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J Biol Chem, Vol. 274, Issue 29, 20406-20414, July 16, 1999

Formation of N-(Hexanonyl)lysine in Protein Exposed to Lipid Hydroperoxide
A PLAUSIBLE MARKER FOR LIPID HYDROPEROXIDE-DERIVED PROTEIN MODIFICATION

Yoji Kato, Yoko Mori^§, Yuko Makino^§, Yasujiro Morimitsu^§, Sadayuki Hiroi^¶, Toshitsugu Ishikawa, and Toshihiko Osawa^§

From the  School of Humanities for Environmental Policy and Technology, Himeji Institute of Technology, Himeji 670-0092, the ^§ Department of Applied Biological Sciences, Nagoya University, Nagoya 464-8601, and the ^¶ Department of Pathology and  1st Department of Medicine, National Defense Medical College, Saitama 359-0042, Japan

The objectives of this study were to estimate the structure of the lipid hydroperoxide-modified lysine residue and to prove the presence of the adducts in vivo. The reaction of lipid hydroperoxide toward the lysine moiety was investigated employing N-benzoyl-glycyl-L-lysine (Bz-Gly-Lys) as a model compound of Lys residues in protein and 13-hydroperoxyoctadecadienoic acid (13-HPODE) as a model of the lipid hydroperoxides. One of the products, compound X, was isolated from the reaction mixture of 13-HPODE and Bz-Gly-Lys and was then identified as N-benzoyl-glycyl-N-(hexanonyl)lysine. To prove the formation of N-(hexanonyl)lysine, named HEL, in protein exposed to the lipid hydroperoxide, the antibody to the synthetic hexanonyl protein was prepared and then characterized in detail. Using the anti-HEL antibody, the presence of HEL in the lipid hydroperoxide-modified proteins and oxidized LDL was confirmed. Furthermore, the positive staining by anti-HEL antibody was observed in human atherosclerotic lesions using an immunohistochemical technique. The amide-type adduct may be a useful marker for the lipid hydroperoxide-derived modification of biomolecules.

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Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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