Journal articles on the topic 'Glycolytic enzymes'
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1
Parkhouse, Wade S. "Regulation of skeletal muscle metabolism by enzyme binding." Canadian Journal of Physiology and Pharmacology 70, no. 1 (January 1, 1992): 150–56. http://dx.doi.org/10.1139/y92-022.
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The random diffusion mechanism is usually assumed in analyzing the energetics of specific pathways despite the findings that enzymes associate with each other and (or) with various membranous and contractile elements of the cell. Successive glycolytic enzymes have been shown to associate in the cytosol as enzyme complexes or bind to the thin filaments. Furthermore, the degree of glycolytic enzyme interactions have been shown to change with altered rates of carbon flux through the pathway. In particular, the proportions of aldolase, phosphofructokinase, and glyceraldehyde phosphate dehydrogenase bound to the contractile proteins have been found to increase with increased rates of glycolysis. In addition, decreasing pH and ionic strength are also associated with an increase in glycolytic enzyme interactions. The kinetics displayed by interacting enzymes generally serve to enhance their catalytic efficiencies. The associations of the glycolytic enzymes serve to enhance metabolite transfer rates, increase the local concentrations of intermediates, and provide for regulation of activity via effectors. Therefore these interactions provide an additional mechanism for regulating glycolytic flux in skeletal muscle.Key words: glycolysis, skeletal muscle, enzymes, binding.
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Ayna, Adnan, and Peter C. E. Moody. "Activity of fructose-1,6-bisphosphatase from Campylobacter jejuni." Biochemistry and Cell Biology 98, no. 4 (August 2020): 518–24. http://dx.doi.org/10.1139/bcb-2020-0021.
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The glycolytic pathway of the enteric pathogen Campylobacter jejuni is incomplete; the absence of phosphofructokinase means that the suppression of futile cycling at this point in the glycolytic–gluconeogenic pathway might not be required, and therefore the mechanism for controlling pathway flux is likely to be quite different or absent. In this study, the characteristics of fructose-1,6-bisphosphatase (FBPase) of C. jejuni are described and the regulation of this enzyme is compared with the equivalent enzymes from organisms capable of glycolysis. The enzyme is insensitive to AMP inhibition, unlike other type I FBPases. Campylobacter jejuni FBPase also shows limited sensitivity to other glycolytic and gluconeogenic intermediates. The allosteric cooperative control of the enzyme’s activity found in type I FBPases appears to have been lost.
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Simoneau, Jean-Aimé, and David E. Kelley. "Altered glycolytic and oxidative capacities of skeletal muscle contribute to insulin resistance in NIDDM." Journal of Applied Physiology 83, no. 1 (July 1, 1997): 166–71. http://dx.doi.org/10.1152/jappl.1997.83.1.166.
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Simoneau, Jean-Aimé, and David E. Kelley. Altered glycolytic and oxidative capacities of skeletal muscle contribute to insulin resistance in NIDDM. J. Appl. Physiol. 83(1): 166–171, 1997.—The insulin resistance of skeletal muscle in glucose-tolerant obese individuals is associated with reduced activity of oxidative enzymes and a disproportionate increase in activity of glycolytic enzymes. Because non-insulin-dependent diabetes mellitus (NIDDM) is a disorder characterized by even more severe insulin resistance of skeletal muscle and because many individuals with NIDDM are obese, the present study was undertaken to examine whether decreased oxidative and increased glycolytic enzyme activities are also present in NIDDM. Percutaneous biopsy of vatus lateralis muscle was obtained in eight lean (L) and eight obese (O) nondiabetic subjects and in eight obese NIDDM subjects and was assayed for marker enzymes of the glycolytic [phosphofructokinase, glyceraldehyde phosphate dehydrogenase, hexokinase (HK)] and oxidative pathways [citrate synthase (CS), cytochrome- c oxidase], as well as for a glycogenolytic enzyme (glycogen phosphorylase) and a marker of anaerobic ATP resynthesis (creatine kinase). Insulin sensitivity was measured by using the euglycemic clamp technique. Activity for glycolytic enzymes (phosphofructokinase, glyceraldehye phosphate dehydrogenase, HK) was highest in subjects with subjects with NIDDM, following the order of NIDDM > O > L, whereas maximum velocity for oxidative enzymes (CS, cytochrome- c oxidase) was lowest in subjects with NIDDM. The ratio between glycolytic and oxidative enzyme activities within skeletal muscle correlated negatively with insulin sensitivity. The HK/CS ratio had the strongest correlation ( r = −0.60, P < 0.01) with insulin sensitivity. In summary, an imbalance between glycolytic and oxidative enzyme capacities is present in NIDDM subjects and is more severe than in obese or lean glucose-tolerant subjects. The altered ratio between glycolytic and oxidative enzyme activities found in skeletal muscle of individuals with NIDDM suggests that a dysregulation between mitochondrial oxidative capacity and capacity for glycolysis is an important component of the expression of insulin resistance.
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Jo, Min-Sik, Hyun-Woo Yang, Joo-Hoo Park, Jae-Min Shin, and Il-Ho Park. "Glycolytic reprogramming is involved in tissue remodeling on chronic rhinosinusitis." PLOS ONE 18, no. 2 (February 16, 2023): e0281640. http://dx.doi.org/10.1371/journal.pone.0281640.
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Background Glycolytic reprogramming is a key feature of chronic inflammatory disease. Extracellular matrix (ECM) produced by myofibroblasts plays an important role in tissue remodeling of nasal mucosa in chronic rhinosinusitis (CRS). This study aimed to determine whether glycolytic reprogramming contributes to myofibroblast differentiation and ECM production in nasal fibroblasts. Methods Primary nasal fibroblasts were isolated from the nasal mucosa of patients with CRS. Glycolytic reprogramming was assessed by measuring the extracellular acidification and oxygen consumption rates in nasal fibroblast, with and without transforming growth factor beta 1 (TGF-β1) treatment. Expression of glycolytic enzymes and ECM components was measured by real-time polymerase chain reaction, western blotting, and immunocytochemical staining. Gene set enrichment analysis was performed using whole RNA-sequencing data of nasal mucosa of healthy donors and patients with CRS. Result Glycolysis of nasal fibroblasts stimulated with TGF-B1 was upregulated along with glycolytic enzymes. Hypoxia-inducing factor (HIF)-1α was a high-level regulator of glycolysis, and increased HIF-1α expression promoted glycolysis of nasal fibroblasts, and inhibition of HIF-1α down-regulated myofibroblasts differentiation and ECM production. Conclusion This study suggests that inhibition of the glycolytic enzyme and HIF-1α in nasal fibroblasts regulates myofibroblast differentiation and ECM generation associated with nasal mucosa remodeling.
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van den Brink, Joost, André B. Canelas, Walter M. van Gulik, Jack T. Pronk, Joseph J. Heijnen, Johannes H. de Winde, and Pascale Daran-Lapujade. "Dynamics of Glycolytic Regulation during Adaptation of Saccharomyces cerevisiae to Fermentative Metabolism †." Applied and Environmental Microbiology 74, no. 18 (July 18, 2008): 5710–23. http://dx.doi.org/10.1128/aem.01121-08.
