Relevant bibliographies by topics / Phosphoenol pyruvate kinase (PEPCK)

Academic literature on the topic 'Phosphoenol pyruvate kinase (PEPCK)'

Author: Grafiati
Published: 10 December 2022
Last updated: 29 January 2023

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Journal articles on the topic "Phosphoenol pyruvate kinase (PEPCK)"

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Lewitt, MS, K. Brismar, J. Ohlson, and J. Hartman. "Lithium chloride inhibits the expression and secretion of insulin-like growth factor-binding protein-1." Journal of Endocrinology 171, no. 3 (December 1, 2001): R11—R15. http://dx.doi.org/10.1677/joe.0.171r011.

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Insulin-like growth factor-binding protein-1 (IGFBP-1) regulates IGF availability for glucose homeostasis. The IGFBP-1 promoter shares common regulatory response elements with phosphoenol pyruvate carboxykinase (PEPCK), the expression and activity of which is inhibited by lithium chloride, associated with an inhibition of glycogen synthase kinase (GSK)-3 activity, in the rat hepatoma cell line H4-II-E. We therefore determined the effect of lithium chloride on IGFBP-1 expression and secretion in H4-II-E cells. Lithium chloride inhibited IGFBP-1 secretion in a dose response and reversible manner by approx 80% during 5-h and 16-h incubations. An inhibitory effect on IGFBP-1 mRNA expression was observed at 2 h. The inhibitory effect of lithium and insulin were not additive when used alone, but inhibition by lithium occurred when insulin action was blocked by activating AMP-activated protein kinase with 5-aminoimidazole-4-carboxamide-riboside (AICAR). These findings suggest that GSK-3 inhibition, or another pathway activated by lithium, may be involved in a pathway controlling IGFBP-1, inhibiting synthesis when insulin activity is absent or impaired.
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Jones, C. G., and M. A. Titheradge. "The effect of treatment of the rat with bacterial endotoxin on gluconeogenesis and pyruvate metabolism in subsequently isolated hepatocytes." Biochemical Journal 289, no. 1 (January 1, 1993): 169–72. http://dx.doi.org/10.1042/bj2890169.

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The effect of treatment of rats with bacterial endotoxin on gluconeogenesis and the flux through pyruvate kinase, phosphoenolpyruvate carboxykinase (PEPCK), pyruvate carboxylase and pyruvate dehydrogenase (PDH) was measured in isolated hepatocytes, prepared from animals starved for 18 h, incubated in the presence of 1 mM pyruvate. The lipopolysaccharide reduced gluconeogenesis by 50% and lowered the flux through pyruvate kinase, PEPCK and pyruvate carboxylase by comparable amounts. There was no effect of endotoxaemia on PDH flux, indicating that the lowered rate of gluconeogenesis is not the result of a redistribution of pyruvate metabolism between oxidation and carboxylation. The results confirm that a stimulation of pyruvate kinase activity following treatment with lipopolysaccharide is not involved in the inhibition of gluconeogenesis, but that the effect resides at the level of phosphoenolpyruvate formation. The most favoured mechanism for the inhibition of glucose synthesis is via an inhibition of PEPCK and subsequent feedback inhibition of pyruvate carboxylase, although a secondary effect at the level of the mitochondria and pyruvate carboxylase cannot be excluded.
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Zelle, Rintze M., Josh Trueheart, Jacob C. Harrison, Jack T. Pronk, and Antonius J. A. van Maris. "Phosphoenolpyruvate Carboxykinase as the Sole Anaplerotic Enzyme in Saccharomyces cerevisiae." Applied and Environmental Microbiology 76, no. 16 (June 25, 2010): 5383–89. http://dx.doi.org/10.1128/aem.01077-10.

