Relevant bibliographies by topics / Glucose phosphate isomerase

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Academic literature on the topic 'Glucose phosphate isomerase'

Author: Grafiati
Published: 4 June 2021
Last updated: 4 February 2022

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Journal articles on the topic "Glucose phosphate isomerase"

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Yeom, Soo-Jin, Yeong-Su Kim, and Deok-Kun Oh. "Development of Novel Sugar Isomerases by Optimization of Active Sites in Phosphosugar Isomerases for Monosaccharides." Applied and Environmental Microbiology 79, no. 3 (November 30, 2012): 982–88. http://dx.doi.org/10.1128/aem.02539-12.

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ABSTRACTPhosphosugar isomerases can catalyze the isomerization of not only phosphosugar but also of monosaccharides, suggesting that the phosphosugar isomerases can be used as sugar isomerases that do not exist in nature. Determination of active-site residues of phosphosugar isomerases, including ribose-5-phosphate isomerase fromClostridium difficile(CDRPI), mannose-6-phosphate isomerase fromBacillus subtilis(BSMPI), and glucose-6-phosphate isomerase fromPyrococcus furiosus(PFGPI), was accomplished by docking of monosaccharides onto the structure models of the isomerases. The determinant residues, including Arg133 of CDRPI, Arg192 of BSMPI, and Thr85 of PFGPI, were subjected to alanine substitutions and found to act as phosphate-binding sites. R133D of CDRPI, R192 of BSMPI, and T85Q of PFGPI displayed the highest catalytic efficiencies for monosaccharides at each position. These residues exhibited 1.8-, 3.5-, and 4.9-fold higher catalytic efficiencies, respectively, for the monosaccharides than the wild-type enzyme. However, the activities of these 3 variant enzymes for phosphosugars as the original substrates disappeared. Thus, R133D of CDRPI, R192 of BSMPI, and T85Q of PFGPI are no longer phosphosugar isomerases; instead, they are changed to ad-ribose isomerase, anl-ribose isomerase, and anl-talose isomerase, respectively. In this study, we used substrate-tailored optimization to develop novel sugar isomerases which are not found in nature based on phosphosugar isomerases.
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Kugler, Wilfried, and Max Lakomek. "Glucose-6-phosphate isomerase deficiency." Best Practice & Research Clinical Haematology 13, no. 1 (March 2000): 89–101. http://dx.doi.org/10.1053/beha.1999.0059.

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MORGAN, MICHAEL J., JAMES I. H. WALKER, ALISON A. M. REDMILL, and PELIN FAIK. "Molecular genetics of glucose phosphate isomerase." Biochemical Society Transactions 18, no. 2 (April 1, 1990): 183–84. http://dx.doi.org/10.1042/bst0180183.

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Peleato, Maria Luisa, Teresa Muiño-Blanco, José Alvaro Cebrian Pérez, and Manuel José López-Pérez. "Significance of the Non-Oxidative Pentose Phosphate Pathway in Aspergillus oryzae Grown on Different Carbon Sources." Zeitschrift für Naturforschung C 46, no. 3-4 (April 1, 1991): 223–27. http://dx.doi.org/10.1515/znc-1991-3-411.

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Specific enzyme activities of the non-oxidative pentose phosphate pathway in Aspergillus oryzae mycelia grown on different carbon sources were determined. Mycelia grown on glucose, mannitol and ribose show the highest specific activities, ribose 5-phosphate isomerase being specially very enhanced. Moreover, transketolase, transaldolase, ribose 5-phosphate isomerase and ribulose 5-phosphate 3-epimerase were determined in different developmental stages of mycelia grown on glucose, mannitol and ribose. The non-oxidative pentose phosphate pathway is more active during conidiogenesis, except for ribulose 5-phosphate 3-epimerase, suggesting a fundamental role of this pathway during that stage to supply pentoses for nucleic acids biosynthesis. A general decrease of the enzyme activities was found in sporulated mycelia. Arabinose 5-phosphate was tested as metabolite of the pentose pathway. This pentose phosphate was not converted into hexose phosphates or triose phosphates and inhibits significantly the ribose 5-phosphate utilization, being therefore unappropriate to support the Aspergillus oryzae growth.
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Hassett, Sylvia W., David E. McMillin, and Jerry W. Johnson. "Aconitase and glucose phosphate isomerase variation in hexaploid wheat." Canadian Journal of Plant Science 73, no. 3 (July 1, 1993): 743–48. http://dx.doi.org/10.4141/cjps93-097.