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ABSTRACT The ability of baker's yeast (Saccharomyces cerevisiae) to rapidly increase its glycolytic flux upon a switch from respiratory to fermentative sugar metabolism is an important characteristic for many of its multiple industrial applications. An increased glycolytic flux can be achieved by an increase in the glycolytic enzyme capacities (V max) and/or by changes in the concentrations of low-molecular-weight substrates, products, and effectors. The goal of the present study was to understand the time-dependent, multilevel regulation of glycolytic enzymes during a switch from fully respiratory conditions to fully fermentative conditions. The switch from glucose-limited aerobic chemostat growth to full anaerobiosis and glucose excess resulted in rapid acceleration of fermentative metabolism. Although the capacities (V max) of the glycolytic enzymes did not change until 45 min after the switch, the intracellular levels of several substrates, products, and effectors involved in the regulation of glycolysis did change substantially during the initial 45 min (e.g., there was a buildup of the phosphofructokinase activator fructose-2,6-bisphosphate). This study revealed two distinct phases in the upregulation of glycolysis upon a switch to fermentative conditions: (i) an initial phase, in which regulation occurs completely through changes in metabolite levels; and (ii) a second phase, in which regulation is achieved through a combination of changes in V max and metabolite concentrations. This multilevel regulation study qualitatively explains the increase in flux through the glycolytic enzymes upon a switch of S. cerevisiae to fermentative conditions and provides a better understanding of the roles of different regulatory mechanisms that influence the dynamics of yeast glycolysis.
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Kondoh, Hiroshi, Matilde E. Lleonart, Jesus Gil, Jing Wang, Paolo Degan, Gordon Peters, Dolores Martinez, Amancio Carnero, and David Beach. "Glycolytic Enzymes Can Modulate Cellular Life Span." Cancer Research 65, no. 1 (January 1, 2005): 177–85. http://dx.doi.org/10.1158/0008-5472.177.65.1.
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Abstract An unbiased screen for genes that can immortalize mouse embryonic fibroblasts identified the glycolytic enzyme phosphoglycerate mutase (PGM). A 2-fold increase in PGM activity enhances glycolytic flux, allows indefinite proliferation, and renders cells resistant to ras-induced arrest. Glucosephosphate isomerase, another glycolytic enzyme, displays similar activity and, conversely, depletion of PGM or glucosephosphate isomerase with short interfering RNA triggers premature senescence. Immortalized mouse embryonic fibroblasts and mouse embryonic stem cells display higher glycolytic flux and more resistance to oxidative damage than senescent cells. Because wild-type p53 down-regulates PGM, mutation of p53 can facilitate immortalization via effects on PGM levels and glycolysis.
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Winther, Sally, Marie S. Isidor, Astrid L. Basse, Nina Skjoldborg, Amanda Cheung, Bjørn Quistorff, and Jacob B. Hansen. "Restricting glycolysis impairs brown adipocyte glucose and oxygen consumption." American Journal of Physiology-Endocrinology and Metabolism 314, no. 3 (March 1, 2018): E214—E223. http://dx.doi.org/10.1152/ajpendo.00218.2017.
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During thermogenic activation, brown adipocytes take up large amounts of glucose. In addition, cold stimulation leads to an upregulation of glycolytic enzymes. Here we have investigated the importance of glycolysis for brown adipocyte glucose consumption and thermogenesis. Using siRNA-mediated knockdown in mature adipocytes, we explored the effect of glucose transporters and glycolytic enzymes on brown adipocyte functions such as consumption of glucose and oxygen. Basal oxygen consumption in brown adipocytes was equally dependent on glucose and fatty acid oxidation, whereas isoproterenol (ISO)-stimulated respiration was fueled mainly by fatty acids, with a significant contribution from glucose oxidation. Knockdown of glucose transporters in brown adipocytes not only impaired ISO-stimulated glycolytic flux but also oxygen consumption. Diminishing glycolytic flux by knockdown of the first and final enzyme of glycolysis, i.e., hexokinase 2 (HK2) and pyruvate kinase M (PKM), respectively, decreased glucose uptake and ISO-stimulated oxygen consumption. HK2 knockdown had a more severe effect, which, in contrast to PKM knockdown, could not be rescued by supplementation with pyruvate. Hence, brown adipocytes rely on glucose consumption and glycolytic flux to achieve maximum thermogenic output, with glycolysis likely supporting thermogenesis not only by pyruvate formation but also by supplying intermediates for efferent metabolic pathways.
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Jung, Da-Woon, Woong-Hee Kim, and Darren R. Williams. "Chemical genetics and its application to moonlighting in glycolytic enzymes." Biochemical Society Transactions 42, no. 6 (November 17, 2014): 1756–61. http://dx.doi.org/10.1042/bst20140201.
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Glycolysis is an ancient biochemical pathway that breaks down glucose into pyruvate to produce ATP. The structural and catalytic properties of glycolytic enzymes are well-characterized. However, there is growing appreciation that these enzymes participate in numerous moonlighting functions that are unrelated to glycolysis. Recently, chemical genetics has been used to discover novel moonlighting functions in glycolytic enzymes. In the present mini-review, we introduce chemical genetics and discuss how it can be applied to the discovery of protein moonlighting. Specifically, we describe the application of chemical genetics to uncover moonlighting in two glycolytic enzymes, enolase and glyceraldehyde dehydrogenase. This led to the discovery of moonlighting roles in glucose homoeostasis, cancer progression and diabetes-related complications. Finally, we also provide a brief overview of the latest progress in unravelling the myriad moonlighting roles for these enzymes.
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Chowdhury, Shomeek, Stephen Hepper, Mudassir K. Lodi, Milton H. Saier, and Peter Uetz. "The Protein Interactome of Glycolysis in Escherichia coli." Proteomes 9, no. 2 (April 6, 2021): 16. http://dx.doi.org/10.3390/proteomes9020016.
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Glycolysis is regulated by numerous mechanisms including allosteric regulation, post-translational modification or protein-protein interactions (PPI). While glycolytic enzymes have been found to interact with hundreds of proteins, the impact of only some of these PPIs on glycolysis is well understood. Here we investigate which of these interactions may affect glycolysis in E. coli and possibly across numerous other bacteria, based on the stoichiometry of interacting protein pairs (from proteomic studies) and their conservation across bacteria. We present a list of 339 protein-protein interactions involving glycolytic enzymes but predict that ~70% of glycolytic interactors are not present in adequate amounts to have a significant impact on glycolysis. Finally, we identify a conserved but uncharacterized subset of interactions that are likely to affect glycolysis and deserve further study.
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Lloyd, Pamela G., and Christopher D. Hardin. "Role of microtubules in the regulation of metabolism in isolated cerebral microvessels." American Journal of Physiology-Cell Physiology 277, no. 6 (December 1, 1999): C1250—C1262. http://dx.doi.org/10.1152/ajpcell.1999.277.6.c1250.
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We used13C-labeled substrates and nuclear magnetic resonance spectroscopy to examine carbohydrate metabolism in vascular smooth muscle of freshly isolated pig cerebral microvessels (PCMV). PCMV utilized [2-13C]glucose mainly for glycolysis, producing [2-13C]lactate. Simultaneously, PCMV utilized the glycolytic intermediate [1-13C]fructose 1,6-bisphosphate (FBP) mainly for gluconeogenesis, producing [1-13C]glucose with only minor [3-13C]lactate production. The dissimilarity in metabolism of [2-13C]FBP derived from [2-13C]glucose breakdown and metabolism of exogenous [1-13C]FBP demonstrates that carbohydrate metabolism is compartmented in PCMV. Because glycolytic enzymes interact with microtubules, we disrupted microtubules with vinblastine. Vinblastine treatment significantly decreased [2-13C]lactate peak intensity (87.8 ± 3.7% of control). The microtubule-stabilizing agent taxol also reduced [2-13C]lactate peak intensity (90.0 ± 2.4% of control). Treatment with both agents further decreased [2-13C]lactate production (73.3 ± 4.0% of control). Neither vinblastine, taxol, or the combined drugs affected [1-13C]glucose peak intensity (gluconeogenesis) or disrupted the compartmentation of carbohydrate metabolism. The similar effects of taxol and vinblastine, drugs that have opposite effects on microtubule assembly, suggest that they produce their effects on glycolytic rate by competing with glycolytic enzymes for binding, not by affecting the overall assembly state of the microtubule network. Glycolysis, but not gluconeogenesis, may be regulated in part by glycolytic enzyme-microtubule interactions.