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ABSTRACT Pyruvate carboxylase is the sole anaplerotic enzyme in glucose-grown cultures of wild-type Saccharomyces cerevisiae. Pyruvate carboxylase-negative (Pyc−) S. cerevisiae strains cannot grow on glucose unless media are supplemented with C4 compounds, such as aspartic acid. In several succinate-producing prokaryotes, phosphoenolpyruvate carboxykinase (PEPCK) fulfills this anaplerotic role. However, the S. cerevisiae PEPCK encoded by PCK1 is repressed by glucose and is considered to have a purely decarboxylating and gluconeogenic function. This study investigates whether and under which conditions PEPCK can replace the anaplerotic function of pyruvate carboxylase in S. cerevisiae. Pyc− S. cerevisiae strains constitutively overexpressing the PEPCK either from S. cerevisiae or from Actinobacillus succinogenes did not grow on glucose as the sole carbon source. However, evolutionary engineering yielded mutants able to grow on glucose as the sole carbon source at a maximum specific growth rate of ca. 0.14 h−1, one-half that of the (pyruvate carboxylase-positive) reference strain grown under the same conditions. Growth was dependent on high carbon dioxide concentrations, indicating that the reaction catalyzed by PEPCK operates near thermodynamic equilibrium. Analysis and reverse engineering of two independently evolved strains showed that single point mutations in pyruvate kinase, which competes with PEPCK for phosphoenolpyruvate, were sufficient to enable the use of PEPCK as the sole anaplerotic enzyme. The PEPCK reaction produces one ATP per carboxylation event, whereas the original route through pyruvate kinase and pyruvate carboxylase is ATP neutral. This increased ATP yield may prove crucial for engineering of efficient and low-cost anaerobic production of C4 dicarboxylic acids in S. cerevisiae.
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Radiati, Lilik Eka, Dian Laksamana Hati, Sri Andarini, Dian Handayani, and Djalal Rosyidi. "Potensi Whey Kefir Susu Kambing Sebagai Anti-Obesitas Melalui Penghambatan Sintesis Lipid dan Aktivitas Phosphoenolpyruvate Carboxykinase (PEPCK) pada Sel Model Adiposit 3T3-L1." Indonesian Journal of Human Nutrition 9, no. 2 (December 30, 2022): 207. http://dx.doi.org/10.21776/ub.ijhn.2022.009.02.9.

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Obesitas menjadi salah satu penyebab utama sindrom metabolik dislipidemia, yang dapat sebagai komorbid berbagai penyakit. Penggunaan obat-obatan untuk mengurangi obesitas memiliki akibat yang merugikan, oleh karena itu dikembangkan produk komplementer dari susu fermentasi sebagai strategi non-farmakologis untuk pengelolaan dislipidemia. Pemecahan masalah obesitas dapat dilakukan melalui pendekatan adipogenesis pada sel model adiposit 3T3-L1. Tujuan penelitian ini adalah menganalisis pemberian whey-KSK terhadap TG (Total Trigliserida), TC (Total Kolesterol) dan aktivitas PEPCK (Phosphoenol pyruvate Carboxykinase) sel adiposit 3T3-L1. Metode penelitian adalah percobaan pemberian dosis whey-KSK yang berbeda yaitu P1 (25mg/ml), P2 (50 mg/ml), P3 (75 mg/ml), P4 (100 mg/ml), dan kelompok KN (kontrol negatif) dan KP (kontrol positif) pada adiposit 3T3-L1, dengan empat kali ulangan. Hasil penelitian menunjukkan whey-KSK 25 – 100 µg/mL dapat menurunkan TG sebesar 35,39 – 55,32%, menurunkan TC sebesar 30,46-62,12%, menurunkan aktivitas PEPCK sebesar 27,10-82,52% dan menurunkan aktivitas spesifik PEPCK sebesar 33,06-63,34%. Kesimpulan whey-KSK dapat menghambat adipogenesis sel adiposit 3T3-L1 dan berpotensi sebagai antiobesitas.
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Hosagoudar, V. B. "Computational Screening Of Phytochemicals To Block Phosphoenol Pyruvate Carboxykinase (Pepck) ,A Key Enzyme In Glucose Metabolism." Scientific Transactions in Enviornment and Technovation 4, no. 2 (December 15, 2010): 89–91. http://dx.doi.org/10.20894/stet.116.004.002.008.

