Aquaporins: A class of porins that allow the passage of WATER and other small molecules across CELL MEMBRANES.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 5: 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 4: Aquaporin 4 is the major water-selective channel in the CENTRAL NERVOUS SYSTEM of mammals.Water: 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)Aquaporin 6: Aquaporin 6 is an aquaglyceroporin that is found primarily in KIDNEY COLLECTING DUCTS. AQP6 protein functions as an anion-selective channel.Aquaglyceroporins: A subgroup of aquaporins that transport WATER; GLYCEROL; and other small solutes across CELL MEMBRANES.Aquaporin 2: 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.Mercuric Chloride: 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.Osmosis: Tendency of fluids (e.g., water) to move from the less concentrated to the more concentrated side of a semipermeable membrane.Plant Transpiration: 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)Water-Electrolyte Balance: 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.Plant Proteins: Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.Permeability: Property of membranes and other structures to permit passage of light, heat, gases, liquids, metabolites, and mineral ions.Gold Compounds: Inorganic compounds that contain gold as an integral part of the molecule.Glycerol: 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.Kidney Concentrating Ability: The ability of the kidney to excrete in the urine high concentrations of solutes from the blood plasma.Mimosa: A plant genus of the family FABACEAE that contains kukulkanin, a CHALCONE.Juglans: A plant genus of the family JUGLANDACEAE that provides the familiar walnut.Biological Transport: 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.Cistaceae: 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.Plant Roots: 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)Tulipa: A plant genus of the family LILIACEAE. Members contain tuliposides and tulipalins and have been associated with allergic contact dermatitis in florists.Solidago: A plant genus of the family ASTERACEAE known for allergenic pollen (ALLERGENS).Cell Membrane Permeability: A quality of cell membranes which permits the passage of solvents and solutes into and out of cells.Blood Group Antigens: Sets of cell surface antigens located on BLOOD CELLS. They are usually membrane GLYCOPROTEINS or GLYCOLIPIDS that are antigenically distinguished by their carbohydrate moieties.Body Water: Fluids composed mainly of water found within the body.Mercury Compounds: Inorganic compounds that contain mercury as an integral part of the molecule.Gene Expression Regulation, Plant: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in plants.Trichomes: Hair-like extensions on specialized epidermal surfaces of plants which protect against damage from insects, animals, light degradation and fungal infection. Trichomes may also occur on certain unicellular EUKARYOTES.Calotropis: A plant genus of the family ASCLEPIADACEAE. The downy akund floss fiber from the seeds is used like kapok.Molecular Sequence Data: 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.Osmotic Pressure: 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.Sea Bream: A species of PERCIFORMES commonly used in saline aquaculture.Ejaculatory Ducts: Paired ducts in the human male through which semen is ejaculated into the urethra.Amino Acid Sequence: 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.4-Chloromercuribenzenesulfonate: A cytotoxic sulfhydryl reagent that inhibits several subcellular metabolic systems and is used as a tool in cellular physiology.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Ion Channels: 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.Plant Leaves: 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)Acoustic Maculae: The sensory areas on the vertical wall of the saccule and in the floor of the utricle. The hair cells in the maculae are innervated by fibers of the VESTIBULAR NERVE.Pulvinus: A group of cells at the base of a leaf in certain plants that, by rapidly losing water, brings about changes in the position of the leaves. (Concise Dictionary of Biology, 1990)Spinacia oleracea: A widely cultivated plant, native to Asia, having succulent, edible leaves eaten as a vegetable. (From American Heritage Dictionary, 1982)Plant Structures: The parts of plants, including SEEDS.Exocrine Glands: Glands of external secretion that release its secretions to the body's cavities, organs, or surface, through a duct.Polyuria: Urination of a large volume of urine with an increase in urinary frequency, commonly seen in diabetes (DIABETES MELLITUS; DIABETES INSIPIDUS).Tephritidae: A large family of fruit flies in the order DIPTERA, comprising over 4,500 species in about 100 genera. They have patterned wings and brightly colored bodies and are found predominantly in the tropical latitudes.Kidney Tubules, Collecting: 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.Dehydration: The condition that results from excessive loss of water from a living organism.Brain Edema: 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)Xenopus laevis: 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.Body Fluids: Liquid components of living organisms.

Reduced water permeability and altered ultrastructure in thin descending limb of Henle in aquaporin-1 null mice. (1/1459)

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

Lung fluid transport in aquaporin-1 and aquaporin-4 knockout mice. (2/1459)

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

Switch from an aquaporin to a glycerol channel by two amino acids substitution. (3/1459)

The MIP (major intrinsic protein) proteins constitute a channel family of currently 150 members that have been identified in cell membranes of organisms ranging from bacteria to man. Among these proteins, two functionally distinct subgroups are characterized: aquaporins that allow specific water transfer and glycerol channels that are involved in glycerol and small neutral solutes transport. Since the flow of small molecules across cell membranes is vital for every living organism, the study of such proteins is of particular interest. For instance, aquaporins located in kidney cell membranes are responsible for reabsorption of 150 liters of water/day in adult human. To understand the molecular mechanisms of solute transport specificity, we analyzed mutant aquaporins in which highly conserved residues have been substituted by amino acids located at the same positions in glycerol channels. Here, we show that substitution of a tyrosine and a tryptophan by a proline and a leucine, respectively, in the sixth transmembrane helix of an aquaporin leads to a switch in the selectivity of the channel, from water to glycerol.  (+info)

Modifications to rat lens major intrinsic protein in selenite-induced cataract. (4/1459)

PURPOSE: To identify modifications to rat lens major intrinsic protein (MIP) isolated from selenite-induced cataract and to determine whether m-calpain (EC 3.4.22.17) is responsible for cleavage of MIP during cataractogenesis. METHODS: Cataracts were induced in rats by a single injection of sodium selenite. Control and cataract lenses were harvested on day 16 and dissected into cortical and nuclear regions. Membranes were washed with urea buffer followed by NaOH. The protein was reduced/alkylated, delipidated, and cleaved with cyanogen bromide (CNBr). Cleavage products were fractionated by high-performance liquid chromatography (HPLC), and peptides were characterized by mass spectrometry and tandem mass spectrometry. MIP cleavage by m-calpain was carried out by incubation with purified enzyme, and peptides released from the membrane were analyzed by Edman sequencing. RESULTS: The intact C terminus, observed in the control nuclear and cataractous cortical membranes, was not observed in the cataractous nuclear membranes. Mass spectrometric analysis revealed heterogeneous cleavage of the C terminus of MIP in control and cataract nuclear regions. The major site of cleavage was between residues 238 and 239, corresponding to the major site of in vitro cleavage by m-calpain. However, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and mass spectrometric analysis indicated that in vivo proteolysis during cataract formation also included sites closer to the C terminus not produced by m-calpain in vitro. Evidence for heterogeneous N-terminal cleavage was also observed at low levels with no differences between control and cataractous lenses. The major site of phosphorylation was determined to be at serine 235. CONCLUSIONS: Specific sites of MIP N- and C-terminal cleavage in selenite-induced cataractous lenses were identified. The heterogeneous cleavage pattern observed suggests that m-calpain is not the sole enzyme involved in MIP C-terminal processing in rat lens nuclei.  (+info)

Transport of fluid by lens epithelium. (5/1459)

We report for the first time that cultured lens epithelial cell layers and rabbit lenses in vitro transport fluid. Layers of the alphaTN4 mouse cell line and bovine cell cultures were grown to confluence on permeable membrane inserts. Fluid movement across cultured layers and excised rabbit lenses was determined by volume clamp (37 degrees C). Cultured layers transported fluid from their basal to their apical sides against a pressure head of 3 cmH2O. Rates were (in microliter. h-1. cm-2) 3.3 +/- 0.3 for alphaTN4 cells (n = 27) and 4.7 +/- 1.0 for bovine layers (n = 6). Quinidine, a blocker of K+ channels, and p-chloromercuribenzenesulfonate and HgCl2, inhibitors of aquaporins, inhibited fluid transport. Rabbit lenses transported fluid from their anterior to their posterior sides against a 2.5-cmH2O pressure head at 10.3 +/- 0.62 microliter. h-1. lens-1 (n = 5) and along the same pressure head at 12.5 +/- 1.1 microliter. h-1. lens-1 (n = 6). We calculate that this flow could wash the lens extracellular space by convection about once every 2 h and therefore might contribute to lens homeostasis and transparency.  (+info)

Expression and localization of aquaporins in rat gastrointestinal tract. (6/1459)

A family of water-selective channels, aquaporins (AQP), has been demonstrated in various organs and tissues. However, the localization and expression of the AQP family members in the gastrointestinal tract have not been entirely elucidated. This study aimed to demonstrate the expression and distribution of several types of the AQP family and to speculate on their role in water transport in the rat gastrointestinal tract. By RNase protection assay, expression of AQP1-5 and AQP8 was examined in various portions through the gastrointestinal tract. AQP1 and AQP3 mRNAs were diffusely expressed from esophagus to colon, and their expression was relatively intense in the small intestine and colon. In contrast, AQP4 mRNA was selectively expressed in the stomach and small intestine and AQP8 mRNA in the jejunum and colon. Immunohistochemistry and in situ hybridization demonstrated cellular localization of these AQP in these portions. AQP1 was localized on endothelial cells of lymphatic vessels in the submucosa and lamina propria throughout the gastrointestinal tract. AQP3 was detected on the circumferential plasma membranes of stratified squamous epithelial cells in the esophagus and basolateral membranes of cardiac gland epithelia in the lower stomach and of surface columnar epithelia in the colon. However, AQP3 was not apparently detected in the small intestine. AQP4 was present on the basolateral membrane of the parietal cells in the lower stomach and selectively in the basolateral membranes of deep intestinal gland cells in the small intestine. AQP8 mRNA expression was demonstrated in the absorptive columnar epithelial cells of the jejunum and colon by in situ hybridization. These findings may indicate that water crosses the epithelial layer through these water channels, suggesting a possible role of the transcellular route for water intake or outlet in the gastrointestinal tract.  (+info)

Long-term regulation of aquaporins in the kidney. (7/1459)

The discovery of the aquaporin family of water channels has greatly improved our understanding of how water crosses epithelial cells, particularly in the kidney. The study of the mechanisms involved in the regulation of collecting duct water permeability, in particular, has advanced very rapidly since the identification and characterization of aquaporin-2 (AQP2) in 1993. One of the more surprising findings has been the dramatic long-term changes that are seen in the abundance of this protein, as well as the recognition that these changes represent a way of modulating the acute antidiuretic effects of vasopressin. Furthermore, such changes seem to be of etiological and pathological significance in a number of clinical disorders of water balance. This review focuses on the various conditions in which AQP2 expression is altered (either increased or decreased) and on what this can tell us about the signals and mechanisms controlling these changes. Ultimately, this may be of great value in the clinical management of water balance disorders. Evidence is also now beginning to emerge that there are similar changes in the expression of other renal aquaporins, which had previously been thought to provide an essentially constitutive water permeability pathway, suggesting that they too should be considered as regulatory factors in the control of body water balance.  (+info)

Physiology and pathophysiology of renal aquaporins. (8/1459)

The discovery of aquaporin membrane water channels by Agre and coworkers answered a long-standing biophysical question of how water specifically crosses biologic membranes, and provided insight, at the molecular level, into the fundamental physiology of water balance and the pathophysiology of water balance disorders. Of nine aquaporin isoforms, at least six are known to be present in the kidney at distinct sites along the nephron and collecting duct. Aquaporin-1 (AQP1) is extremely abundant in the proximal tubule and descending thin limb, where it appears to provide the chief route for proximal nephron water reabsorption. AQP2 is abundant in the collecting duct principal cells and is the chief target for vasopressin to regulate collecting duct water reabsorption. Acute regulation involves vasopressin-regulated trafficking of AQP2 between an intracellular reservoir and the apical plasma membrane. In addition, AQP2 is involved in chronic/adaptational regulation of body water balance achieved through regulation of AQP2 expression. Importantly, multiple studies have now identified a critical role of AQP2 in several inherited and acquired water balance disorders. This concerns inherited forms of nephrogenic diabetes insipidus and several, much more common acquired types of nephrogenic diabetes insipidus where AQP2 expression and/or targeting are affected. Conversely, AQP2 expression and targeting appear to be increased in some conditions with water retention such as pregnancy and congestive heart failure. AQP3 and AQP4 are basolateral water channels located in the kidney collecting duct, and AQP6 and AQP7 appear to be expressed at lower abundance at several sites including the proximal tubule. This review focuses mainly on the role of AQP2 in water balance regulation and in the pathophysiology of water balance disorders.  (+info)

*Aquaporin

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. In addition to the maintenance of normal cytosolic osmolarity, aquaporins can play a major role in extension growth ...