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Masters, Colin. "Interactions of glycolytic enzymes." Trends in Biochemical Sciences 14, no. 9 (September 1989): 361. http://dx.doi.org/10.1016/0968-0004(89)90003-0.
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MASTERS, C., and J. CLEGG. "Evolution of glycolytic enzymes." Trends in Biochemical Sciences 11, no. 5 (May 1986): 203. http://dx.doi.org/10.1016/0968-0004(86)90005-8.
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Low, Philip S., Estela M. Campanella, William A. Anong, Nancy J. Wandersee, Cheryl A. Hillary, and Athar Chishti. "Characterization of Glycolytic Enzyme Complexes on Murine Erythrocyte Membranes." Blood 104, no. 11 (November 16, 2004): 1571. http://dx.doi.org/10.1182/blood.v104.11.1571.1571.
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Abstract Glycolytic enzymes have been recently shown to exist as multi-enzyme complexes in association with the cytoplasmic domain of band 3 at the inner surface of the human erythrocyte membrane. Because several of the glycolytic enzyme binding sites have been mapped to sequences near the NH2-terminus of band 3 (DDYED and EEYED) that are not conserved in mice (EEVLE and EELEN), the question naturally arose whether the existence of glycolytic enzyme complexes on erythrocyte membranes might be only a product of recent evolution. To test this hypothesis, fresh murine erythrocytes were fixed and stained with antibodies to glyceraldehyde-3-phosphate dehydrogenase (GAPDH), aldolase, phosphofructokinase (PFK), pyruvate kinase (PK), lactate dehydrogenase (LDH) and carbonic anhydrase II (CA II was used as a control, since it binds to a distant site near the COOH-terminus of band 3). Importantly, analysis of intact murine erythrocytes by confocal microscopy demonstrated that all of the above enzymes are localized to the membrane in oxygenated cells. In contrast, upon deoxygenation of the intact cells, release of the glycolytic enzymes (but not CA II) from the erythrocyte membrane and their uniform redistribution throughout the cytoplasm is observed. Because deoxyhemoglobin has been shown in human erythrocytes to compete with glycolytic enzymes (but not with CA II) for a common binding site at the NH2-terminus of band 3, these data argue that murine band 3, despite its weak homology to human band 3, still constitutes an organization center for glycolytic enzymes on the erythrocyte membrane. To further test this hypothesis, erythrocytes from band 3 knockout mice were similarly examined by confocal microscopy. Not surprisingly, all of the enzymes in all of the cells were evenly distributed throughout the cytoplasm, regardless of the oxygenation state of the cell. Further, immunoblot analyses demonstrated that glycolytic enzyme content of the band 3 knockout erythrocytes was measurably reduced compared to healthy mice, suggesting that the anion transporter may also contribute to enzyme stabilization during the lifetime of the erythrocyte. Finally, to determine whether the integrity of other membrane structures might impact the assembly of glycolytic enzyme complexes on the erythrocyte membrane, α-spectrin deficient mice were also examined for their enzyme distributions. Curiously, > 50% of the cells in any field exhibited glycolytic enzyme staining throughout the cytoplasm, with the remainder showing mainly membrane staining. Conceivably, the stabiity of glycolytic enzyme complexes on the membrane may also depend on the integrity of the membrane skeleton. Taken together, these data argue that glycolytic enzymes assemble in an oxygenation-dependent manner into complexes on murine erythrocyte membranes and that the stability of these complexes depends on the presence of band 3 and to a lesser extent α-spectrin. Supported by NIH grant GM24417.
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Liapounova, Natalia A., Vladimir Hampl, Paul M. K. Gordon, Christoph W. Sensen, Lashitew Gedamu, and Joel B. Dacks. "Reconstructing the Mosaic Glycolytic Pathway of the Anaerobic Eukaryote Monocercomonoides." Eukaryotic Cell 5, no. 12 (October 27, 2006): 2138–46. http://dx.doi.org/10.1128/ec.00258-06.
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ABSTRACT All eukaryotes carry out glycolysis, interestingly, not all using the same enzymes. Anaerobic eukaryotes face the challenge of fewer molecules of ATP extracted per molecule of glucose due to their lack of a complete tricarboxylic acid cycle. This may have pressured anaerobic eukaryotes to acquire the more ATP-efficient alternative glycolytic enzymes, such as pyrophosphate-fructose 6-phosphate phosphotransferase and pyruvate orthophosphate dikinase, through lateral gene transfers from bacteria and other eukaryotes. Most studies of these enzymes in eukaryotes involve pathogenic anaerobes; Monocercomonoides, an oxymonad belonging to the eukaryotic supergroup Excavata, is a nonpathogenic anaerobe representing an evolutionarily and ecologically distinct sampling of an anaerobic glycolytic pathway. We sequenced cDNA encoding glycolytic enzymes from a previously established cDNA library of Monocercomonoides and analyzed the relationships of these enzymes to those from other organisms spanning the major groups of Eukaryota, Bacteria, and Archaea. We established that, firstly, Monocercomonoides possesses alternative versions of glycolytic enzymes: fructose-6-phosphate phosphotransferase, both pyruvate kinase and pyruvate orthophosphate dikinase, cofactor-independent phosphoglycerate mutase, and fructose-bisphosphate aldolase (class II, type B). Secondly, we found evidence for the monophyly of oxymonads, kinetoplastids, diplomonads, and parabasalids, the major representatives of the Excavata. We also found several prokaryote-to-eukaryote as well as eukaryote-to-eukaryote lateral gene transfers involving glycolytic enzymes from anaerobic eukaryotes, further suggesting that lateral gene transfer was an important factor in the evolution of this pathway for denizens of this environment.
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Pagliaro, L., and D. L. Taylor. "2-Deoxyglucose and cytochalasin D modulate aldolase mobility in living 3T3 cells." Journal of Cell Biology 118, no. 4 (August 15, 1992): 859–63. http://dx.doi.org/10.1083/jcb.118.4.859.
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Approximately 23% of the glycolytic enzyme aldolase in the perinuclear region of Swiss 3T3 cells is immobile as measured by FRAP. Previous studies suggest that the immobile fraction may be associated with the actin cytoskeleton (Pagliaro, L. and D. L. Taylor. 1988. J. Cell Biol. 107:981-991), and it has been proposed that the association of some glycolytic enzymes with the cytoskeleton could have functional significance, perhaps involving a fundamental relationship between glycolysis, cytoplasmic organization, and cell motility. We have tested the effect of a key glycolytic inhibitor and an actin cytoskeletal modulator on the mobility of aldolase in living cells directly, using fluorescent analog cytochemistry and FRAP. We report here that the competitive hexokinase inhibitor 2-deoxyglucose releases the bound fraction of aldolase in 3T3 cells within 10 min, and that this process is reversible upon washout of the inhibitor. A similar result is produced with the actin-binding agent, cytochalasin D. These results are consistent with models in which glycolytic enzymes are not exclusively diffusion-limited, soluble proteins, but may exist partially in the solid phase of cytoplasm. Such organization has significant implications for both the modulation of cytoplasmic structure and for cellular metabolism.
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Achs, M. J., and D. Garfinkel. "Pancreatic islet discrimination of hexose anomers. I. Steady-state computer simulation." American Journal of Physiology-Endocrinology and Metabolism 255, no. 2 (August 1, 1988): E189—E200. http://dx.doi.org/10.1152/ajpendo.1988.255.2.e189.
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Pancreatic islets detect glucose level by phosphorylating it and converting the glycolytic rate to a signal to secrete insulin. Insulin secretion is greater from the alpha- than from the beta-anomer when the D-glucose level is below 22 mM. D-mannose behaves similarly but at nearly twofold higher concentrations. Two explanations have been proposed: 1) glucokinase, which has the same anomeric preference, is the principal hexose phosphorylating enzyme and limits glycolytic rate. 2) Phosphofructokinase limits glycolysis and hexokinase is the principal enzyme phosphorylating hexose; hexosediphosphate activators of phosphofructokinase are more readily synthesized from alpha-anomers of hexose phosphates. We have simulated both alternatives with a detailed anomerically specific model of the hexose-metabolizing glycolytic enzymes. The pathway preference for alpha-anomer of both hexoses was adequately reproduced with anomerically active limiting glucokinase. The other mechanism did not reproduce the observed pathway preference.