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Bizeau, Michael E., Chiffon Short, Jeffrey S. Thresher, S. Renee Commerford, Wayne T. Willis, and Michael J. Pagliassotti. "Increased pyruvate flux capacities account for diet-induced increases in gluconeogenesis in vitro." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 281, no. 2 (August 1, 2001): R427—R433. http://dx.doi.org/10.1152/ajpregu.2001.281.2.r427.

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High-fat (HF) and high-sucrose (SU) diets increase gluconeogenesis. The present study was designed to determine the contributions of pyruvate dehydrogenase, pyruvate carboxylase, phospho enolpyruvate carboxykinase (PEPCK), and pyruvate kinase fluxes to this accelerated gluconeogenesis (GNEO) in the absence and presence of fatty acids. Male Sprague-Dawley rats were fed an HF, SU, or starch (ST) diet for 1 wk, and hepatocytes or mitochondria were isolated. In the absence of palmitate, the tracer estimated rates of GNEO (nmol · min−1 · mg−1) were elevated in hepatocytes isolated from SU (32.3 ± 1.8) and HF (35.4 ± 1.8) vs. ST (22.8 ± 1.5). Pyruvate carboxylase and PEPCK flux rates (nmol · min−1 · mg−1) were increased in the SU (47.5 ± 2.2 and 34.8 ± 1.5) and HF (49.4 ± 1.8 and 38.2 ± 1.8) groups compared with the ST group (32.8 ± 3.2 and 44.3 ± 2.0). Palmitate (250–1,000 μM) stimulation of these fluxes was not significantly different among groups. Bromopalmitate, an inhibitor of fat oxidation, abolished differences in GNEO, pyruvate carboxylase, and PEPCK fluxes in HF and SU vs. ST. In isolated mitochondria, pyruvate carboxylation and palmitoyl carnitine oxidation were not significantly different among groups. The results of this study suggest that the increased gluconeogenic flux observed with HF and SU diets is associated with an increased pyruvate flux through pyruvate carboxylase and PEPCK. Moreover, the ability of bromopalmitate to normalize gluconeogenic fluxes suggests that endogenous fatty acids contribute to diet-induced increases in GNEO.
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Nizielski, S. E., C. Arizmendi, A. R. Shteyngarts, C. J. Farrell, and J. E. Friedman. "Involvement of transcription factor C/EBP-beta in stimulation of PEPCK gene expression during exercise." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 270, no. 5 (May 1, 1996): R1005—R1012. http://dx.doi.org/10.1152/ajpregu.1996.270.5.r1005.

