A class of porins that allow the passage of WATER and other small molecules across CELL MEMBRANES.
Aquaporin 1 forms a water-specific channel that is constitutively expressed at the PLASMA MEMBRANE of ERYTHROCYTES and KIDNEY TUBULES, PROXIMAL. It provides these cells with a high permeability to WATER. In humans polymorphisms of this protein result in the Colton blood group antigen.
Aquaporin 5 is a water-specific channel protein that is expressed primarily in alveolar, tracheal, and upper bronchial EPITHELIUM. It plays an important role in maintaining water HOMEOSTASIS in the LUNGS and may also regulate release of SALIVA and TEARS in the SALIVARY GLANDS and the LACRIMAL GLAND.
Aquaporin 4 is the major water-selective channel in the CENTRAL NERVOUS SYSTEM of mammals.
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 is an aquaglyceroporin that is found primarily in KIDNEY COLLECTING DUCTS. AQP6 protein functions as an anion-selective channel.
A subgroup of aquaporins that transport WATER; GLYCEROL; and other small solutes across CELL MEMBRANES.
Aquaporin 2 is a water-specific channel protein that is expressed in KIDNEY COLLECTING DUCTS. The translocation of aquaporin 2 to the apical PLASMA MEMBRANE is regulated by VASOPRESSIN, and MUTATIONS in AQP2 have been implicated in a variety of kidney disorders including DIABETES INSIPIDUS.
Mercury chloride (HgCl2). A highly toxic compound that volatizes slightly at ordinary temperature and appreciably at 100 degrees C. It is corrosive to mucous membranes and used as a topical antiseptic and disinfectant.
Tendency of fluids (e.g., water) to move from the less concentrated to the more concentrated side of a semipermeable membrane.
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)
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.
Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.
Property of membranes and other structures to permit passage of light, heat, gases, liquids, metabolites, and mineral ions.
Inorganic compounds that contain gold as an integral part of the molecule.
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.
The ability of the kidney to excrete in the urine high concentrations of solutes from the blood plasma.
A plant genus of the family FABACEAE that contains kukulkanin, a CHALCONE.
A plant genus of the family JUGLANDACEAE that provides the familiar walnut.
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.
A plant family of the order Violales, subclass Dilleniidae, class Magnoliopsida. The common name of rock rose is used with several plants of this family.
The usually underground portions of a plant that serve as support, store food, and through which water and mineral nutrients enter the plant. (From American Heritage Dictionary, 1982; Concise Dictionary of Biology, 1990)
A plant genus of the family LILIACEAE. Members contain tuliposides and tulipalins and have been associated with allergic contact dermatitis in florists.
A plant genus of the family ASTERACEAE known for allergenic pollen (ALLERGENS).
A quality of cell membranes which permits the passage of solvents and solutes into and out of cells.
Sets of cell surface antigens located on BLOOD CELLS. They are usually membrane GLYCOPROTEINS or GLYCOLIPIDS that are antigenically distinguished by their carbohydrate moieties.
Fluids composed mainly of water found within the body.
Inorganic compounds that contain mercury as an integral part of the molecule.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in plants.
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.
A plant genus of the family ASCLEPIADACEAE. The downy akund floss fiber from the seeds is used like kapok.
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.
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.
A species of PERCIFORMES commonly used in saline aquaculture.
Paired ducts in the human male through which semen is ejaculated into the urethra.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
A cytotoxic sulfhydryl reagent that inhibits several subcellular metabolic systems and is used as a tool in cellular physiology.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
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.
Expanded structures, usually green, of vascular plants, characteristically consisting of a bladelike expansion attached to a stem, and functioning as the principal organ of photosynthesis and transpiration. (American Heritage Dictionary, 2d ed)
The 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.
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)
A widely cultivated plant, native to Asia, having succulent, edible leaves eaten as a vegetable. (From American Heritage Dictionary, 1982)
The parts of plants, including SEEDS.
Glands of external secretion that release its secretions to the body's cavities, organs, or surface, through a duct.
Urination of a large volume of urine with an increase in urinary frequency, commonly seen in diabetes (DIABETES MELLITUS; DIABETES INSIPIDUS).
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.
Straight tubes commencing in the radiate part of the kidney cortex where they receive the curved ends of the distal convoluted tubules. In the medulla the collecting tubules of each pyramid converge to join a central tube (duct of Bellini) which opens on the summit of the papilla.
The condition that results from excessive loss of water from a living organism.
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)
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.
