Glycolysis Regulation to Maintain Blood Glucose Homeostasis
https://doi.org/10.24017/Scince.2022.1.10
Abstract views: 1077 / PDF downloads: 679Abstract
Carbohydrates are the major source of energy for the living cells, they are the first cellular constituents that synthesized during photosynthesis from carbon dioxide and water by green plants through absorption of sun light. To be used as source of energy, carbohydrates compounds should undergo series of enzymatic metabolic stages in the cell. Beside the energy productions, catabolism of carbohydrates provides different intermediates molecules for the synthesis of biomolecules like fatty acids, amino acids, DNA, and RNA. Among the three main examples of monosaccharide (i.e: glucose, galactose, and mannose), glucose is considered as the central molecule in carbohydrate metabolism that all the major pathways of carbohydrate metabolism relate to it. Glucose is also an essential component of cellular metabolism in maintaining carbon homeostasis. Liver has shown to play a key role in monitoring and stabilizing blood glucose levels, therefore, it can be considered as glucostate monitor. In this article, we will review the major metabolic pathways of carbohydrate metabolism, their biochemical role in cellular energy production, and latest development in the understanding in these fields. Also, we discuss about the factors that participate in regulation of blood glucose concentration. We believe understand these process is essential for control scarbohydrate-related human disorders.
Keywords:
Carbohydrates, glycolysis, glucose transporters (GLUTs), insulin, glucagon
References
[1] J. S. Park et al., "Mechanical regulation of glycolysis via cytoskeleton architecture," Nature, vol. 578, no.7796, pp. 621-626, Feb 2020.
https://doi.org/10.1038/s41586-020-1998-1
[2] C. Q. Anderson, E. Wechter, and L. A. Siegmund, "Glycogen Storage Disease Type l: Don't Miss the Signs," The Journal for Nurse Practitioners, vol. 16, no. 6, pp. 442-446, 2020.
https://doi.org/10.1016/j.nurpra.2020.02.025
[3] M. Akram et al., "Hexose monophosphate shunt, the role of its metabolites and associated disorders: A review," vol. 234, no. 9, pp. 14473-14482, 2019.
https://doi.org/10.1002/jcp.28228
[4] R. Laurian et al., "Hexokinase and Glucokinases Are Essential for Fitness and Virulence in the Pathogenic Yeast Candida albicans," Front Microbiol, vol. 10, p. 327, 2019.
https://doi.org/10.3389/fmicb.2019.00327
[5] G. M. Kowalski and C. R. Bruce, "The regulation of glucose metabolism: implications and considerations for the assessment of glucose homeostasis in rodents," Am J Physiol Endocrinol Metab, vol. 307, no. 10, pp. E859-71, Nov 15 2014.
https://doi.org/10.1152/ajpendo.00165.2014
[6] J. W. Pelley, "6 - Glycolysis and Pyruvate Oxidation," in Elsevier's Integrated Review Biochemistry (Second Edition), J. W. Pelley, Ed. Philadelphia: W.B. Saunders, 2012, pp. 49-55.
https://doi.org/10.1016/B978-0-323-07446-9.00006-4
[7] M. Akram et al., "Hexose monophosphate shunt, the role of its metabolites and associated disorders: A review," J Cell Physiol, Jan 29 2019.
[8] L. Copeland and J. F. TURNER, "The regulation of glycolysis and the pentose phosphate pathway," in Biochemistry of Metabolism: Elsevier, 1987, pp. 107-128.
https://doi.org/10.1016/B978-0-12-675411-7.50010-0
[9] B. Jiang, "Aerobic glycolysis and high level of lactate in cancer metabolism and microenvironment," Genes Dis, vol. 4, no. 1, pp. 25-27, Mar 2017.
https://doi.org/10.1016/j.gendis.2017.02.003
[10] M. G. Vander Heiden, L. C. Cantley, and C. B. Thompson, "Understanding the Warburg effect: the metabolic requirements of cell proliferation," Science, vol. 324, no. 5930, pp. 1029-33, May 22 2009.
https://doi.org/10.1126/science.1160809
[11] N. S. Chandel, "Carbohydrate Metabolism," Cold Spring Harb Perspect Biol, vol. 13, no. 1, Jan 4 2021.
https://doi.org/10.1101/cshperspect.a040568
[12] H. Kozáková et al., "Brush border enzyme activities in the small intestine after long-term gliadin feeding in animal models of human coeliac disease," (in eng), Folia Microbiol (Praha), vol. 43, no. 5, pp. 497-500, 1998.
https://doi.org/10.1007/BF02820803
[13] N. G. MacFarlane, "Digestion and absorption," Anaesthesia & Intensive Care Medicine, vol. 19, no. 3, pp.125-127, 2018.
https://doi.org/10.1016/j.mpaic.2018.01.001
[14] K. M. Habegger, K. M. Heppner, N. Geary, T. J. Bartness, R. DiMarchi, and M. H. Tschöp, "The metabolic actions of glucagon revisited," (in eng), Nat Rev Endocrinol, vol. 6, no. 12, pp. 689-97, Dec 2010.