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Kim, Jung-whan, and Chi V. Dang. "Multifaceted roles of glycolytic enzymes." Trends in Biochemical Sciences 30, no. 3 (March 2005): 142–50. http://dx.doi.org/10.1016/j.tibs.2005.01.005.
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Kurganov, B. I., N. P. Sugrobova, and L. S. Mil'man. "Supramolecular organization of glycolytic enzymes." Journal of Theoretical Biology 116, no. 4 (October 1985): 509–26. http://dx.doi.org/10.1016/s0022-5193(85)80086-2.
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Papaioannou, Michael D., and Nigel J. Gooderham. "p53 regulation of glycolytic enzymes." Toxicology 253, no. 1-3 (November 2008): 16–17. http://dx.doi.org/10.1016/j.tox.2008.07.018.
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Zimmermann, Friedrich K. "Glycolytic enzymes as regulatory factors." Journal of Biotechnology 27, no. 1 (December 1992): 17–26. http://dx.doi.org/10.1016/0168-1656(92)90027-7.
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Zhan, Huiwang David, Jane Borleis, Chris Janetopoulos, and Peter Devreotes. "Abstract 288: Glycolysis is enriched to propagating waves in cell cortex as a new mechanism for cancer progression." Cancer Research 83, no. 7_Supplement (April 4, 2023): 288. http://dx.doi.org/10.1158/1538-7445.am2023-288.
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Abstract Tumors preferentially metabolize glucose anaerobically through glycolysis with lower ATP production efficiency rather than aerobically even when oxygen is available. This was reported by Otto Warburg 100 years ago, yet the mechanism is hitherto not well-understood. Glycolysis is canonically thought to occur only in cytosol; if and how it is regulated by the actin cytoskeletal network is controversial. I found that, in epithelial cells, 6 of the 9 glycolytic enzymes (HK, PFK, ALDO, GAPDH, ENO, and PK, others not tested) are enriched at newly formed LifeAct labeled waves and protrusions, where mitochondria are barely detected by Mito-Tracker. The application of glycolysis inhibitors but not oxidative phosphorylation inhibitors abolishes cell migration. These results indicate that cells rely on the local ATP production from glycolysis enriched in the cortical waves and protrusions to move. We visualized and measured glycolysis production in confocal and TIRF microscopes using a series of biosensors for ATP, NADH/NAD+ ratio, and pyruvate. We then found glycolysis was enhanced by perturbations that increase wave formation such as EGF/Insulin stimulation or recruiting ActA to membrane, and reduced by wave decrease from PI3K inhibition, hyper- and hypo-osmotic shock, or F-actin assembly inhibition. This suggests that enriching glycolytic enzymes on waves results in higher glycolysis production. We do not think the changes of glycolysis by wave perturbations are merely due to direct regulation on glycolytic enzymes by canonical signaling pathways (e.g., Ras-PI3K-AKT), since ActA recruitment or F-actin inhibition does not lead to acute changes in these signaling pathways but mainly causes the assembly or disassembly of the F-actin/glycolytic waves. These findings together lead to our new theory that energy production from glycolysis is enhanced by recruiting the glycolytic enzymes to the waves and protrusions on the cell cortex. This is potentially paradigm-shifting because for many decades glycolysis - one of the two major ways in a cell to produce ATP - has been thought to only occur in cytosol. Interestingly, we also found glycolytic enzymes enriched in F-actin labeled protrusions of Dictyostelium cells, which indicates that this can possibly be an evolutionally conserved mechanism. Additionally, we investigated non-cancer MCF-10A cells (M1) and a series of M1-derived cancer cell lines (M2 - M4) with increased metastatic index and cancer malignancy, and found a sequential increase in actin wave and glycolysis activities from M1 to M4 cells. Cancer cells such as M3 had a larger drop in glycolysis than non-cancer parental M1 cells upon wave inhibition. These results provide a new explanation for the Warburg effect that increased cortical waves in cancer cells will accelerate and improve glycolysis, which will not only greatly contribute to our understanding of cancer but also the design of new interventions. Citation Format: Huiwang David Zhan, Jane Borleis, Chris Janetopoulos, Peter Devreotes. Glycolysis is enriched to propagating waves in cell cortex as a new mechanism for cancer progression [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2023; Part 1 (Regular and Invited Abstracts); 2023 Apr 14-19; Orlando, FL. Philadelphia (PA): AACR; Cancer Res 2023;83(7_Suppl):Abstract nr 288.
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Crowther, Gregory J., William F. Kemper, Michael F. Carey, and Kevin E. Conley. "Control of glycolysis in contracting skeletal muscle. II. Turning it off." American Journal of Physiology-Endocrinology and Metabolism 282, no. 1 (January 1, 2002): E74—E79. http://dx.doi.org/10.1152/ajpendo.2002.282.1.e74.
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Glycolytic flux in muscle declines rapidly after exercise stops, indicating that muscle activation is a key controller of glycolysis. The mechanism underlying this control could be 1) a Ca2+-mediated modulation of glycogenolysis, which supplies substrate (hexose phosphates, HP) to the glycolytic pathway, or 2) a direct effect on glycolytic enzymes. To distinguish between these possibilities, HP levels were raised by voluntary 1-Hz exercise, and glycolytic flux was measured after the exercise ceased. Glycolytic H+ and ATP production were quantified from changes in muscle pH, phosphocreatine concentration, and Pi concentration as measured by 31P magnetic resonance spectroscopy. Substrate (HP) and metabolite (Pi, ADP, and AMP) levels remained high when exercise stopped because of the occlusion of blood flow with a pressure cuff. Glycolytic flux declined to basal levels within ∼20 s of the end of exercise despite elevated levels of HP and metabolites. Therefore, this flux does not subside because of insufficient HP substrate; rather, glycolysis is controlled independently of glycogenolytic HP production. We conclude that the inactivation of glycolysis after exercise reflects the cessation of contractile activity and is mediated within the glycolytic pathway rather than via the control of glycogen breakdown.
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Mao, Na, Honghao Yang, Jie Yin, Yaqian Li, Fuyu Jin, Tian Li, Xinyu Yang, et al. "Glycolytic Reprogramming in Silica-Induced Lung Macrophages and Silicosis Reversed by Ac-SDKP Treatment." International Journal of Molecular Sciences 22, no. 18 (September 17, 2021): 10063. http://dx.doi.org/10.3390/ijms221810063.
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Glycolytic reprogramming is an important metabolic feature in the development of pulmonary fibrosis. However, the specific mechanism of glycolysis in silicosis is still not clear. In this study, silicotic models and silica-induced macrophage were used to elucidate the mechanism of glycolysis induced by silica. Expression levels of the key enzymes in glycolysis and macrophage activation indicators were analyzed by Western blot, qRT-PCR, IHC, and IF analyses, and by using a lactate assay kit. We found that silica promotes the expression of the key glycolysis enzymes HK2, PKM2, LDHA, and macrophage activation factors iNOS, TNF-α, Arg-1, IL-10, and MCP1 in silicotic rats and silica-induced NR8383 macrophages. The enhancement of glycolysis and macrophage activation induced by silica was reduced by Ac-SDKP or siRNA-Ldha treatment. This study suggests that Ac-SDKP treatment can inhibit glycolytic reprogramming in silica-induced lung macrophages and silicosis.
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Alam, Asrar, Md Kausar Neyaz, and Syed Ikramul Hasan. "Exploiting Unique Structural and Functional Properties of Malarial Glycolytic Enzymes for Antimalarial Drug Development." Malaria Research and Treatment 2014 (December 17, 2014): 1–13. http://dx.doi.org/10.1155/2014/451065.