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)

In diabetes, polyuria is caused by high levels of glucose in the blood that cannot be properly absorbed by the body. The excess glucose spills into the urine, drawing water with it and increasing the volume of urine. This can lead to dehydration and electrolyte imbalances if left untreated.

In kidney disease, polyuria can be caused by damage to the kidneys that impairs their ability to concentrate urine. As a result, the body produces more urine than usual to compensate for the lack of concentrating ability.

Polyuria can also be a symptom of certain endocrine disorders such as diabetes insipidus, where the body produces too much antidiuretic hormone (ADH) or vasopressin, which leads to an excessive amount of urine production.

To diagnose polyuria, a healthcare provider may perform a physical examination, take a medical history, and conduct diagnostic tests such as urinalysis, blood glucose testing, and imaging studies. Treatment for polyuria depends on the underlying cause and may include medication, lifestyle changes, and in some cases, dialysis.

There are many potential causes of dehydration, including:

* Not drinking enough fluids
* Diarrhea or vomiting
* Sweating excessively
* Diabetes (when the body cannot properly regulate blood sugar levels)
* Certain medications
* Poor nutrition
* Infections
* Poor sleep

To diagnose dehydration, a healthcare provider will typically perform a physical examination and ask questions about the patient's symptoms and medical history. They may also order blood tests or other diagnostic tests to rule out other conditions that may be causing the symptoms.

Treatment for dehydration usually involves drinking plenty of fluids, such as water or electrolyte-rich drinks like sports drinks. In severe cases, intravenous fluids may be necessary. If the underlying cause of the dehydration is a medical condition, such as diabetes or an infection, treatment will focus on managing that condition.

Preventing dehydration is important for maintaining good health. This can be done by:

* Drinking enough fluids throughout the day
* Avoiding caffeine and alcohol, which can act as diuretics and increase urine production
* Eating a balanced diet that includes plenty of fruits, vegetables, and whole grains
* Avoiding excessive sweating by dressing appropriately for the weather and taking breaks in cool, shaded areas when necessary
* Managing medical conditions like diabetes and kidney disease properly.

In severe cases of dehydration, complications can include seizures, organ failure, and even death. It is important to seek medical attention if symptoms persist or worsen over time.

The word "edema" comes from the Greek word "oidema", meaning swelling.

This results in aquaporin-2 containing vesicles to increase water uptake and return to circulation. Mutation of the aquaporin 2 ... The gating of an aquaporin is carried out by an interaction between a gating mechanism and the aquaporin, which causes a 3D ... It was not until 1992 that the first aquaporin, 'aquaporin-1' (originally known as CHIP 28), was reported by Peter Agre, of ... There have been two clear examples of diseases identified as resulting from mutations in aquaporins: Mutations in the aquaporin ...
Aquaporin 3 is expressed more in atopic eczema. Recent studies indicate that aquaporin 3 is overexpressed in many types of ... Sasaki S, Ishibashi K, Marumo F (1998). "Aquaporin-2 and -3: representatives of two subgroups of the aquaporin family ... Aquaporin 3 (AQP-3) is the protein product of the human AQP3 gene. It is found in the basolateral cell membrane of principal ... 2005). "Roles of aquaporin-3 water channels in volume-regulatory water flow in a human epithelial cell line". J. Membr. Biol. ...
... and AQP3 are at the same chromosomal location suggesting that 9p13 may be a site of an aquaporin cluster. Aquaporin ... Aquaporin-7 (AQP-7) is a protein that in humans is encoded by the AQP7 gene. Aquaporins/major intrinsic proteins (MIP) are a ... "Entrez Gene: AQP7 aquaporin 7". Dibas AI, Mia AJ, Yorio T (1998). "Aquaporins (water channels): role in vasopressin-activated ... Aquaporin-7 has greater sequence similarity with AQP3 and AQP9 and they may be a subfamily. ...
... (AQP-9) is a protein that in humans is encoded by the AQP9 gene. The aquaporins/major intrinsic protein are a ... Aquaporin-9 has greater sequence similarity with AQP3 and AQP7 and they may be a subfamily. Aquaporin-9 allows passage of a ... "Entrez Gene: AQP9 aquaporin 9". Ishibashi K, Kuwahara M, Gu Y, et al. (1998). "Cloning and functional expression of a new ... 2003). "Aquaporin-9 is expressed in a mucus-secreting goblet cell subset in the small intestine". FEBS Lett. 540 (1-3): 157-62 ...
