TY - JOUR. T1 - Aquaporin water channels - From atomic structure to clinical medicine. AU - Agre, Peter. AU - King, Landon S.. AU - Yasui, Masato. AU - Guggino, Wm B.. AU - Ottersen, Ole Petter. AU - Fujiyoshi, Yoshinori. AU - Engel, Andreas. AU - Nielsen, Søren. PY - 2002/7/1. Y1 - 2002/7/1. N2 - The water permeability of biological membranes has been a longstanding problem in physiology, but the proteins responsible for this remained unknown until discovery of the aquaporin 1 (AQP1) water channel protein. AQP1 is selectively permeated by water driven by osmotic gradients. The atomic structure of human AQP1 has recently been defined. Each subunit of the tetramer contains an individual aqueous pore that permits single-file passage of water molecules but interrupts the hydrogen bonding needed for passage of protons. At least 10 mammalian aquaporins have been identified, and these are selectively permeated by water (aquaporins) or water plus glycerol (aquaglyceroporins). The sites of expression ...

TY - JOUR. T1 - Expression and subcellular localization of aquaporin water channels in the polarized hepatocyte cell line, WIF-B. AU - Gradilone, Sergio A.. AU - Tietz, Pamela S.. AU - Splinter, Patrick L.. AU - Marinelli, Raúl A.. AU - LaRusso, Nicholas F.. PY - 2005/8/18. Y1 - 2005/8/18. N2 - Background: Recent data suggest that canalicular bile secretion involves selective expression and coordinated regulation of aquaporins (AQPs), a family of water channels proteins. In order to further characterize the role of AQPs in this process, an in vitro cell system with retained polarity and expression of AQPs and relevant solute transporters involved in bile formation is highly desirable. The WIF-B cell line is a highly differentiated and polarized rat hepatoma/human fibroblast hybrid, which forms abundant bile canalicular structures. This cell line has been reported to be a good in vitro model for studying hepatocyte polarity. Results: Using RT-PCR, immunoblotting and confocal immunofluorescence, ...

Purpose: The expression of aquaporin water channel genes are shown to be affected in several pathological conditions of retina, such as in diabetic retinopathy, retinal ischemia and in autoimmune uveitis. Human native retinal pigment epithelial (RPE) cells and immortalized human RPEs are formerly shown to express aquaporins, still the expression of aquaporins in stem cell derived RPE have not been previously elucidated. The objective of this study was to determine the expression of several aquaporin genes (aquaporin1,- 3, -4, -5, -6, -7, -10, -11 and -12) and assess the localization of aquaporin 1 water channel protein in human embryonic (hESCs) and induced pluripotent stem cells (hiPSCs) derived RPE cells.. Methods: hESC- and hiPSC derived RPE cells were grown as monolayer in serum-free media. The expression of aquaporin genes was determined with qRT-PCR. The localization of AQP1-protein was studied with confocal microscopy. Finally, the functionality of aquaporins was assessed with dye ...

Aquaporin-5 is a protein that in humans is encoded by the AQP5 gene. Aquaporin 5 (AQP5) is a water channel protein. Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). Aquaporin 5 plays a role in the generation of saliva, tears and pulmonary secretions. AQP0, AQP2, AQP5, and AQP6 are closely related and all map to 12q13. Aquaporin GRCh38: Ensembl release 89: ENSG00000161798 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000044217 - Ensembl, May 2017 Human PubMed Reference:. Mouse PubMed Reference:. Lee MD, Bhakta KY, Raina S, Yonescu R, Griffin CA, Copeland NG, Gilbert DJ, Jenkins NA, Preston GM, Agre P (Jun 1996). The human Aquaporin-5 gene. Molecular characterization and chromosomal localization. J Biol Chem. 271 (15): 8599-604. doi:10.1074/jbc.271.15.8599. PMID 8621489. Entrez Gene: AQP5 aquaporin 5. Verkman AS (2003). Role of aquaporin water channels in eye function. Exp. Eye Res. 76 (2): 137-43. ...

Abstract Background and Aims Diarrhoea is a common, debilitating symptom of gastrointestinal disorders. Pathomechanisms probably involve defects in trans-epithelial water transport, but the role of aquaporin [AQP] family water channels in diarrhoea-predominant diseases is unknown. We investigated the involvement of AQPs in the pathobiology of collagenous colitis [CC], which features chronic, watery diarrhoea despite overtly normal intestinal epithelial cells [IECs]. Methods We assessed the expression of all AQP family members in mucosal samples of CC patients before and during treatment with the corticosteroid drug budesonide, steroid-refractory CC patients and healthy controls. Samples were analysed by genome-wide mRNA sequencing [RNA-seq] and quantitative real-time PCR [qPCR]. In some patients, we performed tissue microdissection followed by RNA-seq to explore the IEC-specific CC transcriptome. We determined changes in the protein levels of the lead candidates

