Academic literature on the topic 'Enzymes; Pentose phosphate pathway'

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Journal articles on the topic "Enzymes; Pentose phosphate pathway"

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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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Kunjara, S., M. Sochor, S. A. Ali, A. L. Greenbaum, and P. McLean. "Hepatic phosphoribosyl pyrophosphate concentration. Regulation by the oxidative pentose phosphate pathway and cellular energy status." Biochemical Journal 244, no. 1 (May 15, 1987): 101–8. http://dx.doi.org/10.1042/bj2440101.

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Measurements have been made of the tissue content of phosphoribosyl pyrophosphate (PPRibP) and of a range of metabolic intermediates involved in the energy charge of the cell, the glycolytic and pentose phosphate pathways, and of the activity of the enzymes of the pentose phosphate pathway and of PPRibP synthetase (EC 2.7.6.1) in the livers of normal, diabetic, insulin-treated diabetic and starved rats and in livers of rats previously starved and then re-fed with high-fat or high-carbohydrate diets. Diabetes, starvation and high-fat diet all caused a fall in the hepatic PPRibP content, whereas insulin treatment and high-carbohydrate diet raised the tissue content. A positive correlation was shown between the PPRibP content and ATP, energy charge and the cytosolic [NAD+]/[NADH] quotient. A positive association between the PPRibP content and the flux of glucose through the pentose phosphate pathway and the synthesis of ribose 5-phosphate via the oxidative enzymes of that pathway, including ribose-5-phosphate isomerase (EC 5.3.1.6), was also observed. A negative correlation was found between the ADP, AMP and Pi contents, and no correlation existed between PPRibP content and the enzymes of the non-oxidative branch of the pentose phosphate pathway. There was no correlation between hepatic PPRibP content and the activity of PPRibP synthetase measured in vitro. These results are considered in relation to the control of PPRibP synthetase in the liver in vivo.
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Maugeri, Dante A., Joaquin J. B. Cannata, and Juan-José Cazzulo. "Glucose metabolism in Trypanosoma cruzi." Essays in Biochemistry 51 (October 24, 2011): 15–30. http://dx.doi.org/10.1042/bse0510015.

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The causative agent of Chagas disease, Trypanosoma cruzi, metabolizes glucose through two major pathways: glycolysis and the pentose phosphate pathway. Glucose is taken up via one facilitated transporter and its catabolism by the glycolytic pathway leads to the excretion of reduced products, succinate and l-alanine, even in the presence of oxygen; the first six enzymes are located in a peroxisome-like organelle, the glycosome, and the lack of regulatory controls in hexokinase and phosphofructokinase results in the lack of the Pasteur effect. All of the enzymes of the pentose phosphate pathway are present in the four major stages of the parasite's life cycle, and some of them are possible targets for chemotherapy. The gluconeogenic enzymes phosphoenolpyruvate carboxykinase and fructose-1,6-bisphosphatase are present, but there is no reserve polysaccharide.
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Hanstveit, A. O., and J. Goksøyr. "The Pathway of Glucose Catabolism in Sporocytophaga myxococcoides." Microbiology 81, no. 1 (January 1, 2000): 27–35. http://dx.doi.org/10.1099/00221287-81-1-27.

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The pathway of glucose metabolism in Sporocytophaga myxococcoides was studied by a radiorespirometric technique and assays of enzyme activity in cell-free extracts. The primary catabolic pathways in the organism were examined by measurement of relative rates of 14CO2-production from different carbon atoms of labelled glucose, pyruvic acid and acetic acid. These substrates appeared to be degraded solely by enzymes of the Embden-Meyerhof-Parnas pathway in conjunction with the tricarboxylic acid cycle. The results were confirmed by studies of enzyme activity, which showed a lack of two enzymes, glucose-6-phosphate dehydrogenase (D-glucose-6-phosphate dehydrogenase, EC. 1.1.1.49) and 6-phospho-gluconate dehydrogenase [6-phospho-D-gluconate: NADP oxidoreductase (decarboxylating), EC. 1.1.1.44], in the pentose pathway, which indicated a biosynthetic function of the non-oxidative part of this pathway.
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Schaaff-Gerstenschläger, Ine, Thomas Miosga, and Friedrich K. Zimmermann. "Genetics of pentose-phosphate pathway enzymes in Saccharomyces cerevisiae." Bioresource Technology 50, no. 1 (January 1994): 59–64. http://dx.doi.org/10.1016/0960-8524(94)90221-6.