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The purpose of this study was to determine if isozyme variation could be found in wheat (Triticum aestivum L. em. Thell) for the isozymes aconitase, alcohol dehydrogenase and glucose phosphate isomerase; these isozymes are encoded by genes on wheat chromosomes with loci conferring pest resistance. Two hundred and fifty wheat accessions were examined for variation in the isozymes aconitase and alcohol dehydrogenase using starch gel electrophoresis. Accessions were chosen at random from a collection of hexaploid wheat lines from all over the world. In addition, twenty-one accessions which exhibited unusual variation for either endopeptidase or aconitase were examined for glucose phosphate isomerase variation using isoelectric focusing. While no isozyme variation was seen for alcohol dehydrogenase, variation was detected for aconitase and glucose phosphate isomerase. In addition, the glucose phosphate isomerase phenotypes of wheat lines with the 1B-1Rs and 1A-1Rs wheat-rye translocations were distinguished. Therefore, evaluation of glucose phosphate phenotypes could potentially be used in wheat improvement programs to identify plants which are homozygous for wheat-rye translocations involving chromosome 1. Key words: Triticum aestivum, isozyme variation, wheat improvement
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Forsyth, R. J., K. Bartlett, A. Burchell, H. M. Scott, and J. A. Eyre. "Astrocytic glucose-6-phosphatase and the permeability of brain microsomes to glucose 6-phosphate." Biochemical Journal 294, no. 1 (August 15, 1993): 145–51. http://dx.doi.org/10.1042/bj2940145.

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Cells from primary rat astrocyte cultures express a 36.5 kDa protein that cross-reacts with polyclonal antibodies to the catalytic subunit of rat hepatic glucose-6-phosphatase on Western blotting. Glucose-6-phosphate-hydrolysing activity of the order of 10 nmol/min per mg of total cellular protein can be demonstrated in cell homogenates. This activity shows latency, and is localized to the microsomal fraction. Kinetic analysis shows a Km of 15 mM and a Vmax. of 30 nmol/min per mg of microsomal protein in disrupted microsomes. Approx. 40% of the total phosphohydrolase activity is specific glucose-6-phosphatase, as judged by sensitivity to exposure to pH 5 at 37 degrees C. Previous reports that the brain microsomal glucose-6-phosphatase system does not distinguish glucose 6-phosphate and mannose 6-phosphate are confirmed in astrocyte microsomes. However, we demonstrate significant phosphomannose isomerase activity in brain microsomes, allowing for ready interconversion between mannose 6-phosphate and glucose 6-phosphate (Vmax. 15 nmol/min per mg of microsomal protein; apparent Km < 1 mM; pH optimum 5-6 for the two-step conversion). This finding invalidates the past inference from the failure of brain microsomes to distinguish mannose 6-phosphate and glucose 6-phosphate that the cerebral glucose-6-phosphatase system lacks a ‘glucose 6-phosphate translocase’ [Fishman and Karnovsky (1986) J. Neurochem. 46, 371-378]. Furthermore, light-scattering experiments confirm that a proportion of whole brain microsomes is readily permeable to glucose 6-phosphate.
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Munikoty, Vinay, D. Tarangini, Vandana Bharadwaj, and Anand Prakash. "The ‘After Thought’ Enzyme: Glucose Phosphate Isomerase (GPI)." Pediatric Hematology Oncology Journal 3, no. 3 (2018): S40. http://dx.doi.org/10.1016/j.phoj.2018.11.115.

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Simon, L. M., M. Kotormán, B. Szajáni, and L. Boross. "Preparation and characterization of immobilized glucose-phosphate isomerase." Enzyme and Microbial Technology 8, no. 4 (April 1986): 222–26. http://dx.doi.org/10.1016/0141-0229(86)90092-x.

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Rajendram, G. F. "ELECTROPHORETIC STUDY OF ENZYMES FROM A GLOSSINA FUSCIPES FUSCIPES NEWSTEAD POPULATION FROM WESTERN KENYA." Canadian Entomologist 123, no. 2 (April 1991): 295–98. http://dx.doi.org/10.4039/ent123295-2.

