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Effect of Glycated Hemoglobin Induced Lipid Peroxidation on Membrane Bound Acetyl Cholinesterase


Affiliations
1 Department of Biomedical Engineering, Velalar College of Engineering and Technology, Erode – 638012, India
 

This study examines the relationship between erythrocyte membrane bound Acetyl cholinesterase (AChE) activity, glycated hemoglobin (HbA1c) level and lipid peroxidation (formation of malondialdehyde). The aim was to elucidate the effect of HbA1c and lipid peroxidation on the activity of acetyl cholinesterase (AChE). Control subjects were non diabetic volunteers and the test group was diabetic patients with fasting glucose level of more than 150mg%. HbA1c, total hemoglobin, plasma glucose, lipid peroxidation and activity of AChE were determined. Observations indicate that elevated levels of lipid peroxidation in erythrocyte membrane of glycated hemoglobin of diabetic patients. HbA1c significantly increases lipid peroxidation and decreases the activity of AChE. Our data indicates that erythrocyte membrane bound enzyme AChE is significantly related to lipid peroxidation. Glycation of the hemoglobin increases the lipid peroxidation and alters the membrane bound enzyme function.

Keywords

Glycosylation, Malondialdehyde MDA, AChE, HbA1c.
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  • Chandalia HB, Krishnaswamy PR. Glycated hemoglobin. Current Science. 2002; 83:1522-31.

  • Gallan MP, Carrascosa A, Gussinye M, Dominguez C. Biomarkers of diabetes associated oxidative stress and antioxidant status in young diabetic patients with or without subclinical complications. Free Radical Biology & Medicine. 2003; 34(12):1563-74. https://doi.org/10.1016/S0891-5849(03)00185-0.

  • Dominguez M, Wasserman JD, Freeman M. Multiple functions of the EGF receptor in Drosophila eye development. Current Biology. 1998; 8(19):1039-48. https://doi.org/10.1016/S0960-9822(98)70441-5.

  • Signal PK, Bello-Klein A, Farahmand F and Sandhawalia V. Oxidative Stress and Functional Deficit in Diabetic Cardiomyopathy. Advances in Experimental Medicine and Biology. 2001; 498:213-20. https://doi.org/10.1007/978-1-4615-1321-6_27.

  • Mercuri F, Quagliaro L and Ceriello A. Oxidative Stress Evaluation in Diabetes. Diabetes Technology & Therapeutics. 2000; 2(4):589-600.

  • Jacob RA and Burri BJ: Oxidative damage and defense. The American Journal of Clinical Nutrition. 1996; 63:985-90.https://doi.org/10.1093/ajcn/63.6.985.

  • Van Ginkel G, Sevanian A. Lipid peroxidation induced membrane structural alterations. Methods in Enzymology.1994; 233:273-88. https://doi.org/10.1016/S0076-6879(94) 33031-X.

  • Weiner K. Tests in disorders of glucose metabolism. Gowenlock AH editor Varley’s practical clinical biochemistry, 6th ed. New Delhi: CBS Publisher. 1988; p. 333-49.

  • Drabkin DL, Austin JM. Spectrophotometric constants for common hemoglobin derivatives in human, dog and rabbit blood. The Journal of Biological Chemistry. 1932; 98:719-33.

  • Karatas F, Halifeoglu I, Karatepe M, Konar V, Canatan H, Colak R. Evaluation of changes in levels of serum selenium, MDA and antioxidant vitamins (A, E, C) in diabetic patients. Aralik 2006; 20(6):391-5.

  • Kaplan E, Herg F and Hsu KS. Erythrocyte acetylcholinesterase activity in ABO emolytic disease of the newborn. Pediatrics. 1964; 33:205 PMid:14117375.

  • Stephen SM Chung, Eric CM Ho, Karen SL Lam and Sookja K Chung. 2003 Contribution of Polyol Pathway to DiabetesInduced Oxidative Stress. Journal of American Society of Nephrology. 2003; l14:S233-6.

