, Jennie B.; Albinder, Bella; Shroyer, ...
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 ... 103 (5): 267-77. doi:10.1034/j.1600-0404.2001.103005267.x. PMID 11328201. Oaklander AL, Lunn MP, Hughes RA, van Schaik IN, ... 16 (1): 5-11. doi:10.1080/14787210.2018.1417836. PMID 29278020. Sharma NC, Efstratiou A, Mokrousov I, Mutreja A, Das B, ...
... colocalization with aquaporin-2 in collecting duct vesicles". The American Journal of Physiology. 275 (5 Pt 2): F752-60. doi: ... 108 (3): 211-5. doi:10.1007/s004390100480. PMID 11354632. Shukla A, Corydon TJ, Nielsen S, Hoffmann HJ, Dahl R (Jul 2001). " ... 10.1152/ajprenal.1998.275.5.F752. PMID 9815132. Valdez AC, Cabaniols JP, Brown MJ, Roche PA (Mar 1999). "Syntaxin 11 is ...
... colocalization with aquaporin-2 in collecting duct vesicles". The American Journal of Physiology. 275 (5 Pt 2): F752-60. doi: ... possible role in aquaporin-2 trafficking". The Journal of Clinical Investigation. 98 (4): 906-13. doi:10.1172/JCI118873. PMC ... 3.0.CO;2-5. PMID 10508479. Paumet F, Le Mao J, Martin S, Galli T, David B, Blank U, Roa M (Jun 2000). "Soluble NSF attachment ... 74 (5): 863-73. doi:10.1016/0092-8674(93)90466-4. PMID 7690687. S2CID 37698687. Li C, Ullrich B, Zhang JZ, Anderson RG, Brose N ...
Some proteins naturally form crystalline arrays, like aquaporin in the lens of the eye. In the process of protein ... "Aquaporins in the eye: Expression, function, and roles in ocular disease". Biochimica et Biophysica Acta (BBA) - General ... 1840 (5): 1513-1523. doi:10.1016/j.bbagen.2013.10.037. PMC 4572841. PMID 24184915. McPherson, Alexander; Gavira, Jose A. (2013- ... 5 (1): 7797. Bibcode:2015NatSR...5E7797C. doi:10.1038/srep07797. ISSN 2045-2322. PMC 4297974. PMID 25597864. McPherson, ...
Aquaporin 7 and AQP3 are at the same chromosomal location suggesting that 9p13 may be a site of an aquaporin cluster. Aquaporin ... Aquaporin-7 is a protein that in humans is encoded by the AQP7 gene. Aquaporins/major intrinsic protein (MIP) are a family of ... "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. ...
Robben JH, Knoers NV, Deen PM (Aug 2006). "Cell biological aspects of the vasopressin type-2 receptor and aquaporin 2 water ... Ishikawa SE (Feb 2002). "[Nephrogenic diabetes insipidus associated with mutations of vasopressin V2 receptors and aquaporin-2 ... 51 (5): 1078-83. PMC 1682836. PMID 1415251. Birnbaumer M, Seibold A, Gilbert S, Ishido M, Barberis C, Antaramian A, Brabet P, ... 357 (6376): 333-5. doi:10.1038/357333a0. PMID 1534149. Lolait SJ, O'Carroll AM, McBride OW, Konig M, Morel A, Brownstein MJ ( ...
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 ... 5 (3): 471-478. doi:10.4161/mabs.24112. PMC 4169038. PMID 23549155. Groves, MA (2015). "Applications of ribosome display to ... 5 (1): 125-135. doi:10.1517/14712598.5.1.125. PMID 15709915. Earnshaw, JC (1999). "Signal amplification in flow cytometry using ...
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 ...
... water permeability of the kidney's collecting duct and distal convoluted tubule by inducing translocation of aquaporin-CD water ... 1. Human urinary system: 2. Kidney, 3. Renal pelvis, 4. Ureter, 5. Urinary bladder, 6. Urethra. (Left side with frontal section ... "Vasopressin increases water permeability of kidney collecting duct by inducing translocation of aquaporin-CD water channels to ...
92 (5): 2633-41. doi:10.1152/jn.00486.2004. PMID 15486420.. *^ Christel C, Lee A (Aug 2012). "Ca2+-dependent modulation of ... doi:10.1124/pr.57.4.5. PMID 16382099.. *^ Shaw RM, Colecraft HM (May 2013). "L-type calcium channel targeting and local ... 273 (30): 18930-5. doi:10.1074/jbc.273.30.18930. PMID 9668070.. *. Liu WS, Soldatov NM, Gustavsson I, Chowdhary BP (1999). " ... 5] Cav1.2 is a subunit of L-type voltage-dependent calcium channel.[6] ...
Competitive vasopressin antagonism leads to decreased number of aquaporin channels in the apical membrane of the renal ... 5. collecting duct Selective vasopressin V2 antagonist (sometimes called aquaretics) tolvaptan,[15] conivaptan ... 5. cortical collecting ducts Thiazides bendroflumethiazide, hydrochlorothiazide Inhibits reabsorption by Na+/Cl− symporter 4. ...
Aquaporin 1 - water transporter, defines the Colton Blood Group;. *Glut1 - glucose and L-dehydroascorbic acid transporter; ... 103 (5): 545-53. doi:10.1161/CIRCRESAHA.108.176867. PMC 2763414. PMID 18658051.. CS1 maint: Uses authors parameter (link). ... 39 (5): 308-314. doi:10.1159/000342534. PMC 3678267. PMID 23801921.. CS1 maint: Uses authors parameter (link). ... 978-0-393-06163-5. .. *^ Maton, Anthea; Jean Hopkins; Charles William McLaughlin; Susan Johnson; Maryanna Quon Warner; David ...
June 1999). "Urinary excretion of aquaporin-2 water channel differentiates psychogenic polydipsia from central diabetes ... 5 May 2016. Retrieved 29 October 2016. Bowen, L.; Glynn, S. M.; Marshall, B. D.; Kurth, C. L.; Hayden, J. L. (1990-03-01). " ... 5 May 2016. Retrieved 29 October 2016. Zerbe, R. L.; Robertson, G. L. (1981-12-24). "A comparison of plasma vasopressin ... 5 May 2016. Retrieved 29 October 2016. Mayo Clinic internal medicine board review. Ghosh, Amit., Mayo Foundation for Medical ...
... it acts on proteins called aquaporins and more specifically aquaporin 2 in the following cascade. When released, ADH binds to ... Nephrogenic DI results from lack of aquaporin channels in the distal collecting duct (decreased surface expression and ... stimulating translocation of the aquaporin 2 channel stored in the cytoplasm of the distal convoluted tubules and collecting ...
inositol 1,4,5 trisphosphate binding. • ion channel activity. • protein binding. • actin binding. • calcium channel activity. • ... It has been associated with depression and anxiety (see below), as well as with focal segmental glomerulosclerosis (FSGS).[5] ...
inositol 1,4,5-trisphosphate receptor, type 1[1]. Crystal structure of the ligand binding suppressor domain of type 1 inositol ... The initial sequencing was reported as an unknown protein enriched in the cerebellum called P400.[5] The large size of this ... December 2002). "Structure of the inositol 1,4,5-trisphosphate receptor binding core in complex with its ligand". Nature. 420 ( ... structure of the ligand binding suppressor domain of type 1 inositol 1,4,5-trisphosphate receptor 6181 Crystal structure of the ...
... highest resolution protein structure solved by electron crystallography of 2D crystals is that of the water channel aquaporin-0 ... 26 (5): 759-766.e4. doi:10.1016/j.str.2018.03.021. ISSN 0969-2126. PMC 6333475. PMID 29706530.. ... ISBN 978-1-4020-3919-5. External links[edit]. *Interview with Aaron Klug Nobel Laureate for work on crystallograph electron ... 5] the nicotinic acetylcholine receptor,[6] and the bacterial flagellum.[7] The ...