*Aquaporin 4

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 essential in the formation of memory as well as synaptic plasticity. Other performances that aquaporin-4 is ... "Aquaporin-4 autoimmune syndrome and anti-aquaporin-4 antibody-negative opticospinal multiple sclerosis in Japanese". Multiple ...

*Aquaporin 3

"Aquaporin-2 and -3: representatives of two subgroups of the aquaporin family colocalized in the kidney collecting duct". Annu. ... Aquaporin 3 is found in the basolateral cell membrane of principal collecting duct cells and provide a pathway for water to ... 2005). "Roles of aquaporin-3 water channels in volume-regulatory water flow in a human epithelial cell line". J. Membr. Biol. ... 2007). "Expression of aquaporin 3 in the human prostate". Int. J. Urol. 14 (12): 1088-92; discussion 1092. doi:10.1111/j.1442- ...

*Aquaporin 1

... at the US National Library of Medicine Medical Subject Headings (MeSH) Gallery of Aquaporin Simulations Human AQP1 ... The gene encoding this aquaporin is a possible candidate for disorders involving imbalance in ocular fluid movement. Aquaporin ... AQP1 aquaporin 1 (Colton blood group)". Knepper MA (1994). "The aquaporin family of molecular water channels". Proc. Natl. Acad ... Aquaporin 1 is a protein that in humans is encoded by the AQP1 gene. AQP1 is a widely expressed water channel, whose ...

*Aquaporin 2

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, ...

*Astrogliosis

Aquaporins. Handbook of Experimental Pharmacology. 190. pp. 159-70. doi:10.1007/978-3-540-79885-9_7. ISBN 978-3-540-79884-2. ... Zador, Zsolt; Stiver, Shirley; Wang, Vincent; Manley, Geoffrey T. (2009). "Role of Aquaporin-4 in Cerebral Edema and Stroke". ...

*Major intrinsic proteins

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 ...

*Tachyon (software)

"Water Permeation Through Aquaporins". Emad Tajkhorshid, Klaus Schulten, Theoretical and Computational Biophysics Group, ...

*Syndrome of inappropriate antidiuretic hormone secretion

... via activation of aquaporins, the site of the ADH receptors - back into the circulation. This has two consequences. First, in ... aquaporin 2), and their insertion into the cells' luminal membranes. Excessive ADH causes an inappropriate increase in the ... "Physiology and pathophysiology of renal aquaporins". Seminars in nephrology. 21 (3): 231-8. doi:10.1053/snep.2001.21647. PMID ... inherited mutations that cause aquaporins always to be "turned on"; and 6) miscellaneous largely transient conditions. ...

*Randy Wayne (biologist)

Am J Bot 84:1522-1529 Christophe Maurel (June 1997). "AQUAPORINS AND WATER PERMEABILITY OF PLANT MEMBRANES". Annual Review of ...

*Transmembrane channels

Aquaporins are dedicated channels for the movement of water across the hydrophobic interior of the cell membrane. Ion channels ... Verkman, A. (2011) Aquaporins at a Glance. Journal of Cell Science 24, 2107 - 2112. Roux, B., and Schulten, K. (2004). ...

*Marine life

Agre, P (2006). "The aquaporin water channels". Proceedings of the American Thoracic Society. 3 (1): 5-13. doi:10.1513/pats. ...

*Blastula

This movement of water is facilitated by aquaporins. A seal is created by tight junctions of the epithelial cells that line the ...

*Cation-chloride cotransporter

... aquaporins versus cotransporters". Biophysical Journal. 99 (11): 3647-3656. doi:10.1016/j.bpj.2010.10.021. ISSN 1542-0086. PMC ...

*Glymphatic system

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 ... Yool AJ (2007). "Aquaporins: multiple roles in the central nervous system". Neuroscientist. 13 (5): 470-85. doi:10.1177/ ...

*AQP5

Aquaporin-5 is a protein that in humans is encoded by the AQP5 gene. Aquaporin 5 (AQP5) is a water channel protein. Aquaporins ... "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- ... 2007). "Stimulation of aquaporin-5 and transepithelial water permeability in human airway epithelium by hyperosmotic stress". ...

*Neuromyelitis optica

Aquaporin 4 is found in the astrocytes that surround the blood-brain barrier (BBB), a system responsible for preventing ... In 2005 they identified the aquaporin 4 protein as the target of the disease, and developed a test to aid in the diagnosis of ... These antibodies target the protein aquaporin 4 in the cell membranes of astrocytes which acts as a channel for the transport ... Since the discovery of AQP-4 involvement, some research studies have focused on targeted treatment aimed at anti-aquaporin 4 ...

*AQP9

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 ... AQP9 aquaporin 9". Ishibashi K, Kuwahara M, Gu Y, et al. (1998). "Cloning and functional expression of a new aquaporin (AQP9) ... 2003). "Aquaporin-9 is expressed in a mucus-secreting goblet cell subset in the small intestine". FEBS Lett. 540 (1-3): 157-62 ...

*AQP7

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. ...

*AQP8

Aquaporin-8 is a protein that in humans is encoded by the AQP8 gene. Aquaporin 8 (AQP8) is a water channel protein. Aquaporins ... "Entrez Gene: AQP8 aquaporin 8". Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of ... 2007). "Aquaporin-8 expression is reduced in ileum and induced in colon of patients with ulcerative colitis". World J. ... Wang S, Chen J, Au KT, Ross MG (2003). "Expression of aquaporin 8 and its up-regulation by cyclic adenosine monophosphate in ...

*AQP6

The protein encoded by this gene is an aquaporin protein, which functions as a water channel in cells. Aquaporins are a family ... Ikeda M, Beitz E, Kozono D, Guggino WB, Agre P, Yasui M (Oct 2002). "Characterization of aquaporin-6 as a nitrate channel in ... Wang W, Hart PS, Piesco NP, Lu X, Gorry MC, Hart TC (Mar 2003). "Aquaporin expression in developing human teeth and selected ... Aquaporin 6, kidney specific is a protein in humans that is encoded by the AQP6 gene. ...

*Balo concentric sclerosis

Nov 2010). "Aquaporin-4 astrocytopathy in Baló's disease". Acta Neuropathol. 120 (5): 651-60. doi:10.1007/S00401-010-0733-7. ... Nevertheless, this model is questioned by recent reports that found astrocyte damage, similar to the one found in aquaporin- ...

*Heterotetramer

Examples include haemoglobin (pictured), the NMDA receptor, some aquaporins, some AMPA receptors, as well as some enzymes. Ion- ... "Heterotetrameric Composition of Aquaporin-4 Water Channels". Biochemistry. 38 (34): 11156-63. doi:10.1021/bi990941s. PMID ...

*Ralf Kaldenhoff

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 ...