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Fridman, Alla, Arindam Saha, Adriano Chan, Darren E. Casteel, Renate B. Pilz, and Gerry R. Boss. "Cell cycle regulation of purine synthesis by phosphoribosyl pyrophosphate and inorganic phosphate." Biochemical Journal 454, no. 1 (July 26, 2013): 91–99. http://dx.doi.org/10.1042/bj20130153.

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Cells must increase synthesis of purine nucleotides/deoxynucleotides before or during S-phase. We found that rates of purine synthesis via the de novo and salvage pathways increased 5.0- and 3.3-fold respectively, as cells progressed from mid-G1-phase to early S-phase. The increased purine synthesis could be attributed to a 3.2-fold increase in intracellular PRPP (5-phosphoribosyl-α-1-pyrophosphate), a rate-limiting substrate for de novo and salvage purine synthesis. PRPP can be produced by the oxidative and non-oxidative pentose phosphate pathways, and we found a 3.1-fold increase in flow through the non-oxidative pathway, with no change in oxidative pathway activity. Non-oxidative pentose phosphate pathway enzymes showed no change in activity, but PRPP synthetase is regulated by phosphate, and we found that phosphate uptake and total intracellular phosphate concentration increased significantly between mid-G1-phase and early S-phase. Over the same time period, PRPP synthetase activity increased 2.5-fold when assayed in the absence of added phosphate, making enzyme activity dependent on cellular phosphate at the time of extraction. We conclude that purine synthesis increases as cells progress from G1- to S-phase, and that the increase is from heightened PRPP synthetase activity due to increased intracellular phosphate.
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Badolia, Rachit, Dinesh K. A. Ramadurai, E. Dale Abel, Peter Ferrin, Iosif Taleb, Thirupura S. Shankar, Aspasia Thodou Krokidi, et al. "The Role of Nonglycolytic Glucose Metabolism in Myocardial Recovery Upon Mechanical Unloading and Circulatory Support in Chronic Heart Failure." Circulation 142, no. 3 (July 21, 2020): 259–74. http://dx.doi.org/10.1161/circulationaha.119.044452.

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Background: Significant improvements in myocardial structure and function have been reported in some patients with advanced heart failure (termed responders [R]) following left ventricular assist device (LVAD)–induced mechanical unloading. This therapeutic strategy may alter myocardial energy metabolism in a manner that reverses the deleterious metabolic adaptations of the failing heart. Specifically, our previous work demonstrated a post-LVAD dissociation of glycolysis and oxidative-phosphorylation characterized by induction of glycolysis without subsequent increase in pyruvate oxidation through the tricarboxylic acid cycle. The underlying mechanisms responsible for this dissociation are not well understood. We hypothesized that the accumulated glycolytic intermediates are channeled into cardioprotective and repair pathways, such as the pentose-phosphate pathway and 1-carbon metabolism, which may mediate myocardial recovery in R. Methods: We prospectively obtained paired left ventricular apical myocardial tissue from nonfailing donor hearts as well as R and nonresponders at LVAD implantation (pre-LVAD) and transplantation (post-LVAD). We conducted protein expression and metabolite profiling and evaluated mitochondrial structure using electron microscopy. Results: Western blot analysis shows significant increase in rate-limiting enzymes of pentose-phosphate pathway and 1-carbon metabolism in post-LVAD R (post-R) as compared with post-LVAD nonresponders (post-NR). The metabolite levels of these enzyme substrates, such as sedoheptulose-6-phosphate (pentose phosphate pathway) and serine and glycine (1-carbon metabolism) were also decreased in Post-R. Furthermore, post-R had significantly higher reduced nicotinamide adenine dinucleotide phosphate levels, reduced reactive oxygen species levels, improved mitochondrial density, and enhanced glycosylation of the extracellular matrix protein, α-dystroglycan, all consistent with enhanced pentose-phosphate pathway and 1-carbon metabolism that correlated with the observed myocardial recovery. Conclusions: The recovering heart appears to direct glycolytic metabolites into pentose-phosphate pathway and 1-carbon metabolism, which could contribute to cardioprotection by generating reduced nicotinamide adenine dinucleotide phosphate to enhance biosynthesis and by reducing oxidative stress. These findings provide further insights into mechanisms responsible for the beneficial effect of glycolysis induction during the recovery of failing human hearts after mechanical unloading.
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Soderberg, Tim, and Robert C. Alver. "Transaldolase ofMethanocaldococcus jannaschii." Archaea 1, no. 4 (2004): 255–62. http://dx.doi.org/10.1155/2004/608428.