https://doi.org/10.1038/nrendo.2010.187
[15] P. G. J. T. J. o. g. p. LeFevre, "Evidence of active transfer of certain non-electrolytes across the human red cell membrane," vol. 31, no. 6, pp. 505-527, 1948.
https://doi.org/10.1085/jgp.31.6.505
[16] W. J. T. J. o. p. Widdas, "Inability of diffusion to account for placental glucose transfer in the sheep and consideration of the kinetics of a possible carrier transfer," vol. 118, no. 1, pp. 23-39, 1952.
https://doi.org/10.1113/jphysiol.1952.sp004770
[17] L. Sun et al., "Crystal structure of a bacterial homologue of glucose transporters GLUT1-4," Nature, vol. 490, no. 7420, pp. 361-6, Oct 18 2012.
https://doi.org/10.1038/nature11524
[18] J. M. Pascual et al., "GLUT1 deficiency and other glucose transporter diseases," vol. 150, no. 5, pp. 627-634, 2004.
https://doi.org/10.1530/eje.0.1500627
[19] M. J. E. j. o. b. Mueckler, "Facilitative glucose transporters," vol. 219, no. 3, pp. 713-725, 1994.
https://doi.org/10.1111/j.1432-1033.1994.tb18550.x
[20] J. J. E. Klepper, "Glucose transporter deficiency syndrome (GLUT1DS) and the ketogenic diet," vol. 49, pp.46-49, 2008.
https://doi.org/10.1111/j.1528-1167.2008.01833.x
[21] I. E. Scheffer, "GLUT1 deficiency: a glut of epilepsy phenotypes," ed: AAN Enterprises, 2012.
https://doi.org/10.1212/WNL.0b013e318248a245
[22] K. J. B. Brockmann and Development, "The expanding phenotype of GLUT1-deficiency syndrome," vol. 31, no. 7, pp. 545-552, 2009.
https://doi.org/10.1016/j.braindev.2009.02.008
[23] R. Santer, R. Schneppenheim, A. Dombrowski, H. Götze, B. Steinmann, and J. J. N. g. Schaub, "Mutations in GLUT2, the gene for the liver-type glucose transporter, in patients with Fanconi-Bickel syndrome," vol. 17, no. 3, pp. 324-326, 1997.
https://doi.org/10.1038/ng1197-324
[24] A. Leturque, E. Brot-Laroche, M. J. A. J. o. P.-E. Le Gall, and Metabolism, "GLUT2 mutations, translocation, and receptor function in diet sugar managing," vol. 296, no. 5, pp. E985-E992, 2009.
https://doi.org/10.1152/ajpendo.00004.2009
[25] I. A. Simpson et al., "The facilitative glucose transporter GLUT3: 20 years of distinction," vol. 295, no. 2, pp. E242-E253, 2008.
https://doi.org/10.1152/ajpendo.90388.2008
[26] S. E. Leney and J. M. J. T. J. o. e. Tavare, "The molecular basis of insulin-stimulated glucose uptake: signalling, trafficking and potential drug targets," vol. 203, no. 1, pp. 1-18, 2009.
https://doi.org/10.1677/JOE-09-0037
[27] K. S. Polonsky and C. F. Burant, "Chapter 31 - Type 2 Diabetes Mellitus," in Williams Textbook of Endocrinology (Thirteenth Edition), S. Melmed, K. S. Polonsky, P. R. Larsen, and H. M. Kronenberg, Eds. Philadelphia: Elsevier, 2016, pp. 1385-1450.
https://doi.org/10.1016/B978-0-323-29738-7.00031-9
[28] G. W. Löhr and H. D. Waller, "Glucose-6-phosphate Dehydrogenase: (Zwischenferment)," in Methods of Enzymatic Analysis, H.-U. Bergmeyer, Ed.: Academic Press, 1965, pp. 744-751.
https://doi.org/10.1016/B978-0-12-395630-9.50135-3
[29] T. Komoda and T. Matsunaga, "Metabolic Pathways in the Human Body," in Biochemistry for Medical Professionals, 2015, pp. 25-63.
https://doi.org/10.1016/B978-0-12-801918-4.00004-9
[30] T. Kagimoto and K. J. J. o. B. C. Uyeda, "Hormone-stimulated phosphorylation of liver phosphofructokinase in vivo," vol. 254, no. 13, pp. 5584-5587, 1979.
https://doi.org/10.1016/S0021-9258(18)50449-X
[31] I. Mor, E. C. Cheung, and K. H. Vousden, "Control of glycolysis through regulation of PFK1: old friends and recent additions," Cold Spring Harb Symp Quant Biol, vol. 76, pp. 211-6, 2011.
https://doi.org/10.1101/sqb.2011.76.010868
[32] N. Raben and J. B. J. H. m. Sherman, "Mutations in muscle phosphofructokinase gene," vol. 6, no. 1, pp. 1-6, 1995.
https://doi.org/10.1002/humu.1380060102
[33] S. Wang et al., "The Role of Glyceraldehyde-3-Phosphate Dehydrogenases in NADPH Supply in the Oleaginous Filamentous Fungus Mortierella alpina," Front Microbiol, vol. 11, p. 818, 2020.