*Aphid

A. J. Shakesby; I. S. Wallace; H. V. Isaacs; J. Pritchard; D. M. Roberts; A. E. Douglas (2009). "A water-specific aquaporin ...
plasma membrane intrinsic protein 2-7, PIP2;7, plasma membrane intrinsic protein 3, salt stress-induced major intrinsic protein, P93004, Q9ATM4 Plasma membrane aquaporin, PIP2;7 is water channel protein required for water transport across cell membrane
Background: Aquaporins are integral membrane proteins that facilitate the transport of water and small solutes across cell membranes. These proteins are vital for maintaining water homeostasis in living organisms. In mammals, thirteen aquaporins (AQP0-12) have been characterized, but in lower vertebrates, such as fish, the diversity, structure and substrate specificity of these membrane channel proteins are largely unknown. Results: The screening and isolation of transcripts from the zebrafish (Danio rerio) genome revealed eighteen sequences structurally related to the four subfamilies of tetrapod aquaporins, i.e., aquaporins (AQP0, -1 and -4), water and glycerol transporters or aquaglyceroporins (Glps; AQP3 and AQP7-10), a water and urea transporter (AQP8), and two unorthodox aquaporins (AQP11 and -12). Phylogenetic analyses of nucleotide and deduced amino acid sequences demonstrated dual paralogy between teleost and human aquaporins. Three of the duplicated zebrafish isoforms have unlinked ...
TY - JOUR. T1 - Expression and subcellular localization of aquaporin water channels in the polarized hepatocyte cell line, WIF-B. AU - Gradilone, Sergio A.. AU - Tietz, Pamela S.. AU - Splinter, Patrick L.. AU - Marinelli, Raúl A.. AU - LaRusso, Nicholas F.. PY - 2005/8/18. Y1 - 2005/8/18. N2 - Background: Recent data suggest that canalicular bile secretion involves selective expression and coordinated regulation of aquaporins (AQPs), a family of water channels proteins. In order to further characterize the role of AQPs in this process, an in vitro cell system with retained polarity and expression of AQPs and relevant solute transporters involved in bile formation is highly desirable. The WIF-B cell line is a highly differentiated and polarized rat hepatoma/human fibroblast hybrid, which forms abundant bile canalicular structures. This cell line has been reported to be a good in vitro model for studying hepatocyte polarity. Results: Using RT-PCR, immunoblotting and confocal immunofluorescence, ...
Purpose: The expression of aquaporin water channel genes are shown to be affected in several pathological conditions of retina, such as in diabetic retinopathy, retinal ischemia and in autoimmune uveitis. Human native retinal pigment epithelial (RPE) cells and immortalized human RPEs are formerly shown to express aquaporins, still the expression of aquaporins in stem cell derived RPE have not been previously elucidated. The objective of this study was to determine the expression of several aquaporin genes (aquaporin1,- 3, -4, -5, -6, -7, -10, -11 and -12) and assess the localization of aquaporin 1 water channel protein in human embryonic (hESCs) and induced pluripotent stem cells (hiPSCs) derived RPE cells.. Methods: hESC- and hiPSC derived RPE cells were grown as monolayer in serum-free media. The expression of aquaporin genes was determined with qRT-PCR. The localization of AQP1-protein was studied with confocal microscopy. Finally, the functionality of aquaporins was assessed with dye ...
Aquaporins are transmembrane water channel proteins present in biological plasma membranes that aid in biological water filtration processes by transporting water molecules through at high speeds, while selectively blocking out other kinds of solutes. Aquaporin Z incorporated biomimetic membranes are envisaged to overcome the problem of high pressure needed, and holds great potential for use in water purification processes, giving high flux while keeping energy consumption low. The functionality of aquaporin Z in terms of osmotic permeability might be regulated by factors such as pH, temperature, crosslinking and hydrophobic thickness of the reconstituted bilayers. Hence, we reconstituted aquaporin Z into vesicles that are made from a series of amphiphilic block copolymers PMOXA-PDMS-PMOXAs with various hydrophobic molecular weights. The osmotic permeability of aquaporin Z in these vesicles was determined through a stopped-flow spectroscopy. In addition, the temperature and pH value of the vesicle
Aquaporins are channel proteins that facilitate the transport of water across plant cell membranes. In this work, we used a combination of pharmacological and reverse genetic approaches to investigate the overall significance of aquaporins for tissue water conductivity in Arabidopsis (Arabidopsis thaliana). We addressed the function in roots and leaves of AtPIP1;2, one of the most abundantly expressed isoforms of the plasma membrane intrinsic protein family. At variance with the water transport phenotype previously described in AtPIP2;2 knockout mutants, disruption of AtPIP1;2 reduced by 20% to 30% the root hydrostatic hydraulic conductivity but did not modify osmotic root water transport. These results document qualitatively distinct functions of different PIP isoforms in root water uptake. The hydraulic conductivity of excised rosettes (Kros) was measured by a novel pressure chamber technique. Exposure of Arabidopsis plants to darkness increased Kros by up to 90%. Mercury and azide, two ...
Aquaporin-5 is a protein that in humans is encoded by the AQP5 gene. Aquaporin 5 (AQP5) is a water channel protein. Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). Aquaporin 5 plays a role in the generation of saliva, tears and pulmonary secretions. AQP0, AQP2, AQP5, and AQP6 are closely related and all map to 12q13. Aquaporin GRCh38: Ensembl release 89: ENSG00000161798 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000044217 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse PubMed Reference:". Lee MD, Bhakta KY, Raina S, Yonescu R, Griffin CA, Copeland NG, Gilbert DJ, Jenkins NA, Preston GM, Agre P (Jun 1996). "The human Aquaporin-5 gene. Molecular characterization and chromosomal localization". J Biol Chem. 271 (15): 8599-604. doi:10.1074/jbc.271.15.8599. PMID 8621489. "Entrez Gene: AQP5 aquaporin 5". Verkman AS (2003). "Role of aquaporin water channels in eye function". Exp. Eye Res. 76 (2): 137-43. ...
Plant cells contain proteins that are members of the major intrinsic protein (MIP) family, an ancient family of membrane channel proteins characterized by six membrane-spanning domains and two asparagine-proline-alanine (NPA) amino acid motifs in the two halves of the protein. We recently demonstrated that [gamma]-TIP, one of the MIP homologs found in the vacuolar membrane of plant cells, is an aquaporin or water channel protein (C. Maurel, J. Reizer, J.I. Schroeder, M.J. Chrispeels [1993] EMBO J 12: 2241-2247). RD28, another MIP homolog in Arabidopsis thaliana, was first identified as being encoded by a turgor-responsive transcript. To find out if RD28 is a water channel protein, rd28 cRNA was injected into Xenopus laevis oocytes. Expression of RD28 caused a 10- to 15-fold increase in the osmotic water permeability of the oocytes, indicating that the protein creates water channels in the plasma membrane of the oocytes and is an aquaporin just like its homolog [gamma]-TIP. Although RD28 has ...
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 ...
The pre-ovulatory hydration of the oocyte of marine teleosts, a unique process among vertebrates that occurs concomitantly with meiosis resumption (oocyte maturation), is a critical process for the correct development and survival of the embryo. Increasing information is available on the molecular mechanisms that control oocyte maturation in fish, but the identification of the cellular processes involved in oocyte hydration has remained long ignored. During the past few years, a number of studies have identified the major inorganic and organic osmolytes that create a transient intra-oocytic osmotic potential for hydrating the oocytes, whereas water influx was believed to occur passively. Recent work, however, has uncovered the role of a novel molecular water channel (aquaporin), designated aquaporin-1b (Aqp1b), which facilitates water permeation and resultant swelling of the oocyte. The Aqp1b belongs to a teleost-specific subfamily of water-selective aquaporins, similar to mammalian aquaporin-1 ...
Tonoplast intrinsic proteins (TIPs) facilitate the membrane transport of water and other small molecules across the plant vacuolar membrane, and members of this family are expressed in specific developmental stages and tissue types. Delivery of TIP proteins to the tonoplast is thought to occur by vesicle-mediated traffic from the endoplasmic reticulum to the vacuole, and at least two pathways have been proposed, one that is Golgi-dependent and another that is Golgi-independent. However, the mechanisms for trafficking of vacuolar membrane proteins to the tonoplast remain poorly understood. Here we describe a chemical genetic approach to unravel the mechanisms of TIP protein targeting to the vacuole in Arabidopsis seedlings. We show that members of the TIP family are targeted to the vacuole via at least two distinct pathways, and we characterize the bioactivity of a novel inhibitor that can differentiate between them. We demonstrate that, unlike for TIP1;1, trafficking of markers for TIP3;1 and TIP2;1 is
Structural data on AQPs, together with mutagenesis and molecular dynamics simulations, have indicated that single-file transport occurs through a narrow pore in each monomer, where water selectivity is conferred by electrostatic and steric factors (Hub et al., 2009; Khalali-Araghi et al., 2009). Glycerol-transporting AQPs, called aquaglyceroporins, have a less-constricted pore compared with that of water-selective AQPs (diameter of 3.4 Å compared with 2.8 Å, respectively), with relatively more hydrophobic residues lining the pore.. Many mammalian AQPs, including AQP1, AQP2, AQP4, AQP5 and AQP8, function primarily as bidirectional water-selective transporters. Cells expressing AQPs on their plasma membrane have an ~5- to 50-fold higher osmotic water permeability than membranes that do not (Verkman and Mitra, 2000). Water transport through single-file pores poses a biophysical limitation on the efficiency with which AQPs can transport water, so that AQPs must be present in the membrane at a high ...
Significant progress in the understanding of imaging conditions and the interpretation of topographs recorded with the AFM has allowed the surface topography of bacteriorhodopsin to be correlated with the helixconnecting loops to a lateral resolution of 5 Å (Müller et al., 1999b). Here we have used this technology to study the surface of AqpZ, the first bacterial water channel identified (Calamita et al., 1995). Its overexpression, isolation and 2D crystallization have recently been described (Borgnia et al., 1999; Ringler et al., 1999).. 2D crystals adsorbed firmly and without folds or wrinkles to freshly cleaved mica in a high ionic strength buffer (Müller et al., 1997). Subsequent change to a buffer adjusted to compensate for van der Waals interactions allowed their height to be measured accurately (Müller and Engel, 1997). The result, 57 ± 4 Å, compares favorably with the height previously reported for AQP1, 58 ± 3 Å (Walz et al., 1996).. The p4212 crystals of AqpZ with unit cell ...
Aquaporins (AQPs) are membrane proteins that enable water transport across cellular plasma membranes in response to osmotic gradients. Phenotypic analyses have revealed important physiological roles for AQPs, and the potential for AQP water channel modulators in various disease states has been proposed. For example, AQP1 is overexpressed in tumor microvessels, and this correlates with higher metastatic potential and aggressiveness of the malignancy. Chemical modulators would help in identifying the precise contribution of water channel activity in these disease states. These inhibitors would also be important therapeutically, e.g., in anti-cancer treatment. This perceived importance contrasts with the lack of success of high-throughput screens (HTS) to identify effective and specific inhibitors of aquaporins. In this paper, we have screened a library of 1500
Aquaporin 8 (AQP8) is a water channel protein. Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). Aquaporin 8 mRNA is found in pancreas and colon but not other tissues. [provided by RefSeq, Jul 2008 ...
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
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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 ...
The localization and transporting properties of a kidney protein homologous to human erythrocyte protein CHIP28 was evaluated. The cDNA encoding rat kidney protein CHIP28k was isolated from a rat renal cortex cDNA library. A 2.8-kb cDNA was identified which contained an 807 bp open reading frame encoding a 28.8 kD protein with 94% amino acid identity to CHIP28. in vitro translation of CHIP28k cDNA in rabbit reticulocyte lysate generated a 28-kD protein; addition of ER-derived microsomes gave a 32-kD transmembrane glycoprotein. Translation of truncated RNA demonstrated glycosylation of residue Asn42 which is predicted to lie between the first and second transmembrane domains. Expression of in vitro transcribed mRNA encoding CHIP28k in Xenopus oocytes increased oocyte osmotic water permeability (Pf) from (4 +/- 1) x 10(-4) to (33 +/- 4) x 10(-4) cm/s at 10 degrees C; the increase in oocyte Pf was weakly temperature dependent and inhibited by HgCl2. Two-electrode voltage clamp measurements ...
Described is a paving method of fine water-permeable concrete which can be used for roadways, sidewalks, bikeways, parking lots, public squares, etc. A base layer of water-permeable concrete is paved
TY - JOUR. T1 - Aquaporins and the respiratory system. T2 - Advice for a lung investigator. AU - King, Landon S.. AU - Nielsen, Søren. AU - Agre, Peter. PY - 2000/1. Y1 - 2000/1. UR - http://www.scopus.com/inward/record.url?scp=0033986166&partnerID=8YFLogxK. UR - http://www.scopus.com/inward/citedby.url?scp=0033986166&partnerID=8YFLogxK. M3 - Article. C2 - 10619856. AN - SCOPUS:0033986166. VL - 105. SP - 15. EP - 16. JO - Journal of Clinical Investigation. JF - Journal of Clinical Investigation. SN - 0021-9738. IS - 1. ER - ...
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
Using computer simulations and experimental results, researchers at the University of Illinois at Urbana-Champaign and the University of Arizona have identified a key component of the gating mechanism in aquaporins that controls ...
For a proper functioning of epithelial cells, a polarized sorting and localization of channels and transporters that mediate transcellular ion and water movement is essential. Our work focuses on elucidating the routing regulation of wild-type AQP2/V2R, dissolving the underlying mechanisms for missorting of AQP2 mutants, and the identification of pharmacological chaperones, rescuing the cell surface expression of AQP2/V2R mutants in NDI.
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. ...
Buena vista" hypothesis suggests that changes in the sizes of eyes, rather than a shift from fins to limbs, led fish to transition to land more than 300 million years ago. 1 Comment. ...
