Histone Protein Glycation and Diabetes

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Histone Protein Glycation and Diabetes

Glycation and oxidation are two mechanisms that have been widely attributed with the generation of advanced glycation end products upon proteins in various pathological conditions. Histones being lysine and arginine rich are prone to these reactions and hence they are susceptible to glycoxidation reactions. Post translational modifications in the highly conserved basic core histone proteins are...

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[Oxidative stress and protein glycation in diabetes mellitus].

Metabolic alterations of diabetes mellitus are not only informative biological signs, but also factors of degenerative complications. Thus, hyperglycaemia increases non enzymatic glycation, characterized by the binding of simple oses (glucose) or by-products to amino groups of proteins. This reaction leads to the formation of complex compounds, advanced glycation end products (AGEs), which alte...

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Glycation of H1 Histone by 3-Deoxyglucosone: Effects on Protein Structure and Generation of Different Advanced Glycation End Products

Advanced glycation end products (AGEs) culminate from the non-enzymatic reaction between a free carbonyl group of a reducing sugar and free amino group of proteins. 3-deoxyglucosone (3-DG) is one of the dicarbonyl species that rapidly forms several protein-AGE complexes that are believed to be involved in the pathogenesis of several diseases, particularly diabetic complications. In this study, ...

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Protein Glycation in Diabetes as Determined by Mass Spectrometry

Diabetes is a common endocrine disorder characterized by hyperglycemia leading to nonenzymatic glycation of proteins, responsible for chronic complications. The development of mass spectrometric techniques able to give highly specific and reliable results in proteome field is of wide interest for physicians, giving them new tools to monitor the disease progression and the possible complications...

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ژورنال

عنوان ژورنال: Journal of Diabetes Research and Therapy ( ISSN 2380-5544 )

سال: 2015

ISSN: 2380-5544

DOI: 10.16966/2380-5544.109