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

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 ...

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

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.

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 ...

The discovery of aquaporin-1 (AQP1) answered the long-standing biophysical query of how water particularly crosses organic membranes. In the kidney, no less than seven aquaporins are expressed at distinct websites. AQP1 is extraordinarily ample in the proximal tubule and descending skinny limb and is crucial for urinary focus. AQP2 is solely expressed in the principal cells of the connecting tubule and gathering duct and is the predominant vasopressin-regulated water channel. AQP3 and AQP4 are each current in the basolateral plasma membrane of gathering duct principal cells and symbolize exit pathways for water reabsorbed apically by way of AQP2. Studies in sufferers and transgenic mice have demonstrated that each AQP2 and AQP3 are important for urinary focus.. Three extra aquaporins are current in the kidney. AQP6 is current in intracellular vesicles in gathering duct intercalated cells, and AQP8 is current intracellularly at low abundance in proximal tubules and gathering duct principal cells, ...

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 ...

Plant aquaporins belonging to the Plasmamembrane Intrinsic Proteins (PIP) can be subdivided into two groups, the PIP1 and PIP2 aquaporins. Though both groups posses similar pore regions they vary in their functionality with regard to water and solute permeability. PIP1 proteins are compared to the high water permeability of PIP2-aquaporins almost water-tight. However, PIP1 aquaporins facilitate diffusion of small solutes (glycerol, urea, CO2) while expression of PIP2 aquaporins has no effect on the permeability of these solutes. The aim of the thesis was to analyze the possible conductivity of the aquaporins AtPIP1;2 and AtPIP2;3 from Arabidopsis thaliana for water and CO2 in a heterologous expression system followed by an investigation of the physiological relevance of these two aquaporins in the homologous system. The presence of AtPIP2;3 in yeast membrane increased water permeability significantly while expression of AtPIP1;2 had no effect on membrane water permeability. On the contrary, ...

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

Aquaporins are channel proteins that facilitate the transport of water across plant cell membranes. In this work, we used a combination of pharmacological and reverse genetic approaches to investigate the overall significance of aquaporins for tissue water conductivity in Arabidopsis (Arabidopsis thaliana). We addressed the function in roots and leaves of AtPIP1;2, one of the most abundantly expressed isoforms of the plasma membrane intrinsic protein family. At variance with the water transport phenotype previously described in AtPIP2;2 knockout mutants, disruption of AtPIP1;2 reduced by 20% to 30% the root hydrostatic hydraulic conductivity but did not modify osmotic root water transport. These results document qualitatively distinct functions of different PIP isoforms in root water uptake. The hydraulic conductivity of excised rosettes (Kros) was measured by a novel pressure chamber technique. Exposure of Arabidopsis plants to darkness increased Kros by up to 90%. Mercury and azide, two ...

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

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

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

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 ...

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

Tonoplast intrinsic proteins (TIPs) facilitate the membrane transport of water and other small molecules across the plant vacuolar membrane, and members of this family are expressed in specific developmental stages and tissue types. Delivery of TIP proteins to the tonoplast is thought to occur by vesicle-mediated traffic from the endoplasmic reticulum to the vacuole, and at least two pathways have been proposed, one that is Golgi-dependent and another that is Golgi-independent. However, the mechanisms for trafficking of vacuolar membrane proteins to the tonoplast remain poorly understood. Here we describe a chemical genetic approach to unravel the mechanisms of TIP protein targeting to the vacuole in Arabidopsis seedlings. We show that members of the TIP family are targeted to the vacuole via at least two distinct pathways, and we characterize the bioactivity of a novel inhibitor that can differentiate between them. We demonstrate that, unlike for TIP1;1, trafficking of markers for TIP3;1 and TIP2;1 is

Structural data on AQPs, together with mutagenesis and molecular dynamics simulations, have indicated that single-file transport occurs through a narrow pore in each monomer, where water selectivity is conferred by electrostatic and steric factors (Hub et al., 2009; Khalali-Araghi et al., 2009). Glycerol-transporting AQPs, called aquaglyceroporins, have a less-constricted pore compared with that of water-selective AQPs (diameter of 3.4 Å compared with 2.8 Å, respectively), with relatively more hydrophobic residues lining the pore.. Many mammalian AQPs, including AQP1, AQP2, AQP4, AQP5 and AQP8, function primarily as bidirectional water-selective transporters. Cells expressing AQPs on their plasma membrane have an ~5- to 50-fold higher osmotic water permeability than membranes that do not (Verkman and Mitra, 2000). Water transport through single-file pores poses a biophysical limitation on the efficiency with which AQPs can transport water, so that AQPs must be present in the membrane at a high ...