Plant cells contain proteins that are members of the major intrinsic protein (MIP) family, an ancient family of membrane channel proteins characterized by six membrane-spanning domains and two asparagine-proline-alanine (NPA) amino acid motifs in the two halves of the protein. We recently demonstrated that [gamma]-TIP, one of the MIP homologs found in the vacuolar membrane of plant cells, is an aquaporin or water channel protein (C. Maurel, J. Reizer, J.I. Schroeder, M.J. Chrispeels [1993] EMBO J 12: 2241-2247). RD28, another MIP homolog in Arabidopsis thaliana, was first identified as being encoded by a turgor-responsive transcript. To find out if RD28 is a water channel protein, rd28 cRNA was injected into Xenopus laevis oocytes. Expression of RD28 caused a 10- to 15-fold increase in the osmotic water permeability of the oocytes, indicating that the protein creates water channels in the plasma membrane of the oocytes and is an aquaporin just like its homolog [gamma]-TIP. Although RD28 has ...

The pre-ovulatory hydration of the oocyte of marine teleosts, a unique process among vertebrates that occurs concomitantly with meiosis resumption (oocyte maturation), is a critical process for the correct development and survival of the embryo. Increasing information is available on the molecular mechanisms that control oocyte maturation in fish, but the identification of the cellular processes involved in oocyte hydration has remained long ignored. During the past few years, a number of studies have identified the major inorganic and organic osmolytes that create a transient intra-oocytic osmotic potential for hydrating the oocytes, whereas water influx was believed to occur passively. Recent work, however, has uncovered the role of a novel molecular water channel (aquaporin), designated aquaporin-1b (Aqp1b), which facilitates water permeation and resultant swelling of the oocyte. The Aqp1b belongs to a teleost-specific subfamily of water-selective aquaporins, similar to mammalian aquaporin-1 ...

Semantic Scholar extracted view of Aquaporin water channels in liver: their significance in bile formation. by Raúl Alberto Marinelli et al.

Aquaporin membrane protein, molecular model. Computer illustration showing the structure of a molecule of the human aquaporin 1 protein (blue, and white ribbon). Aquaporins are membrane proteins that form channels (centre) that help water molecules (red and white spheres) pass in and out of cells. Unlike ion channels, aquaporins help prevent ions and other dissolved substances carrying electrical charge from entering the cell, as they only allow lone water molecules or certain uncharged solutes to pass through. This helps maintain the electrochemical potential of the cell membrane. - Stock Image C035/5236

Author(s): Chen, Qi; Peng, Hongying; Lei, Li; Zhang, Ying; Kuang, Haibin; Cao, Yujing; Shi, Qi-Xian; Ma, Tonghui; Duan, Enkui | Abstract: In the journey from the male to female reproductive tract, mammalian sperm experience a natural osmotic decrease (e.g., in mouse, from ~415 mOsm in the cauda epididymis to ~310 mOsm in the uterine cavity). Sperm have evolved to utilize this hypotonic exposure for motility activation, meanwhile efficiently silence the negative impact of hypotonic cell swelling. Previous physiological and pharmacological studies have shown that ion channel-controlled water influx/efflux is actively involved in the process of sperm volume regulation; however, no specific sperm proteins have been found responsible for this rapid osmoadaptation. Here, we report that aquaporin3 (AQP3) is a sperm water channel in mice and humans. Aqp3-deficient sperm show normal motility activation in response to hypotonicity but display increased vulnerability to hypotonic cell swelling, characterized by

TY - JOUR. T1 - Identification of a novel aquaporin, AQP12, expressed in pancreatic acinar cells. AU - Itoh, Tomohiro. AU - Rai, Tatemitsu. AU - Kuwahara, Michio. AU - Ko, Shigeru B.H.. AU - Uchida, Shinichi. AU - Sasaki, Sei. AU - Ishibashi, Kenichi. N1 - Funding Information: We thank N. Ozaki (Nagoya university, Japan) for his skillful technical assistance in isolation of pancreatic islet. This work was supported by grants from the Ministry of Education, Culture, Sports, Science and Technology of Japan.. PY - 2005/5/13. Y1 - 2005/5/13. N2 - Members of the aquaporin (AQP) water channel family are widely distributed in various tissues and contribute to the water permeability of epithelial and endothelial cells. Currently 11 members of the AQP family (AQP0-10) have been reported in mammals. Here we report the identification of AQP12, which we found by performing a BLAST program search. Northern blot analysis revealed that AQP12 was specifically expressed in the pancreas. Further analysis by in ...

Aquaporins (AQPs) are membrane proteins that enable water transport across cellular plasma membranes in response to osmotic gradients. Phenotypic analyses have revealed important physiological roles for AQPs, and the potential for AQP water channel modulators in various disease states has been proposed. For example, AQP1 is overexpressed in tumor microvessels, and this correlates with higher metastatic potential and aggressiveness of the malignancy. Chemical modulators would help in identifying the precise contribution of water channel activity in these disease states. These inhibitors would also be important therapeutically, e.g., in anti-cancer treatment. This perceived importance contrasts with the lack of success of high-throughput screens (HTS) to identify effective and specific inhibitors of aquaporins. In this paper, we have screened a library of 1500

Aquaporin (AQP) 6 belongs to the aquaporin water channel family. Unlike other aquaporins, AQP6 functions not as a water channel but as an anion-selective channel. Single-channel analyses have shown AQP6 to flicker rapidly ...