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TheMethanocaldococcus jannaschiigenome contains putative genes for all four nonoxidative pentose phosphate pathway enzymes. Open reading frame (ORF) MJ0960 is a member of themipB/talCfamily of ‘transaldolase-like’ genes, so named because of their similarity to the well-characterized transaldolase B gene family. However, recently, it has been reported that both themipBand thetalCgenes fromEscherichia coliencode novel enzymes with fructose-6-phosphate aldolase activity, not transaldolase activity (Schürmann and Sprenger 2001). The same study reports that other members of themipB/talCfamily appear to encode transaldolases. To confirm the function of MJ0960 and to clarify the presence of a nonoxidative pentose phosphate pathway inM. jannaschii, we have cloned ORF MJ0960 fromM. jannaschiigenomic DNA and purified the recombinant protein. MJ0960 encodes a transaldolase and displays no fructose-6-phosphate aldolase activity. It retained full activity for 4 h at 80 °C, and for 3 weeks at 25 °C.Methanocaldococcus jannaschiitransaldolase has a maximal velocity (Vmax) of 1.0 ± 0.2 µmol min–1mg–1at 25 °C, whereasVmax= 12.0 ± 0.5 µmol min–1mg–1at 50 °C. Apparent Michaelis constants at 50 °C wereKm= 0.65 ± 0.09 mM for fructose-6-phosphate andKm= 27.8 ± 4.3 µM for erythrose-4-phosphate. When ribose-5-phosphate replaced erythrose-4-phosphate as an aldose acceptor,Vmaxdecreased twofold, whereas theKmwas 150-fold higher. The molecular mass of the active enzyme is 271 ± 27 kDa as estimated by gel filtration, whereas the predicted monomer size is 23.96 kDa, suggesting that the native form of the protein is probably a decamer. A readily available source of thermophilic pentose phosphate pathway enzymes including transaldolase may have direct application in enzymatic biohydrogen production.
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Hong, Zhen Quan, and Les Copeland. "Pentose phosphate pathway enzymes in nitrogen-fixing leguminous root nodules." Phytochemistry 29, no. 8 (January 1990): 2437–40. http://dx.doi.org/10.1016/0031-9422(90)85162-9.

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Sprenger, Georg A. "Genetics of pentose-phosphate pathway enzymes ofEscherichia coli K-12." Archives of Microbiology 164, no. 5 (November 1995): 324–30. http://dx.doi.org/10.1007/bf02529978.

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Dissertations / Theses on the topic "Enzymes; Pentose phosphate pathway"

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Chelvarajan, R. E. L. "The enzymes of the reductive pentose phosphate pathway of a green algae." Thesis, University of Liverpool, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.293722.

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Phillips, Christopher. "Crystallographic studies on 6-phosphogluconate dehydrogenase." Thesis, University of Oxford, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.357522.

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Häußler, Kristina Maria Elisabeth [Verfasser]. "Characterization and inhibition of NADPH-producing enzymes from the pentose phosphate pathway of Plasmodium parasites / Kristina Maria Elisabeth Häußler." Gießen : Universitätsbibliothek, 2019. http://d-nb.info/1175873500/34.

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Häußler, Kristina [Verfasser]. "Characterization and inhibition of NADPH-producing enzymes from the pentose phosphate pathway of Plasmodium parasites / Kristina Maria Elisabeth Häußler." Gießen : Universitätsbibliothek, 2019. http://d-nb.info/1175873500/34.

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Roberts, Juliet A. "Evaluation of the quantitative cytochemistry of glutathione, oxidative enzymes of the pentose phosphate pathway and related systems for the functional characterisation of malignant cells." Thesis, Brunel University, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.278886.

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Williams, Jonathan Glyn. "Isoenzyme specific PFK-2/FBPase-2 inhibition as an anti-cancer strategy." Thesis, University of Oxford, 2013. http://ora.ox.ac.uk/objects/uuid:7f47d9bb-7a9d-4dbc-92fa-57d2654640d1.

