Aquaglyceroporins: A subgroup of aquaporins that transport WATER; GLYCEROL; and other small solutes across CELL MEMBRANES.Aquaporins: A class of porins that allow the passage of WATER and other small molecules across CELL MEMBRANES.Glycerol: A trihydroxy sugar alcohol that is an intermediate in carbohydrate and lipid metabolism. It is used as a solvent, emollient, pharmaceutical agent, and sweetening agent.Aquaporin 3: Aquaporin 3 is an aquaglyceroporin that is expressed in the KIDNEY COLLECTING DUCTS and is constitutively localized at the basolateral MEMBRANE.Dihydroxyacetone: A ketotriose compound. Its addition to blood preservation solutions results in better maintenance of 2,3-diphosphoglycerate levels during storage. It is readily phosphorylated to dihydroxyacetone phosphate by triokinase in erythrocytes. In combination with naphthoquinones it acts as a sunscreening agent.Aquaporin 1: Aquaporin 1 forms a water-specific channel that is constitutively expressed at the PLASMA MEMBRANE of ERYTHROCYTES and KIDNEY TUBULES, PROXIMAL. It provides these cells with a high permeability to WATER. In humans polymorphisms of this protein result in the Colton blood group antigen.Water: A clear, odorless, tasteless liquid that is essential for most animal and plant life and is an excellent solvent for many substances. The chemical formula is hydrogen oxide (H2O). (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Biological Transport: The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.Xenopus: An aquatic genus of the family, Pipidae, occurring in Africa and distinguished by having black horny claws on three inner hind toes.Adipose Tissue: Specialized connective tissue composed of fat cells (ADIPOCYTES). It is the site of stored FATS, usually in the form of TRIGLYCERIDES. In mammals, there are two types of adipose tissue, the WHITE FAT and the BROWN FAT. Their relative distributions vary in different species with most adipose tissue being white.Omentum: A double-layered fold of peritoneum that attaches the STOMACH to other organs in the ABDOMINAL CAVITY.Organic Chemicals: A broad class of substances containing carbon and its derivatives. Many of these chemicals will frequently contain hydrogen with or without oxygen, nitrogen, sulfur, phosphorus, and other elements. They exist in either carbon chain or carbon ring form.Pleistophora: A genus of parasitic FUNGI in the family Pleistophoridae that infects humans.Subcutaneous Fat: Fatty tissue under the SKIN through out the body.Glycerol Kinase: An enzyme that catalyzes the formation of glycerol 3-phosphate from ATP and glycerol. Dihydroxyacetone and L-glyceraldehyde can also act as acceptors; UTP and, in the case of the yeast enzyme, ITP and GTP can act as donors. It provides a way for glycerol derived from fats or glycerides to enter the glycolytic pathway. EC 18.104.22.168.Adipocytes: Cells in the body that store FATS, usually in the form of TRIGLYCERIDES. WHITE ADIPOCYTES are the predominant type and found mostly in the abdominal cavity and subcutaneous tissue. BROWN ADIPOCYTES are thermogenic cells that can be found in newborns of some species and hibernating mammals.National Academy of Sciences (U.S.): A United States organization of distinguished scientists and engineers established for the purpose of investigating and reporting upon any subject of art or science as requested by any department of government. The National Research Council organized by NAS serves as the principal operating agency to stimulate and support research.Jervell-Lange Nielsen Syndrome: A form of long QT syndrome that is associated with congenital deafness. It is characterized by abnormal cardioelectrophysiology involving the VOLTAGE-GATED POTASSIUM CHANNEL. It results from mutation of KCNQ1 gene (Subtype 1 or JLN1) or the KCNE1 gene (Subtype 2 or JLN2).Gestalt Therapy: A form of psychotherapy with emphasis on the interplay of organism and environment. Basic to this therapy is the development of awareness and maturity, as well as self-confidence.Institute of Medicine (U.S.): Identifies, for study and analysis, important issues and problems that relate to health and medicine. The Institute initiates and conducts studies of national policy and planning for health care and health-related education and research; it also responds to requests from the federal government and other agencies for studies and advice.Neuropsychology: A branch of psychology which investigates the correlation between experience or behavior and the basic neurophysiological processes. The term neuropsychology stresses the dominant role of the nervous system. It is a more narrowly defined field than physiological psychology or psychophysiology.Nobel PrizeAcademies and Institutes: Organizations representing specialized fields which are accepted as authoritative; may be non-governmental, university or an independent research organization, e.g., National Academy of Sciences, Brookings Institution, etc.Carbon Dioxide: A colorless, odorless gas that can be formed by the body and is necessary for the respiration cycle of plants and animals.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Entomology: A discipline or occupation concerned with the study of INSECTS, including the biology and the control of insects.Ammonia: A colorless alkaline gas. It is formed in the body during decomposition of organic materials during a large number of metabolically important reactions. Note that the aqueous form of ammonia is referred to as AMMONIUM HYDROXIDE.Publications: Copies of a work or document distributed to the public by sale, rental, lease, or lending. (From ALA Glossary of Library and Information Science, 1983, p181)Permeability: Property of membranes and other structures to permit passage of light, heat, gases, liquids, metabolites, and mineral ions.Moon: The natural satellite of the planet Earth. It includes the lunar cycles or phases, the lunar month, lunar landscapes, geography, and soil.Bibliometrics: The use of statistical methods in the analysis of a body of literature to reveal the historical development of subject fields and patterns of authorship, publication, and use. Formerly called statistical bibliography. (from The ALA Glossary of Library and Information Science, 1983)Floods: Sudden onset water phenomena with different speed of occurrence. These include flash floods, seasonal river floods, and coastal floods, associated with CYCLONIC STORMS; TIDALWAVES; and storm surges.Forensic Sciences: Disciplines that apply sciences to law. Forensic sciences include a wide range of disciplines, such as FORENSIC TOXICOLOGY; FORENSIC ANTHROPOLOGY; FORENSIC MEDICINE; FORENSIC DENTISTRY; and others.Research: Critical and exhaustive investigation or experimentation, having for its aim the discovery of new facts and their correct interpretation, the revision of accepted conclusions, theories, or laws in the light of newly discovered facts, or the practical