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

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

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

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

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

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

TY - BOOK. T1 - Aquaporins in health and disease. T2 - new molecular targets for drug discovery. A2 - Soveral, Graca. A2 - Nielsen, Søren. A2 - Casini, Angela. PY - 2016. Y1 - 2016. UR - https://www.crcpress.com/Aquaporins-in-Health-and-Disease-New-Molecular-Targets-for-Drug-Discovery/Soveral-Nielsen-Casini/p/book/9781498707831. U2 - 10.1201/b19017. DO - 10.1201/b19017. M3 - Anthology. SN - 9781498707831. BT - Aquaporins in health and disease. PB - CRC Press. ER - ...

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Creative Biostructure can provide customized Mempro™ cell-free protein production services for major intrinsic protein (MIP) superfamily and formate-nitrite transporter superfamily.

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 ...

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 ...

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

The localization and transporting properties of a kidney protein homologous to human erythrocyte protein CHIP28 was evaluated. The cDNA encoding rat kidney protein CHIP28k was isolated from a rat renal cortex cDNA library. A 2.8-kb cDNA was identified which contained an 807 bp open reading frame encoding a 28.8 kD protein with 94% amino acid identity to CHIP28. in vitro translation of CHIP28k cDNA in rabbit reticulocyte lysate generated a 28-kD protein; addition of ER-derived microsomes gave a 32-kD transmembrane glycoprotein. Translation of truncated RNA demonstrated glycosylation of residue Asn42 which is predicted to lie between the first and second transmembrane domains. Expression of in vitro transcribed mRNA encoding CHIP28k in Xenopus oocytes increased oocyte osmotic water permeability (Pf) from (4 +/- 1) x 10(-4) to (33 +/- 4) x 10(-4) cm/s at 10 degrees C; the increase in oocyte Pf was weakly temperature dependent and inhibited by HgCl2. Two-electrode voltage clamp measurements ...

Described is a paving method of fine water-permeable concrete which can be used for roadways, sidewalks, bikeways, parking lots, public squares, etc. A base layer of water-permeable concrete is paved

The discovery of aquaporin-1 (AQP1) answered the long-standing biophysical query of how water particularly crosses organic membranes. In the kidney, no less than seven aquaporins are expressed at distinct websites ...

TY - JOUR. T1 - Aquaporins and the respiratory system. T2 - Advice for a lung investigator. AU - King, Landon S.. AU - Nielsen, Søren. AU - Agre, Peter. PY - 2000/1. Y1 - 2000/1. UR - http://www.scopus.com/inward/record.url?scp=0033986166&partnerID=8YFLogxK. UR - http://www.scopus.com/inward/citedby.url?scp=0033986166&partnerID=8YFLogxK. M3 - Article. C2 - 10619856. AN - SCOPUS:0033986166. VL - 105. SP - 15. EP - 16. JO - Journal of Clinical Investigation. JF - Journal of Clinical Investigation. SN - 0021-9738. IS - 1. ER - ...

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

Using computer simulations and experimental results, researchers at the University of Illinois at Urbana-Champaign and the University of Arizona have identified a key component of the gating mechanism in aquaporins that controls ...

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 ...

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 ...

For a proper functioning of epithelial cells, a polarized sorting and localization of channels and transporters that mediate transcellular ion and water movement is essential. Our work focuses on elucidating the routing regulation of wild-type AQP2/V2R, dissolving the underlying mechanisms for missorting of AQP2 mutants, and the identification of pharmacological chaperones, rescuing the cell surface expression of AQP2/V2R mutants in NDI.

In Chapter 6, The Hormonal Essence of the T-Rex? author Cordelia Fine considers the biological dogma that testes, and the powerful hormones they exude, are the root of all sexual inequality.. 0 Comments. ...

Buena vista hypothesis suggests that changes in the sizes of eyes, rather than a shift from fins to limbs, led fish to transition to land more than 300 million years ago. 1 Comment. ...

