Clinical aspects of protein glycation

Sabina Galiniak
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Izabela Krawczyk-Marć
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Anna Sęk-Mastej
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Natalia Leksa
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Marek Biesiadecki
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Stanisław Orkisz
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Department of Biochemistry and General Chemistry Medical College of Rzeszów University, Rzeszów, Poland
Faculty of Medicine, University of Rzeszów, Rzeszów, Poland
Institute of Medical Sciences, Medical College, University of Rzeszow, Rzeszow, Poland
Institute of Medical Sciences, Medical College, University of Rzeszow, Rzeszow, Poland
Faculty of Medicine, University of Rzeszów, Rzeszów, Poland
Institute of Medical Sciences, Medical College, University of Rzeszow, Rzeszow, Poland
Received: 4 July 2017 / Accepted: 23 August 2017 / Published: 30 September 2017

Abstract

Introduction. Glycation is a post-translational modification of proteins that depends on the non-enzymatic linkage of a ketone or aldehyde group of sugar with a free amino group of protein. Pathological effects of this process are observed in many disease states under conditions of hyperglycemia, in diabetic complications, and neurodegenerative diseases such as multiple sclerosis.

Aim. In this paper we present the characteristics of the glycation process, its consequences, as well as a review of current knowledge about the role of glycation in multiple sclerosis.

Material and methods. The databases EBSCO, PubMed, ScienceDirect and SpringerLink were used to search the literature.

Analysis of the literature. Intermediate glycation products form a number of derivatives that contribute to oxidative stress and structural changes in the proteins, including induction of aggregation or reduction of affinity for drug proteins. Glucose products may contribute to neurodegenerative changes in patients with multiple sclerosis. Determination of protein glycation products can be successfully used to evaluate the course of multiple sclerosis as a diagnostic marker.

 

Cite

Galiniak S, Krawczyk-Marć I, Sęk-Mastej A, et al. Clinical aspects of protein glycation. Eur J Clin Exp Med. 2017;15(3):263–267. doi: 10.15584/ejcem.2017.3.10

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