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AbstractEnzymes were investigated, by electrophoresis, in a population of Glossina fuscipes fuscipes Newstead collected from Rusinga Island in Lake Victoria, Western Kenya.The following enzymes were tested: glucose phosphate isomerase, glucose-6-phosphate dehydrogenase (G6PDH), hexokinase. isocitrate dehydrogenase (IDH), malate-dehydrogenase (MDH), phosphoglucomutase, and xanthine dehydrogenase (XDH).Single monomorphic bands were stained by the following enzymes apparently under the control of single loci: G6PDH, MDH, and XDH. The enzyme IDH showed two bands with very close mobilities and no variation among individuals in the population. Hence IDH was considered as representing a single locus. Glucose phosphate isomerase manifested three alleles and apparently six genotypes. Phosphoglucomutase manifested a double-banded pattern representing an autosomal locus.
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Hua, Qiang, Chen Yang, Tomoya Baba, Hirotada Mori, and Kazuyuki Shimizu. "Responses of theCentral Metabolism in Escherichia coli to PhosphoglucoseIsomerase and Glucose-6-Phosphate DehydrogenaseKnockouts." Journal of Bacteriology 185, no. 24 (December 15, 2003): 7053–67. http://dx.doi.org/10.1128/jb.185.24.7053-7067.2003.

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ABSTRACT The responses of Escherichia coli central carbon metabolism to knockout mutations in phosphoglucose isomerase and glucose-6-phosphate (G6P) dehydrogenase genes were investigated by using glucose- and ammonia-limited chemostats. The metabolic network structures and intracellular carbon fluxes in the wild type and in the knockout mutants were characterized by using the complementary methods of flux ratio analysis and metabolic flux analysis based on [U-13C]glucose labeling and two-dimensional nuclear magnetic resonance (NMR) spectroscopy of cellular amino acids, glycerol, and glucose. Disruption of phosphoglucose isomerase resulted in use of the pentose phosphate pathway as the primary route of glucose catabolism, while flux rerouting via the Embden-Meyerhof-Parnas pathway and the nonoxidative branch of the pentose phosphate pathway compensated for the G6P dehydrogenase deficiency. Furthermore, additional, unexpected flux responses to the knockout mutations were observed. Most prominently, the glyoxylate shunt was found to be active in phosphoglucose isomerase-deficient E. coli. The Entner-Doudoroff pathway also contributed to a minor fraction of the glucose catabolism in this mutant strain. Moreover, although knockout of G6P dehydrogenase had no significant influence on the central metabolism under glucose-limited conditions, this mutation resulted in extensive overflow metabolism and extremely low tricarboxylic acid cycle fluxes under ammonia limitation conditions.
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Dissertations / Theses on the topic "Glucose phosphate isomerase"

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Sun, An Qiang. "Characterization of Human Glucose-6-Phosphate Isomerase of Different Sizes." Thesis, University of North Texas, 1989. https://digital.library.unt.edu/ark:/67531/metadc500752/.

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Glucose phosphate isomerase (GPI) was purified from human placenta utilizing cross-linked spherical particle phosphocellulose. In three steps, GPI could be purified approximately 5500 fold with greater than 50% recovery. The purified enzyme exhibited four bands upon non-denaturing PAGE and isoelectric focusing (IEF) when stained with GPI specific activity stain. The four isozymes were isolated by preparative IEF. The isoelectric points of the isozymes were determined. Sodium dodecyl sulfate (SDS) gel electrophoresis showed two types of subunits with different molecular weights. Structural analyses showed both types of subunits had blocked amino termini. Other properties of the isozymes and subunits, including immunological reactivity, pH stability, peptide mapping and amino acid composition, were also established.
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Cini, John Kenneth. "Physical, Chemical and Catalytic Properties of the Isozymes of Bovine Glucose Phosphate Isomerase." Thesis, North Texas State University, 1987. https://digital.library.unt.edu/ark:/67531/metadc332289/.

