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
plasma membrane intrinsic protein 2-7, PIP2;7, plasma membrane intrinsic protein 3, salt stress-induced major intrinsic protein, P93004, Q9ATM4 Plasma membrane aquaporin, PIP2;7 is water channel protein required for water transport across cell membrane
Background: Aquaporins are integral membrane proteins that facilitate the transport of water and small solutes across cell membranes. These proteins are vital for maintaining water homeostasis in living organisms. In mammals, thirteen aquaporins (AQP0-12) have been characterized, but in lower vertebrates, such as fish, the diversity, structure and substrate specificity of these membrane channel proteins are largely unknown. Results: The screening and isolation of transcripts from the zebrafish (Danio rerio) genome revealed eighteen sequences structurally related to the four subfamilies of tetrapod aquaporins, i.e., aquaporins (AQP0, -1 and -4), water and glycerol transporters or aquaglyceroporins (Glps; AQP3 and AQP7-10), a water and urea transporter (AQP8), and two unorthodox aquaporins (AQP11 and -12). Phylogenetic analyses of nucleotide and deduced amino acid sequences demonstrated dual paralogy between teleost and human aquaporins. Three of the duplicated zebrafish isoforms have unlinked ...
TY - JOUR. T1 - Expression and subcellular localization of aquaporin water channels in the polarized hepatocyte cell line, WIF-B. AU - Gradilone, Sergio A.. AU - Tietz, Pamela S.. AU - Splinter, Patrick L.. AU - Marinelli, Raúl A.. AU - LaRusso, Nicholas F.. PY - 2005/8/18. Y1 - 2005/8/18. N2 - Background: Recent data suggest that canalicular bile secretion involves selective expression and coordinated regulation of aquaporins (AQPs), a family of water channels proteins. In order to further characterize the role of AQPs in this process, an in vitro cell system with retained polarity and expression of AQPs and relevant solute transporters involved in bile formation is highly desirable. The WIF-B cell line is a highly differentiated and polarized rat hepatoma/human fibroblast hybrid, which forms abundant bile canalicular structures. This cell line has been reported to be a good in vitro model for studying hepatocyte polarity. Results: Using RT-PCR, immunoblotting and confocal immunofluorescence, ...
Purpose: The expression of aquaporin water channel genes are shown to be affected in several pathological conditions of retina, such as in diabetic retinopathy, retinal ischemia and in autoimmune uveitis. Human native retinal pigment epithelial (RPE) cells and immortalized human RPEs are formerly shown to express aquaporins, still the expression of aquaporins in stem cell derived RPE have not been previously elucidated. The objective of this study was to determine the expression of several aquaporin genes (aquaporin1,- 3, -4, -5, -6, -7, -10, -11 and -12) and assess the localization of aquaporin 1 water channel protein in human embryonic (hESCs) and induced pluripotent stem cells (hiPSCs) derived RPE cells.. Methods: hESC- and hiPSC derived RPE cells were grown as monolayer in serum-free media. The expression of aquaporin genes was determined with qRT-PCR. The localization of AQP1-protein was studied with confocal microscopy. Finally, the functionality of aquaporins was assessed with dye ...
Aquaporins are transmembrane water channel proteins present in biological plasma membranes that aid in biological water filtration processes by transporting water molecules through at high speeds, while selectively blocking out other kinds of solutes. Aquaporin Z incorporated biomimetic membranes are envisaged to overcome the problem of high pressure needed, and holds great potential for use in water purification processes, giving high flux while keeping energy consumption low. The functionality of aquaporin Z in terms of osmotic permeability might be regulated by factors such as pH, temperature, crosslinking and hydrophobic thickness of the reconstituted bilayers. Hence, we reconstituted aquaporin Z into vesicles that are made from a series of amphiphilic block copolymers PMOXA-PDMS-PMOXAs with various hydrophobic molecular weights. The osmotic permeability of aquaporin Z in these vesicles was determined through a stopped-flow spectroscopy. In addition, the temperature and pH value of the vesicle
Aquaporins are channel proteins that facilitate the transport of water across plant cell membranes. In this work, we used a combination of pharmacological and reverse genetic approaches to investigate the overall significance of aquaporins for tissue water conductivity in Arabidopsis (Arabidopsis thaliana). We addressed the function in roots and leaves of AtPIP1;2, one of the most abundantly expressed isoforms of the plasma membrane intrinsic protein family. At variance with the water transport phenotype previously described in AtPIP2;2 knockout mutants, disruption of AtPIP1;2 reduced by 20% to 30% the root hydrostatic hydraulic conductivity but did not modify osmotic root water transport. These results document qualitatively distinct functions of different PIP isoforms in root water uptake. The hydraulic conductivity of excised rosettes (Kros) was measured by a novel pressure chamber technique. Exposure of Arabidopsis plants to darkness increased Kros by up to 90%. Mercury and azide, two ...
