Aquaglyceroporins
Aquaporins
Glycerol
Aquaporin 3
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
Water
Biological Transport
Xenopus
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
Organic Chemicals
Osmotic Pressure
Saccharomyces cerevisiae
Arsenic
A shiny gray element with atomic symbol As, atomic number 33, and atomic weight 75. It occurs throughout the universe, mostly in the form of metallic arsenides. Most forms are toxic. According to the Fourth Annual Report on Carcinogens (NTP 85-002, 1985), arsenic and certain arsenic compounds have been listed as known carcinogens. (From Merck Index, 11th ed)
Zebrafish
Zebrafish Proteins
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 2.7.1.30.
Adipocytes
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
Gestalt Therapy
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
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)
Conditional osmotic stress in yeast: a system to study transport through aquaglyceroporins and osmostress signaling<...
Arsenic transport by zebrafish aquaglyceroporins | BMC Molecular Biology | Full Text
Identification of key residues involved in Si transport by the aquaglyceroporins | Journal of General Physiology | Rockefeller...
A role for aquaglyceroporins in adipogenesis
Cooperation between passive and active silicon transporters clarifies the ecophysiology and evolution of biosilicification in...
Dynamic Regulation of Aquaglyceroporin Expression in Erythrocyte Cultu by Venkateshwar Mutyam, Matthew V. Puccetti et al.
Solute transport on the sub 100 ms scale across the lipid bilayer membrane of individual proteoliposomes - Lunds universitet
Solute transport on the sub 100 ms scale across the lipid bilayer membrane of individual proteoliposomes
Claudin-2, a component of the tight junction, forms a paracellular water channel | Journal of Cell Science
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The zebrafish genome encodes the largest vertebrate repertoire of functional aquaporins with dual paralogy and substrate...
Characterization and Prediction of Partition Coefficients of Uncharged Solutes into Micelles and Liposomes using Electrokinetic...
Aquaporins at a glance | Journal of Cell Science
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Patent US20040116949 - Apparatus and methods for forming gastrointestinal tissue approximations - Google Patents
Mempro™ Cell-Free Major Intrinsic Protein (MIP)/FNT Superfamily Production - Creative Biostructure
Physical, Chemical, and Biological Methods for the Removal of Arsenic Compounds
Antiproliferative effect of dihydroxyacetone on Trypanosoma brucei bloodstream forms: cell cycle progression, subcellular...
Aquaporin membrane protein, molecular model - Stock Image C035/5236 - Science Photo Library
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IJMS | Free Full-Text | Lipopolysaccharide Modifies Glycerol Permeability and Metabolism in 3T3-L1 Adipocytes
The aquaglyceroporin AQP9 contributes to the sex-specific effects of in utero arsenic exposure on placental gene expression |...
Aquaporin-3 in Keratinocytes and Skin: Its Role and Interaction With Phospholipase D2
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Aquaporin water channels - From atomic structure to clinical medicine<...
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MIPS 2020 Requirements
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Arsenic biochemistry - Wikipedia
Characterization of glycerol uptake and glycerol kinase activity in rat hepatocytes cultured under different hormonal...
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Somatostatin binding in human gastrointestinal tissues: effect of cations and somatostatin analogues. | Gut
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New class of monofluoro acylboronates that is stable in air and water
Estrogen prevents increased hepatic aquaporin-9 expression and glycerol uptake during starvation. | IRIS Univ. Bari
Blocking of α4β7 Gut-Homing Integrin during Acute Infection Leads to Decreased Plasma and Gastrointestinal Tissue Viral Loads...
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Aquaporin-8
GlobPlot 2.3 - Predictor of intrinsic protein disorder & globularity
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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 ...
Aquaporin
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. ...
Peter Agre
Aquaporins and aquaglyceroporins exist in all life forms including invertebrates, plants, microbes, archaea, and parasites ... Permeated by water plus glycerol, aquaglyceroporins confer glycerol uptake to the basal level of skin, glycerol release from ...
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 6 ...
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 6 ... aquaglyceroporins MeSH D12.776.543.585.400.730.040.249.500 - aquaporin 3 MeSH D12.776.543.585.400.730.040.249.750 - aquaporin 6 ...
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". ...
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". ...
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 ...
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 ...
A role for aquaglyceroporins in adipogenesis
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 ...
Identification of key residues involved in Si transport by the aquaglyceroporins | Journal of General Physiology | Rockefeller...