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Prolonged exercise increases gluconeogenesis and activates transcription of the hepatic phosphoenol pyruvate carboxykinase (PEPCK) gene. The mechanisms that regulate the transcriptional control of gene expression depend on the interaction of nuclear proteins with distinct DNA sequences. To determine the involvement with the liver-enriched transcription factor CCAAT/enhancer binding protein beta (C/EMP-beta) in the induction of PEPCK gene transcription during prolonged exercise or adenosine 3',5'-cyclic monophosphate (cAMP) treatment, we examined C/EBP-beta mRNA and nuclear protein concentrations, as well as C/EBP-beta binding to the PEPCK promoter at the cAMP response element (CRE)(-87/-74) and P3I (-248/-230) binding sites. The requirement of these DNA elements for exercise-induced stimulation of PEPCK gene expression was established in transgenic mice carrying -460 +/- 73 of the PEPCK promoter with a mutation in either the CRE or P3I binding domain linked to a bovine growth hormone (bGH) reporter gene. In mice carrying the intact promoter, prolonged exercise increased the concentration of liver bGH mRNA by 510% compared with an increase of only 270% in mice with a mutation in either the CRE or P3I site. Exercise or cAMP injection induced a 7.5- and 13-fold increase in nuclear C/EBP-beta protein, respectively. In electrophoretic mobility shift assays (EMSA), the total quantity of nuclear proteins bound to either oligomer was not altered by treatment. However, addition of C/EBP-beta antisera in the EMSA in a supershift assay indicated that liver nuclear extracts from exercised or cAMP-treated mice demonstrated significantly greater DNA binding due to C/EBP-beta (CRE: control 44.4 +/- 2.3%, exercise 56.7% +/- 2.2%, cAMP 54.5 +/- 3.6% of total binding, P < 0.001; P3I: control 35.8 +/- 2.5%, exercise 64.9 +/- 1.9%, cAMP 57.3 +/- 2.5% of total binding, P < 0.001). Taken together, these results suggest that exercise and cAMP treatment induce a transient increase in C/EBP-beta that may contribute to the molecular mechanism for signaling PEPCK gene transcription and increasing gluconeogenesis during exercise.
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O'Brien, R. M., R. S. Streeper, J. E. Ayala, B. T. Stadelmaier, and L. A. Hornbuckle. "Insulin-regulated gene expression." Biochemical Society Transactions 29, no. 4 (August 1, 2001): 552–58. http://dx.doi.org/10.1042/bst0290552.

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Insulin regulates the expression of more than 150 genes, indicating that this is a major action of this hormone. At least eight distinct consensus insulin response sequence (IRSs) have been defined through which insulin can regulate gene transcription. These include the serum response element, the activator protein 1 (‘AP-1’) motif, the Ets motif, the E-box motif and the thyroid transcription factor 2 (‘TTF-2’) motif. All of these IRSs mediate stimulatory effects of insulin on gene transcription. In contrast, an element with the consensus sequence T(G/A)TTT(T/G)-(G/T), which we refer to as the phosphoenol-pyruvate carboxykinase (PEPCK)-like motif, mediates the inhibitory effect of insulin on transcription of the genes encoding PEPCK, insulinlike-growth-factor-binding protein 1 (IGFBP-1), tyrosine aminotransferase and the glucose-6-phos-phatase (G6Pase) catalytic subunit. The forkhead transcription factor FKHR has recently been shown to bind this PEPCK-like IRS motif and a model has been proposed in which insulin inhibits gene transcription by stimulating the phosphorylation and nuclear export of FKHR. Our results suggest that this model is consistent with the action of insulin on transcription of the gene encoding IGFBP-1 but not that of the G6Pase catalytic subunit. Thus, even though the IRSs in both promoters seem identical, they are functionally distinct. In addition, in the G6Pase catalytic subunit promoter, hepatocyte nuclear factor 1 (‘HNF-1’), acts as an accessory factor to enhance the effect of insulin mediated through the IRS.
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Tielens, A. G. M., P. Van Der Meer, J. M. Van Den Heuvel, and S. G. Van Den Bergh. "The enigmatic presence of all gluconeogenic enzymes in Schistosoma mansoni adults." Parasitology 102, no. 2 (April 1991): 267–76. http://dx.doi.org/10.1017/s0031182000062582.