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Glucose phosphate isomerase (GPI) occurs in different bovine tissues as multiple, catalytically active isozymes which can be resolved by polyacrylamide gel electrophoresis and isoelectric focusing. GPI from bovine heart was purified to homogeneity and each of the isozymes was resolved. Four of the five isozymes were characterized with regard to their physical, chemical and catalytic properties in order to establish their possible physiological significance and to ascertain their molecular basis. The isozymes exhibited identical native (118 Kd) and subunit (59 Kd) molecular weights but had different apparent pi values of 7.2, 7.0, 6.8 and 6.6. Structural analyses showed that the amino terminus was blocked and the carboxyl terminal sequence was -Glu-Ala-Ser-Gly for all four isozymes. The most basic isozyme was more stable than the more acidic isozymes (lower pi values) at pH extremes, at high ionic strength, in the presence of denaturants or upon exposure to proteases. Kinetic constants, such as turnover number, Km and Ki values, were identical for all isozymes. Identical amino acid composition and peptide mapping by chemical cleavage at methionine and cysteine residues of the isozymes suggest a postsynthetic modification rather then a genetic origin for the in vivo isozymes. When the most basic isozyme was incubated in vitro under mild alkaline conditions, there was a spontaneous generation of the more acidic isozymes with electrophoretic properties identical to those found in vivo. The simultaneous release in ammonia along with the spontaneous shift to more acidic isozymes and changes in the specific cleavage of the Asn-Gly bonds by hydroxylamine of the acidic isozyme indicates deamidation as the probable molecular basis. In summary the isozymes appear to be the result of spontaneous, postsynthetic modifications involving the addition of an equal number of negative charges and are consistent with the deamidation process.
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Hassan-Walker, Aycan Fatma. "The molecular genetics of glucose phosphate isomerase and phosphoglycerate kinase." Thesis, King's College London (University of London), 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.243321.

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Alagoz, Eda. "Kinetic Analysis Of Glucose-6-phosphate Branch Point In Saccharomyces Cerevisiae." Master's thesis, METU, 2005. http://etd.lib.metu.edu.tr/upload/12606556/index.pdf.

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Glycolysis is the main metabolic route in Saccharomyces cerevisiae and it is the sequence of enzyme catalyzed reactions that oxidatively convert glucose to pyruvic acid in the yeast cytoplasm. In addition to the basic steps, glycolysis involves branch points providing the intermediary building blocks of the cell (i.e amino acids and nucleotides). One of these pathways is glucose-6-phosphate branch point which is a junction of glycolytic pathway and pentose phosphate pathway. At this point glucose-6-phosphate can be converted to fructose-6-phosphate a metabolite of glycolytic pathway by phosphoglucoisomerase or it can be dehydrogenated to 6-phosphogluconolactone by glucose-6-phosphate dehydrogenase which is the first enzyme of the pentose phosphate pathway. In this study, the influence of different nitrogen sources on the flux distribution through the pentose phosphate pathway and glycolysis in Saccharomyces cerevisiae was examined. For this purpose, four different compositions of nitrogen sources were used in growth media. The growth medium contained one of the following composition of nitrogen sources
only ammonium sulfate, only yeast nitrogen base, ammonium sulfate and histidine, yeast nitrogen base and histidine. Histidine was added because its synthesis branches from pentose phosphate pathway. In order to analyse the effect of the different compositions of nitrogen sources on the physiology of the yeast, specific activities of hexokinase, phosphoglucose isomerase, glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase enzymes were measured in the crude extracts of the biomass samples taken in the late exponential phase of the cultures. Addition of histidine caused an increase in the specific activities of all the enzymes analysed in medium containing ammonium sulfate. The specific activity of hexokinase, phosphoglucose isomerase and glucose-6-phosphate dehydrogenase in medium containing yeast nitrogen base and histidine were higher than medium containing yeast nitrogen base. However, the specific activity of 6-phosphogluconate dehydrogenase decreased 3.1% in medium containing yeast nitrogen base and histidine medium with respect to medium with only yeast nitrogen base. The OD value and dry weight in the culture containing histidine aminoacid was higher than the cultures contaning only ammonium sulfate and only yeast nitrogen base. Also the period of the exponential phase was shorter in medium containing ammonium sulfate and histidine and yeast nitrogen base and histidine than medium only ammonium sulfate and only yeast nitrogen base.
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Sun, Fangfang. "Development of Building Blocks - Thermostable Enzymes for Synthetic Pathway Biotransformation (SyPaB)." Thesis, Virginia Tech, 2012. http://hdl.handle.net/10919/77009.