Aquaporin-5 is a protein that in humans is encoded by the AQP5 gene. Aquaporin 5 (AQP5) is a water channel protein. Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). Aquaporin 5 plays a role in the generation of saliva, tears and pulmonary secretions. AQP0, AQP2, AQP5, and AQP6 are closely related and all map to 12q13. Aquaporin GRCh38: Ensembl release 89: ENSG00000161798 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000044217 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse PubMed Reference:". Lee MD, Bhakta KY, Raina S, Yonescu R, Griffin CA, Copeland NG, Gilbert DJ, Jenkins NA, Preston GM, Agre P (Jun 1996). "The human Aquaporin-5 gene. Molecular characterization and chromosomal localization". J Biol Chem. 271 (15): 8599-604. doi:10.1074/jbc.271.15.8599. PMID 8621489. "Entrez Gene: AQP5 aquaporin 5". Verkman AS (2003). "Role of aquaporin water channels in eye function". Exp. Eye Res. 76 (2): 137-43. ...
Plant cells contain proteins that are members of the major intrinsic protein (MIP) family, an ancient family of membrane channel proteins characterized by six membrane-spanning domains and two asparagine-proline-alanine (NPA) amino acid motifs in the two halves of the protein. We recently demonstrated that [gamma]-TIP, one of the MIP homologs found in the vacuolar membrane of plant cells, is an aquaporin or water channel protein (C. Maurel, J. Reizer, J.I. Schroeder, M.J. Chrispeels [1993] EMBO J 12: 2241-2247). RD28, another MIP homolog in Arabidopsis thaliana, was first identified as being encoded by a turgor-responsive transcript. To find out if RD28 is a water channel protein, rd28 cRNA was injected into Xenopus laevis oocytes. Expression of RD28 caused a 10- to 15-fold increase in the osmotic water permeability of the oocytes, indicating that the protein creates water channels in the plasma membrane of the oocytes and is an aquaporin just like its homolog [gamma]-TIP. Although RD28 has ...
Marinelli RA, Pham L, Agre P, La Russo NF. Secretin promotes osmotic water transport in rat cholangiocytes by incresing aquaporin-1 water channels in plasma membrane. Evidence for a secretin-induced vesicular translocation of aquaporin-1. J Biol Chem 1997; 272: 12984-12988 ...
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
Aquaporin 8 (AQP8) is a water channel protein. Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). Aquaporin 8 mRNA is found in pancreas and colon but not other tissues. [provided by RefSeq, Jul 2008 ...
Aquaporin membrane protein, molecular model. Computer illustration showing the structure of a molecule of the human aquaporin 1 protein (blue, and white ribbon). Aquaporins are membrane proteins that form channels (centre) that help water molecules (red and white spheres) pass in and out of cells. Unlike ion channels, aquaporins help prevent ions and other dissolved substances carrying electrical charge from entering the cell, as they only allow lone water molecules or certain uncharged solutes to pass through. This helps maintain the electrochemical potential of the cell membrane. - Stock Image C035/5236
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This paper strongly supports the conclusion that AQP0 has a high permeability mode and a low permeability mode. How do these two modes differ? Available structural data on the nature of the water-filled pore through AQP1 and the glycerol facilitator suggest a possible answer. For both, water and glycerol must move through the pore by single-file diffusion. The crystal structure and molecular dynamic simulations suggest that there are multiple water molecules in the pore. There are ∼6 waters seen in the narrow constriction of the pore in the X-ray structure (Sui et al., 2001), and molecular dynamic simulations suggest that there are ∼7 or 8 water molecules moving in concert in the single-file portion of the pore (Tajkhorshid et al., 2002; Zhu et al., 2004). The lack of passage of ionic current through AQP0 and AQP1 is explained by electrostatic considerations that strongly inhibit the movement of protons into the NPA region or hydroxyls into regions flanking either side of the NPA region (de ...
The localization and transporting properties of a kidney protein homologous to human erythrocyte protein CHIP28 was evaluated. The cDNA encoding rat kidney protein CHIP28k was isolated from a rat renal cortex cDNA library. A 2.8-kb cDNA was identified which contained an 807 bp open reading frame encoding a 28.8 kD protein with 94% amino acid identity to CHIP28. in vitro translation of CHIP28k cDNA in rabbit reticulocyte lysate generated a 28-kD protein; addition of ER-derived microsomes gave a 32-kD transmembrane glycoprotein. Translation of truncated RNA demonstrated glycosylation of residue Asn42 which is predicted to lie between the first and second transmembrane domains. Expression of in vitro transcribed mRNA encoding CHIP28k in Xenopus oocytes increased oocyte osmotic water permeability (Pf) from (4 +/- 1) x 10(-4) to (33 +/- 4) x 10(-4) cm/s at 10 degrees C; the increase in oocyte Pf was weakly temperature dependent and inhibited by HgCl2. Two-electrode voltage clamp measurements ...