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High aerobic glycolytic capacity is correlated with poor prognosis and increased tumour aggressiveness. 6Phosphofructo-1-kinase catalyses the first irreversible step of glycolysis, and is activated by fructose-2,6-bisphosphate, a product of the kinase activity of four bifunctional isoenzymes, 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase (PFK-2/FBPase-2:PFKFB1-4). These are potential anti-tumour targets, but their individual and collective role requires further investigation. This thesis had three aims; to validate the PFK-2/FBPase-2 isoenzymes as anti-cancer targets, to investigate the requirement for isoenzyme-specific targeting, and to initiate assay development, enabling future identification of novel inhibitors. A panel of cancer cell lines was examined and PFKFB3 and PFKFB4 were confirmed to be the most strongly induced isoenzymes in hypoxia, regulated by HIF-1α. Basal and hypoxic relative PFKFB3/PFKFB4 expression varied markedly, and three cell lines with varying expression ratios (MCF-7, U87, PC3) were selected for further study. siRNA knockdown of each isoenzyme individually, markedly reduced 2D and 3D cell growth. The effect of PFKFB3 knockdown was consistently more pronounced, particularly in hypoxia. Double PFKFB3/PFKFB4 knockdown was significantly less effective than PFKFB3 knockdown alone. Direct antagonism of PFKFB3 and PFKFB4 on F-2,6-BP concentration was observed, with PFKFB3 exhibiting high kinase activity, as anticipated, and PFKFB4 exhibiting high bisphosphatase activity. The degree of antagonism was dependent on the relative PFKFB3/PFKFB4 expression ratio. Extensive efforts were made to examine the wider metabolic effect of PFKFB3/PFKFB4 on flux towards glycolysis or the pentose phosphate pathway (PPP), including using metabolite, lipid droplet, 13C NMR and mass spectrometry assays. No significant change in metabolic flux was detected, the evidence presented therefore suggesting the impact of the antagonistic effects of the isoenzymes on [F-2,6-BP] extends beyond regulation of metabolic flux alone. This study concluded that the most effective therapeutic strategy will be one that involves a PFKFB3-specific inhibitor, preferably hypoxia-targeted. Accordingly, steps were taken to validate and optimise a robust medium-throughput assay system.
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Puta, Chilunga. "The pentose phosphate pathway and NADPH utilization in rat liver." Thesis, Royal Holloway, University of London, 1985. http://repository.royalholloway.ac.uk/items/5f2760c2-5ca0-4055-bfee-97ff9879c783/1/.

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The role of the pentose phosphate pathway as a source of NADPH required for cytoplasmic processes such as lipogenesis and detoxification reactions has been examined. G6PDH and 6PGDH are known to be strongly inhibited by the high NADPH/NADP ratio which is thought to occur in the cytoplasm but no effector at physiological concentrations has yet been found which can overcome this inhibition. Initially a possible role for F2, 6P2 as an activator of G6PDH, 6PGDH and FAS was investigated but no significant effect of this regulatory metabolite on any of these enzymes was discovered. An attempt was also made to demonstrate the reported reversal of the inhibition by GSSG and the cofactor reported by Eggleston and Krebs (1974). This too could not be demonstrated. In the course of the work, a cytosolic NADPH-consuming reaction has been characterized. This has been shown to involve the reaction of a peptide-substrate with a cytoplasmic reductase specific for NADPH and a high affinity for the peptide. The physiological role of this reaction remains to be established, but it has been observed that the reaction exhibits a diurnal variation, the pattern of which is the reverse of that observed with lipogenesis. The low molecular weight peptide, which appears to be distinct from glutathione, contains cystine residues which are apparently reduced in the presence of NADPH, resulting in the appearance of free thiol groups. The peptide may be phosphorylated but the nature of the linkage between the peptide and phosphate has not been established. A possible role for this and other NADPH-dependent reactions in the regulation of the pentose phosphate pathway is discussed in this thesis.
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Polat, Ibrahim H. "Functional role of pentose phosphate pathway and glutamine in cancer cell metabolism." Doctoral thesis, Universitat de Barcelona, 2016. http://hdl.handle.net/10803/402580.