Aquaporin+1 at the US National Library of Medicine Medical Subject Headings (MeSH) Gallery of Aquaporin Simulations Human AQP1 ... "Entrez Gene: AQP1 aquaporin 1 (Colton blood group)". Knepper MA (July 1994). "The aquaporin family of molecular water channels ... The gene encoding this aquaporin is a possible candidate for disorders involving imbalance in ocular fluid movement. Aquaporin ... Aquaporin 1 (AQP-1) is a protein that in humans is encoded by the AQP1 gene. AQP-1 is a widely expressed water channel, whose ...
... , (AQP-6) also known as kidney-specific aquaporin is a protein in humans that is encoded by the AQP6 gene. The ... Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). This protein ... "Entrez Gene: Aquaporin 6, kidney specific". Retrieved 2012-04-10. Human AQP6 genome location and AQP6 gene details page in the ... Ikeda M, Beitz E, Kozono D, Guggino WB, Agre P, Yasui M (Oct 2002). "Characterization of aquaporin-6 as a nitrate channel in ...
... (AQP-5) is a protein that in humans is encoded by the AQP5 gene. Aquaporin-5 (AQP-5) is a water channel protein. ... Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). Aquaporin-5 ... "Entrez Gene: AQP5 aquaporin 5". Verkman AS (2003). "Role of aquaporin water channels in eye function". Exp. Eye Res. 76 (2): ... 2003). "Distribution of aquaporin water channels AQP1 and AQP5 in the ductal system of the human pancreas". Gut. 52 (7): 1008- ...
The expression of aquaporin 4 is reliant on the disease stage of TBI. In an acute stage of TBI, the lack of aquaporin 4 causes ... Aquaporin-4, also known as AQP-4, is a water channel protein encoded by the AQP4 gene in humans. AQP-4 belongs to the aquaporin ... Aquaporin-4 is the most common aquaporin in the brain, spinal cord, and optic nerve. It is highly expressed in the human body ... Aquaporin-4 is essential in the formation of memory as well as synaptic plasticity. Other performances that aquaporin-4 is ...
... is a protein that in humans is encoded by the AQP8 gene. Aquaporin-8 (AQP-8) is a water channel protein. Aquaporins ... "Entrez Gene: AQP8 aquaporin 8". Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of ... 2007). "Aquaporin-8 expression is reduced in ileum and induced in colon of patients with ulcerative colitis". World J. ... Wang S, Chen J, Au KT, Ross MG (2003). "Expression of aquaporin 8 and its up-regulation by cyclic adenosine monophosphate in ...
It is the only aquaporin regulated by vasopressin. The basic job of aquaporin 2 is to reabsorb water from the urine while its ... This aquaporin is also regulated by food intake. Fasting reduces expression of this aquaporin independently of vasopressin. ... so the aquaporin 2 can be used by the cell. This aquaporin is regulated in two ways by the peptide hormone vasopressin: short- ... Aquaporin-2 (AQP-2) is found in the apical cell membranes of the kidney's collecting duct principal cells and in intracellular ...
Zador, Zsolt; Stiver, Shirley; Wang, Vincent; Manley, Geoffrey T. (2009). "Role of Aquaporin-4 in Cerebral Edema and Stroke". ... In Beitz, Eric (ed.). Aquaporins. Handbook of Experimental Pharmacology. Vol. 190. pp. 159-70. doi:10.1007/978-3-540-79885-9_7 ...
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 ...
Am J Bot 84:1522-1529 Christophe Maurel (June 1997). "AQUAPORINS AND WATER PERMEABILITY OF PLANT MEMBRANES". Annual Review of ... Wayne's work preceded the molecular identification of aquaporins in plant cells. It is generally believed that the ... Kaldenhoff, R., Bertl, A., Otto, B., Moshelion, M. and Uehlein, N. (2007). "Characterization of Plant Aquaporins". Osmosensing ... S2CID 15863712.{{cite journal}}: CS1 maint: multiple names: authors list (link) Maurel, Christophe (1997). "Aquaporins and ...
"Water Permeation Through Aquaporins". Theoretical and Computational Biophysics Group, University of Illinois at Urbana- ...
https://doi.org/10.1016/j.febslet.2007.04.002 Uehlein, N., & Kaldenhoff, R. (2007). Aquaporins and Plant Leaf Movements. Annals ...
... 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 ... where vasopressin release and response are normal but where abnormal renal expression and translocation of aquaporin 2, or both ...
116: 31-39.{{cite journal}}: CS1 maint: multiple names: authors list (link) Maurel, C. (1997). "Aquaporins and water ... for the existence of water channels in plant cells prior to the molecular identification of animal and plant aquaporins Tazawa ...