Aquaporin (AQP) 6 belongs to the aquaporin water channel family. Unlike other aquaporins, AQP6 functions not as a water channel but as an anion-selective channel. Single-channel analyses have shown AQP6 to flicker rapidly ...

Aquaporins facilitate the diffusion of water across cell membranes. We previously showed that acid pH or low Ca2+ increase the water permeability of bovine AQP0

Aquaporin 8 (AQP8) is a water channel protein. Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). Aquaporin 8 mRNA is found in pancreas and colon but not other tissues. [provided by RefSeq, Jul 2008 ...

Purpose: : To demonstrate in the conjunctiva the presence of aquaporin type 5 (AQP5), a water channel homologue found in the apical membrane of several tissues including the cornea. Presently, there are no reports indicating as to which AQP might be expressed apically in the conjunctiva; only AQP3 has been identified in the lateral membranes of rat and human conjunctival epithelia. Because we had data from gene-expression microarray assays (Turner; ARVO 2004) indicating message for AQP5 in the human conjunctiva, tissue samples from human, as well as from rats and rabbits (given the ease of their procurement), were analyzed to confirm that the AQP5 protein was indeed expressed in mammalian conjunctivae. Methods: : Goat polyclonal IgG against AQP5 was purchased commercially and used in immunoblotting and immunohistochemical techniques to identify and localize the water channel in rat, rabbit and human epithelia. Results: : Immunoblot analysis of rabbit bulbar-plus-palpebral plasma membrane ...

Aquaporin A/S is a global cleantech company located in Kongens Lyngby, Denmark. Aquaporin is dedicated to revolutionizing water purification through the use of industrial biotechn

Peptides , Phosphopeptides , Aquaporin-2 (254-267), pSER261, human; This peptide is a fragment of the human aquaporin-2 (AQP2) phosphorylated at Ser261. Protein phosphorylation plays a key role in vasopressin signaling in renal-collecting duct. Phosphorylation at several AQP2 residues including Ser256 and Ser261, is altered in response to vasopressin. It is possible that both sites are involved in vasopressin-dependent AQP2 trafficking.; RQSVELH-pS-PQSLPR; H-Arg-Gln-Ser-Val-Glu-Leu-His-pSer-Pro-Gln- Ser-Leu-Pro-Arg-OH

The researchers showed that this technique was successful in monitoring gene expression in a brain tumor in mice. After implanting the tumor, they gave the mice a drug to trigger the tumor cells to express the aquaporin reporter gene, which made the tumor look darker in MRI images.. Overexpression of aquaporin has no negative impact on cells because it is exclusive to water and simply allows the molecules to go back and forth across the cell membrane, Shapiro says. Under normal physiological conditions the number of water molecules entering and exiting an aquaporin-expressing cell is the same, so that the total amount of water in each cell does not change. Aquaporin is a very convenient way to genetically change the way that cells look under MRI.. Though the work was done in mice, it has the potential for clinical translation, according to Shapiro. Aquaporin is a naturally occurring gene and will not cause an immune reaction. Previously developed reporter genes for MRI have been much more ...

Kit contents: 1. MICROTITER PLATE * 1 2. ENZYME CONJUGATE*1 vial 3. STANDARD A*1 vial 4. STANDARD B*1 vial 5. STANDARD C*1 vial 6. STANDARD D*1 vial 7. STANDARD E*1 vial 8. STANDARD F*1 vial 9. SUBSTRATE A*1 vial 10. SUBSTRATE B*1 vial 11. STOP ...

Kit contents: 1. MICROTITER PLATE * 1 2. ENZYME CONJUGATE*1 vial 3. STANDARD A*1 vial 4. STANDARD B*1 vial 5. STANDARD C*1 vial 6. STANDARD D*1 vial 7. STANDARD E*1 vial 8. STANDARD F*1 vial 9. SUBSTRATE A*1 vial 10. SUBSTRATE B*1 vial 11. STOP ...

C. elegans AQP-4 protein; contains similarity to Pfam domain PF00230 (Major intrinsic protein)contains similarity to Interpro domains IPR000425 (Major intrinsic protein), IPR012269 (Aquaporin ...

InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.

collections, groups of modules structured into books or course notes, or for other uses. Our open license allows for free use and reuse of all our content. ...

