Abstract
The activity of enzymes of glycolysis has been studied in erythrocytes from type-II diabetic patients in comparison with control. RBC lysate was the source of enzymes. In the diabetics the hexokinase (HK) activity increased 50 % while activities of phosphoglucoisomerase (PGI), phosphofructokinase (PFK) and aldolase (ALD) decreased by 37, 75 and 64 % respectively but were still several folds higher than that of HK. Hence, it is possible that in the diabetic erythrocytes the process of glycolysis could proceed in an unimpaired or in fact may be augmented due to increased levels of G6P. The lactate dehydrogenase (LDH) activity was comparatively high in both the groups; the diabetic group showed 85 % increase. In control group the HK, PFK and ALD activities showed strong positive correlation with blood sugar level while PGI activity did not show any correlation. In the diabetic group only PFK activity showed positive correlation. The LDH activity only in the control group showed positive correlation with marginal increase with increasing concentrations of glucose.
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Alberti KGMM, Press CM. The biochemistry of the complications of diabetes mellitus. In: Keen M, Jarrett J, editors. Complications of diabetes. London: Edward Arnold Ltd.; 1982. p 231–70.
Asgary S, Naderi GA, Sarraf-Zadegan N, Vakili R. The inhibitory effects of pure flavonoids on in vitro protein glycosylation. J Herb Pharmacother. 2002;2:47–55.
Allen DW, Schroeder WA, Balog J. Observations on the chromatographic heterogeneity of normal adult and fetal hemoglobin: a study of the effects of crystallization and chromatography on the heterogeneity and isoleucine content. J Am Chem Soc. 1958;80:1628–34.
Rahbar S. An abnormal hemoglobin in red cells of diabetics. Clin Chim Acta. 1968;22:296–8.
Trivelli LA, Ranney HM, Lai HT. Hemoglobin components in patients with diabetes mellitus. N Engl J Med. 1971;284:353–7.
Haney DN, Bunn HF. Glycosylation of hemoglobin in vitro: affinity labeling of hemoglobin by glucose-6-phosphate. Proc Natl Acad Sci. 1976;73:3534–8.
Stevens VJ, Vlassara H, Abati A, Cerami A. Nonenzymatic glycosylation of hemoglobin. J Biol Chem. 1977;252:2998–3002.
McDonald MJ, Shapiro R, Bleichman M, Solway J, Bunn HF. Glycosylated minor components of human adult hemoglobin. Purification, identification, and partial structural analysis. J Biol Chem. 1978;253:2327–32.
Tegos C, Beutler E. Red cell glycolytic intermediates in diabetic patients. J Lab Clin Med. 1980;96:85–9.
Fujii S, Beutler E. High glucose concentrations partially release hexokinase from inhibition by glucose 6 phosphate. Proc Natl Acad Sci. 1985;82:1552–4.
Gerber G, Preissler H, Heinrich R, Rapoport SM. Hexokinase of human erythrocytes. Eur J Biochem. 1974;45:39–52.
Sangwan RS, Singh R. Characterization of cytosolic phosphoglucose isomerase from immature wheat (Triticum aestivum L.) endosperm. J Biosci. 1989;14:47–54.
Katyare SS, Howland JL. Defective allosteric regulation of phosphofructokinase regulation in genetically obese mice. FEBS Lett. 1974;43:17–9.
Richards OC, Rutter WJ. Preparation and properties of yeast aldolase. J Biol Chem. 1961;236:3177–84.
Buhl SN, Jackson KY, Lubinski R, Vanderlinde RE. Effect of reaction initiator on human LDH assay. Clin Chem. 1976;22:1098–9.
Bakhtiari N, Hosseinkhani S, Larijani B, Mohajeri-Tehrani MR, Fallah A. Red blood cell ATP/ADP and nitric oxide: the best vasodilators in diabetic patients. J Diabetes Metab Disord. 2012; 11.
Besch W, Blücher H, Bettin D, Wolf E, Michaelis D, Kohnert KD. Erythrocyte sodium-lithium countertransport, adenosine triphosphatase activity and sodium-potassium fluxes in insulin-dependent diabetes. Int J Clin Lab Res. 1995;25:104–9.
Dave KR, Patel TH, Katyare SS. Insulin or sulfonylurea treatments of the diabetics differentially affect erythrocyte membrane and serum enzymes and extent of protein glycosylation. Indian J Clin Biochem. 2001;16:81–8.
Flecha FLG, Cbermúdez M, Cédola NV, Gagliardino JJ, Rossi JR. Decreased Ca2+-ATPase activity after glycosylation of erythrocyte membranes in vivo and in vitro. Diabetes. 1990;39:707–11.
Wagner-Britza L, Wang J, Kaestner L, Bernhardt I. Protein kinase Cα and P-Type Ca2+ Channel CaV 2.1 in red blood cell calcium signalling. Cell Physiol Biochem. 2013;31:883–91.
Brown JB, Pedula K, Barzilay J, Herson MK, Latare P. Lactic acidosis rates in type 2 diabetes. Diabetes Care. 1998;21:1659–63.
Diabetes Control and Complication Trial Research Group. The effect of intensive diabetes therapy on the development and progression of neuropathy. Ann Intern Med. 1995;122:561–8.
Fox CJ. Studies of unusual hemoglobin in patients with diabetes mellitus. Br Med J. 1997;2:605–7.
Baynes JW, Monnier VM. The maillard reaction in aging, diabetes, and nutrition: proceedings of an NIH conference on the maillard reaction in aging, diabetes, and nutrition, held in Bethesda, Maryland, September 22–23, Vol. 304, 1988.
Shin S, Ku Y, Babu N, Singh M. Erythrocyte deformability and its variation in diabetes mellitus. Indian J Exp Biol. 2007;45:121–8.
Singh M, Shin S. Changes in erythrocyte aggregation and deformability in diabetes mellitus: a brief review. Indian J Exp Biol. 2009;47:7–15.
Chien S. Red cell deformability and its relevance to blood flow. Annu Rev Physiol. 1987;49:177–92.
Paueksakon P, Revelo MP, Ma LJ, Marcantoni C, Fogo AB. Microangiopathic injury and augmented PAI-1 in human diabetic nephropathy. Kidney Int. 2002;61:2142–8.
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The authors would like to thank Dr. Anjali Kelkar for her help in procuring the human blood samples.
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Mali, A.V., Bhise, S.S., Hegde, M.V. et al. Altered Erythrocyte Glycolytic Enzyme Activities in Type-II Diabetes. Ind J Clin Biochem 31, 321–325 (2016). https://doi.org/10.1007/s12291-015-0529-6
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DOI: https://doi.org/10.1007/s12291-015-0529-6