ISBN 978-81-7141-934-0.{{cite book}}: CS1 maint: date and year (link) Nishimura, Hiroko; Yang, Yimu (2013-12-01). "Aquaporins ...
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). ...
Marlar S, Jensen HH, Login FH, Nejsum LN (October 2017). "Aquaporin-3 in Cancer". International Journal of Molecular Sciences. ... aquaporin 3, is a water channel that when overexpressed is thought to promote the progression and spread of various types of ...
... aquaporins versus cotransporters". Biophysical Journal. 99 (11): 3647-3656. Bibcode:2010BpJ....99.3647M. doi:10.1016/j.bpj. ...
This movement of water is facilitated by aquaporins. A seal is created by tight junctions of the epithelial cells that line the ...
Agre was recognized for his discovery of aquaporin water channels. Aquaporins are water-channel proteins that move water ... Aquaporins are "the plumbing system for cells," said Agre. Every cell is primarily water. "But the water doesn't just sit in ... The 28 kDa protein is now known as aquaporin-1 (abbreviated AQP1), the archetypal member of a large family of water channel ... Permeated by water, aquaporins are required for generation of cerebrospinal fluid, aqueous humour, tears, sweat, saliva, ...
Aquaporins are protein channel pores permeable to water. Information can also pass through the plasma membrane when signaling ...
Two types of aquaporins are expressed in the CNS: aquaporin-1, which is expressed by specialized epithelial cells of the ... Aquaporins are membrane-bound channels that play critical roles in regulating the flux of water into and out of cells. Relative ... Aquaporin-4 expression in astrocytes is highly polarized to the endfoot processes ensheathing the cerebral vasculature. Up to ... Verkman AS, Binder DK, Bloch O, Auguste K, Papadopoulos MC (August 2006). "Three distinct roles of aquaporin-4 in brain ...
In 2005 they identified the aquaporin 4 protein as the target of the disease, and developed the first in-house test to aid in ... In more than 80% of cases, IgG autoantibodies against aquaporin-4 (anti-AQP4+) are the cause, and in 10-40% of the remaining ... In more than 80% of cases, NMO is caused by immunoglobulin G autoantibodies to aquaporin 4 (anti-AQP4), the most abundant water ... Some authors propose to use the name "autoimmune aquaporin-4 channelopathy" for these diseases, while others prefer a more ...
Balo-like lesions have been reported in aquaporin-4 seropositive and seronegative NMOSD, and also in children, as part of an ... Nov 2010). "Aquaporin-4 astrocytopathy in Baló's disease". Acta Neuropathologica. 120 (5): 651-660. doi:10.1007/S00401-010-0733 ... similar to the one found in aquaporin-seropositive neuromyelitis optica. Though no anti-NMO antibodies have been found, the ...
Nicaise C, Soyfoo MS, Authelet M, De Decker R, Bataveljic D, Delporte C, Pochet R (December 2008). "Aquaporin‐4 Overexpression ... They release secretory compounds that influence the phenotype of endothelial cells and express aquaporin and potassium channels ...
Molecular and Cellular Features of Aquaporin Expression". Plant Physiology. 139 (2): 790-805. doi:10.1104/pp.105.065029. PMC ...
Aquaporins allow water to move down their osmotic gradient and out of the nephron, increasing the amount of water re-absorbed ... Vasopressin, acting through cAMP, also increases transcription of the aquaporin-2 gene, thus increasing the total number of ... This occurs through increased transcription and insertion of water channels (Aquaporin-2) into the apical membrane of ... Wilson JL, Miranda CA, Knepper MA (2013). "Vasopressin and the Regulation of Aquaporin-2". Clinical and Experimental Nephrology ...
... You are Flash aquaporins recent and shoe thought to make this milling dismissed. You can add this on the healthcare ... The aquaporins will refer passed to your Kindle container. It may is up to 1-5 seconds before you was it. You can be a control ... not, aquaporins appeared complete. We ve going on it and well be it used not accurately as we can. Your Web content is not ... If we need refried books that m aquaporins of EU-US Privacy Shield, we may be accounts to them, as they apply online ...
Learn about Aquaporin 4 at online-medical-dictionary.org ... Aquaporin 4 is the major water-selective channel in the CENTRAL ...
The design of aquaporin library was performed with implementation of two different approaches: flexible docking and high ... The library was designed to find molecules which target both end-chains of water channels (Aquaporins) AQ1, AQ4, AQ5 monomers ...
aquaporin Z [Klebsiella quasipneumoniae] aquaporin Z [Klebsiella quasipneumoniae]. gi,1320058681,gb,PLN00049.1,,gnl,WG H,CWN07_ ...
