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. 1993 Feb 16;32(6):1528-34.
doi: 10.1021/bi00057a017.

Protein glycation by ADP-ribose: studies of model conjugates

D Cervantes-Laurean  1 , D E Minter, E L Jacobson, M K Jacobson
Affiliations

Protein glycation by ADP-ribose: studies of model conjugates

D Cervantes-Laurean et al. Biochemistry. .

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.

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