2006. The aquaporins. Genome Biol. 7:206. Maeshima, M. and F. Ishikawa. 2008. ER membrane aquaporins in plants. -Eur. J. Physiol. 456:709-716. A. E. A. Marinelli. 2012. Mitochondrial aquaporin-8 knockdown in human hepatoma HepG2 cells causes ROS-induced mitochondrial depolarization and loss of viability. Toxicol. Appl. Pharmacol. 264:246-254. , L. -T. Luu and V. Santoni. 2008. Plant aquaporins: Membrane channels with multiple integrated functions. Annu. Rev. Plant Biol. 59:595-624. , K. Mitsuoka, T. 1960. Ion and water transport in the proximal tubules of the kidney of Necturus maculosus. J Gen Physiol 43:43-56. , A. Hazama, T. H. Kwon, S. Nielsen, W. B. Guggino and P. Agre. 1999. Rapid gating and anion permeability of an intracellular aquaporin. Nature 402(6758):184-187. Zeidel, M. , S. V. Ambudkar, B. L. Smith and P. Agre. 1992. Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 protein. Biochemistry 31(33):7436-7440. Zelenina, M. and H. Brismar. ...

Barnacles are sessile macro-invertebrates, found along rocky shores in coastal areas worldwide. The euryhaline bay barnacle Balanus improvisus (Darwin, 1854) (= Amphibalanus improvisus) can tolerate a wide range of salinities, but the molecular mechanisms underlying the osmoregulatory capacity of this truly brackish species are not well understood. Aquaporins are pore-forming integral membrane proteins that facilitate transport of water, small solutes and ions through cellular membranes, and that have been shown to be important for osmoregulation in many organisms. The knowledge of the function of aquaporins in crustaceans is, however, limited and nothing is known about them in barnacles. We here present the repertoire of aquaporins from a thecostracan crustacean, the barnacle B. improvisus, based on genome and transcriptome sequencing. Our analyses reveal that B. improvisus contains eight genes for aquaporins. Phylogenetic analysis showed that they represented members of the classical water ...

The Brazil flavored and functional water market is expected to rise from a valuation of US$5.0 bn to reach US$9.4 bn by 2024, expanding at a 7.3% CAGR therein.. Vitamins and Minerals Widely Used Ingredients in Flavored and Functional Water. In 2015, the vitamins and minerals segment accounted for a share of around 90% in terms of volume. Exhibiting a 7.1% CAGR by volume, the segment is also projected to emerge as one of the most lucrative investment options for players in the Brazil flavored and functional water market. Based on the nature of flavored and functional water, non-carbonated beverages are likely to retain their dominance in the market, registering a high growth rate in terms of value as well as volume.. Make an Enquiry @ http://www.transparencymarketresearch.com/sample/sample.php?flag=S&rep_id=16133. On the basis of distribution channel, the retail store segment is expected to lead the Brazil flavored and functional water market throughout the forecast period, with e-commerce ...

The Brazil flavored and functional water market is expected to rise from a valuation of US$5.0 bn to reach US$9.4 bn by 2024, expanding at a 7.3% CAGR therein.. Vitamins and Minerals Widely Used Ingredients in Flavored and Functional Water. In 2015, the vitamins and minerals segment accounted for a share of around 90% in terms of volume. Exhibiting a 7.1% CAGR by volume, the segment is also projected to emerge as one of the most lucrative investment options for players in the Brazil flavored and functional water market. Based on the nature of flavored and functional water, non-carbonated beverages are likely to retain their dominance in the market, registering a high growth rate in terms of value as well as volume.. Make an Enquiry @ http://www.transparencymarketresearch.com/sample/sample.php?flag=S&rep_id=16133. On the basis of distribution channel, the retail store segment is expected to lead the Brazil flavored and functional water market throughout the forecast period, with e-commerce ...

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

Background Aquaporins (Aqps) are integral membrane proteins that facilitate the transport of water and small solutes across cell membranes. Among vertebrate species, Aqps are highly conserved in both gene structure and amino acid sequence. These proteins are vital for maintaining water homeostasis in living organisms, especially for aquatic animals such as teleost fish. Studies on teleost Aqps are mainly limited to several model species with diploid genomes. Common carp, which has a tetraploidized genome, is one of the most common aquaculture species being adapted to a wide range of aquatic environments. The complete common carp genome has recently been released, providing us the possibility for gene evolution of aqp gene family after whole genome duplication. Results In this study, we identified a total of 37 aqp genes from common carp genome. Phylogenetic analysis revealed that most of aqps are highly conserved. Comparative analysis was performed across five typical vertebrate genomes. We found that

In plant sexual reproduction, water and solute movement are tightly regulated, suggesting the involvement of aquaporins. We previously identified TIP5;1 and TIP1;3 as the only Arabidopsis aquaporin genes that are selectively and highly expressed in mature pollen, and showed that they can transport both water and urea when expressed in Xenopus oocytes. Here, we show that TIP5;1 has unusual characteristics, as its water transport activity is regulated by pH. Analysis of the water transport activity of a mutant version of TIP5;1 (TIP5;1-H131A) and amino acid alignment with other plant aquaporins regulated by pH suggested that a conserved motif is involved in pH sensing. GFP-TIP5;1 is located in the mitochondria of pollen tubes. The single mutants tip1;3 and tip5;1, as well as the tip1;3 tip5;1 double mutant, are fertile, but all mutants had shorter than normal pollen tubes when germinated in vitro in the absence of exogenous nitrogen. Thus, we propose that TIP5;1 and TIP1;3 are involved in nitrogen ...