Identification of key residues involved in Si transport by the aquaglyceroporins Gabriel A. Carpentier , Gabriel A. Carpentier ... We recently demonstrated that the aquaglyceroporins (AQGPs) could act as potent transporters for orthosilicic acid (H4SiO4). ... the aquaglyceroporins [AQGPs]) that also operate as channels for water but that exhibit selectivity for substrates such as ... Identification of key residues involved in Si transport by the aquaglyceroporins. J Gen Physiol 1 September 2016; 148 (3): 239- ...
Arsenic transport by zebrafish aquaglyceroporins. - Science Exchange
These aquaglyceroporins also facilitate uptake of inorganic AsIII, MAsIII and SbIII. Arsenic accumulation in fish larvae and in ... Genes for at least seven aquaglyceroporins have been annotated in the zebrafish genome project. Here, five genes which are ... The ability of these five aquaglyceroporins to transport water, glycerol and the metalloids arsenic and antimony was examined ... Arsenic transport by zebrafish aquaglyceroporins.. BMC Mol Biol. 10:104. doi: 10.1186/1471-2199-10-104. November 25, 2009. View ...
Yeast Aquaglyceroporins Use the Transmembrane Core to Restrict Glycerol Transport
Aquaglyceroporins are transmembrane proteins belonging to the family of aquaporins, which facilitate the passage of specific ... Yeast Aquaglyceroporins Use the Transmembrane Core to Restrict Glycerol Transport Artikel i vetenskaplig tidskrift, 2012 ... Aquaglyceroporins are transmembrane proteins belonging to the family of aquaporins, which facilitate the passage of specific ...
Conditional osmotic stress in yeast: a system to study transport through aquaglyceroporins and osmostress signaling<...
Conditional osmotic stress in yeast: a system to study transport through aquaglyceroporins and osmostress signaling. Journal of ... Conditional osmotic stress in yeast : a system to study transport through aquaglyceroporins and osmostress signaling. In: ... Conditional osmotic stress in yeast : a system to study transport through aquaglyceroporins and osmostress signaling. / ... title = "Conditional osmotic stress in yeast: a system to study transport through aquaglyceroporins and osmostress signaling", ...
Yeast Aquaglyceroporins Use the Transmembrane Core to Restrict Glycerol Transport
Aquaglyceroporins are transmembrane proteins belonging to the family of aquaporins, which facilitate the passage of specific ... Aquaglyceroporins are transmembrane proteins belonging to the family of aquaporins, which facilitate the passage of specific ... Yeast Aquaglyceroporins Use the Transmembrane Core to Restrict Glycerol Transport Journal article, 2012 ...
Arsenic transport by zebrafish aquaglyceroporins | BMC Molecular Biology | Full Text
These aquaglyceroporins also facilitate uptake of inorganic AsIII, MAsIII and SbIII. Arsenic accumulation in fish larvae and in ... Genes for at least seven aquaglyceroporins have been annotated in the zebrafish genome project. Here, five genes which are ... The ability of these five aquaglyceroporins to transport water, glycerol and the metalloids arsenic and antimony was examined ... Our results demonstrated that these aquaglyceroporins exhibited different tissue expression. They are all detected in more than ...
Frontiers | Gender Differences in Adipocyte Metabolism and Liver Cancer Progression | Genetics
Genders, Aquaglyceroporins and HCC. Glycerol-3-phosphate (G3P), which is also known as glycerol, is an important metabolite for ... Chen, X., Li, C., Lü, L., and Mei, Z. (2016). Expression and clinical significance of aquaglyceroporins in human hepatocellular ... 2011b). Insulin- and leptin-mediated control of aquaglyceroporins in human adipocytes and hepatocytes is mediated via the PI3K/ ... Rodríguez, A., Catalán, V., Gómez-Ambrosi, J., and Frühbeck, G. (2011a). Aquaglyceroporins serve as metabolic gateways in ...
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 ...
Distinct transport selectivity of two structural subclasses of the nodulin-like intrinsic protein family of plant...
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, ...
Mouse monoclonal to OCT4 | Regulation of human neutrophil-mediated cartilage proteoglycan degradation
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Sonntag, Y., Gena, P., Maggio, A., Singh, T., Artner, I., Oklinski, M. K., Johanson, U., Kjellbom, P., Nieland, J. D., Nielsen, S., Calamita, G. & Rützler, M., 3 May 2019, In: The Journal of Biological Chemistry. 294, 18, p. 7377-7387 11 p.. Research output: Contribution to journal › Journal article › Research › peer-review ...
Major intrinsic proteins - Wikipedia
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 ...
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 ...
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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) ...
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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 ...