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Hydrogen production from abundant renewable biomass would decrease reliance on crude oils, achieve nearly zero net greenhouse gas emissions, create more jobs, and enhance national energy security. Cell-free synthetic pathway biotransformation (SyPaB) is the implementation of complicated chemical reaction by the in vitro assembly of numerous enzymes and coenzymes that microbes cannot do. One of the largest challenges is the high cost and instability of enzymes and cofactors. To overcome this obstacle, strong motivations have driven intensive efforts in discovering, engineering, and producing thermostable enzymes. In this project, ribose-5-phosphate isomerase (RpiB), one of the most important enzymes in the pentose phosphate pathway, was cloned from a thermophile Thermotoga maritima, and heterologously expressed in Escherichia coli, purified and characterized. High-purity RpiB was obtained by heat pretreatment through its optimization in buffer choice, buffer pH, as well as temperature and duration of pretreatment. This enzyme had the maximum activity at 80°C and pH 6.5-8.0. It had a half lifetime of 71 h at 60°C, resulting in its turn-over number of more than 2 x108 mol of product per mol of enzyme. Another two thermostable enzymes glucose-6-phosphate dehydrogenase (G6PDH) and diaphorase (DI) and their fusion proteins G6PDH-DI and DI-G6PDH were cloned from Geobacillus stearothermophilus, heterologouely expressed in E. coli and purified through its His-tag. The individual proteins G6PDH and DI have good thermostability and reactivity. However, the presence of DI in fusion proteins drastically decreased G6DPH activity. However, a mixture of G6PDH and a fusion protein G6PDH-DI not only restored G6PDH activity through the formation of heteromultimeric network but also facilitated substrate channeling between DI and G6PDH, especially at low enzyme concentrations. My researches would provide important building blocks for the on-going projects: high-yield hydrogen production through cell-free enzymatic pathways and electrical energy production through enzymatic fuel cells.
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Schlichting, Bettina [Verfasser]. "Neuartige Glucose-6-Phosphat-Isomerasen und Glucosamin-6-Phosphat-Deaminasen in Archaea / Bettina Schlichting." Kiel : Universitätsbibliothek Kiel, 2009. http://d-nb.info/1019811994/34.

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Reichel, Andreas [Verfasser], Thomas [Gutachter] Kamradt, Rolf [Gutachter] Bräuer, and Manfred [Gutachter] Blessing. "Der Einfluss CD4+CD25+ regulatorischer T-Zellen auf die Glucose-6-Phosphat-Isomerase induzierte Arthritis / Andreas Reichel ; Gutachter: Thomas Kamradt, Rolf Bräuer, Manfred Blessing." Jena : Friedrich-Schiller-Universität Jena, 2009. http://d-nb.info/1178543730/34.

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Nowitzki, Ulrich. "Studien zum Gentransfer aus Organellen nach Endosymbiose anhand der Chloroplast-Cytosol-Isoenzyme von Glucose-6-phosphat-Isomerase aus Spinacia oleracea und der 3-Phosphoglycerat-Kinase aus Euglena gracilis." [S.l.] : [s.n.], 2002. http://deposit.ddb.de/cgi-bin/dokserv?idn=964591677.

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Schubert, David. "Arthritisinduktion durch Immunität gegen ein systemisch exprimiertes Autoantigen." Doctoral thesis, Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2005. http://dx.doi.org/10.18452/15271.

