Protein glycation by ADP-ribose: Studies of model conjugates

Citations Over TimeTop 10% of 1993 papers

Abstract

Protein glycation by hexoses has been implicated in the pathophysiology of a number of diseases as well as the aging process. Studies of ADP-ribose polymer metabolism have shown that free ADP-ribose is generated at high rates in the cell nucleus following DNA damage. Protein glycation by ADP-ribose has been reported although the chemistry is not understood. Described here is the synthesis and characterization of model conjugates for protein glycation of lysine residues by ADP-ribose. Two stable conjugates derived from ADP-ribose and n-butylamine were isolated and characterized. Both conjugates were shown to be ketoamines derived from a Schiff base by an Amadori rearrangement. The chemical stability of the ketamines allowed them to be differentiated from all classes of enzymic protein modification by ADP-ribose. Further, their chemical properties suggest that a previous report of histone H1 modification in carcinogen treated cells was due to glycation by ADP-ribose.

Related Papers

• → Decrease in Glycation of Lens Proteins by Lysine and Glycine by Scavenging of Glucose and Possible Mitigation of Cataractogenesis(1993)45 cited
• → Nonenzymatic glycosylation of isolated human immunoglobulin‐G by D‐ribose(2022)12 cited
• → Inihbition of Protein Glycation with Varying Concentrations of Lysine(2008)4 cited
• → Lysine proximity significantly affects glycation of lysine-containing collagen model peptides(2011)4 cited
• → LEVELS OF FRUCTOSYLLYSINE IN COLLAGEN ARE LOW COMPARED WITH THE LOSS OF LYSINE IN DIABETIC RATS: INVOLVEMENT OF OXIDATION IN INCREASED CROSS‐LINKING(1997)