application of such new or revised conclusions, theories, or laws. (Webster, 3d ed)Phaeophyta: A division of predominantly marine EUKARYOTA, commonly known as brown algae, having CHROMATOPHORES containing carotenoid PIGMENTS, BIOLOGICAL. ALGINATES and phlorotannins occur widely in all major orders. They are considered the most highly evolved algae because of their well-developed multicellular organization and structural complexity.Chlorella: Nonmotile unicellular green algae potentially valuable as a source of high-grade protein and B-complex vitamins.Phycodnaviridae: A family of DNA plant viruses that infect eukaryotic algae.Germ Cells, Plant: The reproductive cells of plants.Chlorella vulgaris: A species of green microalgae in the family Chlorellaceae. It is used as a model organism for PHOTOSYNTHESIS, and as a food supplement (DIETARY SUPPLEMENTS).Potassium Channels: Cell membrane glycoproteins that are selectively permeable to potassium ions. At least eight major groups of K channels exist and they are made up of dozens of different subunits.Ion Channels: Gated, ion-selective glycoproteins that traverse membranes. The stimulus for ION CHANNEL GATING can be due to a variety of stimuli such as LIGANDS, a TRANSMEMBRANE POTENTIAL DIFFERENCE, mechanical deformation or through INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS.Trypanosoma brucei brucei: A hemoflagellate subspecies of parasitic protozoa that causes nagana in domestic and game animals in Africa. It apparently does not infect humans. It is transmitted by bites of tsetse flies (Glossina).Trypanosomiasis, African: A disease endemic among people and animals in Central Africa. It is caused by various species of trypanosomes, particularly T. gambiense and T. rhodesiense. Its second host is the TSETSE FLY. Involvement of the central nervous system produces "African sleeping sickness." Nagana is a rapidly fatal trypanosomiasis of horses and other animals.Trypanosoma cruzi: The agent of South American trypanosomiasis or CHAGAS DISEASE. Its vertebrate hosts are man and various domestic and wild animals. Insects of several species are vectors.Trypanocidal Agents: Agents destructive to the protozoal organisms belonging to the suborder TRYPANOSOMATINA.Dihydroxyacetone Phosphate: An important intermediate in lipid biosynthesis and in glycolysis.Osmeriformes: An order of fish including smelts, galaxiids, and salamanderfish.Salmoniformes: An order of fish comprising salmons, trouts, whitefish, graylings, and other families. They are both marine and freshwater fish, found in all oceans and are quite numerous in the Northern Hemisphere. (From Nelson: Fishes of the World)Anura: An order of the class Amphibia, which includes several families of frogs and toads. They are characterized by well developed hind limbs adapted for jumping, fused head and trunk and webbed toes. The term "toad" is ambiguous and is properly applied only to the family Bufonidae.Vocalization, Animal: Sounds used in animal communication.Sound: A type of non-ionizing radiation in which energy is transmitted through solid, liquid, or gas as compression waves. Sound (acoustic or sonic) radiation with frequencies above the audible range is classified as ultrasonic. Sound radiation below the audible range is classified as infrasonic.Intestine, Large: A segment of the LOWER GASTROINTESTINAL TRACT that includes the CECUM; the COLON; and the RECTUM.Skin: The outer covering of the body that protects it from the environment. It is composed of the DERMIS and the EPIDERMIS.
Channel-dependent permeation of water and glycerol in mouse morulae. (1/34)The cryosensitivity of mammalian embryos depends on the stage of development. Because permeability to water and cryoprotectants plays an important role in cryopreservation, it is plausible that the permeability is involved in the difference in the tolerance to cryopreservation among embryos at different developmental stages. In this study, we examined the permeability to water and glycerol of mouse oocytes and embryos, and tried to deduce the pathway for the movement of water and glycerol. The water permeability (L(P), microm min(-1) atm(-1)) of oocytes and four-cell embryos at 25 degrees C was low (0.63-0.70) and its Arrhenius activation energy (E(a), kcal/mol) was high (11.6-12.3), which implies that the water permeates through the plasma membrane by simple diffusion. On the other hand, the L(p) of morulae and blastocysts was quite high (3.6-4.5) and its E(a) was quite low (5.1-6.3), which implies that the water moves through water channels. Aquaporin inhibitors, phloretin and p-(chloromercuri) benzene-sulfonate, reduced the L(p) of morulae significantly but not that of oocytes. By immunocytochemical analysis, aquaporin 3, which transports not only water but also glycerol, was detected in the morulae but not in the oocytes. Accordingly, the glycerol permeability (P(GLY), x 10(-3) cm/min) of oocytes was also low (0.01) and its E(a) was remarkably high (41.6), whereas P(GLY) of morulae was quite high (4.63) and its E(a) was low (10.0). Aquaporin inhibitors reduced the P(GLY) of morulae significantly. In conclusion, water and glycerol appear to move across the plasma membrane mainly by simple diffusion in oocytes but by facilitated diffusion through water channel(s) including aquaporin 3 in morulae. (+info)
Chlorella virus MT325 encodes water and potassium channels that interact synergistically. (2/34)Fast and selective transport of water through cell membranes is facilitated by water channels. Water channels belonging to the major intrinsic proteins (MIPs) family have been found in all three domains of life, Archaea, Bacteria, and Eukarya. Here we show that Chlorella virus MT325 has a water channel gene, aqpv1, that forms a functional aquaglyceroporin in oocytes. aqpv1 is transcribed during infection together with MT325 kcv, a gene encoding a previously undescribed type of viral potassium channel. Coexpression of AQPV1 and MT325-Kcv in Xenopus oocytes synergistically increases water transport, suggesting a possible concerted action of the two channels in the infection cycle. The two channels operate by a thermodynamically coupled mechanism that simultaneously alters water conductance and driving force for water movement. Considering the universal role of osmosis, this mechanism is relevant to any cell coexpressing water and potassium channels and could have pathological as well as basic physiological relevance. (+info)