https://doi.org/10.3389/fmicb.2020.00818
[34] P. F. Kantor, G. D. Lopaschuk, and L. H. Opie, "CHAPTER 32 - Myocardial Energy Metabolism," in Heart Physiology and Pathophysiology (Fourth Edition), N. Sperelakis, Y. Kurachi, A. Terzic, and M. V. Cohen, Eds. San Diego: Academic Press, 2001, pp. 543-569.
https://doi.org/10.1016/B978-012656975-9/50034-1
[35] L. R. Gray, S. C. Tompkins, and E. B. Taylor, "Regulation of pyruvate metabolism and human disease," Cell Mol Life Sci, vol. 71, no. 14, pp. 2577-604, Jul 2014.
https://doi.org/10.1007/s00018-013-1539-2
[36] B. Quistorff and N. J. A. Grunnet, "The isoenzyme pattern of LDH does not play a physiological role; except perhaps during fast transitions in energy metabolism," vol. 3, no. 5, p. 457, 2011.
https://doi.org/10.18632/aging.100329
[37] F. M. Matschinsky et al., "The network of glucokinase-expressing cells in glucose homeostasis and the potential of glucokinase activators for diabetes therapy," vol. 55, no. 1, pp. 1-12, 2006.
https://doi.org/10.2337/diabetes.55.01.06.db05-0926
[38] F. M. Matschinsky and D. F. Wilson, "The Central Role of Glucokinase in Glucose Homeostasis: A Perspective 50 Years After Demonstrating the Presence of the Enzyme in Islets of Langerhans," Front Physiol, vol. 10, p. 148, 2019.
https://doi.org/10.3389/fphys.2019.00148
[39] N. Al Hasawi, M. F. Alkandari, and Y. A. Luqmani, "Phosphofructokinase: a mediator of glycolytic flux in cancer progression," Crit Rev Oncol Hematol, vol. 92, no. 3, pp. 312-21, Dec 2014.
https://doi.org/10.1016/j.critrevonc.2014.05.007
[40] T. E. J. C. t. i. c. r. Mansour, "Phosphofructokinase," vol. 5, pp. 1-46, 1972.
[41] W. Yang and Z. Lu, "Regulation and function of pyruvate kinase M2 in cancer," Cancer Lett, vol. 339, no. 2, pp. 153-8, Oct 10 2013.
https://doi.org/10.1016/j.canlet.2013.06.008
[42] V. Gupta and R. N. Bamezai, "Human pyruvate kinase M2: a multifunctional protein," Protein Sci, vol. 19,no. 11, pp. 2031-44, Nov 2010.
https://doi.org/10.1002/pro.505
[43] J. F. Turner and D. H. Turner, "7 - The Regulation of Glycolysis and the Pentose Phosphate Pathway," in Metabolism and Respiration, D. D. Davies, Ed.: Academic Press, 1980, pp. 279-316.
https://doi.org/10.1016/B978-0-12-675402-5.50013-1
[44] L. J. P. o. t. N. S. Agius, "Dietary carbohydrate and control of hepatic gene expression: mechanistic links from ATP and phosphate ester homeostasis to the carbohydrate-response element-binding protein," vol. 75, no. 1, pp. 10-18, 2016.
https://doi.org/10.1017/S0029665115002451
[45] L. B. Bockus et al., "Cardiac Insulin Signaling Regulates Glycolysis Through Phosphofructokinase 2 Content and Activity," J Am Heart Assoc, vol. 6, no. 12, Dec 4 2017.
https://doi.org/10.1161/JAHA.117.007159
[46] P. V. Roder, B. Wu, Y. Liu, and W. Han, "Pancreatic regulation of glucose homeostasis," Exp Mol Med, vol. 48, p. e219, Mar 11 2016.
https://doi.org/10.1038/emm.2016.6
[47] M. H. Lundqvist, K. Almby, N. Abrahamsson, and J. W. Eriksson, "Is the Brain a Key Player in Glucose Regulation and Development of Type 2 Diabetes?," Front Physiol, vol. 10, p. 457, 2019.
https://doi.org/10.3389/fphys.2019.00457
[48] S. Kalra et al., "Hypoglycemia: The neglected complication," (in eng), Indian journal of endocrinology and metabolism, vol. 17, no. 5, pp. 819-834, 2013.
https://doi.org/10.4103/2230-8210.117219
[49] A. C. Hauge-Evans et al., "Somatostatin secreted by islet ?-cells fulfills multiple roles as a paracrine regulator of islet function," vol. 58, no. 2, pp. 403-411, 2009.
https://doi.org/10.2337/db08-0792
[50] N. Wierup, H. Svensson, H. Mulder, and F. J. R. p. Sundler, "The ghrelin cell: a novel developmentally regulated islet cell in the human pancreas," vol. 107, no. 1-3, pp. 63-69, 2002.
https://doi.org/10.1016/S0167-0115(02)00067-8
[51] C. Bouche, S. Serdy, C. R. Kahn, and A. B. Goldfine, "The cellular fate of glucose and its relevance in type 2 diabetes," Endocr Rev, vol. 25, no. 5, pp. 807-30, Oct 2004.
https://doi.org/10.1210/er.2003-0026
[52] Y. Kong et al., "Types of carbohydrate in feed affect the growth performance, antioxidant capacity, immunity, and activity of digestive and carbohydrate metabolism enzymes in juvenile Macrobrachium nipponense," Aquaculture, vol. 512, 2019.
https://doi.org/10.1016/j.aquaculture.2019.734282
[53] S. Brooks et al., "Report of the ad hoc Glycemic (Net) Carbohydrate Definition Committee to AACC International Board of Directors," ed, 2006.