Background Water channel required to promote glycerol permeability and water transport across cell membranes. May contribute to water transport in the upper portion of small intestine. Isoform 2 is not permeable to urea and...
Rabbit polyclonal antibody raised against recombinant Rat Aqp4. Recombinant protein corresponding to Rat Aqp4 C-terminus. (PAB28902) - Products - Abnova
Two previous articles in this series on aquaporins have discussed their history, mechanism and stimulation. The current article describes the role of AQP3 in regulating skin cell growth.
PH, Water, Oocytes, Xenopus, Human, Membrane, Permeability, Proteins, Family, Transient, Acidosis, Plasma, Rat, Antibodies, Aquaporins, Gene, Genes, Membrane Proteins, Blood, Cells
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mqrrddpaar MSRSSGRSGS MDPSGAHPSV RQTPSRQPPL PHRSRGGGGG SRGGARASPA TQPPPLLPPS ATGPDATVGG PAPTPLLPPS ATasvkmepe nkylpelmae kdsldpsfth amqlltaeie kiqkgdskkd deenyldlfs hknmklkerv lipvkqypkf nfvgkilgpq gntikrlqee tgakisvlgk gsmrdkakee elrkgGDPKY ahlnmdlhvf ievfgppcea yalmahamee vkkflvpdmm ddicqeqfle lsylNGVPEP SRGRGVPVRG RGAAPPPPPV PRGRGVGPPR GALVRGtpvr gaitrgATVT RGVPPPPTVR GAPAprarta GIQRIPLPPP PAPETYEEyg yddtyaeqsy egyegYYSQS QGDSEYYDYG hgevqdsyea YGQDDWNGTR PSLKAPPARP VKGayrehpy ...
MGSNKSKPKD asqrrrslep aENVHGAGGG AFPASQTPSK PASADGHRGP SAAfapaaae pKLFGGFNSS DTVTSPQRAG PLAggvttfv alydyesrte tdlsfkkger lqivnntegd wwlahslsTG QTGYIPSNYV apsdsiqaee wyfgkitrre serlllnaen prgtflvres ettkgaycls vsdfdnakgl nvkhykirkl dsggfyitsr tqfnslqqlv ayyskhadgl chrlttVCPT SKPQtqglak daweipresl rlevklgqgc fgevwmgtwn gttrvaiktl kpgtmspeaf lqeaqvmkkl rheklvqlya vvseepiyiv teymskgsll dflkgetgky lrlpqlvdma aqiasgmayv ermnyvhrdl raanilvgen lvckvadfgl arliedneyt arqgakfpik wtapeaalyg rftiksdvws fgillteltt kgrvpypgmv nrevldqver gYRMPCPPEC PESlhdlmcq cwrkepeerp tfeylqafle dyftstepqy ...
Barnacles are sessile macro-invertebrates, found along rocky shores in coastal areas worldwide. The euryhaline bay barnacle Balanus improvisus (Darwin, 1854) (= Amphibalanus improvisus) can tolerate a wide range of salinities, but the molecular mechanisms underlying the osmoregulatory capacity of this truly brackish species are not well understood. Aquaporins are pore-forming integral membrane proteins that facilitate transport of water, small solutes and ions through cellular membranes, and that have been shown to be important for osmoregulation in many organisms. The knowledge of the function of aquaporins in crustaceans is, however, limited and nothing is known about them in barnacles. We here present the repertoire of aquaporins from a thecostracan crustacean, the barnacle B. improvisus, based on genome and transcriptome sequencing. Our analyses reveal that B. improvisus contains eight genes for aquaporins. Phylogenetic analysis showed that they represented members of the classical water ...
The Brazil flavored and functional water market is expected to rise from a valuation of US$5.0 bn to reach US$9.4 bn by 2024, expanding at a 7.3% CAGR therein.. Vitamins and Minerals Widely Used Ingredients in Flavored and Functional Water. In 2015, the vitamins and minerals segment accounted for a share of around 90% in terms of volume. Exhibiting a 7.1% CAGR by volume, the segment is also projected to emerge as one of the most lucrative investment options for players in the Brazil flavored and functional water market. Based on the nature of flavored and functional water, non-carbonated beverages are likely to retain their dominance in the market, registering a high growth rate in terms of value as well as volume.. Make an Enquiry @ http://www.transparencymarketresearch.com/sample/sample.php?flag=S&rep_id=16133. On the basis of distribution channel, the retail store segment is expected to lead the Brazil flavored and functional water market throughout the forecast period, with e-commerce ...
The Brazil flavored and functional water market is expected to rise from a valuation of US$5.0 bn to reach US$9.4 bn by 2024, expanding at a 7.3% CAGR therein.. Vitamins and Minerals Widely Used Ingredients in Flavored and Functional Water. In 2015, the vitamins and minerals segment accounted for a share of around 90% in terms of volume. Exhibiting a 7.1% CAGR by volume, the segment is also projected to emerge as one of the most lucrative investment options for players in the Brazil flavored and functional water market. Based on the nature of flavored and functional water, non-carbonated beverages are likely to retain their dominance in the market, registering a high growth rate in terms of value as well as volume.. Make an Enquiry @ http://www.transparencymarketresearch.com/sample/sample.php?flag=S&rep_id=16133. On the basis of distribution channel, the retail store segment is expected to lead the Brazil flavored and functional water market throughout the forecast period, with e-commerce ...
Aquaporins are a family of water channel proteins that provide a major pathway for osmotically driven water transport through cell membranes. So far, 13 aquaporin isoforms (AQP0-AQP12) have been identified in mammalian species (Verkman, 2005). AQP4, the predominant isoform in adult brain, is primarily expressed at the border between brain parenchyma and major fluid compartments, including astrocyte foot processes and glia limitans, as well as ependymal cells and subependymal astrocytes (Venero et al., 2001). The bidirectional water channel AQP4 has an important role in water homeostasis in the brain. It probably helps in the redistribution and absorption of edema fluid, because disruption of AQP4 is found to contribute to the pathophysiology of brain edema (Zador et al., 2007). AQP4 knockout markedly reduced brain swelling in mouse models of cytotoxic brain edema, whereas it significantly worsened outcome in mouse models of vasogenic brain edema (Papadopoulos and Verkman, 2007). Thus, AQP4 ...
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
According to recent reports, millions of people across the globe are suffering from arsenic (As) toxicity. Arsenic is present in different oxidative states in the environment and enters in the food chain through soil and water. In the agricultural field, irrigation with arsenic contaminated water, that is, having a higher level of arsenic contamination on the top soil, which may affects the quality of crop production. The major crop like rice (Oryza sativa L.) requires a considerable amount of water to complete its lifecycle. Rice plants potentially accumulate arsenic, particularly inorganic arsenic (iAs) from the field, in different body parts including grains. Different transporters have been reported in assisting the accumulation of arsenic in plant cells; for example, arsenate (AsV) is absorbed with the help of phosphate transporters, and arsenite (AsIII) through nodulin 26-like intrinsic protein (NIP) by the silicon transport pathway and plasma membrane intrinsic protein aquaporins. Researchers and
In plant sexual reproduction, water and solute movement are tightly regulated, suggesting the involvement of aquaporins. We previously identified TIP5;1 and TIP1;3 as the only Arabidopsis aquaporin genes that are selectively and highly expressed in mature pollen, and showed that they can transport both water and urea when expressed in Xenopus oocytes. Here, we show that TIP5;1 has unusual characteristics, as its water transport activity is regulated by pH. Analysis of the water transport activity of a mutant version of TIP5;1 (TIP5;1-H131A) and amino acid alignment with other plant aquaporins regulated by pH suggested that a conserved motif is involved in pH sensing. GFP-TIP5;1 is located in the mitochondria of pollen tubes. The single mutants tip1;3 and tip5;1, as well as the tip1;3 tip5;1 double mutant, are fertile, but all mutants had shorter than normal pollen tubes when germinated in vitro in the absence of exogenous nitrogen. Thus, we propose that TIP5;1 and TIP1;3 are involved in nitrogen ...
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
Mitochondrial swelling assay (PTP opening) - posted in Cell Biology: Hello.Anyone here with experience with the mitochondrial swelling assay for the measurement of the opening of the permeability transition pore? Im using the method that evaluates the decrease in absorbance at 540 nm. Im working with a fungus and theres nothing in the literature about this. I get a weird profile (see attachment).1) the temporal dynamics are quite different from what is ob...
The methylotrophic yeast P. pastoris has, during the last decades, increased in popularity as a eukaryotic host for recombinant protein expression [7]. Numerous reports have described successful overexpression of soluble proteins as well as of membrane proteins in this system, but sufficient protein yields have not always been obtained. Several methods have been described that could be used to improve the outcome of expression trials, among which an optimisation of recombinant gene dosage has proven to be one of the most potent ones [21]. When it comes to the aquaporin family of membrane proteins, optimisation of the nucleotide sequence both regarding codon composition and AT content [38] and controlled growth in bioreactors [36] have been reported to improve the yields of heterologous protein. However, in no reports has a systematic examination of the effect of gene dosage on recombinant aquaporin expression in P. pastoris been done and results obtained for other membrane proteins [12, 15, 33] ...
Sucrose as a product of photosynthesis is the major carbohydrate translocated from photosynthetic leaves to growing nonphotosynthetic organs such as roots and seeds. These growing tissues, besides carbohydrate supply, require uptake of water through aquaporins to enhance cell expansion during growth. Previous work revealed Sucrose Induced Receptor Kinase, SIRK1, to control aquaporin activity via phosphorylation in response to external sucrose stimulation. Here, we present the regulatory role of AT3G02880 (QSK1), a receptor kinase with a short external domain, in modulation of SIRK1 activity. Our results suggest that SIRK1 autophosphorylates at Ser-744 after sucrose treatment. Autophosphorylated SIRK1 then interacts with and transphosphorylates QSK1 and QSK2. Upon interaction with QSK1, SIRK1 phosphorylates aquaporins at their regulatory C-terminal phosphorylation sites. Consequently, in root protoplast swelling assays, the qsk1qsk2 mutant showed reduced water influx rates under iso-osmotic ...
The figure at the left displays the protein interaction network for human AQP2(red dot in center) as generated using STRING (4). Below is a pie chart depicting the biological processes that the proteins identified in this network are involved in. The ontologies of these interactors were visualized using PANTHER (5). The most dominant functional categories of the interacting proteins are involvement in cellular processes(including signal transduction), localization(including transport), multicellular organism processes, and biological regulation. One result of note is the inclusion of several other aquaporins within this network, including AQP1, AQP3, and AQP4. This opens the possibility for some overlap in coregulation of these different aquaporins ...
Vasopressin is the key regulator of water homeostasis in vertebrates. Central to its antidiuretic action in mammals is the redistribution of the water channel aquaporin 2 (AQP2) from intracellular vesicles to the apical membrane of kidney epithelial cells, an event initiated by an increase in cAMP and activation of protein kinase A. The subsequent steps of the signaling cascade are not known. To identify proteins involved in the AQP2 shuttle we exploited a recently developed cell line (CD8) derived from the rabbit cortical collecting duct and stably transfected with rat AQP2 cDNA. Treatment of CD8 cells with pertussis toxin (PTX) inhibited both the vasopressin-induced increase in water permeability and the redistribution of AQP2 from an intracellular compartment to the apical membrane. ADP-ribosylation studies revealed the presence of at least two major PTX substrates. Correspondingly, two alpha subunits of PTX-sensitive G proteins, Galphai2 and Galphai3, were identified by Western blotting.
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 ...
We are interested in basic and translational studies looking at the effects of environmental exposures, including cigarette smoke and electronic cigarettes, on lung epithelial function. We are focused on mechanisms to reverse injury to promote lung health, primarily in the context of Chronic Obstructive Pulmonary Disease (COPD).. Research Areas: pulmonary medicine, epithelial cells, biology, aquaporins ...
Abe H, Urao T, Ito T, Seki M, Shinozaki K, Yamaguchi-Shinozaki K. 2003. Arabidopsis AtMYC2 (bHLH) and AtMYB2 (MYB) function as transcriptional activators in abscisic acid signaling. The Plant Cell 15, 63-78.[Abstract/Free Full Text] Abebe T, Guenzi AC, Martin B, Chushman JC. 2003. Tolerance of mannitol-accumulating transgenic wheat to water stress and salinity. Plant Physiology 131, 1748-1755.[Abstract/Free Full Text] Aharon R, Shahak Y, Wininger S, Bendov R, Kapulnik Y, Galili G. 2003. Overexpression of a plasma membrane aquaporin in transgenic tobacco improves plant vigor under favorable growth conditions but not under drought or salt stress. The Plant Cell 15, 439-447.[Abstract/Free Full Text] Allen J. 1993. Control of gene expression by redox potential and the requirement for chloroplast and mitochondrial genomes. Journal of Theoretical Biology 165, 609-631.[CrossRef][ISI][Medline] Alpert P, Oliver MJ. 2002. Drying without dying. In: Black M, Pritchard HW, eds. Desiccation and survival in ...
If the solute concentration in the blood is too high, osmoreceptors in the hypothalamus sense this and signal the pituitary gland to produce a hormone called ADH (anti-diuretic hormone). ADH causes special pores called aquaporins in the collecting duct to open, allowing water to be reabsorbed back into the blood, thus making the blood more dilute. If the solute concentration in the blood is too low, osmoreceptors in the hypothalamus sense this and signal the pituitary gland to reduce its production of ADH. This causes the aquaporins in the collecting duct to close, keeping the excess water in the filtrate, which excreted as dilute urine. This is called osmoregulation ...
The collecting duct principle cells (PC) play a major role for concentration of urine and regulation of K+ homeostasis. Two water channels, AQP3 and AQP4, are expressed in the PC basolateral membrane (BLM). Here we present evidence that AQP4 participates in regulation of renal K+ transport. K+ enters the cell via Na+,K+-ATPase mediated transport in BLM. The presence of K+ channels in BLM, which is deeply infolded, thus providing a diffusion limited space, permits K+ recirculation, considered important for maintenance of membrane potential. Here we show with co-immunoprecipitation and GST pulldown assays, that in rat renal papilla, AQP4, but not AQP3, assembles with Na+,K+-ATPase and the K+ channel Kir7.1. This led us to hypothesize that AQP4, Na+,K+-ATPase and Kir7.1 form a K+ transporting microdomain, where AQP4 water transport maintains a favorable gradient for K+ efflux and stabilizes membrane potential. A mathematical model of K+ transport across an epithelial cells with a deeply infolded ...
Question 5: ________ (alcohol) acts as an antagonist for AVP in the collecting ducts of the kidneys, which prevents aquaporins from binding to the collecting ducts, and prevents water reabsorption. ...