2004). „Antidiuretic action of oxytocin is associated with increased urinary excretion of aquaporin-2". Nephrology, Dialysis, ...
Competitive vasopressin antagonism leads to decreased number of aquaporin channels in the apical membrane of the renal ... 5. collecting duct Selective vasopressin V2 antagonist (sometimes called aquaretics) tolvaptan,[14] conivaptan ... 5. cortical collecting ducts Thiazides bendroflumethiazide, hydrochlorothiazide Inhibits reabsorption by Na+/Cl− symporter 4. ... The thiazides and potassium-sparing diuretics are considered to be calcium-sparing diuretics.[5] ...
However, when plasma blood volume is low and ADH is released the aquaporins that are opened are also permeable to urea. This ... ADH binds to principal cells in the collecting duct that translocate aquaporins to the membrane, allowing water to leave the ... ADH acts on the V2 receptor and inserts aquaporins on the luminal side ... but at the same time setting up an osmotic gradient for water to follow should the aquaporins of the collecting duct be opened ...
Such molecules can diffuse passively through protein channels such as aquaporins in facilitated diffusion or are pumped across ... In the field of synthetic biology, cell membranes can be artificially reassembled.[4][5][6] ...
All Kir channels require phosphatidylinositol 4,5-bisphosphate (PIP2) for activation.[10] PIP2 binds to and directly activates ...
aquaporin 5, calmodulin, pacsin 3 2 TRPV5 calcium-selective TRP channel intestine, kidney, placenta 100:1 TRPV6 annexin II / ... There are about 28 TRP channels that share some structural similarity to each other.[5] These are grouped into two broad groups ...
Yeum CH, Kim SW, Kim NH, Choi KC, Lee J (July 2002). "Increased expression of aquaporin water channels in hypothyroid rat ... பெரியவர்களுக்கு, தைராய்டு சுரப்புக் குறையானது பின்வரும் அறிகுறிகளுடன் இருக்கின்றது:[5][7][8]. ஆரம்ப அறிகுறிகள்[தொகு]. *மோசமான ... தைராய்டு சுரப்புக் குறையானது பேற்றுக்குப்பின் தைராய்டழற்சியை விளைவிக்கும், இந்த நிலையானது அனைத்து பெண்களில் 5% பேருக்கு ... 5]. -. மூன்றாம் நிலை. ஹைப்போதலாமஸ். ஹைப்போதலாமஸ் போதிய தைரோட்ரோபின் வெளியிடப்படும் ...
exocytosis of aquaporin 2 to apical membrane.[12]. *synthesis of aquaporin 2[12] ... Protein kinase A, more precisely known as adenosine 3',5'-monophosphate (cyclic AMP)-dependent protein kinase was discovered by ... 5][6] In contrast, experimentally induced supra physiological concentrations of cAMP are able to cause separation of the ... holoenzymes, and release of the catalytic subunits.[5]. Extracellular hormones such as glucagon and epinephrine begin an ...
98 (2): 172-5. doi:10.1007/s004390050183. PMID 8698335.. *^ a b c d e f g h i j "GJB1 gene". Genetics Home Reference. US ... 5] Gap junction beta-1 protein is a member of the gap junction connexin family of proteins that regulates and controls the ...
Аквапорин-1, AQP1 (англ. Aquaporin 1 (Colton blood group)) - білок, який кодується геном AQP1, розташованим у людей на ... de Groot B.L., Engel A., Grubmueller H. (2001). A refined structure of human aquaporin-1.. FEBS Lett. 504: 206 - 211. PubMed ... AQP1, AQP-CHIP, CHIP28, CO, aquaporin 1 (Colton blood group). Зовнішні ІД. OMIM: 107776 MGI: 103201 HomoloGene: 68051 GeneCards ... Сполуки, які фізично взаємодіють з Aquaporin 1 переглянути/редагувати посилання на ВікіДаних. ...
Evidence for a secretin-induced vesicular translocation of aquaporin-1" (PDF). J. Biol. Chem. 272 (20): 12984-12988. PMID ... 5,0 5,1 Chu JY, Chung SC, Lam AK, Tam S, Chung SK, Chow BK (2007). "Phenotypes developed in secretin receptor-null mice ... Recentemente descubriuse que xoga tamén un papel na osmorregulación no hipotálamo, hipófise, e riles.[5][6] ... ISBN 0-7216-2888-5.. *↑ Polak JM, Coulling I, Bloom S, Pearse AG (1971). "Immunofluorescent localization of secretin and ...
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 ... Fig.5) Proximal tubule cell showing pumps involved in acid base balance, left is the lumen of tubule ... 5) tan - podocytes lining Bowman's capsule adjacent to capillaries, and parietal layer of capsule, 6)center - five glomerular ...
... occurs in one of two ways: either the osmoreceptor-aquaporin feedback loop is overwhelmed, or it is interrupted. ... "Physiology and pathophysiology of renal aquaporins". Seminars in nephrology. 21 (3): 231-8. doi:10.1053/snep.2001.21647. PMID ... Relatively common[5][6]. Hyponatremia is a low sodium level in the blood.[3] It is generally defined as a sodium concentration ... 29 (5): 549-76. doi:10.1111/j.1365-2265.1988.tb03704.x. PMID 3075528.. [needs update] ...
"Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains". Biochimica et ... 15 (5): 461-71. doi:10.1038/ncb2721. PMC 4052425. PMID 23563491.. *^ Rungaldier S, Oberwagner W, Salzer U, Csaszar E, Prohaska ... 5: 3608. Bibcode:2014NatCo...5.3608L. doi:10.1038/ncomms4608. PMC 3988805. PMID 24699711.. ... In some EIG12 patients seizures may remit with age.[4][5] Inheritance of this disease is autosomal dominant.[10] ...
Aquaporin 1. *Arachidonate 5-lipoxygenase. *Atrophin 1. *BH3 interacting-domain death agonist ...
Nielsen, J.; Kwon, T.H.; Christensen, B.M.; Frokiaer, J.; Nielsen, S. (May 2008). "Dysregulation of renal aquaporins and ... 2 (5): 193-202. doi:10.1093/jat/2.5.193.. *^ R. Baselt, Disposition of Toxic Drugs and Chemicals in Man, 8th edition, ... 5O. 7) is also used in conventional pharmacological treatments. Lithium orotate (C. 5H. 3LiN. 2O. 4), has been presented as an ... 29 (5): 608-614. doi:10.1177/0269881115573808. PMID 25735990.. *^ a b Malhi, Gin S.; Tanious, Michelle; Bargh, Danielle; Das, ...
Aquaporins. *Chloride channels. *Outer membrane auxiliary proteins (polysaccharide transporter) - α-helical transmembrane ... In humans, 27% of all proteins have been estimated to be alpha-helical membrane proteins.[5] Beta-barrel proteins are so far ... 18 (5): 581-586. doi:10.1016/j.sbi.2008.07.001. PMC 2580798. PMID 18674618.. ...
5] Excessive activation of VGCCs is a major component of excitotoxicity, as severely elevated levels of intracellular calcium ...
... can sometimes come with abnormal aquaporin 5 in the sweat glands.[70] ... 5] Ceruminous glands are near the ear canals, and produce cerumen (earwax) that mixes with the oil secreted from sebaceous ... 5][26][4] The proportion of eccrine glands decreases with age.[27] ... 5 (1): 35-36. doi:10.1111/j.1600-0560.1978.tb00935.x. ISSN 1600-0560.. ...