[54] C. Hurtado and C. Waasdorp, "Carbohydrate Digestion and Absorption NASPGHAN Physiology Series," ed, 2018.
[55] S. C. Moore et al., "Leisure time physical activity of moderate to vigorous intensity and mortality: a large pooled cohort analysis," PLoS Med, vol. 9, no. 11, p. e1001335, 2012.
https://doi.org/10.1371/journal.pmed.1001335
[56] P. Zimmet, K. Alberti, and J. J. N. Shaw, "Global and societal implications of the diabetes epidemic," vol. 414, no. 6865, pp. 782-787, 2001.
https://doi.org/10.1038/414782a
[57] M. A. Atkinson and N. K. J. N. E. j. o. m. Maclaren, "The pathogenesis of insulin-dependent diabetes mellitus," vol. 331, no. 21, pp. 1428-1436, 1994.
https://doi.org/10.1056/NEJM199411243312107
[58] A. R. J. C. Saltiel, "New perspectives into the molecular pathogenesis and treatment of type 2 diabetes," vol. 104, no. 4, pp. 517-529, 2001.
https://doi.org/10.1016/S0092-8674(01)00239-2
[59] G. Wilcox, "Insulin and insulin resistance," (in eng), The Clinical biochemist. Reviews, vol. 26, no. 2, pp. 19- 39, 2005.
[60] M. Mishra and J. J. C. P. D. Fomusi Ndisang, "A critical and comprehensive insight on heme oxygenase and related products including carbon monoxide, bilirubin, biliverdin and ferritin in type-1 and type-2 diabetes," vol. 20, no. 9, pp. 1370-1391, 2014.
https://doi.org/10.2174/13816128113199990559
[61] M. C. Petersen, D. F. Vatner, and G. I. J. N. r. e. Shulman, "Regulation of hepatic glucose metabolism in health and disease," vol. 13, no. 10, pp. 572-587, 2017.
https://doi.org/10.1038/nrendo.2017.80
[62] J. F. Ndisang and M. J. A. j. o. h. Mishra, "The heme oxygenase system selectively suppresses the proinflammatory macrophage m1 phenotype and potentiates insulin signaling in spontaneously hypertensive rats," vol. 26, no. 9, pp. 1123-1131, 2013.
https://doi.org/10.1093/ajh/hpt082
[63] L. Duvnjak and M. J. J. P. P. Duvnjak, "The metabolic syndrome-an ongoing story," vol. 60, no. Suppl 7, pp. 19-24, 2009.
[64] B. K. Pedersen, "Anti-inflammatory effects of exercise: role in diabetes and cardiovascular disease," Eur J Clin Invest, vol. 47, no. 8, pp. 600-611, Aug 2017.
https://doi.org/10.1111/eci.12781
[65] J. E. Gerich, M. Langlois, C. Noacco, J. H. Karam, and P. H. J. S. Forsham, "Lack of glucagon response to hypoglycemia in diabetes: evidence for an intrinsic pancreatic alpha cell defect," vol. 182, no. 4108, pp. 171- 173, 1973.
https://doi.org/10.1126/science.182.4108.171
[66] A. Cherrington, J. Chiasson, J. Liljenquist, W. Lacy, and C. Park, "Control of hepatic glucose output by glucagon and insulin in the intact dog," in Biochemical Society symposium, 1978, no. 43, pp. 31-45.
[67] P. S. Kishnani et al., "Diagnosis and management of glycogen storage disease type I: a practice guideline of the American College of Medical Genetics and Genomics," Genet Med, vol. 16, no. 11, p. e1, Nov 2014.
https://doi.org/10.1038/gim.2014.128
[68] G. Jiang, B. B. J. A. J. o. P.-E. Zhang, and Metabolism, "Glucagon and regulation of glucose metabolism," vol. 284, no. 4, pp. E671-E678, 2003.
https://doi.org/10.1152/ajpendo.00492.2002
[69] N. Kedia, "Treatment of severe diabetic hypoglycemia with glucagon: an underutilized therapeutic approach," Diabetes Metab Syndr Obes, vol. 4, pp. 337-46, 2011.
https://doi.org/10.2147/DMSO.S20633
[70] N. J. M. B. Bhagavan, "Carbohydrate Metabolism II: Gluconeogenesis, Glycogen Synthesis and Breakdown, and Alernative Pathways," vol. 4, 2001.