Rabbit polyclonal antibody raised against recombinant Rat Aqp1. Recombinant protein corresponding to Aqp1 N-terminus. (PAB28844) - Products - Abnova
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Vīrusveidīgo daļiņu, jeb t.s. VLP (virus-like particles) proteīnu inženierijas idejas pieteikšana un tās pamatu izveidošana (kopā ar E. Grēnu). Vīrusu proteīnu imunoloģisko epitopu kartēšana (kopā ar P. Puško un I. Sominsku). Proteīnu inženierijas VLP vektoru, jeb nesēju, radīšana; himēro VLP konstruēšana uz to pamata. HBcAg izveidošana par universālu VLP nesēju - tradicionālāko himēro VLP struktūru pamatu; svešu epitopu iebūvēšana HBcAg struktūrā - no HIV, HBV, HCV, FMDV un daudziem citiem vīrusu un nevīrusu izcelsmes proteīniem (kopā ar G. Borisovu, I. Sominsku, A. Dišleru, I. Petrovski, A. Kazāku, K. Sasnausku, R. Ulrichu, H. Meiseli u. c.). HBcAg telpiskās struktūras atšifrēšana (kopā ar R. A. Krovčeru (R. A. Crowther), N. Kiseļevu, E. Grēnu u. c.). HBcAg pakojošo īpašību atšifrēšana un izmantošana (kopā ar M. Bahmanu (M. Bachmann) un A.Kazāku). HBcAg imunoloģisko īpašību atšifrēšana (kopā ar R. M. Cinkernāgelu (R. M. ...
Vīrusveidīgo daļiņu, jeb t.s. VLP (virus-like particles) proteīnu inženierijas idejas pieteikšana un tās pamatu izveidošana (kopā ar E. Grēnu). Vīrusu proteīnu imunoloģisko epitopu kartēšana (kopā ar P. Puško un I. Sominsku). Proteīnu inženierijas VLP vektoru, jeb nesēju, radīšana; himēro VLP konstruēšana uz to pamata. HBcAg izveidošana par universālu VLP nesēju - tradicionālāko himēro VLP struktūru pamatu; svešu epitopu iebūvēšana HBcAg struktūrā - no HIV, HBV, HCV, FMDV un daudziem citiem vīrusu un nevīrusu izcelsmes proteīniem (kopā ar G. Borisovu, I. Sominsku, A. Dišleru, I. Petrovski, A. Kazāku, K. Sasnausku, R. Ulrichu, H. Meiseli u. c.). HBcAg telpiskās struktūras atšifrēšana (kopā ar R. A. Krovčeru (R. A. Crowther), N. Kiseļevu, E. Grēnu u. c.). HBcAg pakojošo īpašību atšifrēšana un izmantošana (kopā ar M. Bahmanu (M. Bachmann) un A.Kazāku). HBcAg imunoloģisko īpašību atšifrēšana (kopā ar R. M. Cinkernāgelu (R. M. ...
Endoplasmic reticulum Small and Basic Intrinsic Protein; (SIP1;1) water channel (present in all plant tissues except seeds) (Ishikawa et al., 2005) May play a role in gas and water exchange between the plant and its environment via stromata (turgor-driven epidermal valves) and the hydathode pore (Pillitteri et al., 2008 ...
The relation between the expressed amounts and conferred water permeabilities of AQP2-S256D-F. Of oocytes, injected with 0.1, 0.2, 0.3, or 0.4 ng of AQP2-S256D-
BACKGROUND: Plant leaf movements can be mediated by specialized motor organs, the pulvini, or can be epinastic (i.e. based on different growth velocities of the adaxial and abaxial halves of the leaf). Both processes are associated with diurnally regulated increases in rates of membrane water transport, which in many cases has been shown to be facilitated by aquaporins. Rhythmic leaf movements are known from many plant species, but few papers deal with the involvement of aquaporins in such movements. SCOPE: Many details of the architecture and function of pulvini were worked out by Ruth Satter and co-workers using Samanea saman as a model organism. More recently a contribution of aquaporins to pulvinar movement in Samanea was demonstrated. Another model plant to study pulvinus-mediated leaf movements is Mimosa pudica. The contribution of both plasma membrane- and tonoplast-localized aquaporins to the seismonastic leaf movements in Mimosa was analysed. In tobacco, as an example of epinastic leaf ...
Aquaporins and ABC transporters were the major transporters identified in our study. ABC transporters are known to transport fatty acids that are required for proper cuticle development in leaves [45]. The cuticle plays an important role in maintaining the structural integrity of salt glands. Under saline conditions, it becomes important for the salt glands to form a thick cuticular layer to prevent water loss and also diffusion of ions into neighbouring cells [6]. The observed high level of expression of ABC transporters in the salt gland-rich tissue could explain this in Avicennia salt gland cells. Aquaporins are known to regulate water movement across the membranes. During drought and salt exposure, aquaporins are known to maintain water balance in the cells [46] and have been shown to play a crucial role in salt secretion of A. officinalis [9]. Although aquaporins have been identified from the leaves of other salt secretors [41], its precise function in regulating water movement during ...
Water deficit (WD) is a growing problem in agriculture. In citrus crops, genetically-determined characteristics of the rootstock are important factors in plant responses to WD. Aquaporins are involved in regulating the water supply to the plant by mediating water flow through the cell membranes. Recent studies support a direct role for aquaporins in plant water relations and demonstrate their involvement in tolerance to WD. This study investigates the relationship between photosynthetic and water-balance parameters with levels of expression of aquaporins in conditions of moderate WD in the rootstocks Poncirus trifoliata (L.) Raf. (PT), Cleopatra Mandarin (Citrus reshni Hort. ex Tan.) (CM) and 030115 (a hybrid of the two former rootstocks). Under conditions of WD, the hybrid 030115 drastically reduced aquaporin expression, accompanied by a loss of plant vigour but without reducing the net CO2 assimilation (ACO2). PT maintained the same level of aquaporin expression under WD as under normal ...
Water excretion by the kidney is regulated by the peptide hormone vasopressin. Vasopressin increases the water permeability of the renal collecting duct cells, allowing more water to be reabsorbed from collecting duct urine to blood. Despite long-standing interest in this process, the mechanism of the water permeability increase has remained undetermined. Recently, a molecular water channel (AQP-CD) has been cloned whose expression appears to be limited to the collecting duct. Previously, we immunolocalized this water channel to the apical plasma membrane (APM) and to intracellular vesicles (IVs) of collecting duct cells. Here, we test the hypothesis that vasopressin increases cellular water permeability by inducing exocytosis of AQP-CD-laden vesicles, transferring water channels from IVs to APM. Rat collecting ducts were perfused in vitro to determine water permeability and subcellular distribution of AQP-CD in the same tubules. The collecting ducts were fixed for immunoelectron microscopy ...
Peter Agre discovered the first aquaporin in 1992 in red blood cells and was awarded the 2003 Nobel Prize. Since then, 13 variants of aquaporin have been found in animals and humans and 35 in plants. There are thousands of these aquaporins in every cell membrane. Aquaporins contain a conduit that is so tiny that only a single water molecule at a time can pass through it. But this traffic can be lively indeed. In one second, several billion water molecules can get through. The direction of this water flow is contingent on the osmotic pressure. The water moves in a direction away from a low and toward a high concentration of salt and nutritional substances. But the conduit isnt always open. The Lund scientists have found out how it opens and closes. This was done in collaboration with a team at Chalmers University of Technology in Göteborg, Sweden, under the direction of Richard Neutze, and with Emad Tajkhorshid at the University of Illinois ...
In starvation, glycerol is released from adipose tissue and serves as an important precursor for hepatic gluconeogenesis. By unknown gender-specific mechanisms, women suppress the endogenous glucose production better than men and respond to metabolic stress with higher plasma glycerol levels. Hepatic glycerol uptake is facilitated by aquaporin-9 (AQP9), a broad-selectivity neutral solute channel, and represents an insulin-regulated step in supplying gluconeogenesis with glycerol. In the current study, hepatic AQP9 abundance was increased 2.6-fold in starved male rats as assessed by immunoblotting and immunohistochemistry. By contrast, starvation had no significant effect on hepatic AQP9 expression in female rats. Coordinately, plasma glycerol levels remained unchanged upon starvation in male rats whereas it was increased in female rats. The different responses to starvation were paralleled by higher glycerol permeability in basolateral hepatocyte membranes from starved male rats as compared to ...
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.
Advanced hypothyroidism to the clinical stage of myxedema is associated with hyponatremia involving both the nonosmotic release of AVP and diminished GFR (1,13-15). These events, which impair urinary dilution in advanced hypothyroidism, override the defect in urinary concentrating capacity, which also has been observed with hypothyroidism (1,2). In the present study, a model of moderate hypothyroidism was investigated in which neither hyponatremia nor a diminished GFR occurred, but a reversible decrease in maximal urine concentration was observed. With the use of molecular probes, it was possible to examine the perturbations in transporters and aquaporins that are involved in this hypothyroid-related defect in urinary concentration.. In the present study, the cardiac hemodynamics characteristic of hypothyroidism were demonstrated, including a decrease in cardiac output, heart rate, and left ventricular fraction of shortening as examined by echocardiography. Perturbations in these hemodynamic ...
Aquaporins facilitate osmotically driven water movement across cell membranes. Aquaporin 4 (AQP4) is a major water channel in the central nervous system where it participates in cerebral water balance. AQP4 is also present in basolateral membranes of lower respiratory tract airway and renal collecting duct epithelial cells, gastric parietal cells and skeletal muscle cells. However, the distribution of AQP4 in many other tissues is still unknown. The aim of this study was to determine the expression and relative abundance of AQP4 in human Tissue MicroArrays (TMAs) and human protein microarrays by immunohistochemistry and chemiluminescence. In the central nervous system AQP4 was abundantly expressed in the cerebral cortex, cerebellar cortex (purkinje/granular layer), ependymal cell layer, hippocampus and spinal cord. Lower levels were detected in choroid plexus, white matter and meninges. In the musculoskeletal system AQP4 was highly expressed in the sarcolemma of skeletal muscle from the chest ...
Two aquaporins have been detected in the crystalline lens. AQP1 is confined to the mitotic epithelial cell layer that lines the anterior surface (14), whereas AQP0 is characteristic of the terminally differentiated fiber cells (33) that constitute the bulk of the lens mass. Although AQP1 is at least 10-fold more active as a water channel than its fiber cell counterpart (23), no spontaneous lens pathology has been associated with AQP1 deficiency in humans (25) or mice (20). In this study, we have shown that AQP0 accounts for ∼80% of the water permeability of mouse lens fiber cell plasma membranes and that heterozygous loss of this MIP is sufficient to compromise lens transparency. These observations suggest that although the lens can compensate for loss of AQP1 function, there is no such redundancy for AQP0 deficiency.. The relative loss of water permeability recorded in Aqp0+/− mouse lenses was similar in magnitude to that measured in the kidney proximal tubules of Aqp1+/− mice (20). This ...
The ability of eukaryotic cells to change their shape and to migrate directionally is highly dependent on active volume regulation in cells building up tissues as well as in individual cells. Transmembrane fluxes of water via specialized water channels, called aquaporins (AQPs), facilitate the changes of volume and shape, which additionally require a complex interplay between the plasma membrane and the cytoskeleton. AQPs have been shown to be involved in the development of inflammatory processes and diseases. The aims of the studies underlying this thesis were to further elucidate the expression and function of AQPs in both bacterial and viral infections as well as in the inflammatory disease, microscopic colitis. For this, molecular techniques qPCR, immunoblotting and live, holographic, confocal and super-resolution imaging were used.. When cells of the innate immune system encounter pathogens they need to respond and prepare for migration and phagocytosis and do so through volume regulatory ...
While synthetic chemists have produced sophisticated architectures able to confine water clusters, most water channel based work is being conducted with natural protein channels as selectivity components, embedded in the diverse arrays of bio-assisted artificial systems. Such systems combine natural proteins that present high water conductance states under natural conditions with artificial lipidic or polymeric matrices. Experimental results have demonstrated that natural biomolecules can be used as bio-assisted building blocks for the construction of highly selective water transport through artificial channels. A next step is the design and construction of simpler compounds that maintain the high conduction activity obtained with natural compounds, leading to fully synthetic artificial biomimetic channels. Such studies aim to use constitutional artificial desalination membranes for highly selective water transport ...
While synthetic chemists have produced sophisticated architectures able to confine water clusters, most water channel based work is being conducted with natural protein channels as selectivity components, embedded in the diverse arrays of bio-assisted artificial systems. Such systems combine natural proteins that present high water conductance states under natural conditions with artificial lipidic or polymeric matrices. Experimental results have demonstrated that natural biomolecules can be used as bio-assisted building blocks for the construction of highly selective water transport through artificial channels. A next step is the design and construction of simpler compounds that maintain the high conduction activity obtained with natural compounds, leading to fully synthetic artificial biomimetic channels. Such studies aim to use constitutional artificial desalination membranes for highly selective water transport ...
It is well-known that the rapid now of water into and out of cells is controlled by membrane proteins called aquaporins (AQPs). However, the mechanisms that allow cells to quickly respond to a changing osmotic environment are less well established. Using GFP-AQP fusion proteins expressed in HEK293 cells, we demonstrate the reversible manipulation of cellular trafficking of AQP1. AQP1 trafficking was mediated by the tonicity of the cell environment in a specific PKC- and microtubule-dependent manner. This suggests that the increased level of water transport following osmotic change may be due it phosphorylation-dependent increase in the level of AQP1 trafficking resulting in membrane localization.. ...