116 (5): 1243-53. doi:10.1172/JCI27186. PMC 1440704. PMID 16628254.. *^ Zhang, Y.; Wang, H.; Kovacs, A.; Kanter, E. M.; Yamada ... 5: 40. doi:10.3389/fphys.2014.00040. PMC 3920094. PMID 24575048.. *^ Barbe, M. T. (1 April 2006). "Cell-Cell Communication ... 69 (5): 1472-80. doi:10.1095/biolreprod.103.016360. PMID 12826585.. *^ El-Sabban, M. E.; Sfeir, AJ; Daher, MH; Kalaany, NY; ... doi:10.1007/s12031-007-9027-5. PMC 2650399. PMID 18236012.. *^ Béla Völgyi, Stewart A. Bloomfield (February 2009). "The diverse ...
Voltage-dependent calcium channel gamma-4 subunit is a protein that in humans is encoded by the CACNG4 gene.[5][6] ... 36 (1): 40-5. doi:10.1038/ng1285. PMID 14702039.. *. Moss FJ, Dolphin AC, Clare JJ (2004). "Human neuronal stargazin-like ...
Rabbit polyclonal Aquaporin 5 antibody. Validated in WB, ELISA and tested in Rat. Independently reviewed in 1 review(s). ... Primary - Rabbit Anti-Aquaporin 5 antibody (ab15119) WB, ELISA Secondary - Goat Anti-Rabbit IgG H&L (HRP) (ab205718) IHC-P, WB ... Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the ... Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) abreview for Anti-Aquaporin 5 antibody. Average ...
Hwang SM, Lee RH, Song JM, Yoon S, Kim YS, Lee SJ, Kang SK, Jung JS (2002) Expression of aquaporin-5 and its regulation in ... Krane CM, Fortner CN, Hand AR, McGraw DW, Lorenz JN, Wert SE, Towne JE, Paul RJ, Whitsett JA, Menon AG (2001) Aquaporin 5- ... Leitch V, Agre P, King LS (2001) Altered ubiquitination and stability of aquaporin-1 in hypertonic stress. Proc Natl Acad Sci U ... Verkman AS, Matthay MA, Song Y (2000) Aquaporin water channels and lung physiology. Am J Physiol Lung Cell Mol Physiol 278(5): ...
In Chapter 6, "The Hormonal Essence of the T-Rex?" author Cordelia Fine considers the biological dogma that testes, and the powerful hormones they exude, are the root of all sexual inequality.. 0 Comments. ...
Order monoclonal and polyclonal Aquaporin 5 antibodies for many applications. Selected quality suppliers for anti-Aquaporin 5 ... Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). Aquaporin 5 ... Top anti-Aquaporin 5 Antibodies at antibodies-online.com. Showing 10 out of 83 products:. Catalog No.. Reactivity. Host. ... Top referenced anti-Aquaporin 5 Antibodies. Show all anti-Aquaporin 5 (AQP5) Antibodies with Pubmed References. * Human ...
By analogy to salivary and submucosal glands, where fluid secretion is aquaporin-5 (AQP5) dependent, we postulated that ... aquaporin water channels might facilitate sweat secretion. Immunol … ... Localization of aquaporin-5 in sweat glands and functional analysis using knockout mice J Physiol. 2002 Jun 1;541(Pt 2):561-8. ... By analogy to salivary and submucosal glands, where fluid secretion is aquaporin-5 (AQP5) dependent, we postulated that ...
Anti-Aquaporin 5 Rabbit pAb Anti-Aquaporin 5, rabbit polyclonal, recognizes the ~28 kDa AQP 5 protein in epithelial tissue ... Anti-Aquaporin 5 Rabbit pAb MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available ... Anti-Aquaporin 5, rabbit polyclonal, recognizes the ~28 kDa AQP 5 protein in epithelial tissue extracts. It is validated for ... More,, Anti-Aquaporin 5, rabbit polyclonal, recognizes the ~28 kDa AQP 5 protein in epithelial tissue extracts. It is validated ...
Molecular Mechanisms and Drug Development in Aquaporin Water Channel Diseases : The Translocation of Aquaporin-5 From Lipid ... Age-related Decreases in the Response of Aquaporin-5 to Acetylcholine in Rat Parotid Glands * * INOUE N. ... Persistent increase in the amount of aquaporin-5 in the apical plasma membrane of rat parotid acinar cells induced by a ... Molecular cloning and characterization of an aquaporin cDNA from salivary, lacrimal, and respiratory tissues RAINA S. ...
We characterized an aquaporin gene HvPIP2;5 from Hordeum vulgare and investigated its physiological roles in heterologous ... We characterized an aquaporin gene HvPIP2;5 from Hordeum vulgare and investigated its physiological roles in heterologous ... Indeed, overexpression of HvPIP2;5 caused higher retention of chlorophylls and water under salt and osmotic stresses than did ... These results suggest that HvPIP2;5 overexpression brought about stress tolerance, at least in part, by reducing the secondary ...
Effect of Prenatal and Neonatal Anti-Androgen Flutamide Treatment on Aquaporin 5 Expression in the Adult Porcine Ovary. ... Androgen AntagonistsAnimalsAnimals, NewbornAquaporin 5FemaleFlutamideGene ExpressionImmunohistochemistryMaternal-Fetal Exchange ... Effect of Prenatal and Neonatal Anti-Androgen Flutamide Treatment on Aquaporin 5 Expression in the Adult Porcine Ovary.. Reprod ... Effect of Prenatal and Neonatal Anti-Androgen Flutamide Treatment on Aquaporin 5 Expression in the Adult Porcine Ovary. Reprod ...
Polymorphisms of aquaporin-5, a key mediator of inflammation, may impact outcome.What This Article Tells Us That Is NewIn acute ... Polymorphisms of aquaporin-5, a key mediator of inflammation, may impact outcome.What This Article Tells Us That Is NewIn acute ... Aquaporin 5 -1364A/C Promoter Polymorphism Is Associated with Pulmonary Inflammation and Survival in Acute Respiratory Distress ... the C-allele of the aquaporin-5 -1364A/C promoter polymorphism is associated with less pulmonary inflammation and greater ...
... *Authors: *Abdalkhalig ... Aquaporin 5 (AQP5) may be involved in NSCLC by promoting lung‑cancer initiation and progression. The present study aimed to ... Elkhider, A., Wang, B., Ouyang, X., Al‑Azab, M., Walana, W., Sun, X., Li, H., Tang, Y., Wei, J., Li, X.Aquaporin 5 promotes ... Elkhider, A., Wang, B., Ouyang, X., Al‑Azab, M., Walana, W., Sun, X., Li, H., Tang, Y., Wei, J., Li, X.Aquaporin 5 promotes ...
5. Descending root temperature from 25°C to 10°C quickly reduced cell hydra … ... These results provide strong evidence for a link between growth at low root temperature and aquaporin-mediated root water ... suggesting that aquaporin phosphorylation/dephosphorylation processes were involved in this response. The temperature ... When the roots were exposed to 10°C for 5 d, L(p) was reduced in wild-type plants and in plants overexpressing PIP1;4, whereas ...
Aquaporin 5 antibody LS-C3809 is an unconjugated rabbit polyclonal antibody to Aquaporin 5 (AQP5) from human, mouse and rat. ... Aquaporin 5 antibody LS-C3809 is an unconjugated rabbit polyclonal antibody to Aquaporin 5 (AQP5) from human, mouse and rat. ... Aquaporin 5 antibody LS-C3809 is an unconjugated rabbit polyclonal antibody to Aquaporin 5 (AQP5) from human, mouse and rat. ... Recognizes rat Aquaporin 5 (AQP5). No significant homology is seen with other AQPs or any other protein. Species sequence ...
The distribution and function of aquaporins (AQPs) have not previously been defined in sweat glands. In this study, AQP1, AQP3 ...