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Ungefähr 1% der Bevölkerung der westlichen Welt leidet an rheumatoider Arthritis (RA). In einem T-Zellrezeptor transgenen Mausmodell, dem K/BxN Modell, wird die ubiquitär exprimierte Glukose-6-phosphat Isomerase (G6PI) von autoreaktiven T- und B-Zellen erkannt. Diese Mäuse entwickeln spontan eine antikörpervermittelte Arthritis, die viele Gemeinsamkeiten mit der humanen RA aufweist. In dieser Arbeit wurde untersucht, ob die Immunisierung mit G6PI eine Arthritis auch in nicht-transgenen Mäuse induzieren kann. Die Immunisierung mit heterologer humaner G6PI führte zur Entwicklung einer peripheren symmetrischen Polyarthritis in über 95% der DBA/1 Mäuse. Damit konnte zum ersten Mal gezeigt werden, dass eine Immunreaktion gegen ein systemisches exprimiertes Antigen zur einer organspezifischen Erkrankung in normalen nicht-transgenen Mäusen führt. Die Tiere entwickeln nach 9 Tagen eine Arthritis, die bis Tag 15 ihr Maximum erreicht hat und dann langsam abnimmt. Histologisch ist die Arthritis durch eine frühe Synovitis charakterisiert, gefolgt von massiven Erosionen des Knorpel und Knochens und anschließenden Reparaturprozessen, inklusive Fibrose. Obwohl die Tiere hohe Antikörpertiter entwickeln, kann die Arthritis nicht durch aufgereinigte Antikörper kranker Mäuse transferiert werden. Trotzdem spielen Antikörper eine große Rolle, da FcR-gamma-Kette defiziente Mäuse eine Arthritis mit geringer Inzidenz und mildem Verlauf entwickeln. Die Depletion der CD4 positiven Zellen verhindert die Entwicklung der Arthritis völlig, und eine Depletion während der Erkrankung führt zur schnellen Heilung. Daneben ist für die Entwicklung der Arthritis auch das Komplementsystem und TNF-alpha entscheidend, was durch Depletion von C5 bzw. durch Blockade von TNF-alpha gezeigt wurde. Zusätzlich wurde die Rolle der G6PI bei der Pathogenese der RA im Menschen untersucht. RA-Patienten zeigten keine erhöhte Frequenz von CD4 positiven T-Zellen, die nach Restimulation mit G6PI TNF-alpha oder IFN-gamma produzierten. Außerdem konnten keine erhöhten anti-G6PI Titer in Patienten mit RA oder anderen rheumatischen Erkrankungen detektiert werden.
About 1% of the of the population of the western world suffers from rheumatoid arthritis (RA). In a T-cell receptor transgenic mouse model, the K/BxN model, the ubiquitously expressed glucose-6-phosphate isomerase (G6PI) is recognized by autoreactive T- and B-cells. These mice do develop an antibody dependent arthritis which show a lot of features of human RA. In this study it was examined whether arthritis could be induced in normal non-transgenic mice by immunization with G6PI. Immunization with heterologous human G6PI induces a symmetric polyarthritis in over 95% of DBA/1 mice. Therewith showing for the first time that an immune reaction against an systemic expressed antigen will lead to the development of an organ specific disease in normal non-transgenic mice. The mice develop arthritis 9d after immunization, reach their maximum at d15 and then arthritis slowly resolve. Histologically, the disease is characterized by early synovitis followed by massive cartilage destruction and erosions of the bones and later repair processes including fibrosis. Although antibody titers in the mice are high, transfer of purified anti-G6PI antibodies of sick mice alone do not transfer disease. Anyway, antibodies seem to play a major role since FcR-gamma-chain deficient mice develop disease with a much lower frequency and reduced severity. Depletion of CD4 positive T cells completely prevents disease and depletion during disease leads to an rapid resolution of arthritis. Aside this, complement and TNF-alpha is critical for the development of arthritis, which could shown by depletion of C5 and blockade of TNF-alpha. In addition, the role of G6PI in the pathogenesis of RA in humans was examined. RA patients do not show a higher frequency of CD4 positive T-cells which produce TNF-alpha and IFN-gamma after restimulation with G6PI. Furthermore, no elevated anti-G6PI titers could be detected in RA patients and in patients with other rheumatic diseases.
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Lee, Wei-Lun, and 李偉綸. "Gene expression and functional study of zebrafish glucose 6-phosphate isomerase b (gpib) during embryonic development." Thesis, 2010. http://ndltd.ncl.edu.tw/handle/37277285221292198380.