Methylarsonous acid transport by aquaglyceroporins. (3/34)Many mammals methylate trivalent inorganic arsenic in liver to species that are released into the bloodstream and excreted in urine and feces. This study addresses how methylated arsenicals pass through cell membranes. We have previously shown that aquaglyceroporin channels, including Escherichia coli GlpF, Saccharomyces cerevisiae Fps1p, AQP7, and AQP9 from rat and human, conduct trivalent inorganic arsenic [As(III)] as arsenic trioxide, the protonated form of arsenite. One of the initial products of As(III) methylation is methylarsonous acid [MAs(III)], which is considerably more toxic than inorganic As(III). In this study, we investigated the ability of GlpF, Fps1p, and AQP9 to facilitate movement of MAs(III) and found that rat aquaglyceroporin conducted MAs(III) at a higher rate than the yeast homologue. In addition, rat AQP9 facilitates MAs(III) at a higher rate than As(III). These results demonstrate that aquaglyceroporins differ both in selectivity for and in transport rates of trivalent arsenicals. In this study, the requirement of AQP9 residues Phe-64 and Arg-219 for MAs(III) movement was examined. A hydrophobic residue at position 64 is not required for MAs(III) transport, whereas an arginine at residue 219 may be required. This is similar to that found for As(III), suggesting that As(III) and MAs(III) use the same translocation pathway in AQP9. Identification of MAs(III) as an AQP9 substrate is an important step in understanding physiologic responses to arsenic in mammals, including humans. (+info)
Enhanced expression of multidrug resistance-associated protein 2 and reduced expression of aquaglyceroporin 3 in an arsenic-resistant human cell line. (4/34)Arsenic-resistant cells (R15), derived from a human lung adenocarcinoma cell line (CL3), were 10-fold more resistant to sodium arsenite (As(III)). Because R15 cells accumulated less arsenic than parental CL3 cells, this arsenic resistance may be due to higher efflux and/or lower uptake of As(III). We therefore compared expression of the multidrug resistance-associated proteins MRP1, MRP2, and MRP3 in these two cell lines. MRP2 expression was 5-fold higher in R15 cells than in CL3 cells, whereas MRP1 and MRP3 expression levels were similar. Furthermore, verapamil and cyclosporin A, inhibitors of multidrug resistance transporters, significantly reduced the efflux of arsenic from R15. Thus, increased arsenic extrusion by MRP2 may contribute to arsenic resistance in R15 cells. We also examined the expression of several aquaglyceroporins (AQPs), which mediate As(III) uptake by cells. Little AQP7 or AQP9 mRNA was detected by reverse transcription-PCR in either cell line, whereas AQP3 mRNA expression was 2-fold lower in R15 cells than in CL3 cells. When AQP3 expression in CL3 cells was knocked down by RNA interference, CL3 cells accumulated less arsenic and became more resistant to As(III). Conversely, overexpression of AQP3 in human embryonic kidney 293T cells increased arsenic accumulation, and the cells were more susceptible to As(III) than 293T cells transfected with vector alone. These results suggest that AQP3 is involved in As(III) accumulation. Taken together, our results suggest that enhanced expression of MRP2 and lower expression of AQP3 are responsible for lower arsenic accumulation in arsenic-resistant R15 cells. (+info)
The structure, function and regulation of the nodulin 26-like intrinsic protein family of plant aquaglyceroporins. (5/34)The nodulin 26-like intrinsic protein family is a group of highly conserved multifunctional major intrinsic proteins that are unique to plants, and which transport a variety of uncharged solutes ranging from water to ammonia to glycerol. Based on structure-function studies, the NIP family can be subdivided into two subgroups (I and II) based on the identity of the amino acids in the selectivity-determining filter (ar/R region) of the transport pore. Both subgroups appear to contain multifunctional transporters with low to no water permeability and the ability to flux multiple uncharged solutes of varying sizes depending upon the composition of the residues of the ar/R filter. NIPs are subject to posttranslational phosphorylation by calcium-dependent protein kinases. In the case of the family archetype, soybean nodulin 26, phosphorylation has been shown to stimulate its transport activity and to be regulated in response to developmental as well as environmental cues, including osmotic stresses. NIPs tend to be expressed at low levels in the plant compared to other MIPs, and several exhibit cell or tissue specific expression that is subject to spatial and temporal regulation during development. (+info)
Sequence and annotation of the 314-kb MT325 and the 321-kb FR483 viruses that infect Chlorella Pbi. (6/34)Viruses MT325 and FR483, members of the family Phycodnaviridae, genus Chlorovirus, infect the fresh water, unicellular, eukaryotic, chlorella-like green alga, Chlorella Pbi. The 314,335-bp genome of MT325 and the 321,240-bp genome of FR483 are the first viruses that infect Chlorella Pbi to have their genomes sequenced and annotated. Furthermore, these genomes are the two smallest chlorella virus genomes sequenced to date, MT325 has 331 putative protein-encoding and 10 tRNA-encoding genes and FR483 has 335 putative protein-encoding and 9 tRNA-encoding genes. The protein-encoding genes are almost evenly distributed on both strands, and intergenic space is minimal. Approximately 40% of the viral gene products resemble entries in public databases, including some that are the first of their kind to be detected in a virus. For example, these unique gene products include an aquaglyceroporin in MT325, a potassium ion transporter protein and an alkyl sulfatase in FR483, and a dTDP-glucose pyrophosphorylase in both viruses. Comparison of MT325 and FR483 protein-encoding genes with the prototype chlorella virus PBCV-1 indicates that approximately 82% of the genes are present in all three viruses. (+info)
Aquaglyceroporin PbAQP during intraerythrocytic development of the malaria parasite Plasmodium berghei. (7/34)The malaria parasite can use host plasma glycerol for lipid biosynthesis and membrane biogenesis during the asexual intraerythrocytic development. The molecular basis for glycerol uptake into the parasite is undefined. We hypothesize that the Plasmodium aquaglyceroporin provides the pathway for glycerol uptake into the malaria parasite. To test this hypothesis, we identified the orthologue of Plasmodium falciparum aquaglyceroporin (PfAQP) in the rodent malaria parasite, Plasmodium berghei (PbAQP), and examined the biological role of PbAQP by performing a targeted deletion of the PbAQP gene. PbAQP and PfAQP are 62% identical in sequence. In contrast to the canonical NPA (Asn-Pro-Ala) motifs in most aquaporins, the PbAQP has NLA (Asn-Leu-Ala) and NPS (Asn-Leu-Ser) in those positions. PbAQP expressed in Xenopus oocytes was permeable to water and glycerol, suggesting that PbAQP is an aquaglyceroporin. In P. berghei, PbAQP was localized to the parasite plasma membrane. The PbAQP-null parasites were viable; however, they were highly deficient in glycerol transport. In addition, they proliferated more slowly compared with the WT parasites, and mice infected with PbAQP-null parasites survived longer. Taken together, these findings suggest that PbAQP provides the pathway for the entry of glycerol into P. berghei and contributes to the growth of the parasite during the asexual intraerythrocytic stages of infection. In conclusion, we demonstrate here that PbAQP plays an important role in the blood-stage development of the rodent malaria parasite during infection in mice and could be added to the list of targets for the design of antimalarial drugs. (+info)