Aquaporin 5 antibody LS-C3810 is an unconjugated rabbit polyclonal antibody to Aquaporin 5 (AQP5) from mouse and rat. Validated ... Aquaporin 5 antibody LS-C3810 is an unconjugated rabbit polyclonal antibody to Aquaporin 5 (AQP5) from mouse and rat. Validated ... Aquaporin 5 antibody LS-C3810 is an unconjugated rabbit polyclonal antibody to Aquaporin 5 (AQP5) from mouse and rat. Validated ... Recognizes rat Aquaporin 5 (AQP5). No significant homology is seen with other AQPs or any other protein. Species sequence ...
aquaporin. ACh. acetylcholine. mAChR. muscarinic acetylcholine receptor. APM. apical plasma membrane. SNI-2011. cevimeline ... 1999) Defective secretion of saliva in transgenic mice lacking aquaporin-5 water channels. J Biol Chem 274:20071-20074. ... Several aquaporins (AQPs), which form water channels that selectively transport water across the plasma membrane, have been ... 2000) Persistent increase in the amount of aquaporin-5 in the apical plasma membrane of rat parotid acinar cells induced by a ...
Journal Article] Novel phosphorylation of aquaporin-5 at its threonine 259 through cAMP signaling in salivary gland cells.2011 ... Physiological roles ofpost-translational modifications of water channel aquaporin-5 in the salivary glands.. Research Project ... Two types of post-translational modifications, phosphorylation and short-chain ubiquitination, of water channel aquaporin-5 ( ... Presentation] 唾液腺細胞におけるアクアポリン 5 の翻訳後修2011. *. Author(s).
Aquaporins (AQPs) are important in controlling water permeability. As AQP1 is known as a serum-responsive gene, we hypothesized ... Expression of AQPs 1 and 5 was maintained even in metastatic lesions in the liver. These findings demonstrate that the ... By reverse transcriptase-polymerase chain reaction analysis, expression of AQPs 1, 3, and 5 was found in seven colon and ... In situ hybridization demonstrated that during colorectal carcinogenesis, the expression of AQPs 1 and 5 was induced in early- ...
14P - The effect of aquaporin-5 knockdown on HT29 colon cancer cell proliferation and migration. ... Aquaporins (AQPs) are a family of integral membrane proteins, known for their role in fluid homeostasis. Overexpression of AQP5 ... The effect of aquaporin-5 knockdown on HT29 colon cancer cell proliferation and migration ... Simultaneous knockdown of both AQP1 and 5 may in fact be needed for improved inhibition of colon cancer cellular proliferation ...
What is Aquaporin 5? Meaning of Aquaporin 5 medical term. What does Aquaporin 5 mean? ... Looking for online definition of Aquaporin 5 in the Medical Dictionary? Aquaporin 5 explanation free. ... aquaporin. (ak″wă-por′ĭn) [ aqua + porin] A cell membrane protein that lets water flow into and out of cells. ... aquaporin. (redirected from Aquaporin 5). Also found in: Dictionary.. Related to Aquaporin 5: Aquaporin 6 ...
Among the seven human aquaporins cloned to date(AQPs 0-6), genes encoding the four most closely related aquaporins(AQP0, AQP2, ... Aquaporin-5;AQP-5;AQP5;. Research Areas. ,signal transduction,metabolism,plasma membrane,channels, metabolism,types of disease, ... AQP5, and AQP6) have been mapped to chromosome band 12q13, suggesting an aquaporin family gene cluster at this locus. Aquaporin ... Background for Aquaporin-5(AQP-5). Aquaporin 5, also known as AQP5, is a water channel protein. The aquaporins(AQPs) are a ...
Rabbit Polyclonal Anti-Aquaporin-7 Antibody. Validated: WB, ICC/IF, IHC, IHC-Fr. Tested Reactivity: Human, Mouse, Porcine, and ... Aquaporin 7 and AQP3 are at the same chromosomal location suggesting that 9p13 may be a site of an aquaporin cluster. Aquaporin ... Aquaporin-7 Antibody Summary. Immunogen. A synthetic peptide from the n-terminal region of human Aquaporin 7 (AQP7) conjugated ... Blogs on Aquaporin-7. There are no specific blogs for Aquaporin-7, but you can read our latest blog posts. ...
Intra-assay Precision (Precision within an assay): 3 samples with low, middle and high level Aquaporin 5 (AQP5) were tested 20 ... Inter-assay Precision (Precision between assays): 3 samples with low, middle and high level Aquaporin 5 (AQP5) were tested on 3 ... This assay has high sensitivity and excellent specificity for detection of Aquaporin 5 (AQP5). ... No significant cross-reactivity or interference between Aquaporin 5 (AQP5) and analogues was observed. ...
Aquaporin 1 forms a water-specific channel that is constitutively expressed at the PLASMA MEMBRANE of ERYTHROCYTES and KIDNEY ... Aquaporin 1. Subscribe to New Research on Aquaporin 1 Aquaporin 1 forms a water-specific channel that is constitutively ... AQP-CHIP Protein; AQP1 Protein; Aquaporin 1 Protein; Aquaporin-CHIP; CHIP28 Protein; Channel-Forming Integral Membrane Protein ... "Effects of different fluid resuscitation regimes on lung injury and expression of pulmonary aquaporin 1 and aquaporin 5 in ...
Aquaporin-2 levels in vitro and in vivo are regulated by VACM-1, a cul 5 gene. , Cellular physiology and biochemistry : ... Aquaporin-2 levels in vitro and in vivo are regulated by VACM-1, a cul 5 gene. Isabelle P Le Sarah Schultz Bradley T Andresen ... Aquaporin-2 levels in vitro and in vivo are regulated by VACM-1, a cul 5 gene. Cell Physiol Biochem. 2012;30(5):1148-58. ... cAMP production and subsequent translocation of water channel aquaporin-2 (AQP2) into the apical plasma membrane. We have ...
Aquaporin zero (AQP0) is a water channel expressed almost exclusively in fiber cells of the lens of the eye. There is a long- ... 1) (5-8). Compelling evidence argues that this circulation is powered by the Na/K ATPase in the equatorial epithelial cells, ... The aquaporin zero puzzle.. @article{Hall2014TheAZ, title={The aquaporin zero puzzle.}, author={James Edwin Hall and Richard T ... The Role of Aquaporins in Ocular Lens Homeostasis. *Kevin L. Schey, Rosica S. Petrova, Romell B. Gletten, Paul James Donaldson ...
Aquaporin 5, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene ... Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). Aquaporin 5 ... The human Aquaporin-5 gene. Molecular characterization and chromosomal localization. (PMID: 8621489) Lee MD … Agre P (The ... AQP5 (Aquaporin 5) is a Protein Coding gene. Diseases associated with AQP5 include Palmoplantar Keratoderma, Bothnian Type and ...
Aquaporins (AQPs) facilitate the transepithelial water flow involved in epithelial fluid secretion in numerous tissues; however ... Aquaporins (AQPs) facilitate the transepithelial water flow involved in epithelial fluid secretion in numerous tissues; however ... Direito, I., Paulino, J., Vigia, E., Brito, M. A., and Soveral, G. (2017). Differential expression of aquaporin-3 and aquaporin ... 2002). Aquaporin 1 regulates GTP-induced rapid gating of water in secretory vesicles. Proc. Natl. Acad. Sci. U.S.A. 99, 4720- ...
Aquaporins in the kidney: from molecules to medicine. * Aquaporin-4 deletion in mice reduces brain edema after acute water ... Aquaporins in the kidney: from molecules to medicine.. *Aquaporin-4 deletion in mice reduces brain edema after acute water ... This Adenylate Cyclase 5 ELISA kit is validated to work with samples from whole blood, serum, plasma and cell culture ... 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 ...
