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Originally published In Press as doi:10.1074/mcp.M400002-MCP200 on September 17, 2004.
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Molecular & Cellular Proteomics 3:1145-1153, 2004.
© 2004 by The American Society for Biochemistry and Molecular Biology, Inc.

Research

Proteomic Analysis of Arginine Adducts on Glyoxal-modified Ribonuclease*

William E. Cotham{ddagger}, Thomas O. Metz{ddagger}, P. Lee Ferguson{ddagger}, Jonathan W. C. Brock{ddagger}, Davinia J. S. Hinton§, Suzanne R. Thorpe{ddagger}, John W. Baynes{ddagger} and Jennifer M. Ames§,¶

From the {ddagger} Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208; and § Hugh Sinclair Unit of Human Nutrition, School of Food Biosciences, The University of Reading, Whiteknights, Reading RG6 6AP, United Kingdom

Accumulation of advanced glycation end-products (AGEs) on proteins is associated with the development of diabetic complications. Although the overall extent of modification of protein by AGEs is limited, localization of these modifications at a few critical sites might have a significant effect on protein structure and function. In the present study, we describe the sites of modification of RNase by glyoxal under physiological conditions. Arg39 and Arg85, which are closest to the active site of the enzyme, were identified as the primary sites of formation of the glyoxal-derived dihydroxyimidazolidine and hydroimidazolone adducts. Lower amounts of modification were detected at Arg10, while Arg33 appeared to be unmodified. We conclude that dihydroxyimidazolidine adducts are the primary products of modification of protein by glyoxal, that Arg39 and Arg85 are the primary sites of modification of RNase by glyoxal, and that modification of arginine residues during Maillard reactions of proteins is a highly selective process.

To whom correspondence should be addressed: Hugh Sinclair Unit of Human Nutrition, School of Food Biosciences, The University of Reading, Whiteknights, Reading, RG6 6AP, United Kingdom. Tel.: 44-118-931-8730; Fax: 44-118-931-0080; E-mail: j.m.ames{at}reading.ac.uk


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