An arsenate-activated glutaredoxin from the arsenic hyperaccumulator fern Pteris vittata L. regulates intracellular arsenite. (8/34)To elucidate the mechanisms of arsenic resistance in the arsenic hyperaccumulator fern Pteris vittata L., a cDNA for a glutaredoxin (Grx) Pv5-6 was isolated from a frond expression cDNA library based on the ability of the cDNA to increase arsenic resistance in Escherichia coli. The deduced amino acid sequence of Pv5-6 showed high homology with an Arabidopsis chloroplastic Grx and contained two CXXS putative catalytic motifs. Purified recombinant Pv5-6 exhibited glutaredoxin activity that was increased 1.6-fold by 10 mm arsenate. Site-specific mutation of Cys(67) to Ala(67) resulted in the loss of both GRX activity and arsenic resistance. PvGrx5 was expressed in E. coli mutants in which the arsenic resistance genes of the ars operon were deleted (strain AW3110), a deletion of the gene for the ArsC arsenate reductase (strain WC3110), and a strain in which the ars operon was deleted and the gene for the GlpF aquaglyceroporin was disrupted (strain OSBR1). Expression of PvGrx5 increased arsenic tolerance in strains AW3110 and WC3110, but not in OSBR1, suggesting that PvGrx5 had a role in cellular arsenic resistance independent of the ars operon genes but dependent on GlpF. AW3110 cells expressing PvGrx5 had significantly lower levels of arsenite when compared with vector controls when cultured in medium containing 2.5 mm arsenate. Our results are consistent with PvGrx5 having a role in regulating intracellular arsenite levels, by either directly or indirectly modulating the aquaglyceroporin. To our knowledge, PvGrx5 is the first plant Grx implicated in arsenic metabolism. (+info)
... are recognized as a subset of the aquaporin family of proteins which conduct water, glycerol and other small ... Aquaglyceroporins are found in many species including bacteria, plants and humans. Because of their ubiquitous nature they are ... They have been identified as a possible source of metalloid contamination in agriculture as aquaglyceroporins were have been ... Madeira, Ana; Moura, Teresa F.; Soveral, Graça (2015-02-01). "Aquaglyceroporins: implications in adipose biology and obesity". ...
Major intrinsic proteins
The aquaglyceroporins are permeable to water, but also to other small uncharged molecules such as glycerol. The third subfamily ... Hub, Jochen S.; de Groot, Bert L. (2008-01-29). "Mechanism of selectivity in aquaporins and aquaglyceroporins". Proceedings of ... The MIP superfamily includes three subfamilies: aquaporins, aquaglyceroporins and S-aquaporins. The aquaporins (AQPs) are water ...
Some of them, known as aquaglyceroporins, also transport other small uncharged dissolved molecules including ammonia, CO2, ... function and regulation of the nodulin 26-like intrinsic protein family of plant aquaglyceroporins". Biochim. Biophys. Acta. ...
List of MeSH codes (D12.776.157)
... aquaglyceroporins MeSH D12.776.157.530.400.500.040.249.500 -- aquaporin 3 MeSH D12.776.157.530.400.500.040.249.750 -- aquaporin ...
List of MeSH codes (D12.776.543)
... aquaglyceroporins MeSH D12.776.543.550.425.730.040.249.500 -- aquaporin 3 MeSH D12.776.543.550.425.730.040.249.750 -- aquaporin ... aquaglyceroporins MeSH D12.776.543.585.400.730.040.249.500 -- aquaporin 3 MeSH D12.776.543.585.400.730.040.249.750 -- aquaporin ...
Aims/objectives: Glycerol cycling plays an essential regulatory role in metabolism in both health and disease. Aquaporins (AQPs) are a recently described family of water transporting membrane proteins, which contain a subset of members that also have the ability to transport glycerol across the cell membrane. This study sought to investigate the adipose tissue expression profile of AQPs in humans, and to assess the role of AQPs in adipocyte differentiation.. Methods: AQP expression was assessed in ex vivo human adipose tissue samples and isolated human adipocytes. Mouse 3T3 L1 and human SGBS cells were also used for expression and differentiation studies. SYBR Green real-time PCR and Western Blotting were used to detect mRNA and protein expression respectively.. Results: AQP 3 and 7 were expressed in omental adipose tissue at a significantly higher level than in corresponding subcutaneous adipose tissue samples. AQP 7 was the most abundantly expressed aquaporin in both depots. In differentiating ...
Solute transport on the sub 100 ms scale across the lipid bilayer membrane of individual proteoliposomes - Lunds universitet
Screening assays designed to probe ligand and drug-candidate regulation of membrane proteins responsible for ion-translocation across the cell membrane are wide spread, while efficient means to screen membrane-protein facilitated transport of uncharged solutes are sparse. We report on a microfluidic-based system to monitor transport of uncharged solutes across the membrane of multiple (,100) individually resolved surface-immobilized liposomes. This was accomplished by rapidly switching (,10 ms) the solution above dye-containing liposomes immobilized on the floor of a microfluidic channel. With liposomes encapsulating the pH-sensitive dye carboxyfluorescein (CF), internal changes in pH induced by transport of a weak acid (acetic acid) could be measured at time scales down to 25 ms. The applicability of the set up to study biological transport reactions was demonstrated by examining the osmotic water permeability of human aquaporin (AQP5) reconstituted in proteoliposomes. In this case, the rate of ...
Stahl, Katja; Rahmani, Soulmaz; Prydz, Agnete; Skauli, Nadia; MacAulay, Nanna; Mylonakou, Maria-Niki; Torp, Reidun; Skare, Øivind; Berg, Torill; Leergaard, Trygve Brauns; Paulsen, Ragnhild Elisabeth; Ottersen, Ole Petter & Amiry-Moghaddam, Mahmood (2018). Targeted deletion of the aquaglyceroporin AQP9 is protective in a mouse model of Parkinsons disease. PLOS ONE. ISSN 1932-6203. 13(3) . doi: 10.1371/journal.pone.0194896 Fulltekst i vitenarkiv. Vis sammendrag More than 90% of the cases of Parkinsons disease have unknown etiology. Gradual loss of dopaminergic neurons of substantia nigra is the main cause of morbidity in this disease. External factors such as environmental toxins are believed to play a role in the cell loss, although the cause of the selective vulnerability of dopaminergic neurons remains unknown. We have previously shown that aquaglyceroporin AQP9 is expressed in dopaminergic neurons and astrocytes of rodent brain. AQP9 is permeable to a broad spectrum of substrates including ...