  • Expression of aquaporin-5 (AQP5), studied by immunofluorescence and confocal microscopy, showed an increase in parallel with the increase in P f following hyperosmotic stress. (springer.com)
  • Aquaporin 5 (AQP5) is a water channel protein. (antibodies-online.com)
  • Findings show that overexpression of aquaporin 5 (AQP5 ) activated epithelial-mesenchymal transition ( EMT (show ITK Antibodies )) in colorectal cancer ( CRC (show CALR Antibodies )) cells. (antibodies-online.com)
  • Osmotic water permeabilities of aquaporins AQP4 (show AQP4 Antibodies ), AQP5 , and GlpF from near-equilibrium simulations have been presented. (antibodies-online.com)
  • By analogy to salivary and submucosal glands, where fluid secretion is aquaporin-5 (AQP5) dependent, we postulated that aquaporin water channels might facilitate sweat secretion. (nih.gov)
  • This may improve characterization of acute respiratory distress syndrome and ultimately facilitate individualized care.Background The aquaporin-5 (AQP5) -1364A/C promoter single-nucleotide polymorphism is associated with an alteredAQP5 expression and mortality in sepsis. (medworm.com)
  • Aquaporin 5 (AQP5) may be involved in NSCLC by promoting lung‑cancer initiation and progression. (spandidos-publications.com)
  • AQPs 1, 3, 4, 5, 8 and 9 were screened in the NSCLC cell line H1299, and the present results showed that AQP5 mRNA was upregulated compared with the other AQP genes. (spandidos-publications.com)
  • Aquaporin 5 antibody LS-C3809 is an unconjugated rabbit polyclonal antibody to Aquaporin 5 (AQP5) from human, mouse and rat. (lsbio.com)
  • The present study investigated the role of nitric oxide (NO)/cGMP signal transduction in the M 3 muscarinic acetylcholine receptor (mAChR)-stimulated increase in aquaporin-5 (AQP5) levels in the apical plasma membrane (APM) of rat parotid glands. (aspetjournals.org)
  • Pretreatment of rat parotid tissue with the NO scavenger 2-(4carboxyphenyl)-4,4,5,5-tetramethyl-imidazoline-1-oxyl-3-oxide potassium inhibited both acetylcholine (ACh)- and pilocarpine-induced increases in AQP5 in the APM. (aspetjournals.org)
  • A calmodulin kinase II inhibitor [(8)-5-isoquinolinesulfonic acid, 4-[2-(5-isoquinolinyl-sulfonyl)methylamino]-3-oxo-(4-phenyl-1-piperazinyl)-propyl]phenyl ester (KN-62)] decreased the pilocarpine-induced increase of AQP5 in the APM. (aspetjournals.org)
  • Pretreatment of the tissues with a myosin light chain kinase inhibitor [(5-chloronaphthalene-1-sulfonyl)-1H-hexahydro-1,4-diazepine (ML-9)] inhibited a mAChR-stimulated increase in AQP5 levels in the APM. (aspetjournals.org)
  • Two types of post-translational modifications, phosphorylation and short-chain ubiquitination, of water channel aquaporin-5 (AQP5) were investigated in the salivary gland cells. (nii.ac.jp)
  • Rabbit IgG polyclonal antibody for Aquaporin-5(AQP5) detection. (bosterbio.com)
  • Aquaporin 5, also known as AQP5, is a water channel protein. (bosterbio.com)
  • Among the seven human aquaporins cloned to date(AQPs 0-6), genes encoding the four most closely related aquaporins(AQP0, AQP2, AQP5, and AQP6) have been mapped to chromosome band 12q13, suggesting an aquaporin family gene cluster at this locus. (bosterbio.com)
  • This assay has high sensitivity and excellent specificity for detection of Aquaporin 5 (AQP5). (biotecnika.org)
  • No significant cross-reactivity or interference between Aquaporin 5 (AQP5) and analogues was observed. (biotecnika.org)
  • Intra-assay Precision (Precision within an assay): 3 samples with low, middle and high level Aquaporin 5 (AQP5) were tested 20 times on one plate, respectively. (biotecnika.org)
  • Inter-assay Precision (Precision between assays): 3 samples with low, middle and high level Aquaporin 5 (AQP5) were tested on 3 different plates, 8 replicates in each plate. (biotecnika.org)
  • AQP5 (Aquaporin 5) is a Protein Coding gene. (genecards.org)
  • Aquaporin-5 is a protein that in humans is encoded by the AQP5 gene. (wikipedia.org)
  • Human aquaporin 5 AQP5 is highly expressed in the respiratory system and secretory glands where it facilitates the osmotically-driven generation of pulmonary secretions, saliva, sweat and tears. (duhnnae.com)
  • 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. (arvojournals.org)
  • The aquaporin 5 ( AQP5) -1364A/C promoter single nucleotide polymorphism affects key mechanisms of inflammation and immune cell migration. (cdc.gov)
  • We analyzed the prognostic impact of aquaporin 5 (AQP5) in non-small lung cancer (NSCLC). (bvsalud.org)
  • [email protected]#To investigate the mechanism of cAMP-PKA signaling pathway mediated by Chinese medicine formula Shaoyao Gancao Decoction (, SGD) on the regulation of aquaporin 5 (AQP5) and muscarinic receptor 3 (M3R) levels in Sjögren's syndrome (SS). (bvsalud.org)
  • We assessed the distribution of aquaporin-5 (AQP5) in lacrimal gland biopsy samples. (jhu.edu)
  • Aquaporin 5 (Aqp5) is known to play a key role in salivary secretion, but the association between Aqp5 and the circadian rhythm is poorly understood. (deepdyve.com)
  • Water movement within the follicular wall is predominantly transcellular via membranous water channels named aquaporins (AQPs). (unboundmedicine.com)
  • The distribution and function of aquaporins (AQPs) have not previously been defined in sweat glands. (jhu.edu)
  • Several aquaporins (AQPs), which form water channels that selectively transport water across the plasma membrane, have been cloned from a variety of mammalian tissues ( King and Agre, 1996 ). (aspetjournals.org)
  • Aquaporins (AQPs) are important in controlling water permeability. (nature.com)
  • By reverse transcriptase-polymerase chain reaction analysis, expression of AQPs 1, 3, and 5 was found in seven colon and colorectal cancer cell lines. (nature.com)
  • In situ hybridization demonstrated that during colorectal carcinogenesis, the expression of AQPs 1 and 5 was induced in early-stage disease (early dysplasia) and maintained through the late stages of colon cancer development. (nature.com)
  • Expression of AQPs 1 and 5 was maintained even in metastatic lesions in the liver. (nature.com)
  • Of the five AQPs examined, AQPs 1, 3, and 5 were expressed in all the seven cell lines ( Figure 1a ). (nature.com)
  • Western blot analysis demonstrated that AQPs 1, 3, and 5 were expressed concurrently in all four of the tested cancer cell lines ( Figure 1b ), confirming our RT-PCR results. (nature.com)
  • Expression of AQPs 1, 3, and 5 in seven colon and colorectal cancer cell lines. (nature.com)
  • The aquaporins(AQPs) are a family of more than 10 homologous water transporting proteins expressed in many mammalian epithelia and endothelia. (bosterbio.com)
  • Aquaporins (AQPs) are integral membrane proteins that facilitate the transport of water across biological membranes along an osmotic gradient. (genecards.org)
  • Mammalian aquaporins (AQPs) are a family of at least 13 integral membrane proteins expressed in various epithelia, where they function as channels to permeate water and small solutes. (unicam.it)
  • The aquaporins (AQPs) are a family of water-transporting channels that are expressed widely in mammalian fluid-transporting epithelia and endothelia. (arvojournals.org)
  • 1 2 3 4 5 6 Because of this expression pattern, it has been proposed that AQPs play a role in intraocular pressure regulation, corneal and lens transparency, and vision. (arvojournals.org)
  • Cells expressing AQPs on their plasma membrane have an ~5- to 50-fold higher osmotic water permeability than membranes that do not ( Verkman and Mitra, 2000 ). (biologists.org)