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碩士
國立高雄海洋科技大學
海洋生物技術研究所
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Glucose 6-phosphate isomerase (GPI), alternatively named phosphoglucose isomerase (PGI), autocrine motility factor (AMF) or neuroleukin (NLK), is a sugar metabolic enzyme catalyzing the interconversion between glucose-6-phosphate and fructose-6-phosphate. When secreted out of the cell, it can induce cellular activities of neighboring cells. In zebrafish, gpi was duplicated into gpia and gpib. Compared to gpia, gpib was expressed at earlier stage. Using in situ hybridization to detect gpib expression in zebrafish during early development, we found that gpib mRNA was localized in blastomere at cleavage stage, then gpib was expressed in blastomere and yolk syncytial layer (YSL) at blastula stage. The expression pattern of gpib is consistent with the development of YSL from mid-blastula to pharyngula stages. YSL is known to play an important role in embryonic development, therefore we hypothesize that gpib functions in blastula and gastrula development. Gene expression knockdown of gpia and gpib by siRNAs produced similar defective phenotypes. Whereas, inhibition of gpia or gpib expression by antisense morpholinos caused epibolic delay of gpib knockdown morphants in gastrula stage but not in gpia morphants. Defective phenotypes of gpib knockdown embryos at later stages included pericardial edema, bent tail, brain malformation, and abnormal yolk cell extension. These defects could be partially rescued by gpib capped RNA. By analyzing the mesendodermal marker gsc, we showed that gpib morphants with epiboly delay also exhibited delay and abnormalities in endodermal cell migration. To study the mechanisms causing epiboly delay, we analyzed the changes in microtubule organization of gpib morphants by assessing microtubule and tubulin contents in embryos. Our results showed an increase in the tubulin content in gpib knockdown embryos, suggesting a decrease in microtubule stability. In conclusion, our results suggest that gpib expressed in the YSL functions in the epibolic cell movement and development of three germ layers.
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Book chapters on the topic "Glucose phosphate isomerase"

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Below, M., C. Gärtner, D. Tunak, and K. H. Dallüge. "Demonstration of Early Tumor Reactions by Measurement of Glucose-6-Phosphate Isomerase Activity in the Serum of Irradiated Patients." In Tumor Response Monitoring and Treatment Planning, 725–31. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-48681-4_120.

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"Glucose-Phosphate Isomerase." In Encyclopedia of Genetics, Genomics, Proteomics and Informatics, 805. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6754-9_6951.

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Zanella, Alberto, and Paola Bianchi. "Erythrocyte enzymopathies." In Oxford Textbook of Medicine, edited by Chris Hatton and Deborah Hay, 5463–72. Oxford University Press, 2020. http://dx.doi.org/10.1093/med/9780198746690.003.0540.

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Numerous enzymes, including those of the hexose monophosphate and glycolytic pathways, are active in the red cell. They are required for the generation of ATP and the reductants NADH and NADPH. 2,3-Diphosphoglycerate, an intermediate of glucose metabolism, is a key regulator of the affinity of haemoglobin for oxygen, and accessory enzymes are also active for the synthesis of glutathione, disposal of oxygen free radicals, and for nucleotide metabolism. With the exception of heavy metal poisoning and rare cases of myelodysplasia, most red cell enzyme deficiency disorders are inherited. They may cause haematological abnormalities, (most commonly nonspherocytic haemolytic anaemias, but also rarely polycythaemia or methaemoglobinaemia, manifest with autosomal recessive or sex-linked inheritance), and may also be associated with nonhaematological disease when the defective enzyme is expressed throughout the body. Some may mirror important metabolic disorders, without producing haematological problems, making them of diagnostic value. Others are of no known clinical consequence. With rare exceptions, it is impossible to differentiate the enzymatic defects from one another by clinical or routine laboratory methods. Diagnosis depends on the combination of (1) accurate ascertainment of the family history; (2) morphological observations—these can determine whether haemolysis is present, rule out some causes of haemolysis (e.g. hereditary spherocytosis and other red blood cell membrane disorders), and diagnose pyrimidine 5′-nucleotidase deficiency (prominent red cell stippling); (3) estimation of red cell enzyme activity; and (4) molecular analysis. The most common red cell enzyme defects are glucose-6-phosphate dehydrogenase deficiency, pyruvate kinase deficiency, glucose-6-phosphate isomerase deficiency, pyrimidine 5′-nucleotidase deficiency—which may also induced by exposure to environmental lead—and triosephosphate isomerase deficiency.
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Gorodetskiy, Vadim. "Felty’s Syndrome." In Rare Diseases [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.97080.