Significant progress in the understanding of imaging conditions and the interpretation of topographs recorded with the AFM has allowed the surface topography of bacteriorhodopsin to be correlated with the helixconnecting loops to a lateral resolution of 5 Å (Müller et al., 1999b). Here we have used this technology to study the surface of AqpZ, the first bacterial water channel identified (Calamita et al., 1995). Its overexpression, isolation and 2D crystallization have recently been described (Borgnia et al., 1999; Ringler et al., 1999).. 2D crystals adsorbed firmly and without folds or wrinkles to freshly cleaved mica in a high ionic strength buffer (Müller et al., 1997). Subsequent change to a buffer adjusted to compensate for van der Waals interactions allowed their height to be measured accurately (Müller and Engel, 1997). The result, 57 ± 4 Å, compares favorably with the height previously reported for AQP1, 58 ± 3 Å (Walz et al., 1996).. The p4212 crystals of AqpZ with unit cell ...

Marinelli RA, Pham L, Agre P, La Russo NF. Secretin promotes osmotic water transport in rat cholangiocytes by incresing aquaporin-1 water channels in plasma membrane. Evidence for a secretin-induced vesicular translocation of aquaporin-1. J Biol Chem 1997; 272: 12984-12988 ...

Aquaporins are a family of water channel proteins that provide a major pathway for osmotically driven water transport through cell membranes. So far, 13 aquaporin isoforms (AQP0-AQP12) have been identified in mammalian species (Verkman, 2005). AQP4, the predominant isoform in adult brain, is primarily expressed at the border between brain parenchyma and major fluid compartments, including astrocyte foot processes and glia limitans, as well as ependymal cells and subependymal astrocytes (Venero et al., 2001). The bidirectional water channel AQP4 has an important role in water homeostasis in the brain. It probably helps in the redistribution and absorption of edema fluid, because disruption of AQP4 is found to contribute to the pathophysiology of brain edema (Zador et al., 2007). AQP4 knockout markedly reduced brain swelling in mouse models of cytotoxic brain edema, whereas it significantly worsened outcome in mouse models of vasogenic brain edema (Papadopoulos and Verkman, 2007). Thus, AQP4 ...

Aquaporins are transmembrane water channel proteins present in biological plasma membranes that aid in biological water filtration processes by transporting water molecules through at high speeds, while selectively blocking out other kinds of solutes. Aquaporin Z incorporated biomimetic membranes are envisaged to overcome the problem of high pressure needed, and holds great potential for use in water purification processes, giving high flux while keeping energy consumption low. The functionality of aquaporin Z in terms of osmotic permeability might be regulated by factors such as pH, temperature, crosslinking and hydrophobic thickness of the reconstituted bilayers. Hence, we reconstituted aquaporin Z into vesicles that are made from a series of amphiphilic block copolymers PMOXA-PDMS-PMOXAs with various hydrophobic molecular weights. The osmotic permeability of aquaporin Z in these vesicles was determined through a stopped-flow spectroscopy. In addition, the temperature and pH value of the vesicle

This paper strongly supports the conclusion that AQP0 has a high permeability mode and a low permeability mode. How do these two modes differ? Available structural data on the nature of the water-filled pore through AQP1 and the glycerol facilitator suggest a possible answer. For both, water and glycerol must move through the pore by single-file diffusion. The crystal structure and molecular dynamic simulations suggest that there are multiple water molecules in the pore. There are ∼6 waters seen in the narrow constriction of the pore in the X-ray structure (Sui et al., 2001), and molecular dynamic simulations suggest that there are ∼7 or 8 water molecules moving in concert in the single-file portion of the pore (Tajkhorshid et al., 2002; Zhu et al., 2004). The lack of passage of ionic current through AQP0 and AQP1 is explained by electrostatic considerations that strongly inhibit the movement of protons into the NPA region or hydroxyls into regions flanking either side of the NPA region (de ...

Proteins that selectively transport water across the membranes of cells are recognized as important in the normal functioning of the body systems of vertebrates. There are 13 known mammalian aquaporins (AQP0 to AQP12), some of which have been shown to have unexpected cellular roles beyond transmembrane water transport. The availability of non-mammalian vertebrate animal models has the potential to provide insight into the emergence of diverse function in the aquaporins. The domesticated chicken (Gallus gallus) is the premier avian model for biological research; however, only a limited number of studies have compared chicken and mammalian aquaporins. The identification of aquaporins that share functional motifs or are expressed in the same tissues in human and chicken could allow the further functional analyses of homologous aquaporins in both species. We hypothesize that integrative analyses of protein sequences and body site expression of human, mouse, rat and chicken aquaporins has the potential to

We recently demonstrated that the aquaglyceroporins (AQGPs) could act as potent transporters for orthosilicic acid (H4SiO4). Although interesting, this finding raised the question of whether water and H4SiO4, the transportable form of Si, permeate AQGPs by interacting with the same region of the pore, especially in view of the difference in molecular radius between the two substrates. Here, our goal was to identify residues that endow the AQGPs with the ability to facilitate Si diffusion by examining the transport characteristics of mutants in which residues were interchanged between a water-permeable but Si-impermeable channel (aquaporin 1 [AQP1]) and a Si-permeable but water-impermeable channel (AQP10). Our results indicate that the composition of the arginine filter (XX/R), known to include three residues that play an important role in water transport, may also be involved in Si selectivity. Interchanging the identities of the nonarginine residues within this filter causes Si transport to ...