Homeostasis of the central nervous system (CNS) microenvironment is essential for its normal function and is maintained by the blood-brain barrier (BBB). The BBB proper is made up of endothelial cells (ECs) interconnected by tight junctions (TJs) that reveal a unique morphology and biochemical composition of the bodys vasculature. In this article, we focus on developmental aspects of the BBB and describe morphological as well as molecular special features of the neuro-vascular unit (NVU) involved in barrier induction. Recently, we and others identified the Wnt/b-catenin pathway as crucial for brain angiogenesis, TJ and BBB formation. Based on these findings we discuss other pathways and molecular interactions for BBB establishment and maintenance. At the morphological level, our concept favors a major role for polarized astrocytes (ACs) therein. Orthogonal arrays of particles (OAPs) that are the morphological correlate of the water channel protein aquaporin-4 (AQP4) are specifically formed in the
PDB 2B6O, EMDB 2973 - 1.9Å resolutuion electron crystallography structure of the water channel Aquaporin-0 in its closed state. ...
Background Several aquaporins (a family of integral membrane proteins) have been recently identified in the mammalian gastrointestinal tract, and their involvement in the movement of fluid and small...
The genome of PCC 6803 contains a single gene encoding an aquaporin, remains ambiguous. the cells along with decreased PSII activity at ENX-1 pH figures ranging from 7.5 to 8.5. A mutant in mutant, lacking a putative glucose-sensing kinase, both showed higher glucose level of sensitivity Olaparib than the cells. Exam of protein appearance indicated that functioned as a positive regulator of gene appearance but not as the only regulator. Overall, the cells showed problems in macronutrient rate of metabolism, pH homeostasis, and cell division under photomixotrophic conditions, consistent with an essential part of AqpZ in glucose rate of metabolism. sp. PCC 6803 (henceforth referred to as have not been identified, although microarray tests possess recognized a list of genes caused by hyperosmotic stress in both the crazy type (WT) and a strain (5). Moreover, loss of aquaporins in organisms in general does not result in growth problems under a range of environmental conditions (6). Hence, the query ...
Anti-Aquaporin 3 Antibody (#AQP-003) from Alomone Labs is a highly specific rabbit polyclonal Ab directed against an epitope of rat AQP3. Applications: IFC, IHC, IP, WB. Free samples available. Control antigen included. Lyophilized. Global shipping at room temperature. Your top supplier for aquaporin research!
EGFR-mediated expression of aquaporin-3 is involved in human skin fibroblast migration: AQP3 (aquaporin-3), known as an integral membrane channel in epidermal k
Sigma-Aldrich offers abstracts and full-text articles by [C A Ecelbarger, J Terris, G Frindt, M Echevarria, D Marples, S Nielsen, M A Knepper].
Small, uncharged polar molecules and small nonpolar molecules, such as N2, freely pass across the membrane. Hydrophilic substances such as large polar molecules and ions move across the membrane through embedded channel and transport proteins. Water moves across membranes and through channel proteins called aquaporins. ...
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SWISS-MODEL Template Library (SMTL) entry for 1lda. CRYSTAL STRUCTURE OF THE E. COLI GLYCEROL FACILITATOR (GLPF) WITHOUT SUBSTRATE GLYCEROL
I just got a new Betta. He is in a 15 gallon Column tank. (Tall) it came with a filter but after reading a little bit about Bettas I am wondering if I should leave it on there. Is it true that Bettas need very little water movement? Will the HOB filter cause too much water disturbance for him?
PhD Project - Permeable Pavement Engineering for Water Movement in Road Structures and Drainage Effects at University of Greenwich, listed on FindAPhD.com
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folio Ff. 1 3 (first section) Vellum. 21 x 14 cms. Ff. 1 and 2 are stitched together with a thong; a fragment bearing traces of script intervenes. 1 r1. Hand 1. On the constellations. Beg. Fiarfaighter and so ca lin rann fuil annsan aer. With twelve illustrations symbolising signs of zodiac. Ed. Anderson, RC 30, p. 404. Auc , 3r (hand ?21); A Muire , 3v (hand 8). Ff. 4 19 (second section) Vellum. 20 x 14 cms. Two gatherings of bifolia (ff. 4 11, 12 19). As indicated by binder s marks (see table) the correct order of folios is 6, 7, 5, 4, 11, 10, 8, 9; 14, 15, 12, 19, 16, 17; 13, 18 i.e., two gatherings and an isolated bifolium. Ff. 6r, and to a lesser extent 17v and 18v, have suffered above average friction and staining through serving as outside covers. 4 r1. See 6r1. 6 r1. 0Hand 2 begins. On the four humours. Beg. Composisiones sunt quator 7c. ado(n) o do labrumur dona coimplex ib don taib tuas dinn labrum annois dona lennaib 7 ar tus dib go generalta 7 ainnsen go spisialta. Correct order of ...
Cell differentiation occurs when one cell changes into another type of cell. In animals, this usually happens at an early stage of development and occurs to create specialised cells. In mature animal cells, differentiation is mostly restricted to replacement and repair. Many plant cells, however, maintain the ability to differentiate .. Here are some of the specialised cells:. Root hair cells - tiny-hair like extensions increase the surface area of the cell for absorption.. Ovum (egg cell) - large cell that can carry food reserves for the developing embryo.. Xylem - long, thin, hollow cells used to transport water through the stem and root.. Sperm cell - has a tail which allows it to move.. Nerve cell - has long, slender axons that carry nerve impulses.. ...
Aqp4 - Aqp4 (untagged) - Mouse aquaporin 4 (cDNA clone MGC:37514 IMAGE:4985265), (10ug) available for purchase from OriGene - Your Gene Company.
This is a replacement MIP X-DUTY Drive Hub, and is intended for use with the MIP X-DUTY CVD kit for the Traxxas Slash and Slash 4x4. This replacement... MIP10136
In the kidney, the antidiuretic hormone vasopressin (AVP) is a critical regulator of water homeostasis by controlling the water movement from lumen to the interstitium for water reabsorption and adjusting the urinary water excretion. In normal physiology, AVP is secreted into the circulation by the posterior pituitary gland, in response to an increase in serum osmolality or a decrease in effective circulating volume. When reaching the kidney, AVP binds to V2 receptors on the basolateral surface of the collecting duct epithelium, triggering a G-protein-linked signaling cascade, which leads to water channel aquaporin-2 (AQP2) vesicle insertion into the apical plasma membrane. This results in higher water permeability in the collecting duct and, driven by an osmotic gradient, pro-urinary water then passes the membrane through AQP2 and leaves the cell on the basolateral side via AQP3 and AQP4 water channels, which are constitutively expressed on the basolateral side of these cells. When isotonicity ...
Aims/objectives: Glycerol cycling plays an essential regulatory role in metabolism in both health and disease. Aquaporins (AQPs) are a recently described family of water transporting membrane proteins, which contain a subset of members that also have the ability to transport glycerol across the cell membrane. This study sought to investigate the adipose tissue expression profile of AQPs in humans, and to assess the role of AQPs in adipocyte differentiation.. Methods: AQP expression was assessed in ex vivo human adipose tissue samples and isolated human adipocytes. Mouse 3T3 L1 and human SGBS cells were also used for expression and differentiation studies. SYBR Green real-time PCR and Western Blotting were used to detect mRNA and protein expression respectively.. Results: AQP 3 and 7 were expressed in omental adipose tissue at a significantly higher level than in corresponding subcutaneous adipose tissue samples. AQP 7 was the most abundantly expressed aquaporin in both depots. In differentiating ...
Our results identify a water channel protein as the first defined autoantigen pertinent to an inflammatory demyelinating disorder of the human CNS. AQP4 is an integral protein of astrocytic plasma membranes (15-18), and is highly concentrated in foot process domains facing microvessels where it interacts with dystrophin-associated proteins (10, 17). The AQP4 channel is mercurial-insensitive, and is the predominant water channel in the CNS. It has a pathophysiologic role in brain edema formation following water intoxication (14, 19, 20) or focal cerebral ischemia (21). Brain edema occurring in oncologic contexts is attributed to the up-regulation of AQP4 in high-grade astrocytomas and in reactive astrocytes related to cerebral adenocarcinoma metastases (21, 22).. The present study is the first to implicate AQP4 in the pathogenesis of any autoimmune disorder. NMO may represent the first example of a novel class of autoimmune channelopathies. Unlike MS, the cerebrospinal fluid in patients who have ...
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 ...
My dissertation work has focused on identifying regulatory mechanisms that govern Cyclic Guanosine Monophosphate (cGMP)-activation of Aquaprorin-1 (Aqp1) ion channels. Aquaporins serve as pores for water thus allowing enhanced water permeability in biological membranes (Preston, et al., 1992). A subset of Aquaporin proteins behave as ion channels regulated by intracellular signaling pathways (Anthony, et al., 2000; Ehring, et al., 1990; Yasui, et al., 1999a). cGMP is necessary for Aqp1 ion channel activation, but only a small subpopulation of Aqp1 proteins function as cGMP-activated ion channels . This observation indicates the involvement of additional regulatory mechanisms in the gating Aqp1 ion channels. Work from this dissertation provides the first insight into the potential mechanism that dictates Aqp1 ion channel availability to respond to the cGMP signal. I show here that insulin-activated tyrosine kinases positively regulate cGMP-mediated activation of Aqp1 ion channels when expressed ...
Despite his impressive credentials and success in his field, Agre is expected to tell students that a career in science was not a given for him when he was their age - particularly after he withdrew from a high school chemistry class rather than accept a grade of D. "But my life in science did come to fruition, and it had many influences," Agre said. "My experience underscores the importance of education and building relationships.". Agres address will begin at 12:30 p.m. in the UTD Activities Center, the only venue on campus large enough to handle the expected crowd. Students from Dallas, Richardson, Coppell, Plano, Garland and other local communities will attend. The students will arrive on campus around noon, and will be given a t-shirt and a box lunch.. At 10 a.m. the following day, Tuesday, May 9, Agre will speak in the Kusch Auditorium to UTD faculty, staff and students and interested members of the public on the subject of aquaporin water channels. He received the Nobel Prize for his ...
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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 ...
The effect of ethylene and its precursor ACC on root hydraulic properties, including aquaporin expression and abundance, is modulated by relative air humidity and plant sensitivity to ethylene. Relative air humidity (RH) is a main factor contributing to water balance in plants. Ethylene (ET) is known to be involved in the regulation of root water uptake and stomatal opening although its role on plant water balance under different RH is not very well understood. We studied, at the physiological, hormonal and molecular levels (aquaporins expression, abundance and phosphorylation state), the plant responses to exogenous 1-aminocyclopropane-1-carboxylic acid (ACC; precursor of ET) and 2-aminoisobutyric acid (AIB; inhibitor of ET biosynthesis), after 24 h of application to the roots of tomato wild type (WT) plants and its ET-insensitive never ripe (nr) mutant, at two RH levels: regular (50%) and close to saturation RH ...
We generated fusions between three Arabidopsis (Arabidopsis thaliana) tonoplast intrinsic proteins (TIPs; alpha-, gamma-, and delta-TIP) and yellow fluorescent protein (YFP). We also produced soluble reporters consisting of the monomeric red fluorescent protein (RFP) and either the C-terminal vacuolar sorting signal of phaseolin or the sequence-specific sorting signal of proricin. In transgenic Arabidopsis leaves, mature roots, and root tips, all TIP fusions localized to the tonoplast of the central vacuole and both of the lumenal RFP reporters were found within TIP-delimited vacuoles. In embryos from developing, mature, and germinating seeds, all three TIPs localized to the tonoplast of protein storage vacuoles. To determine the temporal TIP expression patterns and to rule out mistargeting due to overexpression, we generated plants expressing YFP fused to the complete genomic sequences of the three TIP isoforms. In transgenic Arabidopsis, gamma-TIP expression was limited to vegetative tissues, ...
Fresh water scarcity is one of the problems that the whole world is facing today. Forward osmosis and low pressure reverse osmosis are possible solutions to provide high quality water. Thus, creating a robust and highly permeable yet selective membrane for water purification has gained much attention worldwide in recent years. This thesis presents a systematic study on the design and fabrication of AquaporinZ (AqpZ)-embedded biomimetic membrane. Firstly, the mechanical property of the artificial AqpZ-embedded lipid bilayer membrane was explored. Secondly, the performance of biomimetic membrane has been has been demonstrated in forward osmosis. Thirdly, a new membrane with enhanced the mechanical property and higher permeability and selectivity has been fabricated. Finally, water transport through the robust AqpZ-embedded vesicular membrane has been investigated through a newly modified transport model in a FO process. This study provides a direction for the further development of the ...
Acquired nephrogenic diabetes insipidus happens when the small tubes or tubules in the kidneys are defective causing a person to eliminate too much water during urination. This occurs because the kidneys do not respond to antidiuretic hormone (ADH)or vasopressin. ADH tells the kidneys to make the urine more concentrated.. Symptoms of acquired nephrogenic diabetes insipidus are extreme thirst especially for ice water and production of large amounts of urine. This commonly occurs because of a problem caused by something else such as blockage in the urinary tract, use of certain medications, high levels of calcium, or low levels of potassium. This acquired nephrogenic diabetes insipidus is an extremely rare form of diabetes. When the cause of this form of diabetes inspidus is identified and corrected, the disease usually clears up. Hereditary nephrogenic diabetes insipidus is treated with fluid intake that matches urine output and medication to lower urine output. Medications used to treat ...
A water deprivation test is also performed to see if the person suffers from nephrogenic diabetes insipidus. The patient has to stay without water for around five hours or more and then the plasma concentration, as well as the volume of urine, is measured. In case the test is positive for nephrogenic diabetes insipidus, the patient will be resistant to the anti diuretic hormone. Hence, after the test, although the patient is dehydrated, dilute urine and blood plasma will still be present in the patient ...