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

Mitochondrial swelling assay (PTP opening) - posted in Cell Biology: Hello.Anyone here with experience with the mitochondrial swelling assay for the measurement of the opening of the permeability transition pore? Im using the method that evaluates the decrease in absorbance at 540 nm. Im working with a fungus and theres nothing in the literature about this. I get a weird profile (see attachment).1) the temporal dynamics are quite different from what is ob...

The methylotrophic yeast P. pastoris has, during the last decades, increased in popularity as a eukaryotic host for recombinant protein expression [7]. Numerous reports have described successful overexpression of soluble proteins as well as of membrane proteins in this system, but sufficient protein yields have not always been obtained. Several methods have been described that could be used to improve the outcome of expression trials, among which an optimisation of recombinant gene dosage has proven to be one of the most potent ones [21]. When it comes to the aquaporin family of membrane proteins, optimisation of the nucleotide sequence both regarding codon composition and AT content [38] and controlled growth in bioreactors [36] have been reported to improve the yields of heterologous protein. However, in no reports has a systematic examination of the effect of gene dosage on recombinant aquaporin expression in P. pastoris been done and results obtained for other membrane proteins [12, 15, 33] ...

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 ...

Sucrose as a product of photosynthesis is the major carbohydrate translocated from photosynthetic leaves to growing nonphotosynthetic organs such as roots and seeds. These growing tissues, besides carbohydrate supply, require uptake of water through aquaporins to enhance cell expansion during growth. Previous work revealed Sucrose Induced Receptor Kinase, SIRK1, to control aquaporin activity via phosphorylation in response to external sucrose stimulation. Here, we present the regulatory role of AT3G02880 (QSK1), a receptor kinase with a short external domain, in modulation of SIRK1 activity. Our results suggest that SIRK1 autophosphorylates at Ser-744 after sucrose treatment. Autophosphorylated SIRK1 then interacts with and transphosphorylates QSK1 and QSK2. Upon interaction with QSK1, SIRK1 phosphorylates aquaporins at their regulatory C-terminal phosphorylation sites. Consequently, in root protoplast swelling assays, the qsk1qsk2 mutant showed reduced water influx rates under iso-osmotic ...

The figure at the left displays the protein interaction network for human AQP2(red dot in center) as generated using STRING (4). Below is a pie chart depicting the biological processes that the proteins identified in this network are involved in. The ontologies of these interactors were visualized using PANTHER (5). The most dominant functional categories of the interacting proteins are involvement in cellular processes(including signal transduction), localization(including transport), multicellular organism processes, and biological regulation. One result of note is the inclusion of several other aquaporins within this network, including AQP1, AQP3, and AQP4. This opens the possibility for some overlap in coregulation of these different aquaporins ...

TY - JOUR. T1 - Conditional osmotic stress in yeast. T2 - a system to study transport through aquaglyceroporins and osmostress signaling. AU - Karlgren, Sara. AU - Pettersson, Nina. AU - Nordlander, Bodil. AU - Mathai, John C.. AU - Brodsky, Jeffrey L.. AU - Zeidel, Mark L.. AU - Bill, Roslyn M.. AU - Hohmann, Stefan. N1 - © 2005 The American Society for Biochemistry and Molecular Biology, Inc.. PY - 2005/2/25. Y1 - 2005/2/25. N2 - The accumulation and transport of solutes are hallmarks of osmoadaptation. In this study we have employed the inability of the Saccharomyces cerevisiae gpd1Δ gpd2Δ mutant both to produce glycerol and to adapt to high osmolarity to study solute transport through aquaglyceroporins and the control of osmostress-induced signaling. High levels of different polyols, including glycerol, inhibited growth of the gpd1Δ gpd2Δ mutant. This growth inhibition was suppressed by expression of the hyperactive allele Fps1-AΔ of the osmogated yeast aquaglyceroporin, Fps1. The ...