Invitrogen Anti-Aquaporin 4 Polyclonal, Catalog # PA5-77716. Tested in Western Blot (WB), Immunocytochemistry (ICC/IF) and ...
Meng JH, Ma XC, Li ZM and Wu DC: Aquaporin-1 and aquaporin-3 expressions in the temporo-mandibular joint condylar cartilage ... Aquaporin 1 (AQP1) is a 28‑kDa water channel formed of six transmembrane domains on the cell membrane. AQP1 is highly expressed ... Gao H, Gui J, Wang L, Xu Y, Jiang Y, Xiong M and Cui Y: Aquaporin 1 contributes to chondrocyte apoptosis in a rat model of ... In mammals, the aquaporin (AQP) family consists of thirteen subtypes (AQP0 to 12) and these proteins are expressed in various ...
... all such models are associated with the loss of aquaporin-2 (AQP2) from collecting duct principal cells, explaining the ... Aquaporin-omics: mechanisms of aquaporin-2 loss in polyuric disorders Angela Mak 1 , Chih-Chien Sung 2 , Trairak Pisitkun 1 3 ... Aquaporin-omics: mechanisms of aquaporin-2 loss in polyuric disorders Angela Mak et al. J Physiol. 2023. . ... An impaired routing of wild-type aquaporin-2 after tetramerization with an aquaporin-2 mutant explains dominant nephrogenic ...
Aquaporin-regulated response of grapevine roots to salinity. AVF Proj. ID: 434 / Year Posted: 2009. /Cat.: Cultural Control, ... Aquaporins are found throughout fine root cellular membranes and can control the efficiency of water extraction from the soil. ... Aquaporin gene expression in numerous rootstocks (Ramsey, Riparia, French Colombard, Thompson seedless, 420A, 101-14, 110R, 039 ... In our grant, we proposed to address the following short-intermediate term goals: 1) to quantify aquaporin response to salinity ...
Electron crystallographic structure of lens Aquaporin-0 (AQP0) (lens MIP) at 1.9A resolution, in a closed pore state ... Lens-specific aquaporin-0 (AQP0) functions as a specific water pore and forms the thin junctions between fibre cells. Here we ... Lens-specific aquaporin-0 (AQP0) functions as a specific water pore and forms the thin junctions between fibre cells. Here we ... Electron crystallographic structure of lens Aquaporin-0 (AQP0) (lens MIP) at 1.9A resolution, in a closed pore state. *PDB DOI ...
Four aquaporins (the aquaglyceroporins AQP3, AQP7, AQP9, AQP10) conduct glycerol, three aquaporins (AQP7, AQP9, AQP10) conduct ... During passive transport by Aquaporins most aquaporins (i.e. AQP0/MIP, AQP1, AQP2, AQP3, AQP4, AQP5, AQP7, AQP8, AQP9, AQP10) ... Passive transport by Aquaporins), a view of the role of specific aquaporins in maintenance of renal water balance (Vasopressin ... Aquaporins in the kidney: from molecules to medicine Marples, D, Knepper, MA, Kwon, TH, Nielsen, S, Agre, P, Frøkiaer, J ...
About Aquaporin. Aquaporin is an innovative water technology company dedicated to preserving the worlds most valuable resource ... With the Aquaporin Inside® membranes, Aquaporin empowers industries to treat and recycle wastewater, paving the way for a ... Aquaporins proprietary technology, Aquaporin Inside®, is based on Nobel Prize-winning research and embedded in all their ... The use of Aquaporins membranes within Forward Waters industrial forward osmosis systems has the potential to deliver a new ...
Regulation of Neuromyelitis Optica via Tolerance Induced by PLG Nanoparticles Encapsulating Aquaporin 4 Epitopes. *Miller, ... autoimmune demyelinating disease of the spinal cord and optic nerve mediated by T cell and antibody responses to aquaporin-4 ( ...
A comparison was made in the TR response to aquaporin (AQP) inhibitors between PI 416937 and N01-11136, a commercial genotype ... Transpiration response of slow-wilting and commercial soybean (Glycine max (L.) Merr.) genotypes to three aquaporin ...
Eucerin Aquaporin Active, vlažilna nega za normalno do mešano kožo je osvežujoč vlažilni izdelek za obraz, ki pomaga ... Eucerin Aquaporin Active, vlažilna nega za normalno do mešano kožo, 50 ml. ... Eucerin Aquaporin Active, vlažilna nega za normalno do mešano kožo je osvežujoč vlažilni izdelek za obraz, ki pomaga izboljšati ... Domov Kozmetika Eucerin Aquaporin Active, vlažilna nega za normalno do mešano kožo, 50 ml ...
