Impact of Diabetes Mellitus Type 2 in the Activity of Glucose-6-Phosphate Dehydrogenase in Human Erythrocyte

Abstract = 1494 times | PDF = 117 times

Main Article Content

Salih Awla Hamzah Luqman Awla Hamza Heshu Sulaman Rahman


Diabetes mellitus is a metabolic affliction saunter that is characterized by a nobler than normal blood glucose poise. Glucose-6-phosphate dehydrogenase (G6PD) enzyme code (E.C. is an underlying enzyme in the phosphogluconate pathway. In this study, G6PD vitality in the mortal erythrocyte of male and female patients with type 2 diabetes mellitus was assessed utilizing a spectrophotometer at 340 nm. The activity of the enzyme increased with elevated glycated hemoglobin (HbA1C) levels. G6PD activity was found to be significantly associated with type 2 diabetes mellitus. The association between G6PD and diabetes mellitus was significant (P < 0.001). Moreover, G6PD was positively correlated with HbA1C levels (r = 0.572). The following mean ± standard deviation values were obtained: G6PD activity (IU/g Hb), 3.1103 ± 0.79349; HbA1C (%), 8.6600 ± 1.63120; Hb (g/dL), 13.4933 ± 1.38836; platelet count (103/µl), 283.4667 ± 58.59312; WBC (103/µl), 7.4890 ± 1.49842; HCT (%), 45.0100 ± 2.63430; and BS (mg/dL), 230.2667 ± 75.67760. The results showed that an elevated HbA1C up leads to increased G6PD performance in the human erythrocyte, which is concerning to glucose levels in the special (blood).


G6PD, diabetes mellitus, human erythrocyte


Download data is not yet available.