  • Water channel proteins named aquaporins (AQPs) have been found in the cell membranes of these organisms. (hindawi.com)
  • Among 13 AQPs, AQP4 has a characteristic ultrastructural feature, since AQP4 can be identified by freeze-fracture (F-F) electron microscopy and can be seen as orthogonal arrays (OAs) in this method [ 4 , 5 ]. (hindawi.com)
  • The aquaporins (AQPs) are small integral membrane proteins that transport water and in some cases small solutes such as glycerol. (springer.com)
  • The eye contains numerous water channel proteins and the roles of AQPs (aquaporins) in the retina are blurred, especially under disease conditions. (portlandpress.com)
  • AQPs (aquaporins) are hydrophobic membrane proteins and the narrowest diameter of the pore of AQPs is 2.8 Å (1 Å=0.1 nm) [ 16 ]. (portlandpress.com)
  • To gain insight into the mechanisms underlying this estrogen-stimulated water transport, we have explored the expression profile and functionality of water channels termed aquaporins (AQPs) in the ovariectomized mouse uterus treated with ovarian steroid hormones. (bioone.org)
  • Aquaporins (AQPs) are integral membrane proteins that form pores in the membrane of biological cells. (cosmeticsandtoiletries.com)
  • Aquaporins (AQPs) belong to a transmembrane protein family of water channels that are permeable to water by the osmotic gradient. (chemweb.com)
  • The results suggest that hyperosmotic stress is an important activator of AQP-5 in human airway epithelium, leading to significantly increased transepithelial water permeability. (springer.com)
  • In vivo analysis of aquaporin 0 function in zebrafish: permeability regulation is required for lens transparency. (semanticscholar.org)
  • In the renal collecting duct, vasopressin regulates water permeability by a process that involves stimulation of adenylyl cyclase activity, cAMP production and subsequent translocation of water channel aquaporin-2 (AQP2) into the apical plasma membrane. (docphin.com)
  • [5] In the presence of PKC, AQP1 was reported to have increased aqueous permeability. (proteopedia.org)
  • Aquaporin-3 function is to promote glycerol permeability across cell membrane. (proteopedia.org)
  • Chou CL, Ma T, Yang B, Knepper MA, Verkman AS (1998) Fourfold reduction of water permeability in inner medullary collecting duct of aquaporin-4 knockout mice. (springer.com)
  • Chou CL, Knepper MA, Hoek AN, Brown D, Yang B, Ma T, Verkman AS (1999) Reduced water permeability and altered ultrastructure in thin descending limb of Henle in aquaporin-1 null mice. (springer.com)
  • Isolated perfused lungs from AQP-5-null mice show normal lung development but disrupted airspace-capillary osmotic permeability ( 7 ). (pubmedcentralcanada.ca)
  • There are currently no images for Aquaporin-7 Antibody (NBP1-30862). (novusbio.com)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Adenylate Cyclase 5 (ADCY5) in Tissue homogenates, cell lysates and other biological fluids. (aquaporins.org)
  • Arima H, Yamamoto N, Sobue K, Umenishi F, Tada T, Katsuya H, Asai K (2003) Hyperosmolar mannitol simulates expression of aquaporins 4 and 9 through a p38 mitogen-activated protein kinase-dependent pathway in rat astrocytes. (springer.com)
  • We characterized an aquaporin gene HvPIP2;5 from Hordeum vulgare and investigated its physiological roles in heterologous expression systems, yeast and Arabidopsis , under high salt and high osmotic stress conditions. (frontiersin.org)
  • In yeast, the expression of HvPIP2;5 enhanced abiotic stress tolerance under high salt and high osmotic conditions. (frontiersin.org)
  • Consistent with these stress tolerant phenotypes, HvPIP2;5 overexpressing Arabidopsis lines showed higher expression and activities of ROS scavenging enzymes such as catalase (CAT), superoxide dismutase (SOD), glutathione reductase (GR), and ascorbate peroxidase (APX) under salt and osmotic stresses than did WT. (frontiersin.org)
  • Together, these results suggested that HvPIP2;5 overexpression enhanced stress tolerance to high salt and high osmotic stresses by increasing activities and/or expression of ROS scavenging enzymes and osmoprotectant biosynthetic genes. (frontiersin.org)
  • TY - JOUR T1 - Effect of Prenatal and Neonatal Anti-Androgen Flutamide Treatment on Aquaporin 5 Expression in the Adult Porcine Ovary. (unboundmedicine.com)
  • Influence of saquinavir (SQV) plus methylprednisolone (MPS) on the expression of aquaporin 5 (AQP 5) in acute lung injury (ALI) model. (thefreedictionary.com)
  • Aquaporin 5 Gene Expression Was Increased in BD-MSCs Treated NOD Mice. (thefreedictionary.com)
  • These data suggest that increased gene expression of the water channel aquaporin 5 might be responsible for the increased tear production obtained following BD-MSC treatment. (thefreedictionary.com)
  • Immunocytochemistry showed strong aquaporin (AQP)-4 water channel expression in Müller cells in mouse retina and fibrous astrocytes in optic nerve. (arvojournals.org)
  • Immunohistochemical expression of P-selectin, SP-A, HSP70, aquaporin 5, and fibronectin in saltwater drowning and freshwater drowning. (unil.ch)
  • 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. (geneticsmr.com)
  • 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. (geneticsmr.com)
  • The aquaporin gene expression in salt-treated cucumber seedling leaves was considerably higher than that in leaves subjected to exogenous ALA. Further, the aquaporin expression levels in Jinchun No.4 were higher than those in Jinyou No.1, reaching 5.20- and 2-fold induction levels, respectively. (geneticsmr.com)
  • Bellemere G, Von Stetten O, Oddos T (2008) Retinoic acid increases aquaporin 3 expression in normal human skin. (springer.com)
  • Boury-Jamot M, Sougrat R, Tailhardat M, Le Varlet B, Bonte F, Dumas M, Verbavatz JM (2006) Expression and function of aquaporins in human skin: Is aquaporin-3 just a glycerol transporter? (springer.com)
  • A versatile aquaporin-2 cell system for quantitative temporal expression and live cell imaging. (nih.gov)
  • Protein expression and location of aquaporin (AQP)1, 5, 8 and 9 were assessed by immunohistochemistry, western blot and immunofluorescence respectively. (biomedcentral.com)
  • Boyle RT, Oliveira LF, Bianchini A, Souza MM (2013) The effects of copper on Na+/K+-ATPase and aquaporin expression in two euryhaline invertebrates. (springer.com)
  • Finally, HSP25 and HSP70i preserved expression of aquaporin 5, which is important for water transport in salivary glands. (eurekalert.org)
  • Aquaporin-1 (AQP1) was first discovered in human red blood cell membranes by Gheorghe Benga's research group in 1986. (proteopedia.org)
  • A limited number of aquaporins are found within the central nervous system (CNS): AQP1, 3, 4, 5, 8, 9, and 11, but more exclusive representation of AQP1, 4, and 9 are found in the brain and spinal cord. (wikipedia.org)
  • Aquaporin-1 (AQP1) passively transports water across the plasma membrane according to the osmotic gradient. (reactome.org)
  • Anti-Aquaporin 5, rabbit polyclonal, recognizes the ~28 kDa AQP 5 protein in epithelial tissue extracts. (emdmillipore.com)
  • Additionally we are shipping Aquaporin 5 Kits (45) and Aquaporin 5 Proteins (4) and many more products for this protein. (antibodies-online.com)
  • Aquaporins belong to major intrinsic proteins (MIPs) that are present from prokaryotes to plants and animals. (frontiersin.org)
  • Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). (genecards.org)