The aquaporins represent a family of transmembrane water channel proteins that play a major role in trans-cellular and ... Aquaporin 1 is overexpressed in lung cancer and stimulates NIH-3T3 cell proliferation and anchorage-independent growth.. ... by reverse transcriptase-polymerase chain reaction and Western blot analysis and identified clear expression of aquaporin 1 ( ...
Aquaporins in Glandular Secretion. Calamita, Giuseppe; Delporte, Christine. Afiliação *Calamita G; Department of Biosciences, ... The release of their products has been shown to rely on secretory mechanisms often involving aquaporins (AQPs). This chapter ...
The technical storage or access is strictly necessary for the legitimate purpose of enabling the use of a specific service explicitly requested by the subscriber or user, or for the sole purpose of carrying out the transmission of a communication over an electronic communications network. ...
Beschermd de huid tegen transepidermaal vochtverlies en verhoogt het hydratatieniveau. Avocado-, olijf-, en macadamianotenolie hydrateren de droge, schilferende huid opnieuw en kalmeert irritatie, terwijl vitamine E beschermt tegen vrije radicalen.
Aquaporins, also known as water channels, form pores in cell membranes and selectively transport water in and out of the cell. ... Aquaporin 2 (AQP2) is located in the collecting duct of the kidney, and is regulated by the peptide hormone vasopressin. AQP2 ... Aquaporins are involved in regulation of water balance and blood pressure, and thirteen different isoforms have been found in ...
The metal applicator that the product is squeezed through at the end of the tube feels very cooling on the skin which I think aids in reducing puffiness. I do find that it can be a little hard to control the amount of product that comes out so I tend to squeeze a bit out before pressing it onto my skin and smoothing under the eyes. I end up using my finger to smooth excess product into my skin and to wipe the metal part of the tube as it does end up with cream around it. ...
Red blood cell aquaporin-1 expression is decreased in hereditary spherocytosis. Ann Hematol. 2016 Oct. 95 (10):1595-601. [QxMD ... Aquaporin-1. In addition to abnormal levels of proteins affected by mutations, patients with HS may demonstrate aberrant ... Crisp et al found reduced expression of the water channel protein aquaporin-1 (AQP1) in the membranes of erythrocytes from ...
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Eucerin Aquaporin ACTIVE with SPF 25 and UVA protection is an innovative face moisturizer that enhances the skins own hydration ... Eucerin Aquaporin ACTIVE is clinically and dermatologically proven to be compatible with sensitive skin and is fragrance and ... The velvety texture of Eucerin Aquaporin ACTIVE with SPF 25 and UVA protection for all skin types provides intense, 24-hour ...
Aquaporin 9 (AQP9) is an essential aquaporin in the liver and located in the basolateral membrane of hepatocytes, but its roles ... Aquaporin 9 (AQP9) is an essential aquaporin in the liver and located in the basolateral membrane of hepatocytes, but its roles ... Aquaporin 9 inhibits growth and metastasis of hepatocellular carcinoma cells via Wnt/β-catenin pathway. Aging (Albany NY). 2020 ... Aquaporin 9 inhibits growth and metastasis of hepatocellular carcinoma cells via Wnt/β-catenin pathway ...
2 is a plasma membrane aquaporin, Q9MB99, AS09 490, plant aquaporin antibody ... PIP2;2 , Plasma membrane aquaporin 2b AS09 490 , Clonality: Polyclonal , Host: Rabbit , Reactivity: Arabidopsis thaliana, ... Home / Antibodies Plant/Algal / Membrane Transport System / Plasma membrane / Anti-PIP2;2 , plasma membrane aquaporin 2b ... Related products: PIP2;2 , Plasma membrane aquaporin 2b Agrisera ECL kit (Bright/SuperBright) ...
Central Nervous System Aquaporin 4. Central Nervous System Aquaporin 4 - Manufacturers, Factory, Suppliers. Our pursuit and ...
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Heart and lung aquaporins play a major role in severity of heart failure with preserved ejection fraction in mice and differs ...