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Metabolic enzymes have been known to carry out a variety of functions besides their normal housekeeping roles known as “moonlighting functions.” These functionalities arise from structural changes induced by posttranslational modifications and/or binding of interacting proteins. Glycolysis is the sole source of energy generation for malaria parasite Plasmodium falciparum, hence a potential pathway for therapeutic intervention. Crystal structures of several P. falciparum glycolytic enzymes have been solved, revealing that they exhibit unique structural differences from the respective host enzymes, which could be exploited for their selective targeting. In addition, these enzymes carry out many parasite-specific functions, which could be of potential interest to control parasite development and transmission. This review focuses on the moonlighting functions of P. falciparum glycolytic enzymes and unique structural differences and functional features of the parasite enzymes, which could be exploited for therapeutic and transmission blocking interventions against malaria.
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Godfrey, Wesley H., Kaho Cho, Shruthi Shanmukha, Jodie Deng, and Michael Kornberg. "Inhibition of distinct glycolytic enzymes produces differential effects on CD4 T cell function." Journal of Immunology 210, no. 1_Supplement (May 1, 2023): 148.12. http://dx.doi.org/10.4049/jimmunol.210.supp.148.12.
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Abstract Introduction: When T cells are activated, they upregulate glycolysis and take on a requisite Warburg phenotype. In this study, we evaluated the effect of inhibiting two distinct glycolytic enzymes, GAPDH and PGAM, on CD4 T cell differentiation. Methods/Results: Using the GAPDH inhibitor heptelidic acid, we found that GAPDH inhibition produces a potent anti-inflammatory phenotype in Th1 cells, significantly reducing IFNγ expression. We further showed that GAPDH inhibition produces the anti-inflammatory metabolite methylglyoxal, which is necessary for its anti-inflammatory effect. GAPDH inhibition also produced anti-inflammatory effects in vivo, as heptelidic acid significantly reduced disease severity and altered immune subsets in a therapeutic treatment paradigm in the MOG 35–55EAE model of multiple sclerosis. Furthermore, we showed that GAPDH inhibition enhances Treg polarization, while inhibiting PGAM, a downstream glycolytic enzyme, potently blocked Treg polarization. Additionally, we found that inhibition of PGAM increases serine biosynthesis and subsequently alters 1-carbon metabolism. We also found that PGAM gene expression is associated with Treg differentiation and response to immunotherapy in lung cancer patients. Conclusion: Overall, our in vitroand in vivoresults indicate that targeting the glycolytic enzyme GAPDH produces an anti-inflammatory phenotype via the methylglyoxal pathway, while targeting the downstream enzyme PGAM produces an opposite effect via regulation of serine synthesis. Our findings suggest that the functional consequences of glycolysis inhibition depend on the specific enzymes targeted, which represent promising novel therapeutic targets for immunological disease. This work was supported by NIH/NINDS grant K08NS104266 and Conrad N. Hilton Foundation Marilyn Hilton Bridging Award for Physician Scientists grant 17316 to MDK. WHG was supported by NIH MSTP Grant T32 GM136577 and the American Association of Immunologists’ Careers in Immunology Fellowship Program.
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Pagliaro, L. "Glycolysis Revisited - A Funny Thing Happened on the Way to the Krebs Cycle." Physiology 8, no. 5 (October 1, 1993): 219–23. http://dx.doi.org/10.1152/physiologyonline.1993.8.5.219.
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Glycolysis is generally considered to be the archetypal "soluble" metabolic pathway, despite growing evidence to the contrary. Direct biophysical measurements in living cells have revealed that some glycolytic enzymes exist partially in the solid phase of cytoplasm and that solid-phase partitioning of enzymes responds to metabolic changes.
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Wojtas, K., N. Slepecky, L. von Kalm, and D. Sullivan. "Flight muscle function in Drosophila requires colocalization of glycolytic enzymes." Molecular Biology of the Cell 8, no. 9 (September 1997): 1665–75. http://dx.doi.org/10.1091/mbc.8.9.1665.
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Structural relationships between the myofibrillar contractile apparatus and the enzymes that generate ATP for muscle contraction are not well understood. We explored whether glycolytic enzymes are localized in Drosophila flight muscle and whether localization is required for function. We find that glycerol-3-phosphate dehydrogenase (GPDH) is localized at Z-discs and M-lines. The glycolytic enzymes aldolase and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) are also localized along the sarcomere with a periodic pattern that is indistinguishable from that of GPDH localization. Furthermore, localization of aldolase and GAPDH requires simultaneous localization of GPDH, because aldolase and GAPDH are not localized along the sarcomere in muscles of strains that carry Gpdh null alleles. In an attempt to understand the process of glycolytic enzyme colocalization, we have explored in more detail the mechanism of GPDH localization. In flight muscle, there is only one GPDH isoform, GPDH-1, which is distinguished from isoforms found in other tissues by having three C-terminal amino acids: glutamine, asparagine, and leucine. Transgenic flies that can produce only GPDH-1 display enzyme colocalization similar to wild-type flies. However, transgenic flies that synthesize only GPDH-3, lacking the C-terminal tripeptide, do not show the periodic banding pattern of localization at Z-discs and M-lines for GPDH. In addition, neither GAPDH nor aldolase colocalize at Z-discs and M-lines in the sarcomeres of muscles from GPDH-3 transgenic flies. Failure of the glycolytic enzymes to colocalize in the sarcomere results in the inability to fly, even though the full complement of active glycolytic enzymes is present in flight muscles. Therefore, the presence of active enzymes in the cell is not sufficient for muscle function; colocalization of the enzymes is required. These results indicate that the mechanisms by which ATP is supplied to the myosin ATPase, for muscle contraction, requires a highly organized cellular system.
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Webb, Bradley A., Anne M. Dosey, Torsten Wittmann, Justin M. Kollman, and Diane L. Barber. "The glycolytic enzyme phosphofructokinase-1 assembles into filaments." Journal of Cell Biology 216, no. 8 (June 23, 2017): 2305–13. http://dx.doi.org/10.1083/jcb.201701084.
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Despite abundant knowledge of the regulation and biochemistry of glycolytic enzymes, we have limited understanding on how they are spatially organized in the cell. Emerging evidence indicates that nonglycolytic metabolic enzymes regulating diverse pathways can assemble into polymers. We now show tetramer- and substrate-dependent filament assembly by phosphofructokinase-1 (PFK1), which is considered the “gatekeeper” of glycolysis because it catalyzes the step committing glucose to breakdown. Recombinant liver PFK1 (PFKL) isoform, but not platelet PFK1 (PFKP) or muscle PFK1 (PFKM) isoforms, assembles into filaments. Negative-stain electron micrographs reveal that filaments are apolar and made of stacked tetramers oriented with exposed catalytic sites positioned along the edge of the polymer. Electron micrographs and biochemical data with a PFKL/PFKP chimera indicate that the PFKL regulatory domain mediates filament assembly. Quantified live-cell imaging shows dynamic properties of localized PFKL puncta that are enriched at the plasma membrane. These findings reveal a new behavior of a key glycolytic enzyme with insights on spatial organization and isoform-specific glucose metabolism in cells.
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Navarro, Juan A., Juan Decara, Dina Medina-Vera, Rubén Tovar, Juan Suarez, Javier Pavón, Antonia Serrano, et al. "D-Pinitol from Ceratonia siliqua Is an Orally Active Natural Inositol That Reduces Pancreas Insulin Secretion and Increases Circulating Ghrelin Levels in Wistar Rats." Nutrients 12, no. 7 (July 8, 2020): 2030. http://dx.doi.org/10.3390/nu12072030.