Aquaporins play a direct role in plant water relation under salt stress, but the effects of 5-aminolevulinic acid (ALA) on aquaporin gene expression in salt-treated plants remain unknown. This study investigated the potential effects of exogenous ALA (50 mg/dm3) on aquaporin expression levels under salt stress (75 mM NaCl) in the salt-sensitive (Jinchun No.4) and the relatively salt-tolerant cucumber (Jinyou No.1) seedlings.

We investigated the in vivo ramifications of a book aquaporin 4 (AQP4) inhibitor 2-(nicotinamide)-1,3,4-thiadiazole, TGN-020, inside a mouse style of focal cerebral ischemia using 7. research convincingly exhibited that pretreatment using the AQP4 inhibitor TGN-020 considerably reduced the quantity of mind edema connected with ischemic damage. Ischemic edema is usually thought to be initiated by influx of Na+ connected with energy failing. Higher osmolarity circumstances create the generating force for drinking water influx into cells, leading to ionic edema [17]. This early edema stage, so-called cytotoxic edema, is certainly thought to last a long time before mass leakage of drinking water into the human brain ensues, making so-called vasogenic edema [18]. AQP4 is certainly thought to play a substantial function in the real drinking water flux in both procedures. Flux through AQP4 is certainly buy 154992-24-2 bidirectional and solely reliant on osmolarity distinctions between your two spaces ...

Müller glial cells are important regulators of physiological function of retina. In a model disease of retinal inflammation and spontaneous recurrent uveitis in horses (ERU), we could show that retinal Müller glial cells significantly change potassium and water channel protein expression during autoimmune pathogenesis. The most significantly changed channel protein in neuroinflammatory ERU was aquaporin 11 (AQP11). Aquaporins (AQP, 13 members) are important regulators of water and small solute transport through membranes. AQP11 is an unorthodox member of this family and was assigned to a third group of AQPs because of its difference in amino acid sequence (conserved sequence is only 11 %) and especially its largely unknown function. In order to gain insight into the distribution, localization, and function of AQP11 in the retina, we first developed a novel monoclonal antibody for AQP11 enabling quantification, localization, and functional studies. In the horse retina, AQP11 was exclusively expressed

Background: Aquaporins are integral membrane proteins that facilitate the transport of water and small solutes across cell membranes. These proteins are vital for maintaining water homeostasis in living organisms. In mammals, thirteen aquaporins (AQP0-12) have been characterized, but in lower vertebrates, such as fish, the diversity, structure and substrate specificity of these membrane channel proteins are largely unknown. Results: The screening and isolation of transcripts from the zebrafish (Danio rerio) genome revealed eighteen sequences structurally related to the four subfamilies of tetrapod aquaporins, i.e., aquaporins (AQP0, -1 and -4), water and glycerol transporters or aquaglyceroporins (Glps; AQP3 and AQP7-10), a water and urea transporter (AQP8), and two unorthodox aquaporins (AQP11 and -12). Phylogenetic analyses of nucleotide and deduced amino acid sequences demonstrated dual paralogy between teleost and human aquaporins. Three of the duplicated zebrafish isoforms have unlinked ...

After producing a recombinant form of AqpZ in E. coli, the proteins were crystallized--capturing five water molecules inside--and then analyzed by state-of-the-art high-resolution X-ray diffraction techniques. The architecture of aquaporin Z is typical of aquaporins, with a spiral of eight oxygens providing water-binding sites inside the channel. The outer membrane and cytoplasmic ends of the channel are wider than the interior, which is long and narrow. This structure demonstrates that aquaporin selectivity arises in part from erecting a physical barrier: small molecules, like water, can easily pass, but larger ones simply cant fit. And the strategic positioning of amino acid residues with hydrophilic or hydrophobic properties along the channel helps police the influx of molecules based on their affinity for water. While it seems two amino acid chains located in the middle of the channel also provide a water-friendly surface, Stroud et al. say they play a more intriguing role. Noting that the ...

Transmembrane glycerol transport is an ancient biophysical property that evolved in selected subfamilies of water channel (aquaporin) proteins. Here, we conducted broad level genome (,550) and transcriptome (,300) analyses ...

