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

Title
Glycation of H1 Histone by 3-Deoxyglucosone: Effects on Protein Structure and Generation of Different Advanced Glycation End Products
Author(s)
최인호모하메드아쉬라프Gulam Rabbani[Gulam Rabbani]Saheem Ahmad[Saheem Ahmad]캄바하산Rizwan Hasan Khan[Rizwan Hasan Khan]Khursheed Alam[Khursheed Alam]
Keywords
SIDE-CHAIN MODIFICATIONS; PHYSICOCHEMICAL ANALYSIS; HUMAN DNA; NONENZYMATIC GLYCATION; DIABETES-MELLITUS; ENDPRODUCTS AGES; IN-VITRO; METHYLGLYOXAL; GLYCOXIDATION; ASSAY
Issue Date
201506
Publisher
PUBLIC LIBRARY SCIENCE
Citation
PLOS ONE, v.10, no.6
Abstract
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, the generation of AGEs (N-epsilon-carboxymethyl lysine and pentosidine) by 3-DG in H1 histone protein was characterized by evaluating extent of side chain modification (lysine and arginine) and formation of Amadori products as well as carbonyl contents using several physicochemical techniques. Results strongly suggested that 3-DG is a potent glycating agent that forms various intermediates and AGEs during glycation reactions and affects the secondary structure of the H1 protein. Structural changes and AGE formation may influence the function of H1 histone and compromise chromatin structures in cases of secondary diabetic complications.
URI
http://hdl.handle.net/YU.REPOSITORY/32099http://dx.doi.org/10.1371/journal.pone.0130630
ISSN
1932-6203
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