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In this thesis, tumor metabolic reprogramming has been exploited in order to propose new targets in cancer treatment. On one hand, we explored the pentose phosphate pathway (PPP) enzymes as putative therapeutic targets against breast and colon cancer. We observed that inhibition of ox-PPP enzymes G6PD in colon cancer cells and 6PGD in breast cancer cells halted cell prolifertion, resulted in cell cycle arrest and apoptosis. We also demosntrated that in colon cancer cells G6PD is strongly regulated by the glutamine availability mediated by NRF2 transcription factor. Moreover, 6PGD inhibition decreased mammosphere formation capacity of breast cancer cells implying that stem cell characteristics of breast cancer cells were altered by 6PGD inhibition. Besides that, 6PGD inhibition also altered the central carbon metabolism of breast cancer cells leading to decreased glucose consumption and increased glutamine consumption. Observing that both pathways are deeply related to glutamine metabolism, we decided to investigate the metabolic network adaptations that breast cancer cells undergo when the glutamine is scarce. Knowing that hypoxic conditions are common features of tumor microenvironments, we also investigated the characterization of a hypoxia mimicking condition which leads to defective mitochondria. In fact, in these two conditions, we produced huge amount of transcriptomics, metabolomics and fluxomics data in order to produce a genome scale metabolic model (GSMM) combining multi-omics data in the frame of a European project which helps us to understand the regulation of metabolic alterations in breast cancer cells. While produced data is to be used in production of GSMM, we also took advantage of the data to study the metabolic adaptations that breast cancer cells undergo in the deprivation of glutamine or when mitochondria are defected. We propose that increased pyruvate cycle with glutamine deprivation and increased reductive carboxylation with not fully functional mitochondria could be targeted in combination therapies to fight against cancer. All in all, besides showing the importance of metabolism in cancer cell proliferation and survival, the results presented in this study also highlights the importance of Systems Biology approaches to understand the molecular mechanisms underlying complex multifactorial diseases in order to develop new potential therapeutic targets.
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Nulit, Rosimah. "Manipulation of the oxidative pentose phosphate pathway in the cytosol of Arabidopsis thaliana." Thesis, University of Sheffield, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.489735.

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Polat, Ibrahim Halil. "Rôle fonctionnel des pentoses phosphates et glutamine dans le métabolisme des cellules cancéreuses." Thesis, Université Grenoble Alpes (ComUE), 2016. http://www.theses.fr/2016GREAS031/document.