Human and rodent erythrocytes are known to be highly permeable to glycerol. Aquaglyceroporin aquaporin (AQP)3 is the major glycerol channel in human and rat erythrocytes. However, AQP3 expression has not been observed in ...
The zebrafish genome encodes the largest vertebrate repertoire of functional aquaporins with dual paralogy and substrate...
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 ...
Characterization and Prediction of Partition Coefficients of Uncharged Solutes into Micelles and Liposomes using Electrokinetic...
Liposome and micelle electrokinetic chromatography (EKC) were used to determine retention factors (k) that are directly related to partition coefficients (K) and the phase ratio (φ) as: k = K*φ. Linear solvation energy relationship (LSER) models were used to elucidate the contributions of solute partitioning into liposomes. In addition, an LSER model for both MEKC and LEKC was used to determine partition coefficients for solutes without observed partition coefficients. The observed partition coefficients and those determined from LSER were then used to predict partition coefficients with the group contribution approach (GCA) and the fragmental constant approach (FCA) from solute structure. In the GCA, a relatively small number of key monosubstituted aromatic and aliphatic solutes are used to determine the substituent constants of functional groups. These substituent constants as well as the contributions from aromatic and aliphatic carbon plus hydrogen are used to predict partition ...
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 ...
Aquaglyceroporin PbAQP during intraerythrocytic development of the malaria parasite Plasmodium berghei. (2007 Feb 13, Proc Natl Acad Sci U S A) PubMed / full text ...
Patent US20040116949 - Apparatus and methods for forming gastrointestinal tissue approximations - Google Patents
Apparatus and methods are provided for forming a gastrointestinal tissue fold by engaging tissue at a first tissue contact point, moving the first tissue contact point from a position initially distal to a second tissue contact point to a position proximal of the second contact point to form a tissue fold, and extending an anchor assembly through the tissue fold near the second tissue contact point.
Arsenic is a toxic metalloid which is widely distributed in nature. It is normally present as arsenate under oxic conditions while arsenite is predominant under reducing condition. The major discharges of arsenic in the environment are mainly due to natural sources such as aquifers and anthropogenic sources. It is known that arsenite salts are more toxic than arsenate as it binds with vicinal thiols in pyruvate dehydrogenase while arsenate inhibits the oxidative phosphorylation process. The common mechanisms for arsenic detoxification are uptaken by phosphate transporters, aquaglyceroporins, and active extrusion system and reduced by arsenate reductases via dissimilatory reduction mechanism. Some species of autotrophic and heterotrophic microorganisms use arsenic oxyanions for their regeneration of energy. Certain species of microorganisms are able to use arsenate as their nutrient in respiratory process. Detoxification operons are a common form of arsenic resistance in microorganisms. Hence, the use of
Antiproliferative effect of dihydroxyacetone on Trypanosoma brucei bloodstream forms: cell cycle progression, subcellular...
We evaluated the effects of dihydroxyacetone (DHA) on Trypanosoma brucei bloodstream forms. DHA is considered an energy source for many different cell types. T. brucei takes up DHA readily due to the presence of aquaglyceroporins. However, the parasi
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
Companies Related to 'Collection of Gastrointestinal Tissue Samples for the Characterization and ex Vivo Functional Assessment...
Search Results for Collection of Gastrointestinal Tissue Samples for the Characterization and ex Vivo Functional Assessment of Chemoreceptors company records on BioPortfolio
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IJMS | Free Full-Text | Lipopolysaccharide Modifies Glycerol Permeability and Metabolism in 3T3-L1 Adipocytes
Aquaglyceroporins-aquaporin membrane channels (AQP) that conduct glycerol and other small neutral solutes in addition to water-play major roles in obesity. In adipocytes, aquaglyceroporins mediate glycerol uptake and release across the plasma membrane, which are two key steps for triacylglycerols (TAGs) synthesis (lipogenesis) and hydrolysis (lipolysis). The aim of this study was to assess both glycerol permeability and metabolism in undifferentiated 3T3-L1 cells (UDCs) as well as in untreated (CTL-DCs) versus lipopolysaccharide (LPS-DCs)-treated differentiated 3T3-L1 adipocytes. Glycerol release, TAGs content and whole membrane glycerol permeability were significantly increased in DCs as compared to UDCs. Moreover, in DCs, LPS treatment significantly increased TAGs content and decreased glycerol permeability. In addition, a significant reduction in whole membrane glycerol permeability was observed in LPS-DCs as compared to CTL-DCs. The relative contributions of AQP3, AQP7 and AQP9 (facilitated
The aquaglyceroporin AQP9 contributes to the sex-specific effects of in utero arsenic exposure on placental gene expression |...
Open peer review is a system where authors know who the reviewers are, and the reviewers know who the authors are. If the manuscript is accepted, the named reviewer reports are published alongside the article. Pre-publication versions of the article and author comments to reviewers are available by contacting [email protected] All previous versions of the manuscript and all author responses to the reviewers are also available.. You can find further information about the peer review system here.. ...
Dr Tim Downing, one of the papers first authors from NUI Galway and the Sanger Institute said: "We discovered that many of the parasites that were resistant to antimonial drug treatment had just two additional DNA bases in the gene LdAQP1, which produces an aquaglyceroporin protein. This insertion produces a scrambled version of this protein that can no longer move small molecules - including antimonials - across its cell membrane. These strains of L. donovani are likely to be resistant because they cannot take in the drugs.". Dr James Cotton, senior author of the study from the Sanger Institute said: "If you want to control visceral leishmaniasis, you need to understand what is going on at the geographic epicentre of the disease, and you need to be able to see changes at the level of individual DNA bases in the parasites genomes. Until now studies have been limited to looking at small regions of the parasites DNA or at what happens in the laboratory. To truly understand what is happening in ...
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Free delivery and returns on eligible orders. Buy Magic Show 100g 99.99% Pure Bismuth Metal Metalloid Element 83 With Label at UK.
This page is designed to be viewed by a browser which supports Netscapes Frames extension. This text will be shown by browsers which do not support the Frames extension.. ...
metalloid: A chemical element with properties intermediate between those of typical metals and nonmetals. Usually considered under this classification are the chemical elements boron, silicon,...