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To characterize the metabolic actions of D-Pinitol, a dietary inositol, in male Wistar rats, we analyzed its oral pharmacokinetics and its effects on (a) the secretion of hormones regulating metabolism (insulin, glucagon, IGF-1, ghrelin, leptin and adiponectin), (b) insulin signaling in the liver and (c) the expression of glycolytic and neoglucogenesis enzymes. Oral D-Pinitol administration (100 or 500 mg/Kg) resulted in its rapid absorption and distribution to plasma and liver compartments. Its administration reduced insulinemia and HOMA-IR, while maintaining glycaemia thanks to increased glucagon activity. In the liver, D-Pinitol reduced the key glycolytic enzyme pyruvate kinase and decreased the phosphorylation of the enzymes AKT and GSK-3. These observations were associated with an increase in ghrelin concentrations, a known inhibitor of insulin secretion. The profile of D-Pinitol suggests its potential use as a pancreatic protector decreasing insulin secretion through ghrelin upregulation, while sustaining glycaemia through the liver-based mechanisms of glycolysis control.
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Journet, E. P., R. Bligny, and R. Douce. "Is the availability of substrate for the tricarboxylic acid cycle a limiting factor for uncoupled respiration in sycamore (Acer pseudoplatanus) cells?" Biochemical Journal 233, no. 2 (January 15, 1986): 571–76. http://dx.doi.org/10.1042/bj2330571.
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Protoplasts obtained from sycamore (Acer pseudoplatanus) cell suspensions were found to be highly intact and to retain a high rate of O2 consumption. If the protoplasts were taken up and expelled through a fine nylon mesh, all the protoplasts were ruptured, leaving the fragile amyloplasts largely intact. Distribution of enzymes of glycolysis in plastids and soluble phase of sycamore protoplasts indicated that the absolute maximum activity for each glycolytic enzyme under optimum conditions exceeded the estimates of the maximal rate at which sycamore cells oxidize triose phosphate. Passage of protoplasts through the fine nylon mesh produced a 3-5-fold decrease in O2 consumption. However, addition of saturating amounts of respiratory substrates and ADP restored an O2 consumption equal to that observed with uncoupled intact protoplasts. Taken together, these results demonstrated that neither the overall capacity of the glycolytic enzymes in sycamore cells nor the availability of respiratory substrates for the mitochondria is ultimately responsible for determining the rate of uncoupled respiration in sycamore cells.
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Tobisch, Steffen, Daniela Zühlke, Jörg Bernhardt, Jörg Stülke, and Michael Hecker. "Role of CcpA in Regulation of the Central Pathways of Carbon Catabolism in Bacillus subtilis." Journal of Bacteriology 181, no. 22 (November 15, 1999): 6996–7004. http://dx.doi.org/10.1128/jb.181.22.6996-7004.1999.
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ABSTRACT The Bacillus subtilis two-dimensional (2D) protein index contains almost all glycolytic and tricarboxylic acid (TCA) cycle enzymes, among them the most abundant housekeeping proteins of growing cells. Therefore, a comprehensive study on the regulation of glycolysis and the TCA cycle was initiated. Whereas expression of genes encoding the upper and lower parts of glycolysis (pgi,pfk, fbaA, and pykA) is not affected by the glucose supply, there is an activation of the glycolytic gap gene and the pgk operon by glucose. This activation seems to be dependent on the global regulator CcpA, as shown by 2D polyacrylamide gel electrophoresis analysis as well as by transcriptional analysis. Furthermore, a high glucose concentration stimulates production and excretion of organic acids (overflow metabolism) in the wild type but not in the ccpAmutant. Finally, CcpA is involved in strong glucose repression of almost all TCA cycle genes. In addition to TCA cycle and glycolytic enzymes, the levels of many other proteins are affected by theccpA mutation. Our data suggest (i) that ccpAmutants are unable to activate glycolysis or carbon overflow metabolism and (ii) that CcpA might be a key regulator molecule, controlling a superregulon of glucose catabolism.
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Conjard, A., B. Ferrier, M. Martin, A. Caillette, H. Carrier, and G. Baverel. "Effects of chronic renal failure on enzymes of energy metabolism in individual human muscle fibers." Journal of the American Society of Nephrology 6, no. 1 (July 1995): 68–74. http://dx.doi.org/10.1681/asn.v6168.
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In order to improve knowledge about the mechanisms underlying the alterations of energy metabolism recently observed in the skeletal muscle of patients suffering from chronic renal failure, this study was designed to test (1) whether changes in the activity of key enzymes of energy metabolism occur in the muscle of these patients, and if so (2) whether the different muscle fiber types are equally altered in their metabolic machinery. For this, the maximum activities of 14 enzymes were measured in individual muscle fibers microdissected from biopsies of rectus abdominis muscle obtained from seven normal subjects and seven patients with end-stage renal failure before renal replacement therapy. A large decrease in the activities of beta-hydroxyacyl-coenzyme A dehydrogenase, a key enzyme of the beta-oxidation pathway, of citrate synthase, which initiates the tricarboxylic acid cycle, and of fructose-1,6-bisphosphatase, which contributes to the synthesis of glycogen from lactate, was observed in the three fiber types (slow-twitch oxidative, fast-twitch oxidative-glycolytic, and fast-twitch glycolytic). A smaller reduction of the activities of phosphofructokinase and/or pyruvate kinase, two key enzymes of glycolysis, was also observed in slow-twitch oxidative and/or fast-twitch oxidative-glycolytic fibers. These results demonstrate that the abnormalities of muscle energy metabolism observed in patients with chronic renal failure are due, at least in part, to intrinsic changes in the key enzymes of major energy-providing pathways; they also offer a satisfactory explanation for the defect of oxidative metabolism recently demonstrated in the muscle of these patients.
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Mohammad, Goran Hamid, Vessela Vassileva, Pilar Acedo, Steven W. M. Olde Damink, Massimo Malago, Dipok Kumar Dhar, and Stephen P. Pereira. "Targeting Pyruvate Kinase M2 and Lactate Dehydrogenase A Is an Effective Combination Strategy for the Treatment of Pancreatic Cancer." Cancers 11, no. 9 (September 16, 2019): 1372. http://dx.doi.org/10.3390/cancers11091372.
Full textAbstract:
Reprogrammed glucose metabolism is one of the hallmarks of cancer, and increased expression of key glycolytic enzymes, such as pyruvate kinase M2 (PKM2) and lactate dehydrogenase A (LDHA), has been associated with poor prognosis in various malignancies. Targeting these enzymes could attenuate aerobic glycolysis and inhibit tumor proliferation. We investigated whether the PKM2 activator, TEPP-46, and the LDHA inhibitor, FX-11, can be combined to inhibit in vitro and in vivo tumor growth in preclinical models of pancreatic cancer. We assessed PKM2 and LDHA expression, enzyme activity, and cell proliferation rate after treatment with TEPP-46, FX-11, or a combination of both. Efficacy was validated in vivo by evaluating tumor growth, PK and LDHA activity in plasma and tumors, and PKM2, LDHA, and Ki-67 expression in tumor tissues following treatment. Dual therapy synergistically inhibited pancreatic cancer cell proliferation and significantly delayed tumor growth in vivo without apparent toxicity. Treatment with TEPP-46 and FX-11 resulted in increased PK and reduced LDHA enzyme activity in plasma and tumor tissues and decreased PKM2 and LDHA expression in tumors, which was reflected by a decrease in tumor volume and proliferation. The targeting of glycolytic enzymes such as PKM2 and LDHA represents a promising therapeutic approach for the treatment of pancreatic cancer.
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Wilkinson, R. S., and P. M. Nemeth. "Metabolic fiber types of snake transversus abdominis muscle." American Journal of Physiology-Cell Physiology 256, no. 6 (June 1, 1989): C1176—C1183. http://dx.doi.org/10.1152/ajpcell.1989.256.6.c1176.