Publikationen | Max-Planck-Institut für biophysikalische Chemie
AQP3AQPsUreaPermeabilityAQP9Glycerol uptakeSubset of the aquaporinRole of aquaglyceroporinsAquaporins and aquaglyceroporinsMetalloidsSolutesTransportersMammalian aquaglyceroporinsUptakeTrypanosomaFacilitatorsProteinsRolesArsenicArseniteResiduesSoluteFacilitateSelectivityPermeableTransmembraneMoleculesMetabolic diseasesObesityFunctionalLipidChannelTissueFound
AQP33
- 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 latter AQPs are called aquaglyceroporins in which AQP3, AQP7, AQP9 and AQP10 are included [ 5 , 9 ]. (omicsonline.org)
- Conversely, the eutherian water- and glycerol-transporting aquaporins (aquaglyceroporins, Glps) represented by AQP3, -7, -9, and -10, which range in size from 31.4-37.0 kDa for the human channels, have a more open structure due to a longer polypeptide region in loop E (Verma et al. (thefreedictionary.com)
AQPs4
- The aquaporins (AQPs) are a family of integral membrane proteins composed of two subfamilies: the orthodox aquaporins, which transport only water, and the aquaglyceroporins, which transport glycerol, urea, or other small solutes [ PMID: 16650285 ]. (ebi.ac.uk)
- These AQPs are classified into two groups: one is water selective channel (orthodox AQPs) and another is water, glycerol, and urea channel (aquaglyceroporins). (hindawi.com)
- AQPs 3, 7, 9 and 10, termed aquaglyceroporins, transport water as well as glycerol and possibly other small solutes. (cosmeticsandtoiletries.com)
- 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. (biologists.org)
Urea5
- Aquaporins in this latter class, the so-called aquaglyceroporins, transport small uncharged molecules such as glycerol and urea as well as water. (nih.gov)
- 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)
- This family of integral membrane proteins includes both water selective pores (aquaporins) and transport facilitators of other small molecules such as glycerol and urea (aquaglyceroporins). (lu.se)
- Aquaporins have been classified into two subfamilies: i) strict aquaporins that only allow the passage of water and ii) the less selective aquaglyceroporins that transport water and other neutral solutes, such as glycerol, CO2 or urea. (ebscohost.com)
- Some aquaporins can also permeate non-ionic compounds, such as glycerol and urea, and are termed glycerol facilitators (Glps) or aquaglyceroporins. (biomedcentral.com)
Permeability2
- Commonly, the aquaglyceroporins are stated to have dual permeability, both for water and solutes such as glycerol (Laforenza et al. (springer.com)
- Ammonia permeability of the aquaglyceroporins from Plasmodium falciparum, Toxoplasma gondii and Trypansoma brucei. (nih.gov)
AQP91
- Previously we examined the aquaglyceroporins (such as AQP7 and AQP9) expression in the skeletal muscles of genetically obese leptindeficient ob/ob mice [ 14 ] and we found the up-regulated expression of AQP7 in the skeletal muscles of these mice [ 14 ]. (omicsonline.org)
Glycerol uptake1
- 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). (mdpi.com)
Subset of the aquaporin2
- 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)
Role of aquaglyceroporins1
- Evolution of greater silicon transport efficiency appears constrained by the additional role of aquaglyceroporins in transporting essential metalloids other than silicon. (csic.es)
Aquaporins and aquaglyceroporins2
Metalloids3
- They have been identified as a possible source of metalloid contamination in agriculture as aquaglyceroporins were have been shown to conduct As(III) and Sb(III) in yeast and could be a possible source of metalloids entering the food sources of humans. (wikipedia.org)
- The ability of these five aquaglyceroporins to transport water, glycerol and the metalloids arsenic and antimony was examined following expression in oocytes from Xenopus leavis. (scienceexchange.com)
- CONCLUSION This is the first molecular identification of fish arsenite transport systems and we propose that the extensive expression of the fish aquaglyceroporins and their ability to transport metalloids suggests that aquaglyceroporins are the major pathways for arsenic accumulation in a variety of zebrafish tissues. (scienceexchange.com)
Solutes3
- Aquaglyceroporins are transmembrane proteins belonging to the family of aquaporins, which facilitate the passage of specific uncharged solutes across membranes of cells. (chalmers.se)
- Aquaglyceroporins-aquaporin membrane channels (AQP) that conduct glycerol and other small neutral solutes in addition to water-play major roles in obesity. (mdpi.com)
- Many plant aquaporin homologues are believed to specifically conduct water, whereas several homologues also conduct other small neutral solutes, such as glycerol, and are, therefore, called aquaglyceroporins [ 1 - 3 ]. (portlandpress.com)