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Cancer est un terme qui rassemble plusieurs ensembles hétérogène de maladies et il est caractérisé par la perte de contrôle physiologique et la transformation maligne des cellules saines. Il est essentiel de comprendre le cancer de la biologie cellulaire afin d'identifier de nouveaux biomarqueurs pour le diagnostic précoce et la conception de nouvelles stratégies thérapeutiques. Reprogrammation métabolique est une caractéristique émergente de cancer, ce qui signifie que les cellules cancéreuses passent leur métabolisme de base pour répondre aux exigences accrues de la croissance et la division cellulaire. Par conséquent, explorer reprogrammant métabolique que les cellules cancéreuses subissent est une stratégie clé pour identifier de nouvelles cibles pour le traitement du cancer. Dans cette thèse, de nouvelles possibilités pour le traitement du cancer ont été explorés en analysant la reprogrammation métabolique de la tumeur. À cet égard, nous avons étudié et proposé voie des pentoses phosphates (PPP) enzymes cibles thérapeutiques putatifs contre les cancers du sein et du côlon. En outre, nous avons exploré le métabolisme de la glutamine dans les cellules du cancer du sein et les adaptations du réseau métaboliques qu'ils subissent dans le but de contourner la privation de glutamine et la déficience mitochondriale générale. Ainsi, le ciblage PPP est l'intérêt des chercheurs d'utiliser à la fois oxydantes et non oxydantes phases de cette voie métabolique comme une cible de médicament thérapeutique. Pour tester cela, nous inhibés bœuf PPP enzymes 6PGD dans les cellules cancéreuses du sein et G6PD dans les cellules du côlon.Nous avons effectué la caractérisation de la reprogrammation métabolique induite par l'inhibition de l'enzyme de bœuf PPP par l'ARN interferase (ARNi) silençage médiation, afin d'explorer le potentiel de cette enzyme comme une cible de médicament thérapeutique dans deux lignées de cellules de cancer du sein. Nous avons demontré que l'inhibition 6PGD a entraîné une diminution taux de prolifération, arrêt du cycle cellulaire et induction de l'apoptose médiée par l'activation de p53, en diminuant les capacités de formation mammosphere et le métabolisme altéré de carbone central par modulation de Warburg phenomenan et en améliorant le métabolisme de la glutamine. D'autre part, nous avons montré l'effet de l'inhibition de la G6PD sur la prolifération des cellules du cancer du côlon et du PPP est régulée par la disponibilité de la glutamine dans les cellules cancéreuses du côlon.De plus, nous avons caractérisé les adaptations métaboliques que les cellules cancéreuses du sein subissent la privation de glutamine ou lorsque les mitochondries sont fait défection. Nous avons effectué une analyse des flux métaboliques utilisant métabolomique et Fluxomique et nous avons utilisé la biologie des systèmes afin d'estimer une vision globale des modifications de flux dans différentes conditions de culture. Nous avons observé une augmentation du cycle de pyruvate avec privation glutamine, ce qui indique que le ciblage des enzymes de cette voie telle que l'enzyme malique pourrait être une approche prometteuse combinée à l'inhibition de l'enzyme de glutaminase. D'autre part, nous avons observé que mimant une hypoxie par des cellules de cancer du sein de traitement redirigée oligomycine pour augmenter la carboxylation réductrice. Considérant que l'hypoxie est une condition commune dans l'environnement de la tumeur, le ciblage mécanisme de carboxylation réductrice pourrait être une nouvelle stratégie de lutte contre le cancer. Collectivement, les résultats présentés dans cette thèse démontre l'importance du métabolisme de la prolifération des cellules cancéreuses et la survie. Ce travail met également en évidence l'importance de la biologie des systèmes se rapproche de comprendre les mécanismes moléculaires sous-jacents des maladies multifactorielles complexes afin de souligner de nouvelles cibles thérapeutiques potentielles
Moreover, we characterized the metabolic adaptations that breast cancer cells undergo in the deprivation of glutamine or when mitochondria are defected. We conducted metabolic flux analysis using metabolomics and fluxomics approaches and we employed Systems Biology approaches in order to estimate a global view of flux alterations in different culture conditions. We observed an increased pyruvate cycle with glutamine deprivation, thus indicating that targeting the enzymes of this pathway such as malic enzyme could be a promising approach combined with inhibition of glutaminase enzyme. On the other hand, we observed that mimicking hypoxia by oligomycin treatment redirected breast cancer cells to increase reductive carboxylation. Considering that hypoxia is a common condition in the tumor environment, targeting reductive carboxylation mechanism could be a novel strategy to fight against cancer. Collectively, all the results provided in this thesis demosntrate the importance of metabolism in cancer cell proliferation and survival. This work also highlights the importance of Systems Biology approaches to comprehend the molecular mechanisms underlying complex multifactorial diseases in order to point out new potential therapeutic targets
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Books on the topic "Enzymes; Pentose phosphate pathway"

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The pentose phosphate pathway. London: Academic Press, 1985.

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Roberts, Juliet A. Evaluation of the quantitative cytochemistry of glutathione, oxidative enzymes of the pentose phosphate pathway and related systems for the functional characterisation of malignant cells. Uxbridge: Brunel University, 1990.

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Wood, Terry. The pentose phosphate pathway. Orlando: Academic Press, 1985.

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Meijer, A. E. F. Hugo. The pentose phosphate pathway in skeletal muscle under patho-physiological conditions: A combined histochemical and biochemical study. Stuttgart: G. Fischer, 1991.

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Toivari, Mervi. Engineering the pentose phosphate pathway of Saccharomyces cerevisiae for production of ethanol and xylitol. [Espoo, Finland]: VTT Technical Research Centre of Finland, 2007.

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Al-Bader, Dhia A. Investigating the role of the oxidative pentose phosphate pathway as the major route of carbohydrate catabolism in the cyanobacterium Synechocystis sp. PCC 6803. [s.l.]: typescript, 1999.

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The Pentose Phosphate Pathway. Elsevier, 1985. http://dx.doi.org/10.1016/b978-0-12-762860-8.x5001-8.