Article Details


[1] L. Luzzatto and U. Testa, “Human erythrocyte glucose 6-phosphate dehydrogenase: Structure and function in normal and mutant subjects,” Curr. Top. Hematol., vol. 1, pp. 1-70, 1978.
[2] W. Ying, “NAD+/NADH and NADP+/NADPH in cellular functions and cell death: Regulation and biological consequences,” Antioxid. Redox Signal., pp.10, vol. 10, no. 2, pp. 179-206, 2008.
[3] R. C. Stanton, “Glucose-6-phosphate dehydrogenase, NADPH, and cell survival,” IUBMB Life, vol. 64, no. 5, pp. 362-369, 2012.
[4] L. D. DeLeve and N. Kaplowitz, “Glutathione metabolism and its role in hepatotoxicity Pharmacol”, Ther., vol. 52, no. 3, pp. 287-305, 1991.
[5] B. N. Ames, M.K. Shigenage MK, T.M. Hagen, "Oxidants, antioxidants, and the degenerative diseases of aging" Proc. Natl. Acad. Sci. U. S. A., vol. 90, no. 17, pp. 7915-7922, 1993.
[6] W. Ying, “NAD /NADPH in cellular Functions and Cell Death, ‘Regulation and biological Consequences’.”, Antioxidants & Redox Signaling, vol. 10, no. 2, pp. 179-206, 2008.
[7] M. A. Ibrahim, A.H.M. Ghazy, A.H.M. Salem, “Biochemical characterization of buffalo liver glucose-6-phosphate dehydrogenase isoforms,” Protein J., vol. 34, no. 3, pp. 193-204, 2015.
[8] S. Adem, V. Comakli, M. Kuzu, R. Demirdag,“Investigation of the effects of some phenolic compounds on the activities of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase from human erythrocytes,” J. Biochem. Mol. Toxicol., vol. 28, no. 11, pp. 510-514, 2014.
[9] I. Carlberg and B. Mannervik, “Purification and characterization of the flavoenzyme glutathione reductase from rat liver,” J. Biol. Chem., vol. 250, no. 14, pp. 5475-5480, 1975.
[10] M. Senturk, O.I. Kufrevioglu, M. Ciftci,“Effects of some antibiotics on human erythrocyte glutathione reductase: An in vitro study,” J. Enzyme Inhib. Med. Chem., vol. 23, no. 1, pp. 144-148, 2008.
[11] B. Tekman, H. Ozdemir, M. Senturk, M. Ciftci,“Purification and characterization of glutathione reductase from rainbow trout (Oncorhynchus mykiss) liver and inhibition effects of metal ions on enzyme activity,” Comp. Biochem. Physiol. C Toxicol. Pharmacol., vol. 148, no. 2, pp. 117-121, 2008.
[12] R. N. Martins, G.B. Stokes, C.L. Masters “ Regulation of liver and brain hexose monophosphate dehydrogenase by insulin and dietary intake in the female rat,” Mol. Cell. Biochem., vol. 70, no. 2, pp. 169-175, 1986.
[13] C. Karasu, “Glycoxidative stress and cardiovascular complications in experimentally induced diabetes: Effects of antioxidant treatment,” Open Cardiovasc. Med. J., vol. 4, pp. 240-256, 2010.
[14] M. Stefek and C. Karasu, “Eye lens in aging and diabetes: Effect of quercetin,” Rejuvenation Res., vol. 14, no. 5, pp. 525-534, 2011.
[15] A. Sakul, A. Cumaoğlu, E. Aydin, N. Ari, N. Dilsiz, C. Karasu, “Age- and diabetes-induced regulation of oxidative protein modification in rat brain and peripheral tissues: Consequences of treatment with antioxidant pyridoindole,” Exp. Gerontol., vol. 48, no. 5, pp. 476-484, 2013.
[16] A. L. Lehninger, DL. Nelson, MM. Cox, “Principles of Biochemistry”, Second Editions. New York: Worth, pp. 558-560, 2000.
[17] E. Keha, ve Ö. Î. Küfrevioğlu, “Yayınevi.” in Sigara ve Gebelik. Şişli Etfal Hastanesi Tıp Bülteni. 38, pp. 7-14, 2004.
[18] J. M. Berg, JL. Tymoczko, L. Stryer,“Biochemistry.5th eEdition, New York: W.H H. Freeman”, 2002.
[19] R. W. Grunewald, II. Weber, E. Kinne-Saffran,“Control of sorbitol metabolism in renal inner medulla of diabetic rats,” Biochim. Biophys. Acta, vol. 1225, no. 1, pp. 39-47, 1993.
[20] P. F. Hollenberg, “Mechanisms of cytochrome P-450 and peroxidase catalyzed xenobiothic metabolism,” The FASEB Journal, vol. 6, no. 2, pp. 686-694, 1992.
[21] N. Borregaard, JH. Schwartz, A. Tauber,“Proton secretion by stimulated neutrophils. Significance of hexose monophosphate shunt activity as source of electrons and protons for the respiratory burst,” J. Clin. Invest., vol. 74, no. 2, p. 455-459, 1984.
[22] M. I. Kazeem, M.A. Akanji, M. Hafizur Rahman,“Antiglycation, antioxidant and toxicological potential of polyphenol extracts of alligator pepper, ginger and nutmeg from Nigeria,” Asian Pac. J. Trop. Biomed., vol. 2, no. 9, pp. 727-732, 2012.