https://doi.org/10.1016/B978-012095440-7/50017-2
[71] B. Y. Pan et al., "Role of phosphoglucomutase in regulating trehalose metabolism in Nilaparvata lugens," 3 Biotech, vol. 10, no. 2, p. 61, Feb 2020.
https://doi.org/10.1007/s13205-020-2053-5
[72] M. J. Pereira et al., "Direct effects of glucagon on glucose uptake and lipolysis in human adipocytes," Mol Cell Endocrinol, vol. 503, p. 110696, Mar 1 2020.
https://doi.org/10.1016/j.mce.2019.110696
https://doi.org/10.1038/s41586-020-1998-1
[2] C. Q. Anderson, E. Wechter, and L. A. Siegmund, "Glycogen Storage Disease Type l: Don't Miss the Signs," The Journal for Nurse Practitioners, vol. 16, no. 6, pp. 442-446, 2020.
https://doi.org/10.1016/j.nurpra.2020.02.025
[3] M. Akram et al., "Hexose monophosphate shunt, the role of its metabolites and associated disorders: A review," vol. 234, no. 9, pp. 14473-14482, 2019.
https://doi.org/10.1002/jcp.28228
[4] R. Laurian et al., "Hexokinase and Glucokinases Are Essential for Fitness and Virulence in the Pathogenic Yeast Candida albicans," Front Microbiol, vol. 10, p. 327, 2019.
https://doi.org/10.3389/fmicb.2019.00327
[5] G. M. Kowalski and C. R. Bruce, "The regulation of glucose metabolism: implications and considerations for the assessment of glucose homeostasis in rodents," Am J Physiol Endocrinol Metab, vol. 307, no. 10, pp. E859-71, Nov 15 2014.
https://doi.org/10.1152/ajpendo.00165.2014
[6] J. W. Pelley, "6 - Glycolysis and Pyruvate Oxidation," in Elsevier's Integrated Review Biochemistry (Second Edition), J. W. Pelley, Ed. Philadelphia: W.B. Saunders, 2012, pp. 49-55.
https://doi.org/10.1016/B978-0-323-07446-9.00006-4
[7] M. Akram et al., "Hexose monophosphate shunt, the role of its metabolites and associated disorders: A review," J Cell Physiol, Jan 29 2019.
[8] L. Copeland and J. F. TURNER, "The regulation of glycolysis and the pentose phosphate pathway," in Biochemistry of Metabolism: Elsevier, 1987, pp. 107-128.
https://doi.org/10.1016/B978-0-12-675411-7.50010-0
[9] B. Jiang, "Aerobic glycolysis and high level of lactate in cancer metabolism and microenvironment," Genes Dis, vol. 4, no. 1, pp. 25-27, Mar 2017.
https://doi.org/10.1016/j.gendis.2017.02.003
[10] M. G. Vander Heiden, L. C. Cantley, and C. B. Thompson, "Understanding the Warburg effect: the metabolic requirements of cell proliferation," Science, vol. 324, no. 5930, pp. 1029-33, May 22 2009.
https://doi.org/10.1126/science.1160809
[11] N. S. Chandel, "Carbohydrate Metabolism," Cold Spring Harb Perspect Biol, vol. 13, no. 1, Jan 4 2021.
https://doi.org/10.1101/cshperspect.a040568
[12] H. Kozáková et al., "Brush border enzyme activities in the small intestine after long-term gliadin feeding in animal models of human coeliac disease," (in eng), Folia Microbiol (Praha), vol. 43, no. 5, pp. 497-500, 1998.
https://doi.org/10.1007/BF02820803
[13] N. G. MacFarlane, "Digestion and absorption," Anaesthesia & Intensive Care Medicine, vol. 19, no. 3, pp.125-127, 2018.
https://doi.org/10.1016/j.mpaic.2018.01.001
[14] K. M. Habegger, K. M. Heppner, N. Geary, T. J. Bartness, R. DiMarchi, and M. H. Tschöp, "The metabolic actions of glucagon revisited," (in eng), Nat Rev Endocrinol, vol. 6, no. 12, pp. 689-97, Dec 2010.
https://doi.org/10.1038/nrendo.2010.187
[15] P. G. J. T. J. o. g. p. LeFevre, "Evidence of active transfer of certain non-electrolytes across the human red cell membrane," vol. 31, no. 6, pp. 505-527, 1948.
https://doi.org/10.1085/jgp.31.6.505
[16] W. J. T. J. o. p. Widdas, "Inability of diffusion to account for placental glucose transfer in the sheep and consideration of the kinetics of a possible carrier transfer," vol. 118, no. 1, pp. 23-39, 1952.
https://doi.org/10.1113/jphysiol.1952.sp004770
[17] L. Sun et al., "Crystal structure of a bacterial homologue of glucose transporters GLUT1-4," Nature, vol. 490, no. 7420, pp. 361-6, Oct 18 2012.
https://doi.org/10.1038/nature11524
[18] J. M. Pascual et al., "GLUT1 deficiency and other glucose transporter diseases," vol. 150, no. 5, pp. 627-634, 2004.