Characterization of glycerol uptake and glycerol kinase activity in rat hepatocytes cultured under different hormonal...
Glycerol uptake and glycerol kinase activity were studied in primary cultures of rat hepatocytes in the presence of either 1 nM insulin, 1 nM glucagon, or 100 nM dexamethasone, alone or in combination in
SWISS-MODEL Template Library (SMTL) entry for 1lda. CRYSTAL STRUCTURE OF THE E. COLI GLYCEROL FACILITATOR (GLPF) WITHOUT SUBSTRATE GLYCEROL
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Somatostatin binding in human gastrointestinal tissues: effect of cations and somatostatin analogues. | Gut
This study characterises the somatostatin binding site in human gastrointestinal cancer and mucosa in terms of cationic specificity and relative affinity for three somatostatin analogues. Competitive displacement assays were performed on plasma membranes from human gastric and colonic tissues using radiolabelled somatostatin-14 as ligand. Comparison was made with the somatostatin binding site in rat cerebral cortex. In gastrointestinal tissue, magnesium decreased and sodium increased specific binding. By contrast, in rat cerebral cortex, the converse cationic effect was seen. These changes resulted from alterations in receptor density, with no change in receptor affinity. Displacement studies were then performed with somatostatin-14 and somatostatin analogues RC-160, somatuline, and octreotide. RC-160 and somatuline displaced radiolabel from binding sites in gastric and colonic cancer and mucosa with 10-fold lower affinity than the native peptide. Octreotide did not displace radioligand in ...
(Phys.org) -Boron is the ambivert of atoms. Technically classified as a metalloid, boron can undergo organic reactions, forming covalent bonds like carbon, but it can also form ions resulting in metal-like bonds. Several ...
Estrogen prevents increased hepatic aquaporin-9 expression and glycerol uptake during starvation. | IRIS Univ. Bari
In starvation, glycerol is released from adipose tissue and serves as an important precursor for hepatic gluconeogenesis. By unknown gender-specific mechanisms, women suppress the endogenous glucose production better than men and respond to metabolic stress with higher plasma glycerol levels. Hepatic glycerol uptake is facilitated by aquaporin-9 (AQP9), a broad-selectivity neutral solute channel, and represents an insulin-regulated step in supplying gluconeogenesis with glycerol. In the current study, hepatic AQP9 abundance was increased 2.6-fold in starved male rats as assessed by immunoblotting and immunohistochemistry. By contrast, starvation had no significant effect on hepatic AQP9 expression in female rats. Coordinately, plasma glycerol levels remained unchanged upon starvation in male rats whereas it was increased in female rats. The different responses to starvation were paralleled by higher glycerol permeability in basolateral hepatocyte membranes from starved male rats as compared to ...
Iron and Metals & Metalloids. Chapters 179 & 184 Arthur Amin Olyai. Iron Physiology and Pharmacology. Approx. 30 000 calls to Poison center yearly Usually involves young children < 6 y/o Risk of death without aggressive measures Slideshow 175976 by issac
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 ...
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 ...
Aquaglyceroporins - Wikipedia
Aquaglyceroporins are recognized as a subset of the aquaporin family of proteins which conduct water, glycerol and other small ... Aquaglyceroporins are found in many species including bacteria, plants and humans. Because of their ubiquitous nature they are ... They have been identified as a possible source of metalloid contamination in agriculture as aquaglyceroporins were have been ... Madeira, Ana; Moura, Teresa F.; Soveral, Graça (2015-02-01). "Aquaglyceroporins: implications in adipose biology and obesity". ...https://en.wikipedia.org/wiki/Aquaglyceroporins
A current view of the mammalian aquaglyceroporins. - PubMed - NCBI
A current view of the mammalian aquaglyceroporins.. Rojek A1, Praetorius J, Frøkiaer J, Nielsen S, Fenton RA. ... Aquaglyceroporins have a wide tissue distribution, and emerging data suggest that several of them may play previously ... Aquaporins in this latter class, the so-called aquaglyceroporins, transport small uncharged molecules such as glycerol and urea ... This review comprehensively discusses the recent discoveries in the field of aquaglyceroporins, alongside a brief overview of ...https://www.ncbi.nlm.nih.gov/pubmed/17961083?dopt=Abstract
A role for aquaglyceroporins in adipogenesis
... James Brown1, Matthew Conner1, Roslyn Bill1, Manjunath Ramanjaneya2, Clifford ...http://www.endocrine-abstracts.org/ea/0021/ea0021p153.htm
Quantification of the Intracellular Life Time of Water Molecules to Measure Transport Rates of Human Aquaglyceroporins |...
... while aquaglyceroporins facilitate the diffusion of small uncharged molecules such as glycerol and... ... The Human Aquaglyceroporins Facilitate the Transport of Glycerol. The main substrate for aquaglyceroporins is known to be ... Quantification of aquaglyceroporins levels in the plasma membrane. a Quantitative Western blot analyses of aquaglyceroporins ... where the endogenous aquaporins/aquaglyceroporins have been removed and human aquaglyceroporins AQP3, AQP7, and AQP9 are ...https://link.springer.com/article/10.1007/s00232-017-9988-4
Insulin- and Leptin-Mediated Control of Aquaglyceroporins in Human Adipocytes and Hepatocytes Is Mediated via the PI3K/Akt/mTOR...