Described is a paving method of fine water-permeable concrete which can be used for roadways, sidewalks, bikeways, parking lots, public squares, etc. A base layer of water-permeable concrete is paved
TY - JOUR. T1 - Aquaporins and the respiratory system. T2 - Advice for a lung investigator. AU - King, Landon S.. AU - Nielsen, Søren. AU - Agre, Peter. PY - 2000/1. Y1 - 2000/1. UR - http://www.scopus.com/inward/record.url?scp=0033986166&partnerID=8YFLogxK. UR - http://www.scopus.com/inward/citedby.url?scp=0033986166&partnerID=8YFLogxK. M3 - Article. C2 - 10619856. AN - SCOPUS:0033986166. VL - 105. SP - 15. EP - 16. JO - Journal of Clinical Investigation. JF - Journal of Clinical Investigation. SN - 0021-9738. IS - 1. ER - ...
Müller glial cells are important regulators of physiological function of retina. In a model disease of retinal inflammation and spontaneous recurrent uveitis in horses (ERU), we could show that retinal Müller glial cells significantly change potassium and water channel protein expression during autoimmune pathogenesis. The most significantly changed channel protein in neuroinflammatory ERU was aquaporin 11 (AQP11). Aquaporins (AQP, 13 members) are important regulators of water and small solute transport through membranes. AQP11 is an unorthodox member of this family and was assigned to a third group of AQPs because of its difference in amino acid sequence (conserved sequence is only 11 %) and especially its largely unknown function. In order to gain insight into the distribution, localization, and function of AQP11 in the retina, we first developed a novel monoclonal antibody for AQP11 enabling quantification, localization, and functional studies. In the horse retina, AQP11 was exclusively expressed
Using computer simulations and experimental results, researchers at the University of Illinois at Urbana-Champaign and the University of Arizona have identified a key component of the gating mechanism in aquaporins that controls ...
For a proper functioning of epithelial cells, a polarized sorting and localization of channels and transporters that mediate transcellular ion and water movement is essential. Our work focuses on elucidating the routing regulation of wild-type AQP2/V2R, dissolving the underlying mechanisms for missorting of AQP2 mutants, and the identification of pharmacological chaperones, rescuing the cell surface expression of AQP2/V2R mutants in NDI.
In Chapter 6, "The Hormonal Essence of the T-Rex?" author Cordelia Fine considers the biological dogma that testes, and the powerful hormones they exude, are the root of all sexual inequality.. 0 Comments. ...
Buena vista" hypothesis suggests that changes in the sizes of eyes, rather than a shift from fins to limbs, led fish to transition to land more than 300 million years ago. 1 Comment. ...
Background Water channel required to promote glycerol permeability and water transport across cell membranes. May contribute to water transport in the upper portion of small intestine. Isoform 2 is not permeable to urea and...
Rabbit polyclonal antibody raised against recombinant Rat Aqp4. Recombinant protein corresponding to Rat Aqp4 C-terminus. (PAB28902) - Products - Abnova
Two previous articles in this series on aquaporins have discussed their history, mechanism and stimulation. The current article describes the role of AQP3 in regulating skin cell growth.
PH, Water, Oocytes, Xenopus, Human, Membrane, Permeability, Proteins, Family, Transient, Acidosis, Plasma, Rat, Antibodies, Aquaporins, Gene, Genes, Membrane Proteins, Blood, Cells
Background Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein...
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mqrrddpaar MSRSSGRSGS MDPSGAHPSV RQTPSRQPPL PHRSRGGGGG SRGGARASPA TQPPPLLPPS ATGPDATVGG PAPTPLLPPS ATasvkmepe nkylpelmae kdsldpsfth amqlltaeie kiqkgdskkd deenyldlfs hknmklkerv lipvkqypkf nfvgkilgpq gntikrlqee tgakisvlgk gsmrdkakee elrkgGDPKY ahlnmdlhvf ievfgppcea yalmahamee vkkflvpdmm ddicqeqfle lsylNGVPEP SRGRGVPVRG RGAAPPPPPV PRGRGVGPPR GALVRGtpvr gaitrgATVT RGVPPPPTVR GAPAprarta GIQRIPLPPP PAPETYEEyg yddtyaeqsy egyegYYSQS QGDSEYYDYG hgevqdsyea YGQDDWNGTR PSLKAPPARP VKGayrehpy ...