https://doi.org/10.1530/eje.0.1500627
[19] M. J. E. j. o. b. Mueckler, "Facilitative glucose transporters," vol. 219, no. 3, pp. 713-725, 1994.
https://doi.org/10.1111/j.1432-1033.1994.tb18550.x
[20] J. J. E. Klepper, "Glucose transporter deficiency syndrome (GLUT1DS) and the ketogenic diet," vol. 49, pp.46-49, 2008.
https://doi.org/10.1111/j.1528-1167.2008.01833.x
[21] I. E. Scheffer, "GLUT1 deficiency: a glut of epilepsy phenotypes," ed: AAN Enterprises, 2012.
https://doi.org/10.1212/WNL.0b013e318248a245
[22] K. J. B. Brockmann and Development, "The expanding phenotype of GLUT1-deficiency syndrome," vol. 31, no. 7, pp. 545-552, 2009.
https://doi.org/10.1016/j.braindev.2009.02.008
[23] R. Santer, R. Schneppenheim, A. Dombrowski, H. Götze, B. Steinmann, and J. J. N. g. Schaub, "Mutations in GLUT2, the gene for the liver-type glucose transporter, in patients with Fanconi-Bickel syndrome," vol. 17, no. 3, pp. 324-326, 1997.
https://doi.org/10.1038/ng1197-324
[24] A. Leturque, E. Brot-Laroche, M. J. A. J. o. P.-E. Le Gall, and Metabolism, "GLUT2 mutations, translocation, and receptor function in diet sugar managing," vol. 296, no. 5, pp. E985-E992, 2009.
https://doi.org/10.1152/ajpendo.00004.2009
[25] I. A. Simpson et al., "The facilitative glucose transporter GLUT3: 20 years of distinction," vol. 295, no. 2, pp. E242-E253, 2008.
https://doi.org/10.1152/ajpendo.90388.2008
[26] S. E. Leney and J. M. J. T. J. o. e. Tavare, "The molecular basis of insulin-stimulated glucose uptake: signalling, trafficking and potential drug targets," vol. 203, no. 1, pp. 1-18, 2009.
https://doi.org/10.1677/JOE-09-0037
[27] K. S. Polonsky and C. F. Burant, "Chapter 31 - Type 2 Diabetes Mellitus," in Williams Textbook of Endocrinology (Thirteenth Edition), S. Melmed, K. S. Polonsky, P. R. Larsen, and H. M. Kronenberg, Eds. Philadelphia: Elsevier, 2016, pp. 1385-1450.
https://doi.org/10.1016/B978-0-323-29738-7.00031-9
[28] G. W. Löhr and H. D. Waller, "Glucose-6-phosphate Dehydrogenase: (Zwischenferment)," in Methods of Enzymatic Analysis, H.-U. Bergmeyer, Ed.: Academic Press, 1965, pp. 744-751.
https://doi.org/10.1016/B978-0-12-395630-9.50135-3
[29] T. Komoda and T. Matsunaga, "Metabolic Pathways in the Human Body," in Biochemistry for Medical Professionals, 2015, pp. 25-63.
https://doi.org/10.1016/B978-0-12-801918-4.00004-9
[30] T. Kagimoto and K. J. J. o. B. C. Uyeda, "Hormone-stimulated phosphorylation of liver phosphofructokinase in vivo," vol. 254, no. 13, pp. 5584-5587, 1979.
https://doi.org/10.1016/S0021-9258(18)50449-X
[31] I. Mor, E. C. Cheung, and K. H. Vousden, "Control of glycolysis through regulation of PFK1: old friends and recent additions," Cold Spring Harb Symp Quant Biol, vol. 76, pp. 211-6, 2011.
https://doi.org/10.1101/sqb.2011.76.010868
[32] N. Raben and J. B. J. H. m. Sherman, "Mutations in muscle phosphofructokinase gene," vol. 6, no. 1, pp. 1-6, 1995.
https://doi.org/10.1002/humu.1380060102
[33] S. Wang et al., "The Role of Glyceraldehyde-3-Phosphate Dehydrogenases in NADPH Supply in the Oleaginous Filamentous Fungus Mortierella alpina," Front Microbiol, vol. 11, p. 818, 2020.
https://doi.org/10.3389/fmicb.2020.00818
[34] P. F. Kantor, G. D. Lopaschuk, and L. H. Opie, "CHAPTER 32 - Myocardial Energy Metabolism," in Heart Physiology and Pathophysiology (Fourth Edition), N. Sperelakis, Y. Kurachi, A. Terzic, and M. V. Cohen, Eds. San Diego: Academic Press, 2001, pp. 543-569.
https://doi.org/10.1016/B978-012656975-9/50034-1
[35] L. R. Gray, S. C. Tompkins, and E. B. Taylor, "Regulation of pyruvate metabolism and human disease," Cell Mol Life Sci, vol. 71, no. 14, pp. 2577-604, Jul 2014.