... and Leptin-Mediated Control of Aquaglyceroporins in Human Adipocytes and Hepatocytes Is Mediated via the PI3K/Akt/mTOR ... Insulin- and Leptin-Mediated Control of Aquaglyceroporins in Human Adipocytes and Hepatocytes Is Mediated via the PI3K/Akt/mTOR ... Insulin- and Leptin-Mediated Control of Aquaglyceroporins in Human Adipocytes and Hepatocytes Is Mediated via the PI3K/Akt/mTOR ... and obesity-associated type 2 diabetes as well as the potential regulatory role of insulin and leptin on aquaglyceroporins (AQP ...https://www.cun.es/pt/investigacao/publicacoes-cientificas/insulin-leptin-mediated-control-aquaglyceroporins-human-adipocytes-hepatocytes
IJMS | Free Full-Text | Lipopolysaccharide Modifies Glycerol Permeability and Metabolism in 3T3-L1 Adipocytes
In adipocytes, aquaglyceroporins mediate glycerol uptake and release across the plasma membrane, which are two key steps for ... Aquaglyceroporins-aquaporin membrane channels (AQP) that conduct glycerol and other small neutral solutes in addition to water- ... studies will be required to determine if modifications in either subcellular localization and/or activity of aquaglyceroporins ... In adipocytes, aquaglyceroporins mediate glycerol uptake and release across the plasma membrane, which are two key steps for ...http://www.mdpi.com/1422-0067/18/12/2566
Regulation of insulin secretion: a matter of phase control and amplitude modulation - Semantic Scholar
Aquaglyceroporins: Drug Targets for Metabolic Diseases?. *Giuseppe Calamita, Jason Perret, Christine Delporte ...https://www.semanticscholar.org/paper/Regulation-of-insulin-secretion%3A-a-matter-of-phase-Henquin/fcc4e4d1b5d1358be5a9b2c1543c58a585e00ee5
Arsenite transport by mammalian aquaglyceroporins AQP7 and AQP9 Rosen, B P; Agre, P; Mukhopadhyay, R; Carbrey, J M; Shen, J; ... Aquaglyceroporins form the subset of the aquaporin water channel family that is permeable to glycerol and certain small, ...https://jscholarship.library.jhu.edu/handle/1774.2/33785/discover?filtertype=author&filter_relational_operator=equals&filter=Carbrey%2C+J+M
Laboratory for Metabolism Modifying Medicine - Aalborg University's Research Portal
Kenari, A. N., Kastaniegaard, K., Greening, D. W., Shambrook, M., Stensballe, A., Cheng, L. & Hill, A. F., Apr 2019, In : Proteomics. 19, 8, 20 p., 1800161.. Research output: Contribution to journal › Journal article › Research › peer-review ...https://vbn.aau.dk/en/organisations/laboratory-for-metabolism-modifying-medicine
Michal Krystian Egelund Oklinski - Aalborg Universitets forskningsportal
Mørkholt, A. S., Kastaniegaard, K., Trabjerg, M. S., Gopalasingam, G., Niganze, W., Oklinski, M. K., Larsen, A., Nieland, J. G. K., Stensballe, A., Nielsen, S. & Nieland, J. D., 2017, I : International Journal of MS Care. 19, Suppl. 1, s. 54 (NP01).. Publikation: Bidrag til tidsskrift › Konferenceabstrakt i tidsskrift › Forskning › peer review ...https://vbn.aau.dk/da/persons/138071
Aquaporins and aquaglyceroporins (AQPs) are membrane route proteins in charge of January 10, 2019. Published by: antibody ... Aquaporins and aquaglyceroporins (AQPs) are membrane route proteins in charge of transportation of drinking water and for ...http://www.antibodyassay.com/index.php/2019/01/10/
Similar articles for PubMed (Select 16889642) - PubMed - NCBI
Aquaglyceroporins Are the Entry Pathway of Boric Acid in Trypanosoma brucei.. Marsiccobetre S, Rodríguez-Acosta A, Lang F, ... Yeast aquaglyceroporins use the transmembrane core to restrict glycerol transport.. Geijer C, Ahmadpour D, Palmgren M, ... Trypanosoma brucei aquaglyceroporins facilitate the uptake of arsenite and antimonite in a pH dependent way. ... Cloning, heterologous expression, and characterization of three aquaglyceroporins from Trypanosoma brucei.. Uzcategui NL, ...https://www.ncbi.nlm.nih.gov/pubmed?db=pubmed&cmd=link&linkname=pubmed_pubmed&uid=16889642
Frontiers | Molecular Characterization of Aquaporin 1 and Aquaporin 3 from the Gills of the African Lungfish, Protopterus...
Jensen, M. Ø., Tajkhorshid, E., and Schulten, K. (2001). The mechanism of glycerol conduction in aquaglyceroporins. Structure 9 ... aquaglyceroporins (AQP3, −7, −9, and −10) permeable to glycerol, urea, and ammonia in addition to water, and unorthodox AQP ( ... crystal structure had been resolved and based on which theories of water and glycerol conduction by aquaglyceroporins had been ...https://www.frontiersin.org/articles/10.3389/fphys.2016.00532/full
Frontiers | The Importance of Aquaporin 1 in Pancreatitis and Its Relation to the CFTR Cl- Channel | Physiology
Madeira, A., Moura, T. F., and Soveral, G. (2015). Aquaglyceroporins: implications in adipose biology and obesity. Cell. Mol. ... Rodriguez, A., Catalan, V., Gomez-Ambrosi, J., and Fruhbeck, G. (2011). Aquaglyceroporins serve as metabolic gateways in ...https://www.frontiersin.org/articles/10.3389/fphys.2018.00854/full
Identification and functional characterization of an ovarian aquaporin from the cockroach Blattella germanica L. (Dictyoptera,...