[23] D. E. Kelly and L. J. Mandarino, “Fuel selection in human skeletal muscle in insulin resistance,” Diabetes, vol. 40, pp. 677-681, 2004.
[24] I. Ripoll and B. C. Leutholtz, Ignacio. Exercise and Disease Management, Boca, 2nd ed. Raton: CRC Press, 2011 4398-2759, p. 25. ISBN. 978.
[25] M. Dobson, “Nature of the urine in diabetes, Medical Observations and Inquiries,”, vol. 5, pp. 298-310, 1776.
[26] M. Patlak, “New weapons to combat an ancient disease, treating diabetes,” FASEB J.. December 14, vol. 16, no. 14, 1853, 2002.
[27] P. Leonid, Principles of Diabetes Mellitus, 2nd ed. New York: Springer ISBN 978-0-387-09840-1, 2009, p. 3. (2009).
[28] R. S. Yalow and S. A. Berson, “Immunoassay of endogenous plasma insulin in man,” J. Clin. Invest., vol. 39, no. 7, pp. 1157-1175, 1960.
[29] A. Pollack, Lizard-Derived Diabetes Drug Is Approved by the F.D.A, The New York Times, 2005 ISSN 0362-4331.
[30] D. J. Liska, “The detoxification enzyme systems,” Altern. Med. Rev., vol. 3, no. 3, pp. 187-198, 1998.
[31] B. Koncuk Cebecİ et al., “In vitro effects of pesticide exposure on the activity of the Paraoxonase-1 enzyme from sheep liver mic rosomes,” Turk. J. Chem., vol. 38, pp. 512-520, 2014.
[32] S. Serpillon, B.C. Floyd, R.S. Gupte, S. George, M. Kozicky, V. Neito, F. Recchia, W. Stanley, M.S. Wolin, A.S. Gupte “Superoxideproduction by NAD(P)H oxidase and mitochondria is increased in genetically obese and hyperglycemias rat heart and aorta before the development of cardiac dysfunction. The role of glucose-6-phosphate dehydrogenase-derived NADPH,” Am. J. Physiol. Heart Circ. Physiol., vol. 70, no. 1:169–175, pp. H153-HH162Biochem, 2009.
[33] B. Halliwell and J. M. C. Gutteridge, Free Radical in Biology and Medicine, 4th ed. Oxford: Clarendon Press, 2007.
[34] R. Matsui, S. Xu, KA. Maitland, A. Hayes, JA. Leopold, DE. Handy, J. Loscalzo, RA. Cohen, R. Matsui “Glucose-6 phosphate dehydrogenase deficiency decreases the vascular response to angiotensin II,”. Circulation, vol. 112, no. 2:, pp. 257–-263, 2005.
[35] E. Beutler, “Red Cell Metabolizm Manual of Biochemical Methods”, vol. 12. London: Academic Press, pp. 68-70, 1971.
[36] K. Pagana and T. J. Pagana, Eds., Mosby’s Manual of Diagnostic and Laboratory Tests, 5th ed. St. Louis, Missouri, 2014.
[37] H. Y. Ho et al., “Glucose-6-phosphate dehydrogenase from oxidative stress to cellular functions and degenerative diseases,” Redox Rep., vol. 12, no. 3, pp. 109-118, 2007.
[38] M. D. Scott et al., “NADPH, not glutathione, status modulates oxidant sensitivity in normal and glucose-6-phosphate dehydrogenase deficient erythrocytes,” Blood, vol. 77, no. 9, pp. 2059-2064, 1991.
[39] E. Wright Jr, J. L. Scism-Bacon, and L. C. Glass, “Oxidative stress in type 2 diabetes: The role of fasting and postprandial glycaemia,” Int. J. Clin. Pract., vol. 60, no. 3, pp. 308-314, 2006.
[40] Jung Hee Kim, Dae Jung Kim, Hak Chul Jang, and Sung Hee Choicorresponding author “Epidemiology of Micro- and Macrovascular Complications of Type 2 Diabetes in Korea” Diabetes Metab J. 2011 Dec; 35(6): 571–577.
[41] B. Halliwell, “Role of free radicals in the neurodegenerative diseases: Therapeutiimplications for antioxidant treatment,” Drugs Aging, vol. 18, no. 9, pp. 685-716, 2001.
[42] F. Giacco, M. Brownlee, and A. M. Schmidt, “Oxidative stress and diabetic complications,” Circulation Research, vol. 107, no. 9, pp. 1058–1070, 2010.
[43] M. Gök et al., “Flaxseed protects against diabetes-induced Glucotoxicity by modulating pentose phosphate pathway and glutathione-dependent enzyme activities in rats,” J. Diet Suppl., vol. 13, no. 3, pp. 339-351, 2016.
[44] C. Peiró, T. Romacho, V. Azcutia, L. Villalobos, E. Fernández, JP. Bolaños, S. Moncada, CF. Sánchez-Ferrer, “Inflammation, glucose, and vascular cell damage: The role of the pentose phosphate pathway. Cardiovasc Diabetol,”, vol. 82, p. 15, 2016.
[45] A. Khanam, Q.S. Akter, F. Karim, M.R. Zannat, “Karim F, Zannat MR ‘Erythrocyte glucose-6-phosphate dehydrogenase Level in Type 2 Diabetes Male.’,” Mymensingh Med. J. MMJ, Akter QS, vol. 27, no. 1, pp. 103-107, Jan. 01 2018.
[46] H. C. Yang et al., “What has passed is prolog: new cellular and physiological roles of G6PD,” Free Radic. Res., vol. 50, no. 10, pp. 1047-1064, 2016.