https://doi.org/10.1007/s00018-013-1539-2
[36] B. Quistorff and N. J. A. Grunnet, "The isoenzyme pattern of LDH does not play a physiological role; except perhaps during fast transitions in energy metabolism," vol. 3, no. 5, p. 457, 2011.
https://doi.org/10.18632/aging.100329
[37] F. M. Matschinsky et al., "The network of glucokinase-expressing cells in glucose homeostasis and the potential of glucokinase activators for diabetes therapy," vol. 55, no. 1, pp. 1-12, 2006.
https://doi.org/10.2337/diabetes.55.01.06.db05-0926
[38] F. M. Matschinsky and D. F. Wilson, "The Central Role of Glucokinase in Glucose Homeostasis: A Perspective 50 Years After Demonstrating the Presence of the Enzyme in Islets of Langerhans," Front Physiol, vol. 10, p. 148, 2019.
https://doi.org/10.3389/fphys.2019.00148
[39] N. Al Hasawi, M. F. Alkandari, and Y. A. Luqmani, "Phosphofructokinase: a mediator of glycolytic flux in cancer progression," Crit Rev Oncol Hematol, vol. 92, no. 3, pp. 312-21, Dec 2014.
https://doi.org/10.1016/j.critrevonc.2014.05.007
[40] T. E. J. C. t. i. c. r. Mansour, "Phosphofructokinase," vol. 5, pp. 1-46, 1972.
[41] W. Yang and Z. Lu, "Regulation and function of pyruvate kinase M2 in cancer," Cancer Lett, vol. 339, no. 2, pp. 153-8, Oct 10 2013.
https://doi.org/10.1016/j.canlet.2013.06.008
[42] V. Gupta and R. N. Bamezai, "Human pyruvate kinase M2: a multifunctional protein," Protein Sci, vol. 19,no. 11, pp. 2031-44, Nov 2010.
https://doi.org/10.1002/pro.505
[43] J. F. Turner and D. H. Turner, "7 - The Regulation of Glycolysis and the Pentose Phosphate Pathway," in Metabolism and Respiration, D. D. Davies, Ed.: Academic Press, 1980, pp. 279-316.
https://doi.org/10.1016/B978-0-12-675402-5.50013-1
[44] L. J. P. o. t. N. S. Agius, "Dietary carbohydrate and control of hepatic gene expression: mechanistic links from ATP and phosphate ester homeostasis to the carbohydrate-response element-binding protein," vol. 75, no. 1, pp. 10-18, 2016.
https://doi.org/10.1017/S0029665115002451
[45] L. B. Bockus et al., "Cardiac Insulin Signaling Regulates Glycolysis Through Phosphofructokinase 2 Content and Activity," J Am Heart Assoc, vol. 6, no. 12, Dec 4 2017.
https://doi.org/10.1161/JAHA.117.007159
[46] P. V. Roder, B. Wu, Y. Liu, and W. Han, "Pancreatic regulation of glucose homeostasis," Exp Mol Med, vol. 48, p. e219, Mar 11 2016.
https://doi.org/10.1038/emm.2016.6
[47] M. H. Lundqvist, K. Almby, N. Abrahamsson, and J. W. Eriksson, "Is the Brain a Key Player in Glucose Regulation and Development of Type 2 Diabetes?," Front Physiol, vol. 10, p. 457, 2019.
https://doi.org/10.3389/fphys.2019.00457
[48] S. Kalra et al., "Hypoglycemia: The neglected complication," (in eng), Indian journal of endocrinology and metabolism, vol. 17, no. 5, pp. 819-834, 2013.
https://doi.org/10.4103/2230-8210.117219
[49] A. C. Hauge-Evans et al., "Somatostatin secreted by islet ?-cells fulfills multiple roles as a paracrine regulator of islet function," vol. 58, no. 2, pp. 403-411, 2009.
https://doi.org/10.2337/db08-0792
[50] N. Wierup, H. Svensson, H. Mulder, and F. J. R. p. Sundler, "The ghrelin cell: a novel developmentally regulated islet cell in the human pancreas," vol. 107, no. 1-3, pp. 63-69, 2002.
https://doi.org/10.1016/S0167-0115(02)00067-8
[51] C. Bouche, S. Serdy, C. R. Kahn, and A. B. Goldfine, "The cellular fate of glucose and its relevance in type 2 diabetes," Endocr Rev, vol. 25, no. 5, pp. 807-30, Oct 2004.
https://doi.org/10.1210/er.2003-0026
[52] Y. Kong et al., "Types of carbohydrate in feed affect the growth performance, antioxidant capacity, immunity, and activity of digestive and carbohydrate metabolism enzymes in juvenile Macrobrachium nipponense," Aquaculture, vol. 512, 2019.
https://doi.org/10.1016/j.aquaculture.2019.734282
[53] S. Brooks et al., "Report of the ad hoc Glycemic (Net) Carbohydrate Definition Committee to AACC International Board of Directors," ed, 2006.
[54] C. Hurtado and C. Waasdorp, "Carbohydrate Digestion and Absorption NASPGHAN Physiology Series," ed, 2018.