Aquaporin (AQP) proteins comprise a group of membrane intrinsic proteins (MIPs) that are responsible for transporting water and other small molecules, which is crucial for plant survival under stress conditions including salt stress. Despite the vital role of AQPs, little is known about them in cucumber (Cucumis sativus L.). In this study, we identified 39 aquaporin-encoding genes in cucumber that were separated by phylogenetic analysis into five sub-families (PIP, TIP, NIP, SIP, and XIP). Their substrate specificity was then assessed based on key amino acid residues such as the aromatic/Arginine (ar/R) selectivity filter, Frogers positions, and specificity-determining positions. The putative cis-regulatory motifs available in the promoter region of each AQP gene were analyzed and results revealed that their promoter regions contain many abiotic related cis-regulatory elements. Furthermore, analysis of previously released RNA-seq data revealed tissue- and treatment-specific expression patterns of

I think it will be found that aquaporin 3 will be the item of interest (1).. Aquaporin 3 is found in normal skeletal myofibres (2).. I suspect it will be found that the problem is not a mutation, but something interfering with the normal proper function of the aqp3 channels.. Aquaporin 3 is, in addition to being a water channel, also an arsenic transporter.. Arsenic has been implicated in Alzheimers in at least a few instances. For example, this statement appears in Reference 3 below:. Arsenic can induce apoptosis in cortical neurons of rats. This process is based on the activation of JNK3 and p38 MAPK by arsenic...[which] can activate p38 MAPK and JNK3..... And the title of the last paper speaks for itself: Arsenic exposure may be a risk factor for Alzheimers disease.. ...

TY - JOUR. T1 - An experimental study on water transport through the membrane of a PEFC operating in the dead-end mode. AU - Lee, Yongtaek. AU - Kim, Bosung. AU - Kim, Yongchan. N1 - Funding Information: This work was supported by a grant (No. R01-2006-000-11014-0) from the Basic Research Program of the Korea Science & Engineering Foundation. PY - 2009/9. Y1 - 2009/9. N2 - Water transport through the membrane of a polymer electrolyte fuel cell (PEFC) was investigated by not only measuring the voltage variation but also visualizing the accumulation of water at the anode for various values of operating parameters, such as the humidity, current density, stoichiometry, location of humidification, and membrane properties. The PEFC was operated in the dead-end mode to prevent the discharge of water from the anode. The water transport in the PEFC was characterized by the elapsed time for the voltage to reach its limit. Anode visualization showed water transport under various conditions. In addition, ...

S6 - Northeastern. This pod is released every hour at past 20 and 50. It travels a very big distance and it is a really long trip. It goes very far in East, close to Linden Village. It exits Snowlands very fast. It goes North, through Tethis sim, where is located the highest mountain of Sansara (see Altitude for details). There are a few other very high mountains in this sim and nearby places. Then, it follows the tundra to East, close to the border with endless snow-coverd land. Then, close to Clarksberg, it changes route to North-East. This road connects a group of long islands. Water channels are to left and to rignt. Altitude is not too high, but land is never complete flat. It is up to your imagination to decide if these channels are rivers or straights of salt, oceanic water. The high number of bridges is to be noted. Then, the pod makes a small stop at Waterhead infohub. This is a good place to meet people, since it is one of the most active of all infohubs, but also a very good place to ...

Using PLIF to analyse water channel simulations of turbulent diffusion in the atmospheric boundary layer A. Butet METEO-FRANCE CNRM/GMEI/SPEA,...

Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.

Polyclonal antibody for AQUAPORIN 3/AQP3 detection. Host: Rabbit.Size: 100μg/vial. Tested applications: IHC-P. Reactive species: Human. AQUAPORIN 3/AQP3 information: Molecular Weight: 31544 MW; Subcellular Localization: Basolateral cell membrane; Multi-pa

Aquaporin 10 antibody, C-term (aquaporin 10) for WB. Anti-Aquaporin 10 pAb (GTX45889) is tested in Human samples. 100% Ab-Assurance.

Free ground shippingShips directly from Da-Lite within 4-5 business days Whats Included? 1 Da-Lite UTB Contour Fixed-Frame Projection Screen 58x136.5 viewable area - 148 Diag / 2.35:1 Cinemascope format Extruded aluminum frame with 0.25 wide bezel Black, acid etch finish on frame and bezel Wall hanging bracket(s)

摘要(Abstract)： 目的探讨头孢曲松钠在水通道蛋白4(AQP4)抗体诱导的星形胶质细胞损伤中的作用以及机制。方法常规体外培养新生SD大鼠大脑皮质细胞,将培养的细胞分为4组,分别加入健康人血清(对照组)、AQP4抗体阳性患者血清、头孢曲松钠+AQP4抗体阳性血清以及单纯头孢曲松钠。细胞培养24h后采用免疫组织化荧光染色观察不同组星形胶质细胞数目的变化,采用比色法测定上清液谷氨酸浓度以及免疫印迹分析谷氨酸转运体-1(GLT-1)蛋白表达水平。结果和对照组比较,AQP4抗体阳性血清组星形胶质细胞数目和谷氨酸转运体-1(GLT-1)蛋白表达明显减少,上清液谷氨酸浓度明显增高(均 ...