Also indicated are the aquaglyceroporins (Glp) AQP-Bom2 from Bombyx mori and AQP-Gra2 from Grapholita molesta, in the node of ... 2008). A current view of the mammalian aquaglyceroporins. Annu. Rev. Physiol. 70, 301-327. ... known as aquaglyceroporins, transport other non-charged solutes such as glycerol and urea in addition to water (Gomes et al., ... His is replaced by the smaller amino acid Gly in aquaglyceroporins) (Beitz et al., 2006), and five other residues (P1-P5) ...http://jeb.biologists.org/content/214/21/3630
TCDB » SEARCH
Aquaglyceroporins are most probably key elements in the renal regulation of nitrogen balance and maintenance of the correct pH ... 2006). Ammonia permeability of the aquaglyceroporins from Plasmodium falciparum, Toxoplasma gondii and Trypansoma brucei. Mol. ... 2) The aquaglyceroporins are permeable to water, but also to other small uncharged molecules. (3) The third subfamily, with ... Michalek, K. (2016). Aquaglyceroporins in the kidney: present state of knowledge and prospects. J. Physiol. Pharmacol 67: 185- ...http://www.tcdb.org/search/result.php?tc=1.A.8
University of Glasgow - Research Institutes - Institute of Infection, Immunity & Inflammation - Our staff - Prof Harry De Koning
Aquaglyceroporins determine sensitivity to pentamidine and melarsoprol in Trypanosoma brucei.. *2014: Al-Baha, Saudi Arabia - ...https://www.gla.ac.uk/researchinstitutes/iii/staff/harrydekoning/
Aquaporin-1 - Proteopedia, life in 3D
Aquaglyceroporins are AQP3, -7, -9, and -10. Aquaporin-1 Structure Aquaporin-1 is an integral membrane protein that is ...http://proteopedia.org/wiki/index.php/Aquaporin-1
Publications | Max Planck Institute for Biophysical Chemistry
Hub, J.; de Groot, B. L.: Mechanism of selectivity in aquaporins and aquaglyceroporins. Proceedings of the National Acadamy of ...https://www.mpibpc.mpg.de/publication-search/103329?page=1&person=%2Fpersons%2Fresource%2Fpersons15254
Entomology - Research Output - Penn State
Hutchison, W. D., Burkness, E. C., Mitchell, P. D., Moon, R. D., Leslie, T. W., Fleischer, S. J., Abrahamson, M., Hamilton, K. L., Steffey, K. L., Gray, M. E., Hellmich, R. L., Kaster, L. V., Hunt, T. E., Wright, R. J., Pecinovsky, K., Rabaey, T. L., Flood, B. R. & Raun, E. S., Oct 8 2010, In : Science. 330, 6001, p. 222-225 4 p.. Research output: Contribution to journal › Article ...https://pennstate.pure.elsevier.com/en/organisations/entomology/publications/?ordering=type&descending=false&page=2
AQP7 Up-Regulation in the Skeletal Muscles of Mice with Diet Induced Obesity | OMICS International
2011) Insulin- and leptin-mediated control of aquaglyceroporins in human adipocytes and hepatocytes is mediated via the PI3K/ ... Previously we examined the aquaglyceroporins (such as AQP7 and AQP9) expression in the skeletal muscles of genetically obese ... 2002) Arsenite transport by mammalian aquaglyceroporins AQP7 and AQP9. ProcNatlAcadSci U S A 99: 6053-6058. ... 2015) Sleeve Gastrectomy Reduces Hepatic Steatosis by Improving the Coordinated Regulation of Aquaglyceroporins in Adipose ...https://www.omicsonline.org/open-access/aqp7-upregulation-in-the-skeletal-muscles-of-mice-with-diet-induced-obesity-2157-7013-1000205.php?aid=51610
Scott Landfear - Publications - Oregon Health & Science University
Arsenic transport by zebrafish aquaglyceroporins. Hamdi, M., Sanchez, M., Beene, L. C., Liu, Q., Landfear, S., Rosen, B. P. & ...https://ohsu.pure.elsevier.com/en/persons/scott-landfear/publications/
Simulation Studies of the Mechanism of Membrane Transporters | SpringerLink
Hub J, de Groot B (2008) Mechanism of selectivity in aquaporins and aquaglyceroporins. Proc Natl Acad Sci USA 105:1198-203 ...https://link.springer.com/protocol/10.1007%2F978-1-62703-017-5_14
MIPs and Their Role in the Exchange of Metalloids | Springer for Research & Development
Metalloid Transport by Aquaglyceroporins: Consequences in the Treatment of Human Diseases Rita Mukhopadhyay, Eric Beitz ...https://rd.springer.com/book/10.1007%2F978-1-4419-6315-4
Potassium Ion Channels: Could They Have Evolved from Viruses? | Plant Physiology
Some chloroviruses encode functional aquaglyceroporins (Gazzarrini et al., 2006), K+/H+ transporters (Greiner et al., 2011), ...http://www.plantphysiol.org/content/162/3/1215.full
- Aquaporins in this latter class, the so-called aquaglyceroporins, transport small uncharged molecules such as glycerol and urea as well as water. (nih.gov)
- This review comprehensively discusses the recent discoveries in the field of aquaglyceroporins, alongside a brief overview of the so-called unorthodox aquaporins. (nih.gov)
- Orthodox aquaporins are transmembrane channel proteins that facilitate rapid diffusion of water, while aquaglyceroporins facilitate the diffusion of small uncharged molecules such as glycerol and arsenic trioxide. (springer.com)
- We have developed a unique system applying the strain of the yeast Pichia pastoris , where the endogenous aquaporins/aquaglyceroporins have been removed and human aquaglyceroporins AQP3, AQP7, and AQP9 are recombinantly expressed enabling comparative permeability measurements between the expressed proteins. (springer.com)
- The aquaporin family is commonly divided into three sub-groups, the orthodox aquaporins (sole water facilitators), the aquaglyceroporins (that facilitate the transport of solutes such as glycerol, arsenic trioxide and urea), and the superaquaporins. (springer.com)
- Mechanism of selectivity in aquaporins and aquaglyceroporins. (mpg.de)
- The MIP superfamily includes three subfamilies: aquaporins, aquaglyceroporins and S-aquaporins. (wikipedia.org)
- Aquaglyceroporins are recognized as a subset of the aquaporin family of proteins which conduct water, glycerol and other small, uncharged solutes. (wikipedia.org)
- Aquaglyceroporins form the subset of the aquaporin water channel family that is permeable to glycerol and certain small, uncharged solutes. (jhu.edu)
- Aquaglyceroporins have a wide tissue distribution, and emerging data suggest that several of them may play previously unappreciated physiological or pathophysiological roles. (nih.gov)
- Analyses of transgenic mice have revealed potential roles of aquaglyceroporins in skin elasticity, gastrointestinal function and metabolism, and metabolic diseases such as diabetes mellitus. (nih.gov)
- Aquaglyceroporins play important roles in human physiology, in particular for glycerol metabolism and arsenic detoxification. (springer.com)
- Aquaglyceroporins-aquaporin membrane channels (AQP) that conduct glycerol and other small neutral solutes in addition to water-play major roles in obesity. (mdpi.com)
- Trypanosoma brucei aquaglyceroporins facilitate the uptake of arsenite and antimonite in a pH dependent way. (nih.gov)
- Using a newly established Nuclear Magnetic Resonance approach based on measurement of the intracellular life time of water, we propose that human aquaglyceroporins are poor facilitators of water and that the water transport efficiency is similar to that of passive diffusion across native cell membranes. (springer.com)
- 2016 ). The transport specificity of the aquaglyceroporins is well-documented in the literature, frequently using either Xenopus laevis oocytes to measure the water transport rates, or artificial membranes creating liposomes with inserted proteins. (springer.com)
- 2017 ). Interestingly, in our system, when human aquaglyceroporins are in their native environment (lipid bilayer) and the water transport rate is measured by the non-invasive NMR method, the water transport capability of the human aquaglyceroporins are not significantly different from the passive water diffusion across the plasma membrane of cells without aquaglyceroporins expressed. (springer.com)