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Fibers of the garter snake transversus abdominis muscle fall into three classes according to contraction speed: faster and slower twitch and tonic. To determine the relationship between these physiologically determined classes and established mammalian fiber types, individual fibers were assayed for key enzymes representing the major energy-generating pathways in vertebrate muscle. Five such enzymes were examined: lactate dehydrogenase, malate dehydrogenase, adenylokinase, fumarate hydratase, and beta-hydroxyacyl-CoA dehydrogenase. The muscle contained three principal metabolic fiber types. Fast-contracting twitch fibers had low-oxidative but high-glycolytic capacity and therefore resembled mammalian-type fast-twitch glycolytic (FG) fibers. Slower twitch fibers were high oxidative-high glycolytic, similar to mammalian-type fast-twitch, oxidative, glycolytic (FOG) fibers. Tonic fibers were high oxidative-low glycolytic; this metabolic profile is characteristic of type slow-twitch oxidative (SO) fibers in mammals. Activity of the enzyme adenylokinase, which in mammals correlates with contraction speed and myosin adenosine triphosphatase (ATPase) activity, separated these reptilian fibers into three groups that are similar but not identical to those delineated by oxidative and glycolytic enzymes. Adenylokinase and beta-hydroxyacyl-CoA dehydrogenase showed the widest range of activities in snake muscle and, therefore, the greatest ability to discriminate fiber types.
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Storey, Kenneth B. "Investigations of the mechanisms of glycolytic control during hibernation." Canadian Journal of Zoology 65, no. 12 (December 1, 1987): 3079–83. http://dx.doi.org/10.1139/z87-467.
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Molecular mechanisms of glycolytic rate control during hibernation were investigated in the meadow jumping mouse, Zapus hudsonius. The content of fructose-2, 6-bisphosphate, a potent activator of phosphofructokinase, decreased significantly in brain, heart, and fat pad after 5–8 days of hibernation, rose in kidney, and was unchanged in skeletal muscle. Apparent covalent modification of regulatory enzymes of glycolysis during hibernation was examined in brain, heart, kidney, and skeletal muscle but occurred only in selected instances. Hibernation led to a significant reduction in the percentage of glycogen phosphorylase in the phosphorylated a form in brain and produced kinetic changes (altered Ka AMP, I50 citrate) in phosphofructokinase from heart indicative of enzyme covalent modification. No evidence for covalent modification of pyruvate kinase during hibernation was found in any tissue. Covalent modification of enzymes and alterations in fructose-2, 6-bisphosphate content offer organ-specific control over glycolytic rate during hibernation in response to both the general metabolic rate depression of the hibernating state and the individual adjustments in organ fuel use.
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Moore, P. A., F. A. Sagliocco, R. M. Wood, and A. J. Brown. "Yeast glycolytic mRNAs are differentially regulated." Molecular and Cellular Biology 11, no. 10 (October 1991): 5330–37. http://dx.doi.org/10.1128/mcb.11.10.5330-5337.1991.
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The regulation of glycolytic genes in response to carbon source in the yeast Saccharomyces cerevisiae has been studied. When the relative levels of each glycolytic mRNA were compared during exponential growth on glucose or lactate, the various glycolytic mRNAs were found to be induced to differing extents by glucose. No significant differences in the stabilities of the PFK2, PGK1, PYK1, or PDC1 mRNAs during growth on glucose or lactate were observed. PYK::lacZ and PGK::lacZ fusions were integrated independently into the yeast genome at the ura3 locus. The manner in which these fusions were differentially regulated in response to carbon source was similar to that of their respective wild-type loci. Therefore, the regulation of glycolytic mRNA levels is mediated at the transcriptional level. When the mRNAs are ordered with respect to the glycolytic pathway, two peaks of maximal induction are observed at phosphofructokinase and pyruvate kinase. These enzymes (i) catalyze the two essentially irreversible steps on the pathway, (ii) are the two glycolytic enzymes that are circumvented during gluconeogenesis and hence are specific to glycolysis, and (iii) are encoded by mRNAs that we have shown previously to be coregulated at the translational level in S. cerevisiae (P. A. Moore, A. J. Bettany, and A. J. P. Brown, NATO ASI Ser. Ser. H Cell Biol. 49:421-432, 1990). This differential regulation of glycolytic mRNA levels might therefore have a significant influence upon glycolytic flux in S. cerevisiae.
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Moore, P. A., F. A. Sagliocco, R. M. Wood, and A. J. Brown. "Yeast glycolytic mRNAs are differentially regulated." Molecular and Cellular Biology 11, no. 10 (October 1991): 5330–37. http://dx.doi.org/10.1128/mcb.11.10.5330.
Full textAbstract:
The regulation of glycolytic genes in response to carbon source in the yeast Saccharomyces cerevisiae has been studied. When the relative levels of each glycolytic mRNA were compared during exponential growth on glucose or lactate, the various glycolytic mRNAs were found to be induced to differing extents by glucose. No significant differences in the stabilities of the PFK2, PGK1, PYK1, or PDC1 mRNAs during growth on glucose or lactate were observed. PYK::lacZ and PGK::lacZ fusions were integrated independently into the yeast genome at the ura3 locus. The manner in which these fusions were differentially regulated in response to carbon source was similar to that of their respective wild-type loci. Therefore, the regulation of glycolytic mRNA levels is mediated at the transcriptional level. When the mRNAs are ordered with respect to the glycolytic pathway, two peaks of maximal induction are observed at phosphofructokinase and pyruvate kinase. These enzymes (i) catalyze the two essentially irreversible steps on the pathway, (ii) are the two glycolytic enzymes that are circumvented during gluconeogenesis and hence are specific to glycolysis, and (iii) are encoded by mRNAs that we have shown previously to be coregulated at the translational level in S. cerevisiae (P. A. Moore, A. J. Bettany, and A. J. P. Brown, NATO ASI Ser. Ser. H Cell Biol. 49:421-432, 1990). This differential regulation of glycolytic mRNA levels might therefore have a significant influence upon glycolytic flux in S. cerevisiae.
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Davis, M. Benjamin, and Helga Guderley. "Energy Metabolism in the Locomotor Muscles of the Common Murre (Uria aalge) and the Atlantic Puffin (Fratercula arctica)." Auk 104, no. 4 (October 1, 1987): 733–39. http://dx.doi.org/10.1093/auk/104.4.733.
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Abstract To compare the metabolic systems that support the combination of flying and diving with those used to support burst flying and sustained flying, myoglobin concentrations and maximum enzyme activities were determined for selected enzymes of glycolysis, the Krebs cycle, and amino acid metabolism in the pectoral, supracoracoideus, and sartorius muscles of the Common Murre (Uria aalge), Atlantic Puffin (Fratercula arctica), Rock Dove (Columba livia; hereafter "pigeon"), and Ring-necked Pheasant (Phasianus colchicus). Glycolytic enzyme levels in the flight muscles were lower in the murre and the puffin than in the pheasant, while both glycolytic and Krebs-cycle enzyme levels resembled those in the pigeon. We believe puffins and murres do not rely extensively on anaerobic glycolysis during diving. In concordance with a role in oxygen storage for diving, the levels of myoglobin in the flight muscles of murres and puffins were higher than those in pigeons or pheasants. They were lower than published values for penguins, however. In contrast to the trends for pigeon and pheasant muscles, the alcid sartorius muscles had a considerably lower aerobic orientation than the flight muscles.
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Voronkova, Olga S., Tetiana M. Shevchenko, and Albert I. Vinnikov. "Activity of Catabolic Enzymes of Film-Forming Strains of Staphylococcus aureus." International Letters of Natural Sciences 61 (January 2017): 8–13. http://dx.doi.org/10.18052/www.scipress.com/ilns.61.8.