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Aquaporin-1 (AQP1) water channels are present in the apical and basolateral plasma membrane domains of bile duct epithelial cells, or cholangiocytes, and mediate the transport of water in these cells. We previously reported that secretin, a hormone known to stimulate ductal bile secretion, increases cholangiocyte osmotic water permeability and stimulates the redistribution of AQP1 from an intracellular vesicular pool to the cholangiocyte plasma membrane. Nevertheless, the target plasma membrane domain (i.e., basolateral or apical) for secretin-regulated trafficking of AQP1 in cholangiocytes is unknown, as is the functional significance of this process for the secretion of ductal bile. In this study, we used primarily an in vivo model (i.e., rats with cholangiocyte hyperplasia induced by bile duct ligation) to address these issues. AQP1 was quantitated by immunoblotting in apical and basolateral plasma membranes prepared from cholangiocytes isolated from rats 20 min after intravenous infusion of secretin

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 ...

Cells release extracellular vesicles (EVs) to communicate over long distances, which requires EVs to traverse the extracellular matrix (ECM). However, given that the size of EVs is usually larger than the mesh size of the ECM, it is not clear how they can travel through the dense ECM. Here we show that, in contrast to synthetic nanoparticles, EVs readily transport through nanoporous ECM. Using engineered hydrogels, we demonstrate that the mechanical properties of the matrix regulate anomalous EV transport under confinement. Matrix stress relaxation allows EVs to overcome the confinement, and a higher crosslinking density facilitates a fluctuating transport motion through the polymer mesh, which leads to free diffusion and fast transport. Furthermore, water permeation through aquaporin-1 mediates the EV deformability, which further supports EV transport in hydrogels and a decellularized matrix. Our results provide evidence for the nature of EV transport within confined environments and demonstrate an

TY - JOUR. T1 - Urine-concentrating mechanism in the inner medulla. T2 - Function of the thin limbs of the loops of henle. AU - Dantzler, William H.. AU - Layton, Anita T.. AU - Layton, Harold E.. AU - Pannabecker, Thomas L.. PY - 2014. Y1 - 2014. N2 - The ability of mammals to produce urine hyperosmotic to plasma requires the generation of a gradient of increasing osmolality along the medulla from the corticomedullary junction to the papilla tip. Countercurrent multiplication apparently establishes this gradient in the outer medulla, where there is substantial transepithelial reabsorption of NaCl from the water-impermeable thick ascending limbs of the loops of Henle. However, this process does not establish the much steeper osmotic gradient in the inner medulla, where there are no thick ascending limbs of the loops of Henle and the water-impermeable ascending thin limbs lack active transepithelial transport of NaCl or any other solute. The mechanism generating the osmotic gradient in the inner ...

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

Brain. 2019 Jun 1;142(6):1598-1615. doi: 10.1093/brain/awz106.. Cotzomi E1,2, Stathopoulos P1,2, Lee CS1,2, Ritchie AM3, Soltys JN3, Delmotte FR2, Oe T2, Sng J2, Jiang R2, Ma AK4, Vander Heiden JA1, Kleinstein SH2,4,5, Levy M6, Bennett JL3, Meffre E2, OConnor KC1,2.. Neuromyelitis optica spectrum disorders (NMOSD) constitute rare autoimmune disorders of the CNS that are primarily characterized by severe inflammation of the spinal cord and optic nerve. Approximately 75% of NMOSD patients harbour circulating pathogenic autoantibodies targeting the aquaporin-4 water channel (AQP4). The source of these autoantibodies remains unclear, but parallels between NMOSD and other autoantibody-mediated diseases posit compromised B cell tolerance checkpoints as common underlying and contributing factors. Using a well established assay, we assessed tolerance fidelity by creating recombinant antibodies from B cell populations directly downstream of each checkpoint and testing them for polyreactivity and ...

The main role of salivary glands (SG) is the production and secretion of saliva, in which aquaporins (AQPs) play a key role by ensuring water flow. The AQPs are transmembrane channel proteins permeable to water to allow water transport across cell membranes according to osmotic gradient. This review gives an insight into SG AQPs. Indeed, it gives a summary of the expression and localization of AQPs in adult human, rat and mouse SG, as well as of their physiological role in SG function. Furthermore, the review provides a comprehensive view of the involvement of AQPs in pathological conditions affecting SG, including Sjögren’s syndrome, diabetes, agedness, head and neck cancer radiotherapy and SG cancer. These conditions are characterized by salivary hypofunction resulting in xerostomia. A specific focus is given on current and future therapeutic strategies aiming at AQPs to treat xerostomia. A deeper understanding of the AQPs involvement in molecular mechanisms of saliva secretion and diseases

INTERNET-DRAFT DTLS as a Transport Layer for RADIUS 9 October 2013 The above paragraph can be rephrased more generically. A session MUST be deleted when non-RADIUS traffic is received over it. This specification is for RADIUS, and there is no reason to allow non- RADIUS traffic over a RADIUS/DTLS connection. A session MUST be deleted when RADIUS traffic fails to pass security checks. There is no reason to permit insecure networks. A session SHOULD NOT be deleted when a well-formed, but unexpected RADIUS packet is received over it. Future specifications may extend RADIUS/DTLS, and we do not want to forbid those specifications. Once a DTLS session is established, a RADIUS/DTLS server SHOULD use DTLS Heartbeats [RFC6520] to determine connectivity between the two servers. A server SHOULD also use watchdog packets from the client to determine that the connection is still active. As UDP does not guarantee delivery of messages, RADIUS/DTLS servers which do not implement an application-layer watchdog ...

