Physicochemical Analysis of Structural Alteration and Advanced Glycation End Products Generation During Glycation of H2A Histone by 3-Deoxyglucosone

Title
Physicochemical Analysis of Structural Alteration and Advanced Glycation End Products Generation During Glycation of H2A Histone by 3-Deoxyglucosone
Author(s)
최인호모하메드아쉬라프Saheem Ahmad[Saheem Ahmad]Gulam Rabbani[Gulam Rabbani]이은주Rizwan Hasan Khan[Rizwan Hasan Khan]아리프타슬림얀
Keywords
TRANSFORM INFRARED-SPECTROSCOPY; SIDE-CHAIN MODIFICATIONS; DIABETIC COMPLICATIONS; MAILLARD REACTION; HUMAN DNA; PROTEIN; ASSAY; METHYLGLYOXAL; DAMAGE; LYSINE
Issue Date
201410
Publisher
WILEY-BLACKWELL
Citation
IUBMB LIFE, v.66, no.10, pp.686 - 693
Abstract
Advanced glycation end-products comprise a complex and heterogeneous group of compounds that have been implicated in diabetes-related complications. The importance of the Maillard reaction is depicted by the formation of reactive intermediate products known as alpha-oxoaldehydes, such as 3-deoxyglucosone (3-DG). This product has been found to be involved in accelerated vascular damage in diabetes. In the present study, calf thymus histone H2A was reacted with 3-DG, and the generation of advanced glycation end products was investigated by determining the degree of side chain modifications (lysine and arginine residues), Amadori products, carbonyl content, Ne-carboxymethyl lysine, and pentosidine using various physicochemical techniques. Moreover, fluorescence, absorbance as well as structural characteristics of glycated-H2A were comprehensively investigated. Overall, this study demonstrates structural perturbation, formation of different intermediates, and AGEs that are believed to hamper the normal functioning of H2A histone, compromising the integrity of chromatin structures and function in secondary complications of diabetes. (C) 2014 IUBMB Life, 66(10): 686-693, 2014
URI
http://hdl.handle.net/YU.REPOSITORY/30664http://dx.doi.org/10.1002/iub.1318
ISSN
1521-6543
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생명공학부 > 생명공학부 > Articles
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