  • Jain SK, Mc Vie R, Duet J, Herbst JJ. Erythrocyte membrane lipid peroxidation and glycosylated haemoglobin in diabetes. Diabetes.1989; 38:1539-43.https://doi.org/10.2337/diabetes.38.12.1539. https://doi.org/10.2337/diab.38.12.1539. PMid:2583378.

  • Gabby KH, Sosenko JM, Banuchi GA, Minin MJ, Fluckigu R. Glycosylated hemoglobins; increased glycosylation of haemoglobin A in diabetes patients. Diabetes. 1979; 28(4):337-40. https://doi.org/10.2337/diab.28.4.337.https://doi.org/10.2337/diabetes.28.4.337.

  • Vadde R, Jailkhani R. Evaluation of oxidative stress in insulin dependent diabetes mellitus (IDDM) patients. Diagnostic Pathology. 2007; 2:22. https://doi.org/10.1186/1746-15962-22. PMid:17603912 PMCid:PMC1936413.

  • Mahboob M, Rahman MF, Groover P. Serum lipid peroxidation and antioxidant enzyme levels in male and female diabetic patients. Singapore Medical Journal. 2005; 46(7):322. PMid:15968442.

  • Agarwal VR, Rastogi AK, Sahib MK and Sagar P. Acta Diabetologica. 1985; 22:359-63.

  • Kaplay SS Acetylcholineesterase and butyrylcholineesterase of developing human brain. Biology of the Neonate. 1976; 28:65-73. https://doi.org/10.1159/000240805.

  • Ott P. Membrane acetylcholinesterases: purification, molecular properties and ... Biochimica et Biophysica Acta. 1985; 822:375-92. https://doi.org/10.1016/0304-4157(85)90016-4.

  • Augustyniak K, Zavodnik I, Palecz D, Szosland K & Bryszewska M. The effect of oxidizing agent and diabetes mellitus on the human red blood cell membrane potential. Clinical Biochemistry 1996; 29:283-6. https://doi.org/10.1016/0009-9120(95)02045-N.

  • Kolling A, Maldonada C, Ojeda F and Dieht HA. Membrane fluidity of microsomal and thymocyte membranes after x-ray and UV irradiation. Radiation and Environmental Biophysics. 1994; 33:303-13.

  • https://doi.org/10.1007/BF01210452. PMid:7708904.

  • Agarwal VR, Rastogi AK, Sahib MK and Sagar P. Acta Diabetologica. 1985; 22:359-63.


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  • Effect of Glycated Hemoglobin Induced Lipid Peroxidation on Membrane Bound Acetyl Cholinesterase

Abstract Views: 558  |  PDF Views: 342

Authors

N. Jeyashanthi
Department of Biomedical Engineering, Velalar College of Engineering and Technology, Erode – 638012, India
P. Ravikumar
Department of Biomedical Engineering, Velalar College of Engineering and Technology, Erode – 638012, India
N. N. Baalakumar
Department of Biomedical Engineering, Velalar College of Engineering and Technology, Erode – 638012, India

Abstract


This study examines the relationship between erythrocyte membrane bound Acetyl cholinesterase (AChE) activity, glycated hemoglobin (HbA1c) level and lipid peroxidation (formation of malondialdehyde). The aim was to elucidate the effect of HbA1c and lipid peroxidation on the activity of acetyl cholinesterase (AChE). Control subjects were non diabetic volunteers and the test group was diabetic patients with fasting glucose level of more than 150mg%. HbA1c, total hemoglobin, plasma glucose, lipid peroxidation and activity of AChE were determined. Observations indicate that elevated levels of lipid peroxidation in erythrocyte membrane of glycated hemoglobin of diabetic patients. HbA1c significantly increases lipid peroxidation and decreases the activity of AChE. Our data indicates that erythrocyte membrane bound enzyme AChE is significantly related to lipid peroxidation. Glycation of the hemoglobin increases the lipid peroxidation and alters the membrane bound enzyme function.

Keywords


Glycosylation, Malondialdehyde MDA, AChE, HbA1c.

References





DOI: https://doi.org/10.15613/sijrs%2F2017%2Fv4i1%2F172388