  • Here we define the cellular and subcellular sites of aquaporin (AQP) water transport proteins in human and rat eyes by immunoblotting, high-resolution immunocytochemistry, and immunoelectron microscopy. (elsevier.com)
  • Many organisms lacking a specific aquaporin have an unobtrusive phenotype, which suggests that aquaporins are unimportant or can be substituted by homolog proteins or compensatory mechanisms. (plantcell.org)
  • Aquaporins are integral membrane proteins that specialize in the regulation of cellular water flow across the cell membrane. (proteopedia.org)
  • Aquaporins are channel producing proteins which regulate the flow of water across the cell membrane. (proteopedia.org)
  • AQP4 belongs to the aquaporin family of integral membrane proteins that conduct water through the cell membrane. (wikipedia.org)
  • Aquaporins are water channel proteins that play a major role in the movement of water in various human tissues. (bvsalud.org)
  • Benga G (2009) Water channel proteins (later called aquaporins) and relatives: past, present, and future. (springer.com)
  • Aquaporins form a large, diverse family of proteins and have been found in bacteria, plants, and animals. (innovations-report.com)
  • Type I cells express a large number of proteins (reviewed in Reference 3 ), among them T1-α ( 6 ), aquaporin 5 (AQP-5) ( 7 ), functional ion channels ( 8 ), caveolins, adenosine receptors ( 9 ), and multidrug resistance genes. (pubmedcentralcanada.ca)
  • Bai C, Fukuda N, Song Y, Ma T, Matthay MA, Verkman AS (1999) Lung fluid transport in aquaporin-1 and aquaporin-4 knockout mice. (springer.com)
  • Examples are autoimmune responses, environmental exposures, and mutations in genes highly expressed by lung epithelium, including those mutations causing endoplasmic reticulum stress ( 5 ). (pnas.org)
  • Biopsy studies have revealed that there are correlations between density of inflammation and intensity of the diseases The effect of specific protein kinase A inhibitor H89 treatment reduced Aq 5 receptor expressions on the lung tissue. (uwi.edu)
  • In this study, we tested the effect of administering MSC directly into the airspaces of the lung 4 h after the intrapulmonary administration of Escherichia coli endotoxin (5 mg/kg). (jimmunol.org)
  • However, therapies applied using drugs directed to those molecules or related pathways have failed to significantly increase survival, especially in the most prevalent cancer types, for example, lung adenocarcinoma ( 3-5 ). (aacrjournals.org)
  • We also do not know if the in vitro reversibility of ATII to ATI transition ( 5 ) occurs in the mammalian lung. (pubmedcentralcanada.ca)
  • In vivo studies of acute lung injury and resolution of alveolar flooding in AQP-5-null mice show no role for it in this function ( 10 ). (pubmedcentralcanada.ca)
  • 500 nl min(-1) cm(-2) in kidney proximal tubules and salivary glands, where active fluid absorption or secretion is aquaporin dependent. (nih.gov)
  • Physiological roles ofpost-translational modifications of water channel aquaporin-5 in the salivary glands. (nii.ac.jp)
  • Aoki M (2003) Intestinal water absorption through aquaporin 1 expressed in the apical membrane of mucosal epithelial cells in seawater-adapted Japanese eel. (springer.com)
  • Extensive research on the function of aquaporins have been implemented into many separate types of cell membranes. (proteopedia.org)
  • Retinal Muller cells and astrocytes exhibit notable concentrations of AQP4, whereas neurons and retinal pigment epithelium do not display aquaporin immunolabeling. (elsevier.com)
  • In the mid nineties of the last century, the OAs turned out to be a water channel named aquaporin 4 (AQP4). (hindawi.com)
  • Aquaporin-4, also known as AQP4, is a water channel protein encoded by the AQP4 gene in humans. (wikipedia.org)
  • In the CNS, AQP4 is the most prevalent aquaporin channel, specifically located at the perimicrovessel astrocyte foot processes, glia limitans, and ependyma. (wikipedia.org)
  • The assembly of AQP4 monomers into tetramers is similar to other aquaporin channels. (wikipedia.org)
  • The 5′-untranslated region (5′-UTR) of M23A mRNA is encoded by four new exons (A, B, C, and D), which are located in the 5′ region from exon-0 of the AQP4 gene. (chemweb.com)
  • Hence, the discussion about the role of aquaporins in the majority of multicellular organisms remains open ( Chrispeels and Maurel, 1994 ). (plantcell.org)
  • Agren J, Zelenin S, Hakansson M, Eklof AC, Aperia A, Nejsum LN, Nielsen S, Sedin G (2003) Transepidermal water loss in developing rats: role of aquaporins in the immature skin. (springer.com)
  • Among its related pathways are Aquaporin-mediated transport and Nanog in Mammalian ESC Pluripotency . (genecards.org)
  • Indeed, overexpression of HvPIP2;5 caused higher retention of chlorophylls and water under salt and osmotic stresses than did control. (frontiersin.org)
  • These results suggest that HvPIP2;5 overexpression brought about stress tolerance, at least in part, by reducing the secondary oxidative stress caused by salt and osmotic stresses. (frontiersin.org)
  • The reduction of L(p) at 10°C in roots of wild-type plants was partly restored to the preexposure level by 5 mm Ca(NO(3))(2) and protein phosphatase inhibitors (75 nm okadaic acid or 1 μm Na(3)VO(4)), suggesting that aquaporin phosphorylation/dephosphorylation processes were involved in this response. (nih.gov)
  • Journal Article] Novel phosphorylation of aquaporin-5 at its threonine 259 through cAMP signaling in salivary gland cells. (nii.ac.jp)
  • Aquaporin 7 facilitates water, glycerol and urea transport. (novusbio.com)
  • A subgroup of aquaporins called aquaglycerporins allow the passage of small solutes such as glycerol, urea, and ammonia. (proteopedia.org)
  • The aquaporin Z channel protein in E. coli can accommodate a flow of water at rates six times higher than GlpF (aquaglyceroporin glycerol facilitator, a channel protein that transports both glycerol and water in E. coli) making it the prime subject for studying the selectivity of a high-conducting water channel. (innovations-report.com)
  • Electroretinograms were recorded over a 10 5 -fold range of flash intensities in dark-adapted mice and analyzed for a- and b-wave amplitude and latency, a-wave normalized slope, and oscillatory potential amplitude and latency. (arvojournals.org)
  • Mutations in aquaporin-0 in mice cause congenital cataracts. (proteopedia.org)
  • METHODS @#Of the 30 mice , 5 were randomly selected as control , and others were used for creating SS model. (bvsalud.org)
  • After successful modeling, mice were randomly divided into 5 groups (n=5 per group) and intragastrically administered with saline (8 mL/kg), pilocarpine (1.4 mg/kg), or low, medium and high doses SGD (0.14, 0.21, 0.35 g/kg Radix paeoniae with 0.01 g/kg Radix glycyrrhizae, respectively) for 6 weeks. (bvsalud.org)
  • Amiry-Moghaddam M, Williamson A, Palomba M, Eid T, de Lanerolle NC, Nagelhus EA, Adams ME, Froehner SC, Agre P, Ottersen OP (2003) Delayed K+ clearance associated with aquaporin-4 mislocalization: phenotypic defects in brains of alpha-syntrophin-null mice. (springer.com)
  • Binder DK, Oshio K, Ma T, Verkman AS, Manley GT (2004) Increased seizure threshold in mice lacking aquaporin-4 water channels. (springer.com)
  • Da T, Verkman AS (2004) Aquaporin-4 gene disruption in mice protects against impaired retinal function and cell death after ischemia. (springer.com)