Category:Aquaporins - Wikimedia CommonsCategory:Aquaporins - Wikimedia Commons

Aquaporin transporter, Aquaporin_transptr, IPR034294 (en); Acquaporina (it); Aquaporin, 水孔蛋白, 水通道 (zh); Canals daigua en la ... aquaporin (en); 水通道蛋白 (zh); Aquaporin (da); Akvaporin (hu); アクアポリン (ja); Acquaporine (it); Υδατοπορίνες (el); akuaporin (id); ... Media in category "Aquaporins". The following 20 files are in this category, out of 20 total. ... Fluxes-of-Water-through-Aquaporin-9-Weaken-Membrane-Cytoskeleton-Anchorage-and-Promote-Formation-of-pone.0059901.s002.ogv 7.0 s ...
more infohttps://commons.wikimedia.org/wiki/Category:Aquaporins

Aquaporins in Melanocytic and Nonmelanocytic Skin TumorsAquaporins in Melanocytic and Nonmelanocytic Skin Tumors

This study investigated the role of aquaporin 1 and aquaporin 3 in the pathobiology of skin cancers. Might they have potential ... Expression Pattern of Aquaporin 1 and Aquaporin 3 in Melanocytic and Nonmelanocytic Skin Tumors ... Expression Pattern of Aquaporin 1 and Aquaporin 3 in Melanocytic and Nonmelanocytic Skin Tumors. ...
more infohttps://www.medscape.com/viewarticle/918420_2

Aquaporins | BPMPAquaporins | BPMP

Aquaporin, Hydraulics, Phosphorylation, Roots, Water stress, Water transport. Presentation. The Aquaporin team studies the ... Maurel C✉, Boursiac Y, Luu D-T, Santoni V, Shahzad Z, Verdoucq L (2015) Aquaporins in plants. Physiol. Rev., 95(4):1321-1358 ... Aquaporins. Group leader : Christophe Maurel. CNRS Research Director. Tél : 04 99 61 20 11. Mail : [email protected] ... Bellati J, Champeyroux C, Hem S, Rofidal V, Krouk G, Maurel C, Santoni V✉ (2016) Novel aquaporin regulatory mechanisms revealed ...
more infohttps://www1.montpellier.inra.fr/wp-inra/bpmp/en/research/the-teams/aquaporins/

Aquaporins in brain: distribution, physiology, and pathophysiology.  - PubMed - NCBIAquaporins in brain: distribution, physiology, and pathophysiology. - PubMed - NCBI

In rodent brain, several recent studies have demonstrated the presence of different types of aquaporins. Aquaporin 1 (AQP1) was ... Aquaporins in brain: distribution, physiology, and pathophysiology.. Badaut J1, Lasbennes F, Magistretti PJ, Regli L. ... Aquaporin 4 may also play a role in pathophysiologic conditions, as shown by the reduced edema formation observed after water ... A water channel family, the aquaporins, facilitates water flux through the plasma membrane of many cell types. ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/11919508?dopt=Abstract

Targeting Aquaporins for Conferring Salinity Tolerance in Crops | SpringerLinkTargeting Aquaporins for Conferring Salinity Tolerance in Crops | SpringerLink

Afzal Z, Howton TC, Sun Y, Mukhtar MS (2016) The roles of aquaporins in plant stress responses. J Dev Biol 4(1):9PubMedCentral ... Xu Y, Hu W, Liu J, Zhang J, Jia C, Miao H, Xu B, Jin Z (2014) A banana aquaporin gene, MaPIP1;1, is involved in tolerance to ... Maurel C, Boursiac Y, Luu DT, Santoni V, Shahzad Z, Verdoucq L (2015) Aquaporins in plants. Physiol Rev 95(4):1321-1358PubMed ... Pang Y, Li L, Ren F, Lu P, Wei P, Cai J, Xin L, Zhang J, Chen J, Wang X (2010) Overexpression of the tonoplast aquaporin AtTIP5 ...
more infohttps://link.springer.com/chapter/10.1007/978-3-319-75671-4_3

Aquaporin A/S ProfileAquaporin A/S Profile

Aquaporin is dedicated to revolutionizing water purification through the use of industrial biotechn ... Aquaporin A/S is a global cleantech company located in Kongens Lyngby, Denmark. ... An essential building block in the water membrane technology of Aquaporin A/S is the aquaporin molecule. The aquaporin molecule ... The understanding of aquaporins and their role in life has opened the possibility of using aquaporins in an industrial context ...
more infohttps://www.environmental-expert.com/companies/aquaporin-a-s-41610

Aquaporin 11/12 (IPR016697) | InterPro | EMBL-EBIAquaporin 11/12 (IPR016697) | InterPro | EMBL-EBI

Aquaporin 11/12 (IPR016697). Short name: Aquaporin_11/12 Family relationships *Major intrinsic protein (IPR000425) *Aquaporin ... The aquaporins (AQPs) are a family of integral membrane proteins composed of two subfamilies: the orthodox aquaporins, which ... AQP11 is functionally distinct from other proteins of the aquaporin superfamily and could represent a new aquaporin subfamily [ ... Aquaporins 11 and 12 are classified as members of a new AQP subfamily: the subcellular AQPs [PMID: 17178102]. AQP 11 and 12 ...
more infohttp://www.ebi.ac.uk/interpro/entry/IPR016697

aquaporin - junctional and nonjunctionalaquaporin - junctional and nonjunctional

AQP0 aquaporin pores are mainly lined with alpha helices, which can be seen clearly using the cartoon representation. ...
more infohttp://employees.csbsju.edu/hjakubowski/Jmol14/aquaporin/AQP0membraneproteins.htm?_USE=HTML5

Recent Articles | Aquaporins And Immunology | The Scientist Magazine®Recent Articles | Aquaporins And Immunology | The Scientist Magazine®

From guiding branching neurons in the developing brain to maintaining a healthy heartbeat, there seems to be no job that the immune cells cant tackle.. 0 Comments. ...
more infohttps://www.the-scientist.com/?articles.list/categoryNo/2625/category/The-Scientist/tagNo/3378,12/tags/aquaporins,immunology/

Quiz & Worksheet - Aquaporins | Study.comQuiz & Worksheet - Aquaporins | Study.com

One way is through the use of aquaporins. Use this assessment to assess how well you understand the functions of aquaporins. ... 2. Aquaporins are protein tunnels that allow which important molecule to travel across a cell membrane?. ... For an effective review, complete the related lesson Aquaporins: Definition & Functions. Use this review to prepare for ... Information recall - access the knowledge youve gained regarding the functions of aquaporins ...
more infohttps://study.com/academy/practice/quiz-worksheet-aquaporins.html

The Role of Tight Junctions and Aquaporins in Skin Dryness | SpringerLinkThe Role of Tight Junctions and Aquaporins in Skin Dryness | SpringerLink

Byakkokaninjinto prevents body water loss by increasing the expression of kidney aquaporin-2 and skin aquaporin-3 in KKAy mice ... Expression and function of aquaporins in human skin: Is aquaporin-3 just a glycerol transporter? Biochim Biophys Acta 1758:1034 ... Verkman AS (2009) Aquaporins: translating bench research to human disease. J Exp Biol 212:1707-1715PubMedGoogle Scholar ... Cao C, Sun Y, Healey S, Bi Z, Hu G, Wan S, Kouttab N, Chu W, Wan Y (2006) EGFR-mediated expression of aquaporin-3 is involved ...
more infohttps://link.springer.com/chapter/10.1007/978-3-642-27606-4_14

Aquaporin 9 peptide (ab56306) | AbcamAquaporin 9 peptide (ab56306) | Abcam

Buy our Aquaporin 9 peptide. Ab56306 is a blocking peptide for ab15127 and has been validated in BL. Abcam provides free ... Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the ...
more infohttps://www.abcam.com/aquaporin-9-peptide-ab56306.html

Frontiers | Mutual Interactions between Aquaporins and Membrane Components | Plant ScienceFrontiers | Mutual Interactions between Aquaporins and Membrane Components | Plant Science

Specific sites of protein-aquaporin interaction have been evaluated and new regulations of aquaporins described based on these ... Aquaporin isoforms heterotetramerizations are considered as novel regulatory mechanisms for plasma membrane (PIPs) and ... Aquaporin isoforms heterotetramerizations are considered as novel regulatory mechanisms for plasma membrane (PIPs) and ... The chemical composition or physical characteristics of the lipid bilayer also influences many aspects of membrane aquaporins, ...
more infohttps://www.frontiersin.org/articles/10.3389/fpls.2016.01322/full

Anti-Aquaporin 0 antibody (ab176308) | AbcamAnti-Aquaporin 0 antibody (ab176308) | Abcam

Rabbit polyclonal Aquaporin 0 antibody validated for WB and tested in Human, Mouse and Rat. Immunogen corresponding to ... Aquaporins contain two tandem repeats each containing two membrane-spanning helices and a pore-forming loop with the signature ... Synthetic peptide corresponding to Human Aquaporin 0 aa 1-263.. Database link: P30301 ...
more infohttp://www.abcam.com/aquaporin-0-antibody-ab176308.html

Novel Regulation of Aquaporins during Osmotic Stress | Plant PhysiologyNovel Regulation of Aquaporins during Osmotic Stress | Plant Physiology

