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

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 (Nε-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.

• Authors: Jalaluddin Mohammad Ashraf, Gulam Rabbani, Saheem Ahmad, Qambar Hasan, Rizwan Hasan Khan, Khursheed Alam, Inho Choi
• Journal: PloS one (PLoS One) Vol. 10 Issue 6 Pg. e0130630 ( 2015) ISSN: 1932-6203 [Electronic] United States
• PMID: 26121680 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Glycation End Products, Advanced
• Histones
• Deoxyglucose
• 3-deoxyglucosone

Topics

• Animals
• Cattle
• Chromatography, High Pressure Liquid
• Circular Dichroism
• Deoxyglucose (analogs & derivatives, pharmacology)
• Enzyme-Linked Immunosorbent Assay
• Glycation End Products, Advanced (metabolism)
• Glycosylation (drug effects)
• Histones (chemistry, metabolism)
• Protein Denaturation (drug effects)
• Spectrophotometry, Ultraviolet
• Spectroscopy, Fourier Transform Infrared
• Temperature