  • Interestingly, AQP-5-null mice exhibit increased airway hyperresponsiveness, but this characteristic probably relates to AQP-5 absence in airway epithelium and not to ATI cells ( 11 ). (pubmedcentralcanada.ca)
  • Aquaporin zero (AQP0) is a water channel expressed almost exclusively in fiber cells of the lens of the eye. (semanticscholar.org)
  • We also observed lower accumulation of reactive oxygen species (ROS) and malondialdehyde (MDA), an end-product of lipid peroxidation in HvPIP2;5 overexpressing plants than in WT. (frontiersin.org)
  • With two structural models of aquaporins down to the atomic level in the same species, scientists can now begin to investigate the molecular mechanisms that facilitate their selectivity. (innovations-report.com)
  • The effects of low root temperature on growth and root cell water transport were compared between wild-type Arabidopsis (Arabidopsis thaliana) and plants overexpressing plasma membrane intrinsic protein 1;4 (PIP1;4) and PIP2;5. (nih.gov)
  • Descending root temperature from 25°C to 10°C quickly reduced cell hydraulic conductivity (L(p)) in wild-type plants but did not affect L(p) in plants overexpressing PIP1;4 and PIP2;5. (nih.gov)
  • Similarly, when the roots of wild-type plants were exposed to 10°C for 1 d, L(p) was lower compared with 25°C. However, there was no effect of low root temperature on L(p) in PIP1;4- and PIP2;5-overexpressing plants after 1 d of treatment. (nih.gov)
  • When the roots were exposed to 10°C for 5 d, L(p) was reduced in wild-type plants and in plants overexpressing PIP1;4, whereas there was still no effect in PIP2;5-overexpressing plants. (nih.gov)
  • These results suggest that the gating mechanism in PIP1;4 may be more sensitive to prolonged low temperature compared with PIP2;5. (nih.gov)
  • However, low root temperature had no effect on growth in plants overexpressing PIP2;5. (nih.gov)
  • Split-ubiquitin screening identified the PIP2;1 aquaporin as an interactor of the βCA4 carbonic anhydrase, which was confirmed in split luciferase, bimolecular fluorescence complementation, and coimmunoprecipitation experiments. (plantcell.org)
  • To explore the possibility underlying this biological process, we identified and characterized a mutant with a T-DNA insertion in PIP2;5 , which encodes an aquaporin with water channel activity in the PIP2 subfamily. (preprints.org)
  • The PIP2;5 protein was located in the cell plasma membrane and was preferentially expressed in the stigma. (preprints.org)
  • Based on our results, we concluded that PIP2;5 might play an important role in water movement during pollen hydration. (preprints.org)
  • Aquaporin, Aqy1 (PIP2-7 7). (tcdb.org)
  • These data could lead to a better understanding of aquaporin function not only at the cellular level but also in the whole plant. (plantcell.org)
  • Aquaporin membrane protein channels mediate cellular water flow. (duhnnae.com)
  • It seems intuitively obvious that plant water channels, aquaporins (AQP), ought to play a dynamic role in maintaining cellular water homeostasis under conditions that necessitate modifications in water flux. (plantphysiol.org)
  • Borgnia M, Nielsen S, Engel A, Agre P (1999) Cellular and molecular biology of the aquaporin, water channels. (springer.com)
  • And because the two main classes of aquaporins occur in E. coli--which means they're exposed to the same cellular environment--the opportunities for comparative structural and functional analyses, combined with site-directed mutagenesis, promise to provide valuable insights into the molecular underpinnings of the selectivity of functionally different aquaporins. (innovations-report.com)
  • Arabidopsis plants overexpressing HvPIP2;5 also showed better stress tolerance in germination and root growth under high salt and high osmotic stresses than the wild type (WT). (frontiersin.org)
  • In addition, the proline biosynthesis genes, Δ 1 -Pyrroline-5-Carboxylate Synthase 1 and 2 ( P5CS1 and P5CS2 ) were up-regulated in HvPIP2;5 overexpressing plants under salt and osmotic stresses, which coincided with increased levels of the osmoprotectant proline. (frontiersin.org)
  • Aquaporin protein regulation and redistribution in response to osmotic stress was investigated. (plantphysiol.org)
  • Akai M, Onai K, Morishita M et al (2012) Aquaporin AqpZ is involved in cell volume regulation and sensitivity to osmotic stress in Synechocystis sp. (springer.com)
  • Aquaporins/major intrinsic protein (MIP) are a family of water-selective membrane channels. (novusbio.com)
  • A synthetic peptide from the c-terminal region of human Aquaporin 5 conjugated to blue carrier protein was used as the antigen. (osenses.com)
  • Other performances that aquaporin-4 is involved in are synaptic plasticity, astrocyte migration, regulation of extracellular space volume, and the homeostasis of potassium. (wikipedia.org)
  • Here, I will summarize our current knowledge of the involvement of aquaporin-formed pores and tight junctions in epidermal water homeostasis - as well as in other functions - and their putative roles in skin dryness. (springer.com)
  • Known also as Adenylate Cyclase 5 elisa. (aquaporins.org)
  • Description: Quantitativesandwich ELISA kit for measuring Human Inosine-5'-monophosphate dehydrogenase 2 (IMPDH2) in samples from serum, plasma, cell culture supernates, tissue homogenates. (aquaporins.org)
  • Aquaporin 7 has greater sequence similarity with AQP3 and AQP9 and they may be a subfamily. (novusbio.com)
  • Aquaporin 7 and AQP3 are at the same chromosomal location suggesting that 9p13 may be a site of an aquaporin cluster. (novusbio.com)
  • Aquaporin-4 regulates water balance in the central nervous system. (proteopedia.org)
  • American Journal of Physiology - Cell Physiology , 274 (5 43-5), C1332-C1345. (elsevier.com)
  • Abdel-Sater KA (2018) Physiology of the aquaporins. (springer.com)
  • Kinetics of inositol 1,4,5-triphosphate and inositol cyclic 1:2,4,5-triphosphate metabolism in intact rat parotid acinar cells. (nii.ac.jp)
  • M 3 mAChRs trigger similar signal transduction pathways that involve the heterotrimeric G protein Gq-mediated activation of phospholipase C (PLC) - β , which results in the generation of inositol 1,4,5-trisphosphate (IP 3 ) and 1,2-diacylglycerol (DAG). (aspetjournals.org)
  • Agre P, Kozono D. Aquaporin water channels: molecular mechanisms for human diseases. (proteopedia.org)
  • Agre P (2006) The aquaporin water channels. (springer.com)
  • Agre went on to establish the family of related channels, which he named "aquaporins. (innovations-report.com)
  • These results provide strong evidence for a link between growth at low root temperature and aquaporin-mediated root water transport in Arabidopsis. (nih.gov)
  • Aquaporin 5 is a water-specific channel protein that is expressed primarily in alveolar, tracheal, and upper bronchial EPITHELIUM. (bioportfolio.com)
  • Since then, 12 other isoforms of aquaporin-1 have been discovered and each have been classified under the family known as Aquaporins. (proteopedia.org)
  • Robert Stroud and colleagues, as reported in this issue of PLoS Biology, have now solved the structure of the water channel from Escherichia coli called aquaporin Z. This channel is especially interesting in that it selectively conducts only water at high rates. (innovations-report.com)
  • A synthetic peptide from the n-terminal region of human Aquaporin 7 (AQP7) conjugated to an immunogenic carrier protein was used as the immunogen. (novusbio.com)
  • Recently, it has been found that aquaporins have influence in the carcinogenesis of human malignancies. (bvsalud.org)