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The activity of glucose catabolism pathways of staphylococci strains able to form biofilm and isolated from vagina of women with dysbiosis of reproductive tract and strains isolated from women without disorders of microflora was studied. It was established that the investigated film-forming strains utilized the carbohydrates by pentose phosphate pathway mainly, as indicated by 23-33% higher enzyme activity compare to strains isolated from healthy women. Instead strains, isolated from women without reproductive tract dysbiosis, have higher activity of glycolytic enzymes on 13-28%. The prevalence of glycolytic transformation of glucose by strains isolated from healthy women also indicates by the depression of glucose oxidation during action of monoiodinacetate – classical inhibitor of glycolysis. It inhibit glycolysis of strains isolated from healthy women more significant. It was established that oxidase activity of film-forming strains isolated from women with dysbiosis, increased over 40% during the use of basic substrates of citric acid cycle. These data indicate a general increase of catabolic activity of oxidative type of staphylococci isolated during vaginal dysbiosis and able to form biofilm.
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Noble, E. G., and C. D. Ianuzzo. "Influence of training on skeletal muscle enzymatic adaptations in normal and diabetic rats." American Journal of Physiology-Endocrinology and Metabolism 249, no. 4 (October 1, 1985): E360—E365. http://dx.doi.org/10.1152/ajpendo.1985.249.4.e360.
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Muscle homogenates representing slow-twitch oxidative, fast-twitch oxidative-glycolytic, fast-twitch glycolytic, and mixed fiber types were prepared from normal, diabetic, and insulin-treated diabetic rats. Diabetes was induced by injection of 80 mg . kg-1 of streptozotocin. The activities of citrate synthase, succinate dehydrogenase, and 3-hydroxyacyl-CoA dehydrogenase were employed as markers of oxidative potential, whereas phosphorylase, hexokinase, and phosphofructokinase activities were used as an indication of glycolytic capacity. Diabetes was associated with a general decrement in the activity of oxidative marker enzymes for all fiber types except the fast-twitch glycolytic fiber. In contrast, the fast-twitch glycolytic fibers demonstrated the greatest decline in glycolytic enzymatic activity. Insulin-treated animals, either trained or untrained, exhibited enzyme activities similar to their normal counterparts. Exercise training of diabetic rats mimicked the effect of insulin treatment and caused a near normalization of the activity of the marker enzymes. These findings suggest that the enzymatic potential of all skeletal muscle fiber types of diabetic rats may be normalized by exercise training even in the absence of significant amounts of insulin.
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Shi, Lewis Zhichang, Ruoning Wang, Douglas Green, and Hongbo Chi. "Metabolic control of T cell fate decision: the HIF1α-glycolysis axis in the differentiation of TH17 and iTreg cells (163.17)." Journal of Immunology 188, no. 1_Supplement (May 1, 2012): 163.17. http://dx.doi.org/10.4049/jimmunol.188.supp.163.17.
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Abstract Activated T cells mainly use glycolysis to suffice their bioenergetic and biosynthetic demands. However, whether glycolysis actively controls the differentiation of activated T cell is not fully understood. As a master regulator of metabolism, HIF1α regulates multiple rate-limiting glycolytic enzymes. We previously reported that HIF1α deficiency inhibited TH17 differentiation and promoted induced Treg (iTreg) generation (Shi et al, J Exp Med 2011). To further explore the roles of the glycolytic pathway in T cell differentiation, we combined genetic and pharmacological approaches to examine T cell metabolism and signaling. Inhibition of glycolysis by multiple agents diminished TH17 differentiation and promoted iTreg induction, while supplementation of the products of the glycolytic flux partially rescued these defects. Importantly, blocking glycolysis ameliorated the pathogenesis of autoimmune neuroinflammation both prophylactically and therapeutically, suggesting that the glycolytic pathway is a potential therapeutic target for autoimmune pathogenesis elicited by TH17 cells. Mechanistic studies further revealed that downregulation of IL-23R expression contributed to the diminished TH17 differentiation in HIF1α-deficient T cells, as forced expression of IL-23R restored the TH17 defects. In conclusion, our results demonstrate that the HIF1α-mediated glycolytic pathway links T cell metabolism and signaling, thereby dictating the cell fate decision between TH17 and iTreg cells.
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Yeshowardhana, M. M. Gupta, Geeta Bansal, Sindhu Goyal, V. S. Singh, and Km Sangita Jain. "Serum Glycolytic Enzymes in Breast Carcinoma." Tumori Journal 72, no. 1 (February 1986): 35–41. http://dx.doi.org/10.1177/030089168607200106.
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Canback, B., S. G. E. Andersson, and C. G. Kurland. "The global phylogeny of glycolytic enzymes." Proceedings of the National Academy of Sciences 99, no. 9 (April 30, 2002): 6097–102. http://dx.doi.org/10.1073/pnas.082112499.
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Crowhurst, G. S. E., M. N. Isupov, T. Fleming, and J. A. Littlechild. "Two glycolytic enzymes from Sulfolobus solfataricus." Biochemical Society Transactions 26, no. 3 (August 1, 1998): S275. http://dx.doi.org/10.1042/bst026s275.
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Muirhead, Hilary, and Herman Watson. "Glycolytic enzymes: From hexose to pyruvate." Current Biology 2, no. 12 (December 1992): 640. http://dx.doi.org/10.1016/0960-9822(92)90105-j.
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Scopes, R. K., and K. Griffiths-Smith. "Fermentation capabilities ofZymomonas mobilis glycolytic enzymes." Biotechnology Letters 8, no. 9 (September 1986): 653–56. http://dx.doi.org/10.1007/bf01025976.
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Ronai, Zeev. "Glycolytic enzymes as DNA binding proteins." International Journal of Biochemistry 25, no. 7 (July 1993): 1073–76. http://dx.doi.org/10.1016/0020-711x(93)90123-v.
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Muirhead, Hilary, and Herman Watson. "Glycolytic enzymes: from hexose to pyruvate." Current Opinion in Structural Biology 2, no. 6 (January 1992): 870–76. http://dx.doi.org/10.1016/0959-440x(92)90113-l.
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Schaaff, Ine, Jürgen Heinisch, and Friedrich K. Zimmermann. "Overproduction of glycolytic enzymes in yeast." Yeast 5, no. 4 (July 1989): 285–90. http://dx.doi.org/10.1002/yea.320050408.
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Raynaud, Sandy, Rémi Perrin, Muriel Cocaign-Bousquet, and Pascal Loubiere. "Metabolic and Transcriptomic Adaptation of Lactococcus lactis subsp. lactis Biovar diacetylactis in Response to Autoacidification and Temperature Downshift in Skim Milk." Applied and Environmental Microbiology 71, no. 12 (December 2005): 8016–23. http://dx.doi.org/10.1128/aem.71.12.8016-8023.2005.
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ABSTRACT For the first time, a combined genome-wide transcriptome and metabolic analysis was performed with a dairy Lactococcus lactis subsp. lactis biovar diacetylactis strain under dynamic conditions similar to the conditions encountered during the cheese-making process. A culture was grown in skim milk in an anaerobic environment without pH regulation and with a controlled temperature downshift. Fermentation kinetics, as well as central metabolism enzyme activities, were determined throughout the culture. Based on the enzymatic analysis, a type of glycolytic control was postulated, which was shared by most of the enzymes during the growth phase; in particular, the phosphofructokinase and some enzymes of the phosphoglycerate pathway during the postacidification phase were implicated. These conclusions were reinforced by whole-genome transcriptomic data. First, limited enzyme activities relative to the carbon flux were measured for most of the glycolytic enzymes; second, transcripts and enzyme activities exhibited similar changes during the culture; and third, genes involved in alternative metabolic pathways derived from some glycolytic metabolites were induced just upstream of the postulated glycolytic bottlenecks, as a consequence of accumulation of these metabolites. Other transcriptional responses to autoacidification and a decrease in temperature were induced at the end of the growth phase and were partially maintained during the stationary phase. If specific responses to acid and cold stresses were identified, this exhaustive analysis also enabled induction of unexpected pathways to be shown.