Aquaporins
Aquaporin 1
Aquaporin 5
Aquaporin 4
Water
Aquaporin 6
Aquaglyceroporins
Aquaporin 2
Mercuric Chloride
Osmosis
Plant Transpiration
Water-Electrolyte Balance
Plant Proteins
Permeability
Glycerol
Kidney Concentrating Ability
Biological Transport
Cistaceae
Plant Roots
Tulipa
Cell Membrane Permeability
Blood Group Antigens
Gene Expression Regulation, Plant
Trichomes
Calotropis
Molecular Sequence Data
Osmotic Pressure
Amino Acid Sequence
4-Chloromercuribenzenesulfonate
Cell Membrane
Ion Channels
Plant Leaves
Acoustic Maculae
Pulvinus
Spinacia oleracea
Exocrine Glands
Polyuria
Tephritidae
Kidney Tubules, Collecting
Brain Edema
Xenopus laevis
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.
Aquaporin
Aquaporin-3
Aquaporin-7
Aquaporin-9
Aquaporin-1
Aquaporin-6
Aquaporin-5
Aquaporin-4
Aquaporin-8
Aquaporin-2
Astrogliosis
Major intrinsic proteins
Randy Wayne (biologist)
Tachyon (software)
Ruth Lyttle Satter
Syndrome of inappropriate antidiuretic hormone secretion
Masashi Tazawa
Kidney (vertebrates)
Transmembrane channels
Primary effusion lymphoma
Cation-chloride cotransporter
Blastulation
Peter Agre
Semipermeable membrane
Glymphatic system
Neuromyelitis optica spectrum disorder
Balo concentric sclerosis
Blood-Spinal Cord Barrier
Arabidopsis thaliana responses to salinity
Vasopressin
Aquaporins
Aquaporin 4 - Medical Dictionary online-medical-dictionary.org
Aquaporins Library - Enamine
aquaporin Z [Klebsiella quasipneumoniae] - Protein - NCBI
Aquaporin 4 Polyclonal Antibody (PA5-77716)
Depletion of aquaporin 1 decreased ADAMTS‑4 expression in human chondrocytes
'Aquaporin-omics': mechanisms of aquaporin-2 loss in polyuric disorders -...
Aquaporin-regulated response of grapevine roots to salinity - American Vineyard Foundation
RCSB PDB - 2B6O: Electron crystallographic structure of lens Aquaporin-0 (AQP0) (lens MIP) at 1.9A resolution, in a closed pore...
Reactome | Aquaporin-mediated transport
Agoracom: Small Cap Investment - Forward Water Technologies Corp. - Forward Water Technologies Corp. and Aquaporin Announce...
Regulation of Neuromyelitis Optica via Tolerance Induced by PLG Nanoparticles Encapsulating Aquaporin 4 Epitopes -...
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, 50 ml - Spletna Lekarna Ljubljana
Aquaporin 1 is overexpressed in lung cancer and stimulates NIH-3T3 cell proliferation and anchorage-independent growth.
Aquaporins in Glandular Secretion. | Adv Exp Med Biol;1398: 225-249, 2023. | MEDLINE
English
AquaPorin Hydrating Cream - Cherish Yourself
Aquaporin 2 Polyclonal Antibodies | Technology Transfer
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Hereditary Spherocytosis: Practice Essentials, Pathophysiology, Etiology
S AQUAPORIN 4 At - Laboratorija Zdravlje
Eucerin Aquaporin Active Uv Rich Cream 50Ml
Aquaporin 9 inhibits growth and metastasis of hepatocellular carcinoma cells via Wnt/β-catenin pathway | Aging
Anti-PIP2;2 | plasma membrane aquaporin 2b antibodies
Central Nervous System Aquaporin 4 - Manufacturers, Factory, Suppliers
Aquaporin 4 Antibodies (Neuromyelitis Optica) | Health Services Laboratories
AQP23
- 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 Active5
- 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)
AQP03
- 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)
AQP14
- 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)
AQP43
- 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)
Glycerol7
- 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)
Antibody1
- 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)
Protein4
- 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)
Cell membranes3
- 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)
Aquaglyceroporins1
- 6. Aquaglyceroporins and orthodox aquaporins in human adipocytes. (nih.gov)
Proteins3
- 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)
AQP91
- 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)
Autoantibody1
- Aquaporin-4 autoantibody associated neuromyelitis optica , a disorder that affects the eye nerves and spinal cord. (nih.gov)
Acinar cells1
- Radiation damages or kills acinar cells, leaving mostly duct cells, which lack aquaporins and can't secrete water. (nih.gov)
Mammals2
- 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)
Monomers1
- 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)
Vasopressin1
- Much of the focus is on regulation of molecular water channels called "aquaporins" by the hormone vasopressin. (nih.gov)
Cells1
- 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)
Saliva1
- 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)
Mechanisms1
- The release of their products has been shown to rely on secretory mechanisms often involving aquaporins (AQPs). (bvsalud.org)
Lung1
- Aquaporin 1 is overexpressed in lung cancer and stimulates NIH-3T3 cell proliferation and anchorage-independent growth. (nih.gov)
Recycle1
- 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)
Gene1
- A viral vector carrying aquaporin 1 gene is infused into a salivary gland via a thin tube. (nih.gov)
Role1
- 7. Role of aquaporin-7 in the pathophysiological control of fat accumulation in mice. (nih.gov)
Fluid1
- Aquaporins are important in fluid and solute transport in various tissues. (reactome.org)
Specific1
- 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)
Recent1
- You are Flash aquaporins recent and shoe thought to make this milling dismissed. (scheinerman.net)
Skin1
- aquaporin-3 (AQP-3) is being reviewed and we learn that it is involved in skin hydration, wound healing and skin tumorigenesis. (cosmeticsandtoiletries.com)
Important1
- Aquaporins are particularly important in plant biology. (nih.gov)
Products1
- 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)
Free1
- 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)
Treat1
- Jonah Scheinerman's Website For aquaporins times, treat use our Marketing Coordinator, Sarah Cannon. (scheinerman.net)
Views1
- This illustration shows two views of a single unit of the aquaporin-0 channel. (nih.gov)
Research1
- Aquaporin's proprietary technology, Aquaporin Inside®, is based on Nobel Prize-winning research and embedded in all their membranes. (agoracom.com)