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The Preventive Effect of L-Lysine on Lysozyme Glycation in Type 2 Diabetes Pubmed



Mirmiranpour H1, 2 ; Khaghani S2 ; Bathaie SZ3 ; Nakhjavani M4 ; Kebriaeezadeh A5 ; Ebadi M4 ; Gerayeshnejad S2 ; Zangooei M2
Authors
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Authors Affiliations
  1. 1. Department of Biochemistry, School of Medicine, Alborz University of Medical Sciences, Karaj, Iran
  2. 2. Department of Clinical Biochemistry, School of Medicine, Tehran University of Medical Sciences, Tehran, Iran
  3. 3. Department of Clinical Biochemistry, School of Medical Sciences, Tarbiat Modares University, Tehran, Iran
  4. 4. Endocrinology and Metabolism Research Center, Vali-Asr Hospital, Tehran University of Medical Sciences, Tehran, Iran
  5. 5. Departments of Toxicology/ Pharmacology, School of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran

Source: Acta Medica Iranica Published:2016


Abstract

Lysozyme is a bactericidal enzyme whose structure and functions change in diabetes. Chemical chaperones are small molecules including polyamines (e.g. spermine), amino acids (e.g. L-lysine) and polyols (e.g. glycerol). They can improve protein conformation in several stressful conditions such as glycation. In this study, the authors aimed to observe the effect of L-lysine as a chemical chaperone on structure and function of glycated lysozyme. In this study, in vitro and in vivo effects of L-lysine on lysozyme glycation were investigated. Lysozyme was incubated with glucose and/or L-lysine, followed by an investigation of its structure by electrophoresis, fluorescence spectroscopy, and circular dichroism spectroscopy and also assessment of its bactericidal activity against M. lysodeikticus. In the clinical trial, patients with type 2 diabetes mellitus (T2DM) were randomly divided into two groups of 25 (test and control). All patients received metformin and glibenclamide for a three months period. The test group was supplemented with 3 g/day of L-lysine. The quantity and activity of lysozyme and other parameters were then measured. Among the test group, L-lysine was found to reduce the advanced glycation end products (AGEs) in the sera of patients with T2DM and in vitro condition. This chemical chaperone reversed the alteration in lysozyme structure and function due to glycation and resulted in increased lysozyme activity. Structure and function of glycated lysozyme are significantly improved by l-lysine; therefore it can be considered an effective therapeutic supplementation in T2DM, decreasing the risk of infection in these patients. © 2015 Tehran University of Medical Sciences. All rights reserved.
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