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The Pentose Phosphate Pathway in Skeletal Muscle Under Patho-Physiological Conditions: A Combined Histochemical and Biochemical Study (Progress in Histochemistry and Cytochemistry). VCH Publishers, 1991.

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Javed, Murid Hussain. Bovine amniotic and allantoic fluids for the culture of murine embryos and determination of pentose phosphate and Embden-Meyerhof pathway activities in bovine embryos. 1990.

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Sedel, Frédéric, and Carla E. M. Hollak. Disorders of Thiamine Metabolism. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199972135.003.0028.

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Thiamine is a water-soluble vitamin acting in the mitochondria as a cofactor for energy metabolism and, in the cytoplasm, in the pentose phosphate biosynthetic pathway. Its transport through the plasma membrane requires two transporters with overlapping functions: THTR1 encoded by SLC19A2, and THTR2 encoded by SLC19A3. Thiamine is transformed into its active form, thiamine pyrophosphate (TPP) by a kinase encoded by the TPK1 gene. Then it may enter the mitochondria through a TPP transporter encoded by SLC25A19. Mutations in SLC19A2 cause thiamine-responsive megaloblastic anemia (TRMA). Mutations in SLC19A3 cause biotin/thiamine–responsive basal ganglia disease. Mutations in SLC25A19 may cause early microcephaly with death in infancy (also called Amish microcephaly) or a later-onset bilateral striatal necrosis with progressive peripheral neuropathy. Recently, mutations in the TPK1 gene have been associated with recurrent encephalopathy with mild lactic acidosis.
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Book chapters on the topic "Enzymes; Pentose phosphate pathway"

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Poliquin, Kelly, Francis X. Cunningham, R. Raymond Gantt, and Elisabeth Gantt. "Interactions of Isoprenoid Pathway Enzymes and Indirect Stimulation of Isoprenoid Biosynthesis by Pentose Phosphate Cycle Substrates in Synechocystis PCC 6803." In Isoprenoid Synthesis in Plants and Microorganisms, 51–63. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4614-4063-5_4.

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Arese, Paolo, and Valentina Gallo. "Pentose Phosphate Pathway." In Encyclopedia of Malaria, 1–14. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-8757-9_5-1.

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Gupta, Rani, and Namita Gupta. "Pentose Phosphate Pathway." In Fundamentals of Bacterial Physiology and Metabolism, 289–305. Singapore: Springer Singapore, 2021. http://dx.doi.org/10.1007/978-981-16-0723-3_10.

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Chesworth, J. M., T. Stuchbury, and J. R. Scaife. "The Pentose Phosphate Pathway." In An Introduction to Agricultural Biochemistry, 201–6. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-009-1441-4_15.

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Verhoeven, Nanda M., and Cornelis Jakobs. "Disorders of the Pentose Phosphate Pathway." In Inborn Metabolic Diseases, 131–34. Berlin, Heidelberg: Springer Berlin Heidelberg, 2006. http://dx.doi.org/10.1007/978-3-540-28785-8_8.

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Wamelink, Mirjam M. C., Vassili Valayannopoulos, and Cornelis Jakobs. "Disorders of the Pentose Phosphate Pathway." In Inborn Metabolic Diseases, 151–55. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-642-15720-2_8.

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Dringen, R., H. H. Hoepken, T. Minich, and C. Ruedig. "1.3 Pentose Phosphate Pathway and NADPH Metabolism." In Handbook of Neurochemistry and Molecular Neurobiology, 41–62. Boston, MA: Springer US, 2007. http://dx.doi.org/10.1007/978-0-387-30411-3_3.

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Wamelink, Mirjam M. C., Vassili Valayannopoulos, and Barbara Garavaglia. "Disorders of Glycolysis and the Pentose Phosphate Pathway." In Inborn Metabolic Diseases, 149–60. Berlin, Heidelberg: Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-662-49771-5_7.

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Comini, Marcelo A., Cecilia Ortíz, and Juan José Cazzulo. "Drug Targets in Trypanosomal and Leishmanial Pentose Phosphate Pathway." In Trypanosomatid Diseases, 297–313. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2013. http://dx.doi.org/10.1002/9783527670383.ch16.