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SUMMARYThe activities of glucose-6-phosphatase (G6Pase), frucrose-1,6-bisphosphatase (FBPase), phosphoenolpyruvate carboxykinase (PEPCK) and pyruvate carboxylase (PC) were determined in homogenates of adult Schistosoma mansoni worms and compared with the activities in homogenates of rat liver and rat skeletal muscle, tissues with a high and a low gluconeogenic capacity, respectively. All four gluconeogenic enzymes were present in S. mansoni. The enzymes were less active than in rat liver, but the activities of G6Pase, PEPCK and PC were at least an order of magnitude higher than in rat skeletal muscle whereas FBPase was approximately equally active in S. mansoni and in rat muscle. Experiments with 14C-labelled substrates or [14C]NaHCO3 failed to demonstrate the actual occurrence of gluconeogenesis in S. mansoni. Some possible other functions of the gluconeogenic enzymes were investigated. Experiments with inhibitors of PEPCK gave no indications that this enzyme was involved in the degradation of glucose. This was confirmed by 13C-NMR experiments which indicated that lactate was formed from phosphoenolpyruvate via the actions of pyruvate kinase and lactate dehydrogenase, and that PEPCK did not participate in the formation of lactate. Substrate cycling between fructose-6-phosphate and fructose-1,6-bisphosphate was demonstrated to occur in adult S. mansoni. This shows that FBPase participates in the glucose metabolism of this parasite.
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Christie, Daphne A., John W. Powell, Jeremy N. Stables, and Robert A. Watt. "A nuclear magnetic resonance study of the role of phosphoenol pyruvate carboxykinase (PEPCK) in the glucose metabolism of Dipetalonema viteae." Molecular and Biochemical Parasitology 24, no. 2 (June 1987): 125–30. http://dx.doi.org/10.1016/0166-6851(87)90098-3.

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Dissertations / Theses on the topic "Phosphoenol pyruvate kinase (PEPCK)"

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Leroyer, Stephanie. "Voies de recyclage des acides gras au sein du tissu adipeux en situation de lipolyse : mécanismes impliqués, altérations dans l'obésité et en réponse aux antirétroviraux, amélioration par les thiazolidinediones." Paris 6, 2007. http://www.theses.fr/2007PA066689.

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Hussain, Rashid. "Exploring metabolic interventions for CIN cancer therapy." Thesis, 2017. http://hdl.handle.net/2440/119191.

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Chromosomal instability (CIN) has been established as one of the hallmarks of cancer, which is prevalent in most of the solid and advanced tumours. CIN enhances genetic heterogeneity in cancer cells. This heterogeneity provides selective advantages to cancer cells against the drugs and the therapies, which are linked to poor prognosis and relapse of cancer. Altered metabolism is another hallmark of cancer, which is being targeted for cancer therapy. In this thesis, I have discussed the therapeutic effect of targeting metabolism in CIN cells and CIN tumours. Chapter 1 is my introduction in which I have reviewed cancer, its therapy, CIN, its types, mechanisms, causes, and therapeutic targeting of CIN. I also review cancer metabolism, its targeting for the treatment, and targeting metabolism in CIN cells. Chapter 2 is a published review article about Drosophila being a model for CIN. In this article I have discussed different CIN models and their limitations, then I described Drosophila as a model for CIN studies. I later discussed different Drosophila CIN model systems which have been studied to understand CIN and cancer. As Drosophila has been extensively studied for CIN and cancer therapy, our lab has focused on targeting CIN cells in Drosophila. In an earlier study (Shaukat et al, 2012) it was found metabolic candidates such as Pas kinase and phosphofructokinase could be crucial for CIN cell survival. Chapter 3 is a further screening of metabolic candidates. We found few potential targets from all the major metabolic pathways whose knock down can specifically kill CIN cells. It was found, mitochondrial activity and oxidative stress was high which induced DNA damage and apoptosis in CIN cells targeted by these metabolic alterations. In chapter 4, I discuss the application of the selected candidates on CIN tumours. We further explain how one of my metabolic candidates stopped the tumour growth. This chapter also discusses the mechanism of ROS (reactive oxygen species) production and implications of high NADH levels in CIN cells, which was deficient in our earlier studies. Chapter 5 is my discussion in which I have collectively discussed my results, the significant of my work, my current model, and future directions. In appendix 1 I have presented a published review article on the role of JNK in response to oxidative DNA damage. This chapter encompasses activation of JNK by ROS, outcomes of JNK in response to ROS. Appendix 2 has figures for SOX drug and ovary numbers of the hosts.
Thesis (Ph.D.) -- University of Adelaide, School of Biological Sciences, 2017
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