  • Animal models of a variety of acquired nephrogenic diabetes insipidus (NDI) disorders have identified a common feature: all such models are associated with the loss of aquaporin-2 (AQP2) from collecting duct principal cells, explaining the associated polyuria. (nih.gov)
  • Vasopressin regulates renal water homeostasis via Aquaporins by regulating the permeability of the epithelium through activation of a signaling cascade leading to the phosphorylation of AQP2 and its translocation from intracellular vesicles to the apical membrane of collecting duct cells. (reactome.org)
  • Aquaporin 2 (AQP2) is located in the collecting duct of the kidney, and is regulated by the peptide hormone vasopressin. (nih.gov)
  • Eucerin Aquaporin Active, vlažilna nega za normalno do mešano kožo je osvežujoč vlažilni izdelek za obraz, ki pomaga izboljšati koži lasten sistem vlaženja, kožo pa naredi voljno, gladko in sijočo. (lekarnaljubljana.si)
  • Eucerin Aquaporin Active Uv Rich Crea. (docibonline.com)
  • Eucerin Aquaporin ACTIVE with SPF 25 and UVA protection is an innovative face moisturizer that enhances the skins own hydration system to leave skin supple, smooth and radiant. (docibonline.com)
  • The velvety texture of Eucerin Aquaporin ACTIVE with SPF 25 and UVA protection for all skin types provides intense, 24-hour hydration and is easily absorbed by the skin. (docibonline.com)
  • Eucerin Aquaporin ACTIVE is clinically and dermatologically proven to be compatible with sensitive skin and is fragrance and paraben-free. (docibonline.com)
  • In mammals, the aquaporin (AQP) family consists of thirteen subtypes (AQP0 to 12) and these proteins are expressed in various tissues ( 9 ). (spandidos-publications.com)
  • Lens-specific aquaporin-0 (AQP0) functions as a specific water pore and forms the thin junctions between fibre cells. (rcsb.org)
  • Aquaporin proteins form water channels between cells and are found in many tissues, but aquaporin zero (AQP0) is found only in the mammalian lens, which focuses light onto the retina, at the back of the eye. (nih.gov)
  • Aquaporin 1 (AQP1) is a 28‑kDa water channel formed of six transmembrane domains on the cell membrane. (spandidos-publications.com)
  • Aquaporin-1 (AQP1) in the proximal tubule and the descending thin limb of Henle is responsible for about 90% of reabsorption (as estimated from mouse knockouts of AQP1). (reactome.org)
  • Here, we tested 10 non-small cell lung cancer cell lines of various origins by reverse transcriptase-polymerase chain reaction and Western blot analysis and identified clear expression of aquaporin 1 (AQP1) in seven cell lines. (nih.gov)
  • AQP1 KO = aquaporin 1 knockout, dehyd = dehydration, furos = furosemide. (nih.gov)
  • AQP4 is a devastating autoimmune demyelinating disease of the spinal cord and optic nerve mediated by T cell and antibody responses to aquaporin-4 (AQP4). (northwestern.edu)
  • The aquaporin-4 protein (AQP4), a normal protein in the body, plays a role in neuromyelitis optica. (nih.gov)
  • The treatment of neuromyelitis optica spectrum disorder (NMOSD) in adult patients who are anti-aquaporin-4 (AQP4) antibody positive ( 1.4 ). (nih.gov)
  • During Transport of glycerol from adipocytes to the liver by Aquaporins, glycerol generated by triglyceride hydrolysis is exported from adipocytes by AQP7 and is imported into liver cells via AQP9. (reactome.org)
  • In the second edition of Dry Skin and Moisturizers-Chemistry and Function of Marie Lodén and Howard Maibach, published in 2006, there are only two references in the index to aquaporin-3, the epidermal water/glycerol transporter. (cosmeticsandtoiletries.com)
  • 3. Aquaporins and glycerol metabolism. (nih.gov)
  • 4. Metabolic impact of adipose and hepatic glycerol channels aquaporin 7 and aquaporin 9. (nih.gov)
  • 9. Adaptation to fasting by glycerol transport through aquaporin 7 in adipose tissue. (nih.gov)
  • 10. Physiological roles of glycerol-transporting aquaporins: the aquaglyceroporins. (nih.gov)
  • 20. Biophysical assessment of human aquaporin-7 as a water and glycerol channel in 3T3-L1 adipocytes. (nih.gov)
  • Approximately 70 percent of people with this disorder produce an immune protein called an antibody that attaches (binds) to the aquaporin-4 protein. (nih.gov)
  • See the reference protein sequence for MULTISPECIES: aquaporin Z (WP_004201355.1). (nih.gov)
  • The aquaporin-4 protein is found in several body systems but is most abundant in tissues of the central nervous system. (nih.gov)
  • The viral vector deposits DNA into glandular cells & instructs them to produce aquaporin protein (green). (nih.gov)
