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

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Authors

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

DOI:

https://doi.org/10.15613/sijrs/2017/v4i1/172388

Keywords:

Glycosylation, Malondialdehyde MDA, AChE, HbA1c.

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.

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Published

2017-06-01

Issue

Volume 4, Issue 1, January-June 2017

Section

Library Science

 

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