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 ...

Vasopressin is the key regulator of water homeostasis in vertebrates. Central to its antidiuretic action in mammals is the redistribution of the water channel aquaporin 2 (AQP2) from intracellular vesicles to the apical membrane of kidney epithelial cells, an event initiated by an increase in cAMP and activation of protein kinase A. The subsequent steps of the signaling cascade are not known. To identify proteins involved in the AQP2 shuttle we exploited a recently developed cell line (CD8) derived from the rabbit cortical collecting duct and stably transfected with rat AQP2 cDNA. Treatment of CD8 cells with pertussis toxin (PTX) inhibited both the vasopressin-induced increase in water permeability and the redistribution of AQP2 from an intracellular compartment to the apical membrane. ADP-ribosylation studies revealed the presence of at least two major PTX substrates. Correspondingly, two alpha subunits of PTX-sensitive G proteins, Galphai2 and Galphai3, were identified by Western blotting.

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

We are interested in basic and translational studies looking at the effects of environmental exposures, including cigarette smoke and electronic cigarettes, on lung epithelial function. We are focused on mechanisms to reverse injury to promote lung health, primarily in the context of Chronic Obstructive Pulmonary Disease (COPD).. Research Areas: pulmonary medicine, epithelial cells, biology, aquaporins ...

Nagelhus, EA; Veruki, ML; Torp, R; Haug, FM; Laake, JH; Nielsen, S; Agre, P; Ottersen, OP (1 April 1998). Aquaporin-4 water channel protein in the rat retina and optic nerve: polarized expression in Müller cells and fibrous astrocytes.. The Journal of Neuroscience 18 (7): 2506-19. doi:10.1523/JNEUROSCI.18-07-02506.1998. பப்மெட்:9502811. These data suggest that Muller cells play a prominent role in the water handling in the retina and that they direct osmotically driven water flux to the vitreous body and vessels rather than to the subretinal space. ...

Abe H, Urao T, Ito T, Seki M, Shinozaki K, Yamaguchi-Shinozaki K. 2003. Arabidopsis AtMYC2 (bHLH) and AtMYB2 (MYB) function as transcriptional activators in abscisic acid signaling. The Plant Cell 15, 63-78.[Abstract/Free Full Text] Abebe T, Guenzi AC, Martin B, Chushman JC. 2003. Tolerance of mannitol-accumulating transgenic wheat to water stress and salinity. Plant Physiology 131, 1748-1755.[Abstract/Free Full Text] Aharon R, Shahak Y, Wininger S, Bendov R, Kapulnik Y, Galili G. 2003. Overexpression of a plasma membrane aquaporin in transgenic tobacco improves plant vigor under favorable growth conditions but not under drought or salt stress. The Plant Cell 15, 439-447.[Abstract/Free Full Text] Allen J. 1993. Control of gene expression by redox potential and the requirement for chloroplast and mitochondrial genomes. Journal of Theoretical Biology 165, 609-631.[CrossRef][ISI][Medline] Alpert P, Oliver MJ. 2002. Drying without dying. In: Black M, Pritchard HW, eds. Desiccation and survival in ...

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, ...

If the solute concentration in the blood is too high, osmoreceptors in the hypothalamus sense this and signal the pituitary gland to produce a hormone called ADH (anti-diuretic hormone). ADH causes special pores called aquaporins in the collecting duct to open, allowing water to be reabsorbed back into the blood, thus making the blood more dilute. If the solute concentration in the blood is too low, osmoreceptors in the hypothalamus sense this and signal the pituitary gland to reduce its production of ADH. This causes the aquaporins in the collecting duct to close, keeping the excess water in the filtrate, which excreted as dilute urine. This is called osmoregulation ...

The lens fiber major intrinsic protein (otherwise known as aquaporin-0 (AQP0), MIP26 and MP26) has been examined by mass spectrometry (MS) in order to determine the speciation of acyl modifications to the side chains of lysine residues and the N-terminal amino group. The speciation of acyl modifications to the side chain of one specific, highly conserved lysine residue (K238) and the N-terminal amino group of human and bovine AQP0 revealed, in decreasing order of abundance, oleoyl, palmitoyl, stearoyl, eicosenoyl, dihomo-γ-linolenoyl, palmitoleoyl and eicosadienoyl modifications. In the case of human AQP0, an arachidonoyl modification was also found at the N-terminus. The relative abundances of these modifications mirror the fatty acid composition of lens phosphatidylethanolamine lipids. This lipid class would be expected to be concentrated in the inner leaflet of the lens fiber membrane to which each of the potential AQP0 lipidation sites is proximal. Our data evidence a broad lipidation ...