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Felty’s syndrome (FS) is an uncommon subset of seropositive rheumatoid arthritis (RA) complicated by neutropenia with or without splenomegaly. The pathogenesis of neutropenia in FS is still not fully understood, but it is believed that the principal cause is neutrophil survival defect. Autoantibodies against peptidylarginine deiminase type 4 deiminated histones, glucose-6-phosphate isomerase, and eukaryotic elongation factor 1A-1 antigen may contribute to neutropenia development in FS patients. Splenic histology in FS shows non-specific findings and spleen size do not correlate with neutropenia. Cases of T-cell large granular lymphocytic leukemia with low tumor burden in blood and concomitant RA are clinically indistinguishable from FS and present a diagnostic challenge. Examination of T-cell clonality, mutations in signal transducer and activator of transcription 3 gene, and the number of large granular lymphocytes in the blood can establish a correct diagnosis. Optimal approaches to therapy for FS have not been developed, but the use of rituximab seems promising. In this chapter, the epidemiology, pathogenesis, clinical manifestations, differential diagnosis, and treatment options for FS are discussed.
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Frey, Perry A., and Adrian D. Hegeman. "Isomerization." In Enzymatic Reaction Mechanisms. Oxford University Press, 2007. http://dx.doi.org/10.1093/oso/9780195122589.003.0011.

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Isomerization reactions are important in metabolism to potentiate further transformations that would otherwise be chemically impossible. A familiar example from glycolysis is phosphohexose isomerase, which catalyzes the interconversion of D-glusose-6-P and D-fructose-6-P. The formation of fructose-6-P makes it chemically feasible at a later step of glycolysis to cleave the six-carbon sugar into two three-carbon sugars, glyceraldehyde-3-P, and dihydroxyacetone-P by aldolase. No such cleavage of glucose-6-P into two three-carbon sugars is possible. The dihydroxyacetone-3-P is converted into glyceraldehyde-3-P by another isomerase, triosephosphate isomerase. In this way, glucose-6-P can be transformed into two molecules of glyceraldehyde-3-P, which can then be metabolized through glycolysis to pyruvate. Both reactions of phosphohexose and triosephosphate isomerases involve aldose/ketose interconversions and proceed by similar chemical mechanisms. Other important isomerases include phosphomutases, epimerases, racemases, and carbon-skeleton mutases, all of which have their roles in metabolism. The chemical mechanisms vary with the classes of isomerases and include enolizations, hydride transfer, oxidation/reduction, phosphotransfer, and radical rearrangements. In this chapter, we consider the mechanisms by which enzymes catalyze isomerization reaction. The interconversions of glucose-6-P and fructose-6-P and of the triose phosphates can be formulated chemically. The transformation in is an internal oxidation-reduction, in which the aldehyde group of the aldose is reduced and the neighboring alcoholic group is oxidized. This reaction can take place by either of two chemical mechanisms: an initial enolization at C2 to produce an enediolate intermediate that can be protonated at C1 to produce the product or a direct hydride transfer from C2 to C1. These mechanisms are outlined in scheme 7-1. Loss of the proton C2(H) by enolization in the upper pathway leads to the enediolate intermediate, and return of the proton to C1 (black arrows in scheme 7-1) leads to the ketose product. The hydride transfer mechanism in the lower pathway begins with the dissociation of the alcoholic proton to form the alcoholate intermediate. The alcoholate provides the driving force for the 1,2-hydride transfer (colored arrows in scheme 7-1) accompanied by protonation of the oxygen at C1. The two mechanisms require different hydrogen transfer regimes.
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Conference papers on the topic "Glucose phosphate isomerase"

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Kurata, I., I. Matsumoto, A. Osada, H. Ebe, H. Kawaguchi, Y. Kondo, H. Tsuboi, and T. Sumida. "THU0077 Increased follicular helper t cell regulates autoantibody hyposialylation in glucose-6-phosphate isomerase induced arthritis." In Annual European Congress of Rheumatology, EULAR 2018, Amsterdam, 13–16 June 2018. BMJ Publishing Group Ltd and European League Against Rheumatism, 2018. http://dx.doi.org/10.1136/annrheumdis-2018-eular.2865.

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Reports on the topic "Glucose phosphate isomerase"

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Doichev, Kostadin, Veselina Georgieva, Elitsa Boteva, and Rumiana Mironova. Modification of DNA with Glucose 6-Phosphate to Examine the Glycolytic Enzyme Phosphoglucose Isomerase for DNA-amadoriase Activity. "Prof. Marin Drinov" Publishing House of Bulgarian Academy of Sciences, June 2021. http://dx.doi.org/10.7546/crabs.2021.06.06.

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