  • When infused into the salivary gland, the viral vector deposits aquaporin DNA into glandular cells and instructs them to start producing the protein. (nih.gov)
  • Aquaporins, also known as water channels, form pores in cell membranes and selectively transport water in and out of the cell. (nih.gov)
  • Found throughout nature, aquaporin water channels confer high water permeability to cell membranes. (nih.gov)
  • Water from the bloodstream flows across the acinar cells through pore-forming proteins called aquaporins in the cell membranes. (nih.gov)
  • 6. Aquaglyceroporins and orthodox aquaporins in human adipocytes. (nih.gov)
  • Aquaporins (AQP's) are six-pass transmembrane proteins that form channels in membranes. (reactome.org)
  • The aquaporins represent a family of transmembrane water channel proteins that play a major role in trans-cellular and transepithelial water movement. (nih.gov)
  • Baum guessed that delivering a gene for one of the pore-forming proteins, called aquaporin 1, into damaged salivary glands might enable existing cells to transport water and restore saliva production. (nih.gov)
  • Aquaporin 9 (AQP9) is an essential aquaporin in the liver and located in the basolateral membrane of hepatocytes, but its roles on HCC has not been completely elucidated. (aging-us.com)
  • Aquaporin-4 autoantibody associated neuromyelitis optica , a disorder that affects the eye nerves and spinal cord. (nih.gov)
  • Radiation damages or kills acinar cells, leaving mostly duct cells, which lack aquaporins and can't secrete water. (nih.gov)
  • Aquaporin 4 is the major water -selective channel in the CENTRAL NERVOUS SYSTEM of mammals . (online-medical-dictionary.org)
  • Aquaporins are involved in regulation of water balance and blood pressure, and thirteen different isoforms have been found in mammals. (nih.gov)
  • The library was designed to find molecules which target both end-chains of water channels (Aquaporins) AQ1, AQ4, AQ5 monomers and internal central pore of AQ5, that possess same physico-chemical properties as those in AQ1 and AQ4. (enamine.net)
  • Much of the focus is on regulation of molecular water channels called "aquaporins" by the hormone vasopressin. (nih.gov)
  • Liao S , Chen H , Liu M , Gan L , Li C , Zhang W , Lv L , Mei Z , . Aquaporin 9 inhibits growth and metastasis of hepatocellular carcinoma cells via Wnt/β-catenin pathway. (aging-us.com)
  • The team eventually showed that the aquaporin 1 gene therapy worked to restore saliva flow in radiation-damaged glands of rats and miniature pigs. (nih.gov)
  • The release of their products has been shown to rely on secretory mechanisms often involving aquaporins (AQPs). (bvsalud.org)
  • Aquaporin 1 is overexpressed in lung cancer and stimulates NIH-3T3 cell proliferation and anchorage-independent growth. (nih.gov)
  • With the Aquaporin Inside® membranes, Aquaporin empowers industries to treat and recycle wastewater, paving the way for a future with zero liquid discharge. (agoracom.com)
  • A viral vector carrying aquaporin 1 gene is infused into a salivary gland via a thin tube. (nih.gov)
  • 7. Role of aquaporin-7 in the pathophysiological control of fat accumulation in mice. (nih.gov)
  • Aquaporins are important in fluid and solute transport in various tissues. (reactome.org)
  • If we need refried books that 'm aquaporins of EU-US Privacy Shield, we may be accounts to them, as they apply online properties in F. If keine of the Mathematical Jews receives specific, we may Bend your several request to the American Javascript. (scheinerman.net)
  • You are Flash aquaporins recent and shoe thought to make this milling dismissed. (scheinerman.net)
  • aquaporin-3 (AQP-3) is being reviewed and we learn that it is involved in skin hydration, wound healing and skin tumorigenesis. (cosmeticsandtoiletries.com)
  • Aquaporins are particularly important in plant biology. (nih.gov)
  • Forward Water will distribute the Aquaporin Inside® Hollow Fiber Forward Osmosis products in the Oil & Gas and mining sectors including lithium-related applications in North America. (agoracom.com)
  • Sheleg centuries understood to a sure aquaporins of new free food for correct strategies of Australia own turbulent tri-saccharides may analyze reasonable for a protection of postcards within Australia, asking ErrorDocument to our enough topic organization and sunburnt depression. (scheinerman.net)
  • Jonah Scheinerman's Website For aquaporins times, treat use our Marketing Coordinator, Sarah Cannon. (scheinerman.net)
  • This illustration shows two views of a single unit of the aquaporin-0 channel. (nih.gov)
  • Aquaporin's proprietary technology, Aquaporin Inside®, is based on Nobel Prize-winning research and embedded in all their membranes. (agoracom.com)