Novel Regulation of Aquaporins during Osmotic Stress. Rosario Vera-Estrella, Bronwyn J. Barkla, Hans J. Bohnert, Omar Pantoja ... Quigley F, Rosenberg JM, Shachar-Hill Y, Bohnert HJ (2002) From genome to function: the Arabidopsis aquaporins. Genome Biol 3: ... Knepper MA, Inoue T (1997) Regulation of aquaporin-2 water channel trafficking by vasopressin. Curr Opin Cell Biol 9: 560-564. ... Uehlein N, Lovisolo C, Siefritz F, Kaldenhoff R (2003) The tobacco aquaporin NtAQP1 is a membrane CO2 pore with physiological ...
more infohttp://www.plantphysiol.org/content/135/4/2318

Aquaporin - Proteopedia, life in 3DAquaporin - Proteopedia, life in 3D

Mutations in aquaporin-2 cause diabitis insipidus. Mutations in aquaporin-0 in mice cause congenital cataracts. Aquaporin-4 is ... Aquaporin-4 regulates water balance in the central nervous system.. *Aquaporin-5 is implicated in the forming of saliva, tears ... Aquaporin-Z is a major water channel in bacteria.. *Aquaglycerolporin (GLpf) is a water channel which can transport glycerol, ... Aquaporins are channel producing proteins which regulate the flow of water across the cell membrane. The image on the left ...
more infohttp://proteopedia.org/wiki/index.php/Aquaporin

PIP1 Plasma Membrane Aquaporins in Tobacco | Plant CellPIP1 Plasma Membrane Aquaporins in Tobacco | Plant Cell

The molecular functions of several aquaporins are well characterized (e.g., by analysis of aquaporin-expressing Xenopus oocytes ... PIP1 Plasma Membrane Aquaporins in Tobacco. Franka Siefritz, Melvin T. Tyree, Claudio Lovisolo, Andrea Schubert, Ralf ... PIP1 Plasma Membrane Aquaporins in Tobacco. Franka Siefritz, Melvin T. Tyree, Claudio Lovisolo, Andrea Schubert, Ralf ... Many organisms lacking a specific aquaporin have an unobtrusive phenotype, which suggests that aquaporins are unimportant or ...
more infohttp://www.plantcell.org/content/14/4/869

Recent Articles | Aquaporins And Culture | The Scientist Magazine®| Page 5Recent Articles | Aquaporins And Culture | The Scientist Magazine®| Page 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. ...
more infohttps://www.the-scientist.com/?articles.list/tagNo/3378,3/tags/aquaporins,culture/pageNo/5/

RS RS22555 aquaporin family protein [Ralstonia solanacearum GMI1000] - Gene - NCBIRS RS22555 aquaporin family protein [Ralstonia solanacearum GMI1000] - Gene - NCBI

WP_043876861.1 aquaporin family protein [Ralstonia solanacearum]. Conserved Domains (1) summary. COG0580. Location:1 → 212. ... aquaporin family protein. Locus tag. RS_RS22555. Gene type. protein coding. Organism. Ralstonia solanacearum GMI1000 (strain: ... RS_RS22555 aquaporin family protein [ Ralstonia solanacearum GMI1000 ] Gene ID: 1223439, updated on 31-May-2017 ... GlpF; Glycerol uptake facilitator and related aquaporins (Major Intrinsic Protein Family) [Carbohydrate transport and ...
more infohttps://www.ncbi.nlm.nih.gov/gene/?term=RS_RS22555

Aquaporin-1 - Proteopedia, life in 3DAquaporin-1 - Proteopedia, life in 3D

Aquaporins Aquaporin-1 (AQP1) was first discovered in human red blood cell membranes by Gheorghe Bengas research group in 1986 ... Aquaporin-1 Structure Aquaporin-1 is an integral membrane protein that is considered to have an "open" structure. Despite being ... Aquaporin-1 Regulation Aquaporin channels may be subject to intense short term regulation via signal transduction. Transducers ... Water selective aquaporins are AQP1, -2, -4, -5, -6, -8, -12, and -0. A subgroup of aquaporins called aquaglycerporins allow ...
more infohttp://proteopedia.org/wiki/index.php/Aquaporin-1

Structure of a Nobel-prize winning molecule: AquaporinStructure of a Nobel-prize winning molecule: Aquaporin

The architecture of aquaporin Z is typical of aquaporins, with a spiral of eight oxygens providing water-binding sites inside ... Aquaporins form a large, diverse family of proteins and have been found in bacteria, plants, and animals. Less than a decade ... The aquaporin Z channel protein in E. coli can accommodate a flow of water at rates six times higher than GlpF ( ... And because the two main classes of aquaporins occur in E. coli--which means theyre exposed to the same cellular environment-- ...
more infohttp://www.innovations-report.com/html/reports/life-sciences/report-24395.html

Aquaporin Membrane Protein (FCYXM8WTA) by 3DBiologyAquaporin Membrane Protein (FCYXM8WTA) by 3DBiology

... on Shapeways. Learn more before you buy, or discover other cool products in ... Aquaporin Biochemistry Biological Models Biology Chemistry Molecular Biology Molecular Models Protein Science ... Human red cell AQP1 is the first functionally defined member of the aquaporin family of membrane water channels. Here we ...
more infohttps://www.shapeways.com/product/FCYXM8WTA/aquaporin-membrane-protein?optionId=61399153

Aquaporin-3: Regulating Skin Cell GrowthAquaporin-3: Regulating Skin Cell Growth

Two previous articles in this series on aquaporins have discussed their history, mechanism and stimulation. The current article ... Aquaporin-3: Regulating Skin Cell Growth. July 12, 2013 , Contact Author , By: Bud Brewster, Cosmetics & Toiletries Magazine. ... Aquaporins (AQPs) are integral membrane proteins that form pores in the membrane of biological cells. At least 13 mammalian ... Aquaporins (AQPs) are integral membrane proteins that form pores in the membrane of biological cells. At least 13 mammalian ...
more infohttp://www.cosmeticsandtoiletries.com/research/biology/premium-aquaporin-3-regulating-skin-cell-growth-214918791.html

One protein, two channels: Scientists explain mechanism in aquaporinsOne protein, two channels: Scientists explain mechanism in aquaporins

... at Urbana-Champaign and the University of Arizona have identified a key component of the gating mechanism in aquaporins that ... A number of aquaporins, including aquaporin-1, have been found to function as ion channels, as well. ... Aquaporins are a class of proteins that form membrane channels in cell walls and allow for water movement between a cell and ... One protein, two channels: Scientists explain mechanism in aquaporins. September 21, 2006 in / Using computer simulations and ...
more infohttps://phys.org/print78071321.html
  • 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)
  • Hence, the discussion about the role of aquaporins in the majority of multicellular organisms remains open ( Chrispeels and Maurel, 1994 ). (plantcell.org)
  • The molecular and cellular bases of this process are addressed by studying the multiple facets of aquaporin regulation. (inra.fr)
  • The team combines molecular, physiological and genetic approaches and characterizes water transport at the level of cloned aquaporins, purified membranes, living cells or organs like excised roots or rosettes. (inra.fr)
  • The molecular driving forces stabilizing the positions of the lipids around aquaporins could define their activity, thereby altering the conformational properties. (frontiersin.org)
  • Agre P, Kozono D. Aquaporin water channels: molecular mechanisms for human diseases. (proteopedia.org)
  • The molecular functions of several aquaporins are well characterized (e.g., by analysis of aquaporin-expressing Xenopus oocytes). (plantcell.org)
  • 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)
  • 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)
  • Taking advantage of the known crystal structure of aquaporin-1 and the power of molecular dynamics simulations, the researchers explored the central pore as a candidate pathway for conducting ions. (phys.org)
  • In the last few years, the team has uncovered novel functions and regulations of plant aquaporins. (inra.fr)
  • In the present chapter, we discussed roles of plant aquaporins in salinity stress and exploitating the same for genetic engineering approach. (springer.com)
  • Bellati J , Champeyroux C , Hem S , Rofidal V , Krouk G , Maurel C , Santoni V ✉ (2016) Novel aquaporin regulatory mechanisms revealed by interactomics . (inra.fr)
  • Afzal Z, Howton TC, Sun Y, Mukhtar MS (2016) The roles of aquaporins in plant stress responses. (springer.com)
  • AQP0 aquaporin pores are mainly lined with alpha helices, which can be seen clearly using the cartoon representation. (csbsju.edu)
  • 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)
  • The physiological importance of the aquaporin in human is perhaps most conspicuous in the kidney, where ~150-200 litres of water need to be reabsorbed from the primary urine each day, that is, aquaporin facilitated water transport is invoked when water rapidly must be retrieved from a body fluid. (environmental-expert.com)
  • This process is vital for any living organism to sustain proper physiological conditions and aquaporins are necessary to sustain this process (i.e. osmosis alone could not provide a sufficient flow of water). (proteopedia.org)
  • Therefore, our studies focused on a homologous aquaporin of the relatively larger tobacco plant. (plantcell.org)
  • Ampah-Korsah H, Sonntag Y, Engfors A, Kirscht A, Kjellbom P, Johanson U (2017) Single amino acid substitutions in the selectivity filter render NbXIP1;1α aquaporin water permeable. (springer.com)
  • 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 can't fit. (innovations-report.com)
  • Aquaporin-4 is the primary autoimmune target of neuromyelitis optica. (proteopedia.org)
  • Aquaporin-4 is the predominant autoimmune target in neuromyelitis optica, or NMO, since a specific AQP4 IgG autoantibody, or NMO-IgG, binds to the extracellular surface of AQP4. (wikipedia.org)
  • Rodrigues O , Reshetnyak G , Grondin A , Saijo Y, Leonhardt N, Maurel C , Verdoucq L ✉ (2017) Aquaporins facilitate hydrogen peroxide entry into guard cells to mediate ABA- and pathogen-triggered stomatal closure . (inra.fr)
  • Aquaporin is dedicated to revolutionizing water purification through the use of industrial biotechnological techniques and thinking. (environmental-expert.com)
  • The Aquaporin Inside platform uses biotechnological principles in a technological context which is a novel upcoming field with large commercial perspectives. (environmental-expert.com)
  • Finally, it is described how the interactions between aquaporins and copolymer matrixes or biological compounds offer an opportunity for the functional incorporation of aquaporins into new biotechnological advances. (frontiersin.org)
  • Wudick MM , Li X, Valentini V , Geldner N, Chory J, Lin J, Maurel C ✉, Luu D-T ✉ (2015) Sub-cellular redistribution of root aquaporins induced by hydrogen peroxide . (inra.fr)
  • 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)
  • 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)
  • J. E. Towne, C. M. Krane, C. J. Bachurski, and A. G. Menon, "Tumor necrosis factor- α inhibits aquaporin 5 expression in mouse lung epithelial cells," The Journal of Biological Chemistry , vol. 276, no. 22, pp. 18657-18664, 2001. (hindawi.com)
  • Use this assessment to assess how well you understand the functions of aquaporins. (study.com)
  • For an effective review, complete the related lesson Aquaporins: Definition & Functions. (study.com)
  • Aquaporin-0 functions as water channel in lens fibers. (proteopedia.org)
  • Taken together, these recent reports suggest that water homeostasis in the brain is maintained by regulatory processes that, by control of aquaporin expression and distribution, induce and organize water movements. (nih.gov)
  • Maurel C ✉, Boursiac Y , Luu D-T , Santoni V , Shahzad Z , Verdoucq L (2015) Aquaporins in plants . (inra.fr)
  • Abdelkader AF, El-khawas S, El-Din El-Sherif NA, Hassanein RA, Emam MA, Hassan RE (2012) Expression of aquaporin gene (OsPIP1-3) in salt-stressed rice ( Oryza sativa L.) plants pre-treated with the neurotransmitter (dopamine). (springer.com)
  • Genetic defects involving aquaporin genes have been associated with several human diseases including nephrogenic diabetes insipidus and neuromyelitis optica. (wikipedia.org)
  • Tanshinone IIA ameliorates seawater exposure-induced lung injury by inhibiting aquaporins (AQP) 1 and AQP5 expression in lung," Respiratory Physiology and Neurobiology , vol. 176, no. 1-2, pp. 39-49, 2011. (hindawi.com)
  • Aquaporins in brain: distribution, physiology, and pathophysiology. (nih.gov)
  • Therefore, an integrative approach to the relevance of the membrane-aquaporin interaction to different processes related to plant cell physiology is provided. (frontiersin.org)