[55] S. C. Moore et al., "Leisure time physical activity of moderate to vigorous intensity and mortality: a large pooled cohort analysis," PLoS Med, vol. 9, no. 11, p. e1001335, 2012.
https://doi.org/10.1371/journal.pmed.1001335
[56] P. Zimmet, K. Alberti, and J. J. N. Shaw, "Global and societal implications of the diabetes epidemic," vol. 414, no. 6865, pp. 782-787, 2001.
https://doi.org/10.1038/414782a
[57] M. A. Atkinson and N. K. J. N. E. j. o. m. Maclaren, "The pathogenesis of insulin-dependent diabetes mellitus," vol. 331, no. 21, pp. 1428-1436, 1994.
https://doi.org/10.1056/NEJM199411243312107
[58] A. R. J. C. Saltiel, "New perspectives into the molecular pathogenesis and treatment of type 2 diabetes," vol. 104, no. 4, pp. 517-529, 2001.
https://doi.org/10.1016/S0092-8674(01)00239-2
[59] G. Wilcox, "Insulin and insulin resistance," (in eng), The Clinical biochemist. Reviews, vol. 26, no. 2, pp. 19- 39, 2005.
[60] M. Mishra and J. J. C. P. D. Fomusi Ndisang, "A critical and comprehensive insight on heme oxygenase and related products including carbon monoxide, bilirubin, biliverdin and ferritin in type-1 and type-2 diabetes," vol. 20, no. 9, pp. 1370-1391, 2014.
https://doi.org/10.2174/13816128113199990559
[61] M. C. Petersen, D. F. Vatner, and G. I. J. N. r. e. Shulman, "Regulation of hepatic glucose metabolism in health and disease," vol. 13, no. 10, pp. 572-587, 2017.
https://doi.org/10.1038/nrendo.2017.80
[62] J. F. Ndisang and M. J. A. j. o. h. Mishra, "The heme oxygenase system selectively suppresses the proinflammatory macrophage m1 phenotype and potentiates insulin signaling in spontaneously hypertensive rats," vol. 26, no. 9, pp. 1123-1131, 2013.
https://doi.org/10.1093/ajh/hpt082
[63] L. Duvnjak and M. J. J. P. P. Duvnjak, "The metabolic syndrome-an ongoing story," vol. 60, no. Suppl 7, pp. 19-24, 2009.
[64] B. K. Pedersen, "Anti-inflammatory effects of exercise: role in diabetes and cardiovascular disease," Eur J Clin Invest, vol. 47, no. 8, pp. 600-611, Aug 2017.
https://doi.org/10.1111/eci.12781
[65] J. E. Gerich, M. Langlois, C. Noacco, J. H. Karam, and P. H. J. S. Forsham, "Lack of glucagon response to hypoglycemia in diabetes: evidence for an intrinsic pancreatic alpha cell defect," vol. 182, no. 4108, pp. 171- 173, 1973.
https://doi.org/10.1126/science.182.4108.171
[66] A. Cherrington, J. Chiasson, J. Liljenquist, W. Lacy, and C. Park, "Control of hepatic glucose output by glucagon and insulin in the intact dog," in Biochemical Society symposium, 1978, no. 43, pp. 31-45.
[67] P. S. Kishnani et al., "Diagnosis and management of glycogen storage disease type I: a practice guideline of the American College of Medical Genetics and Genomics," Genet Med, vol. 16, no. 11, p. e1, Nov 2014.
https://doi.org/10.1038/gim.2014.128
[68] G. Jiang, B. B. J. A. J. o. P.-E. Zhang, and Metabolism, "Glucagon and regulation of glucose metabolism," vol. 284, no. 4, pp. E671-E678, 2003.
https://doi.org/10.1152/ajpendo.00492.2002
[69] N. Kedia, "Treatment of severe diabetic hypoglycemia with glucagon: an underutilized therapeutic approach," Diabetes Metab Syndr Obes, vol. 4, pp. 337-46, 2011.
https://doi.org/10.2147/DMSO.S20633
[70] N. J. M. B. Bhagavan, "Carbohydrate Metabolism II: Gluconeogenesis, Glycogen Synthesis and Breakdown, and Alernative Pathways," vol. 4, 2001.
https://doi.org/10.1016/B978-012095440-7/50017-2
[71] B. Y. Pan et al., "Role of phosphoglucomutase in regulating trehalose metabolism in Nilaparvata lugens," 3 Biotech, vol. 10, no. 2, p. 61, Feb 2020.
https://doi.org/10.1007/s13205-020-2053-5
[72] M. J. Pereira et al., "Direct effects of glucagon on glucose uptake and lipolysis in human adipocytes," Mol Cell Endocrinol, vol. 503, p. 110696, Mar 1 2020.
https://doi.org/10.1016/j.mce.2019.110696
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How to Cite
[1]
K. J. Salih, D. K. Sabir, and H. J. Abdoul, “Glycolysis Regulation to Maintain Blood Glucose Homeostasis”, KJAR, pp. 114–124, Jul. 2022, doi: 10.24017/Scince.2022.1.10.
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14-07-2022
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Pure and Applied Science