MGSNKSKPKD asqrrrslep aENVHGAGGG AFPASQTPSK PASADGHRGP SAAfapaaae pKLFGGFNSS DTVTSPQRAG PLAggvttfv alydyesrte tdlsfkkger lqivnntegd wwlahslsTG QTGYIPSNYV apsdsiqaee wyfgkitrre serlllnaen prgtflvres ettkgaycls vsdfdnakgl nvkhykirkl dsggfyitsr tqfnslqqlv ayyskhadgl chrlttVCPT SKPQtqglak daweipresl rlevklgqgc fgevwmgtwn gttrvaiktl kpgtmspeaf lqeaqvmkkl rheklvqlya vvseepiyiv teymskgsll dflkgetgky lrlpqlvdma aqiasgmayv ermnyvhrdl raanilvgen lvckvadfgl arliedneyt arqgakfpik wtapeaalyg rftiksdvws fgillteltt kgrvpypgmv nrevldqver gYRMPCPPEC PESlhdlmcq cwrkepeerp tfeylqafle dyftstepqy ...
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
According to recent reports, millions of people across the globe are suffering from arsenic (As) toxicity. Arsenic is present in different oxidative states in the environment and enters in the food chain through soil and water. In the agricultural field, irrigation with arsenic contaminated water, that is, having a higher level of arsenic contamination on the top soil, which may affects the quality of crop production. The major crop like rice (Oryza sativa L.) requires a considerable amount of water to complete its lifecycle. Rice plants potentially accumulate arsenic, particularly inorganic arsenic (iAs) from the field, in different body parts including grains. Different transporters have been reported in assisting the accumulation of arsenic in plant cells; for example, arsenate (AsV) is absorbed with the help of phosphate transporters, and arsenite (AsIII) through nodulin 26-like intrinsic protein (NIP) by the silicon transport pathway and plasma membrane intrinsic protein aquaporins. Researchers and
In plant sexual reproduction, water and solute movement are tightly regulated, suggesting the involvement of aquaporins. We previously identified TIP5;1 and TIP1;3 as the only Arabidopsis aquaporin genes that are selectively and highly expressed in mature pollen, and showed that they can transport both water and urea when expressed in Xenopus oocytes. Here, we show that TIP5;1 has unusual characteristics, as its water transport activity is regulated by pH. Analysis of the water transport activity of a mutant version of TIP5;1 (TIP5;1-H131A) and amino acid alignment with other plant aquaporins regulated by pH suggested that a conserved motif is involved in pH sensing. GFP-TIP5;1 is located in the mitochondria of pollen tubes. The single mutants tip1;3 and tip5;1, as well as the tip1;3 tip5;1 double mutant, are fertile, but all mutants had shorter than normal pollen tubes when germinated in vitro in the absence of exogenous nitrogen. Thus, we propose that TIP5;1 and TIP1;3 are involved in nitrogen ...
Aquaporin (AQP) proteins comprise a group of membrane intrinsic proteins (MIPs) that are responsible for transporting water and other small molecules, which is crucial for plant survival under stress conditions including salt stress. Despite the vital role of AQPs, little is known about them in cucumber (Cucumis sativus L.). In this study, we identified 39 aquaporin-encoding genes in cucumber that were separated by phylogenetic analysis into five sub-families (PIP, TIP, NIP, SIP, and XIP). Their substrate specificity was then assessed based on key amino acid residues such as the aromatic/Arginine (ar/R) selectivity filter, Frogers positions, and specificity-determining positions. The putative cis-regulatory motifs available in the promoter region of each AQP gene were analyzed and results revealed that their promoter regions contain many abiotic related cis-regulatory elements. Furthermore, analysis of previously released RNA-seq data revealed tissue- and treatment-specific expression patterns of
Mitochondrial swelling assay (PTP opening) - posted in Cell Biology: Hello.Anyone here with experience with the mitochondrial swelling assay for the measurement of the opening of the permeability transition pore? Im using the method that evaluates the decrease in absorbance at 540 nm. Im working with a fungus and theres nothing in the literature about this. I get a weird profile (see attachment).1) the temporal dynamics are quite different from what is ob...
The methylotrophic yeast P. pastoris has, during the last decades, increased in popularity as a eukaryotic host for recombinant protein expression [7]. Numerous reports have described successful overexpression of soluble proteins as well as of membrane proteins in this system, but sufficient protein yields have not always been obtained. Several methods have been described that could be used to improve the outcome of expression trials, among which an optimisation of recombinant gene dosage has proven to be one of the most potent ones [21]. When it comes to the aquaporin family of membrane proteins, optimisation of the nucleotide sequence both regarding codon composition and AT content [38] and controlled growth in bioreactors [36] have been reported to improve the yields of heterologous protein. However, in no reports has a systematic examination of the effect of gene dosage on recombinant aquaporin expression in P. pastoris been done and results obtained for other membrane proteins [12, 15, 33] ...