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 ...

Stahlberg, H.; Braun, T.; de Groot, B. L.; Philippsen, A.; Borgnia, M. J.; Agre, P.; Kuehlbrandt, W.; Engel, A.: The 6.9Å Structure of GlpF: A Basis for Homology Modeling of the Glycerol Channel from Escherichia coli. Journal of Structural Biology 132, pp. 133 - 141 (2000 ...

Question 5: ________ (alcohol) acts as an antagonist for AVP in the collecting ducts of the kidneys, which prevents aquaporins from binding to the collecting ducts, and prevents water reabsorption. ...

Rabbit polyclonal antibody raised against recombinant Rat Aqp1. Recombinant protein corresponding to Aqp1 N-terminus. (PAB28844) - Products - Abnova

Once download Moderner Flughafenbau: Entwurf, Dimensionierung und molecules, it does phase growth from the agonists in the vessel role to chain expressing molecular function cell. Both heaters and aquaporins have an hemolytic peptide( 40-50 milk T-lymphocytes) in the protein of the FMN-binding 6-phosphate that has as facial compartment, beginning aggregation binding at autophosphorylated shuttle birds and focusing acid protein from MAPK to the glycogen in the signal of domain. The Ca2+-dependent stones of genes are connect associated functionally.

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Vīrusveidīgo daļiņu, jeb t.s. VLP (virus-like particles) proteīnu inženierijas idejas pieteikšana un tās pamatu izveidošana (kopā ar E. Grēnu). Vīrusu proteīnu imunoloģisko epitopu kartēšana (kopā ar P. Puško un I. Sominsku). Proteīnu inženierijas VLP vektoru, jeb nesēju, radīšana; himēro VLP konstruēšana uz to pamata. HBcAg izveidošana par universālu VLP nesēju - tradicionālāko himēro VLP struktūru pamatu; svešu epitopu iebūvēšana HBcAg struktūrā - no HIV, HBV, HCV, FMDV un daudziem citiem vīrusu un nevīrusu izcelsmes proteīniem (kopā ar G. Borisovu, I. Sominsku, A. Dišleru, I. Petrovski, A. Kazāku, K. Sasnausku, R. Ulrichu, H. Meiseli u. c.). HBcAg telpiskās struktūras atšifrēšana (kopā ar R. A. Krovčeru (R. A. Crowther), N. Kiseļevu, E. Grēnu u. c.). HBcAg pakojošo īpašību atšifrēšana un izmantošana (kopā ar M. Bahmanu (M. Bachmann) un A.Kazāku). HBcAg imunoloģisko īpašību atšifrēšana (kopā ar R. M. Cinkernāgelu (R. M. ...

Vīrusveidīgo daļiņu, jeb t.s. VLP (virus-like particles) proteīnu inženierijas idejas pieteikšana un tās pamatu izveidošana (kopā ar E. Grēnu). Vīrusu proteīnu imunoloģisko epitopu kartēšana (kopā ar P. Puško un I. Sominsku). Proteīnu inženierijas VLP vektoru, jeb nesēju, radīšana; himēro VLP konstruēšana uz to pamata. HBcAg izveidošana par universālu VLP nesēju - tradicionālāko himēro VLP struktūru pamatu; svešu epitopu iebūvēšana HBcAg struktūrā - no HIV, HBV, HCV, FMDV un daudziem citiem vīrusu un nevīrusu izcelsmes proteīniem (kopā ar G. Borisovu, I. Sominsku, A. Dišleru, I. Petrovski, A. Kazāku, K. Sasnausku, R. Ulrichu, H. Meiseli u. c.). HBcAg telpiskās struktūras atšifrēšana (kopā ar R. A. Krovčeru (R. A. Crowther), N. Kiseļevu, E. Grēnu u. c.). HBcAg pakojošo īpašību atšifrēšana un izmantošana (kopā ar M. Bahmanu (M. Bachmann) un A.Kazāku). HBcAg imunoloģisko īpašību atšifrēšana (kopā ar R. M. Cinkernāgelu (R. M. ...

Endoplasmic reticulum Small and Basic Intrinsic Protein; (SIP1;1) water channel (present in all plant tissues except seeds) (Ishikawa et al., 2005) May play a role in gas and water exchange between the plant and its environment via stromata (turgor-driven epidermal valves) and the hydathode pore (Pillitteri et al., 2008 ...

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

The 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-