TY - JOUR. T1 - Involvement of aquaporin in thromboxane A2 receptor-mediated, G12/13/RhoA/NHE-sensitive cell swelling in 1321N1 human astrocytoma cells. AU - Saito, Masaki. AU - Tanaka, Hiroyuki. AU - Sasaki, Masako. AU - Kurose, Hitoshi. AU - Nakahata, Norimichi. PY - 2010/1/1. Y1 - 2010/1/1. N2 - The physiological role of the thromboxane A2 (TXA2) receptor expressed on glial cells remains unclear. We previously reported that 1321N1 human astrocytoma cells pretreated with dibutyryl cyclic AMP (dbcAMP) became swollen in response to U46619, a TXA2 analogue. In the present study, we examined the detailed mechanisms of TXA2 receptor-mediated cell swelling in 1321N1 cells. The cell swelling caused by U46619 was suppressed by expression of p115-RGS, an inhibitory peptide of Gα12/13 pathway and C3 toxin, an inhibitory protein for RhoA. The swelling was also inhibited by treatment with Y27632, a Rho kinase inhibitor and 5-(ethyl-N-isopropyl)amiloride (EIPA), a Na+/H+-exchanger inhibitor. Furthermore, ...

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 ...

Industrys need to predict the lifetime of adhesively bonded joints has been met by the development of a wide variety of techniques. One particular approach utilises the fact that adhesives and the joints they form can be susceptible to moisture attack. The ingress of moisture into, and through, an adhesive or polymer is termed water permeation. Such a phenomenon can be measured extremely accurately (e.g. through mass change, dielectric permittivity, etc) and it has been shown that for particular systems and environments, a good correlation can be made between the accelerated ageing protocol and in-service failure. This approach has been studied extensively for application within the electronics sector where adhesive/polymeric systems are used both to retain components and coat them. ...

Aquaporins are channel proteins that facilitate the transport of water across cells. The discovery of aquaporins in 1992, for which researcher Peter Agre received the Nobel Prize in Chemistry, opened the door to a new therapeutic approach for treating many health conditions. On one particular start-ups journey in finding applicable aquaporin modulators, the student has become the master. Water is one of the substances that are essential for life on Earth and for the survival of all plants and animals. Although ...

Aquaporin 1 (CO2-, O2- and nitrous oxide-permeable and water-selective) (Zwiazek et al. 2017). Aquaporin-1 tunes pain perception by interacting with Na(v)1.8 Na+ channels in dorsal root ganglion neurons (Zhang and Verkman, 2010). It is upregulated in skeletal muscle in muscular dystrophy (Au et al. 2008). AQP1 has been reported to first insert as a four-helical intermediate, where helices 2 and 4 are not inserted into the membrane. In a second step this intermediate is folded into a six-helical topology. During this process, the orientation of the third helix is inverted, and it can shift out the membrane core (Virkki et al. 2014). Its synthesis is regluated by Kruppel-like factor 2 (KLF2; Q9Y5W3) which also interacts directly with Aqp1 (Fontijn et al. 2015). A nanoscale ion pump has been derived artificially from Aqp1 (Decker et al. 2017 ...

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].

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

Objective: It is well known that VEGFR expression is correlated with peritumoral brain edema in meningiomas. Also Aquaporin4 seems to induce the perifocal edema. In our study we analyzed the correlation of VEGFR1, VEGFR2 and Aquaporin4 to the brain edema. Additionally a potential correlation between[for full text, please go to the a.m. URL ...

Hi, Bit more than a month ago my mom developed burning sensation on her back and stomach, she went to a doc but he said its nothing lifetreatening and she waited for for her turn for the tests, it was like this for a week or two. Few weeks ago the burning sensation became too much to bear and my mom went to a hospital. They took her in and the next day she had issues walking and day later she couldnt walk on her own at all. After a few days they put her on some steroid IV thing for

Hi, Bit more than a month ago my mom developed burning sensation on her back and stomach, she went to a doc but he said its nothing lifetreatening and she waited for for her turn for the tests, it was like this for a week or two. Few weeks ago the burning sensation became too much to bear and my mom went to a hospital. They took her in and the next day she had issues walking and day later she couldnt walk on her own at all. After a few days they put her on some steroid IV thing for

Purchase Molecular Mechanisms of Water Transport Across Biological Membranes, Volume 215 - 1st Edition. Print Book & E-Book. ISBN 9780123646194, 9780080918846

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The Corps of Engineers, Pittsburgh District has been forced to close several recreation areas due to high water following recent rainfall.

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.

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-

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High-Solids Filtration from DW&PS allows customers to consistently filter high and variable solids while achieving high water recovery.

A new case report about a woman with a UTI who became ill from high water intake raises questions about doctors advice to drink plenty of fluids ...