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Benito, Adrián, Santiago Diaz-Moralli, Johannes F. Coy, Josep J. Centelles, and Marta Cascante. "Role of the Pentose Phosphate Pathway in Tumour Metabolism." In Tumor Cell Metabolism, 143–63. Vienna: Springer Vienna, 2015. http://dx.doi.org/10.1007/978-3-7091-1824-5_7.

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Conference papers on the topic "Enzymes; Pentose phosphate pathway"

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Skelton, D. J., J. S. Hallinan, S. Park, and A. Wipat. "Computational intelligence for metabolic pathway design: Application to the pentose phosphate pathway." In 2016 IEEE Conference on Computational Intelligence in Bioinformatics and Computational Biology (CIBCB). IEEE, 2016. http://dx.doi.org/10.1109/cibcb.2016.7758101.

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Ghanem, Noorhan, Chirine El Baba, Lara Al Saleh, Berthe Hayar, Patrick Aouad, Marwa Al Hassan, Riyad El-Khoury, Julnar Usta, and Nadine Darwiche. "Abstract 236: Therapeutic targeting of the pentose phosphate pathway in colorectal cancer." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-236.

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Villaverde, Marcela Solange, and Jorge Silvio Gutkind. "Abstract 2548: Pentose phosphate pathway inhibition potentiates metformin cytotoxic effects on HNSCC cells." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-2548.

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Yao, H., J. Gong, Z. Feng, X. Lu, A. L. Peterson, X. Ji, and P. A. Dennery. "Pentose Phosphate Pathway Controls Endothelial Cell Proliferation During Hyperoxic Lung Injury in Neonates." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a4663.

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Schito, Luana, Sergio Rey, Bradly G. Wouters, and Marianne Koritzinsky. "Abstract 4499: The oncometabolite fumarate prevents hypoxia-induced ER stress by enhancing the pentose phosphate pathway." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-4499.

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Schito, Luana, Sergio Rey, Judy Pawling, James W. Dennis, Bradly G. Wouters, and Marianne Koritzinsky. "Abstract 1031: Fumarate hydratase deficiency redirects glucose metabolism of hypoxic cancer cells into the pentose phosphate pathway." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-1031.

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Xu, Ming Jing, Kit Ho Lai, Shu Hai Lin, Pui Wah Tse, David Kung Chun Chiu, Hui Yu Koh, Cheuk Ting Law, et al. "Abstract 1058: Targeting pentose phosphate pathway (PPP) represents a novel therapeutic strategy for hepatocellular carcinoma (HCC) treatment." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-1058.

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Aurora, Arin B., VIshal Khivansara, Ashley Leach, Misty Martin-Sandoval, Thomas Mathews, and Sean J. Morrison. "Abstract 85: Metastasizing melanoma cells exhibit increased dependence on the pentose phosphate pathway to manage oxidative stress." In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-85.

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Kowalik, Marta A., Giulia Guzzo, Andrea Morandi, Andrea Perra, Silvia Menegon, Maria M. Angioni, Silvia Giordano, Paola Chiarugi, Andrea Rasola, and Amedeo Columbano. "Abstract A02: OXPHOS inhibition and pentose phosphate pathway induction are early events priming preneoplastic lesions toward HCC development." In Abstracts: AACR Special Conference: Metabolism and Cancer; June 7-10, 2015; Bellevue, WA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1557-3125.metca15-a02.

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Debeb, BG, RA Larson, L. Lacerda, W. Xu, DL Smith, NT Ueno, JM Reuben, et al. "Abstract P5-03-05: Histone deacetylase (HDAC)-inhibitor mediated reprogramming drives cancer cells to the pentose phosphate metabolic pathway." In Abstracts: Thirty-Fifth Annual CTRC‐AACR San Antonio Breast Cancer Symposium‐‐ Dec 4‐8, 2012; San Antonio, TX. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/0008-5472.sabcs12-p5-03-05.

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Reports on the topic "Enzymes; Pentose phosphate pathway"

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Bolo, N. R. Nuclear magnetic resonance studies of the regulation of the pentose phosphate pathway. Office of Scientific and Technical Information (OSTI), November 1991. http://dx.doi.org/10.2172/5313663.

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Bolo, Nicolas Robin. Nuclear magnetic resonance studies of the regulation of the pentose phosphate pathway. Office of Scientific and Technical Information (OSTI), November 1991. http://dx.doi.org/10.2172/10133997.

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