Transporters2
- We recently demonstrated that the aquaglyceroporins (AQGPs) could act as potent transporters for orthosilicic acid (H 4 SiO 4 ). (rupress.org)
- We propose that sponges incorporate DSi combining passive (aquaglyceroporins) and active (ArsB) transporters, while only active transporters (SITs) operate in diatoms and choanoflagellates. (csic.es)
Mammalian aquaglyceroporins1
- A current view of the mammalian aquaglyceroporins. (nih.gov)
Uptake2
- These aquaglyceroporins also facilitate uptake of inorganic AsIII, MAsIII and SbIII. (scienceexchange.com)
- Trypanosoma brucei aquaglyceroporins facilitate the uptake of arsenite and antimonite in a pH dependent way. (nih.gov)
Trypanosoma3
- Cloning, heterologous expression, and characterization of three aquaglyceroporins from Trypanosoma brucei. (nih.gov)
- Aquaglyceroporins Are the Entry Pathway of Boric Acid in Trypanosoma brucei. (nih.gov)
- Trypanosoma brucei aquaglyceroporins mediate the transport of metabolic end-products: Methylglyoxal, D-lactate, L-lactate and acetate. (xenbase.org)
Facilitators1
- 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)
Proteins6
- 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)
- 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)
- A comparison of the NIPs and tonoplast-intrinsic proteins (TIP) shows that the H2 residue can predict the transport profile for water and glycerol with histidine found in TIP-like aquaporins, tryptophan found in aquaglyceroporins (NIP I), and alanine found in water-impermeable glyceroporins (AtNIP6;1). (nih.gov)
- Aquaglyceroporins: channel proteins with a conserved core, multiple functions, and variable surfaces. (biomedsearch.com)
- Remarkably, MIP is the charter member of a sequence-related gene family encoding over 150 channel proteins that facilitate the transport of water (aquaporins) and glycerol (aquaglyceroporins) across the plasma membranes of microbial, plant, and animal cells ( 12 ). (physiology.org)
- Accord ingly, these proteins are designated aquaglyceroporins. (micrornaassay.com)
Roles3
- 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)
Arsenic1
- Arsenic transport by zebrafish aquaglyceroporins. (scienceexchange.com)
Arsenite1
- NIPs are related to aquaglyceroporins found in microbes and mammalian cells and which have already been shown to function as arsenite channels in these other organisms. (rxpgnews.com)
Residues1
- We sequenced 1790 bp from cloned cDNA that codes for a 315 amino acid protein, HC ‐9, containing the predicted six transmembrane spanning domains, two Asn‐Pro‐Ala ( NPA ) motifs, and five amino acid residues characteristic of aquaglyceroporins. (physiology.org)
Solute1
- 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. (aston.ac.uk)
Facilitate1
- Still, all aquaglyceroporins investigated significantly facilitate the transport of glycerol and As(III) in the same system. (springer.com)
Selectivity1
- These observations provide a framework for understanding the basis of glycerol efflux and selectivity in aquaglyceroporins and pave the way for future design of AQP7 inhibitors. (proteopedia.org)
Permeable1
- The aquaglyceroporins are permeable to water, but also to other small uncharged molecules such as glycerol. (wikipedia.org)
Transmembrane1
- Transmembrane glycerol transport is typically facilitated by aquaglyceroporins in Prokaryota and Eukaryota. (bibsys.no)
Molecules1
- Aquaglyceroporins, one channel for two molecules. (nchu.edu.tw)
Metabolic diseases1
- Aquaglyceroporins: Drug Targets for Metabolic Diseases? (semanticscholar.org)
Obesity1
- The impact of obesity and obesity-associated type 2 diabetes as well as the potential regulatory role of insulin and leptin on aquaglyceroporins (AQP) 3, 7, and 9 were analyzed. (cun.es)
Functional1
- We discuss the possibility that lower energy costs may have driven replacement of ancestral SITs by less efficient aquaglyceroporins, and discuss the functional implications of conservation of aquaglyceroporin-mediated DSi utilization in vertebrates. (csic.es)
Lipid1
- 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)
Channel1
- In addition, MD simulation results suggest that AqpM combines characteristics of strict aquaporins, such as the narrow SF and channel radius, with those of aquaglyceroporins, such as a more hydrophobic and less polar SF. (ebscohost.com)
Tissue1
- Our results demonstrated that these aquaglyceroporins exhibited different tissue expression. (scienceexchange.com)
Found2
- Aquaglyceroporins are found in many species including bacteria, plants and humans. (wikipedia.org)
- In AqpM, isoleucine replaces a key histidine residue found in the lumen of water channels, which becomes a glycine residue in aquaglyceroporins. (tcdb.org)