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A more recent version of this article appeared on June 1, 2003

Papers In Press, published online ahead of print April 16, 2003
J. Lipid Res., doi:10.1194/jlr.M200442-JLR200
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Submitted on November 20, 2002
Revised on March 31, 2003
Accepted on April 1, 2003

Immunochemical characterization of a novel esterified lipid-protein adduct in rabbit atherosclerotic lesions using an antibody to 13-hydroperoxyoctadecadienoic acid-modified protein

Yoshichika Kawai, Yoji Kato, Hiroyuki Fujii, Yuko Makino, Yoko Mori, Michitaka Naito, and Toshihiko Osawa

Laboratory of Food and Dynamics, Nagoya University, Nagoya, Aichi 464-8601

Corresponding Author: osawat{at}agr.nagoya-u.ac.jp

We have previously prepared the polyclonal antibody to the 13-hydroperoxyoctadecadienoic acid-modified protein (13Ab) (Kato et al. 1997 J. Lipid Res. 38: 1334-1346), however, the epitopes have not yet been structurally identified. In this study, we identified a novel amide-type adduct as one of the major epitopes of 13Ab and characterized the endogenous formation. Upon incubation of the lysine derivative with peroxidized linoleic acid, the formation of NƒÕ-(azelayl)lysine (AZL) was confirmed using liquid chromatography-mass spectrometry. The chemically synthesized azelayl protein was significantly recognized by 13Ab. The peroxidation products of different polyunsaturated fatty acids also generated several analogous carboxyalkylamide-type adducts to AZL by the reaction with the lysine derivative, whereas 13Ab specifically recognized AZL, suggesting that the AZL moiety may be one of the major epitopes of 13Ab. The immunoreactive materials of 13Ab were immunohistochemically detected in atherosclerotic lesions from hypercholesterolemic rabbits. More strikingly, the immunoreactivity was significantly enhanced when the sections were treated with alkali or phospholipase A2 for hydrolyzing the ester bonds prior to the staining. These results suggest that the lipid hydroperoxide-derived carboxylic adducts, such as AZL, and their esters linked with phospholipids may be generated in vivo and involved in the pathogenesis of atherosclerosis associated with oxidative stress.


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Y. Kawai, H. Fujii, M. Okada, Y. Tsuchie, K. Uchida, and T. Osawa
Formation of N{epsilon}-(succinyl)lysine in vivo: a novel marker for docosahexaenoic acid-derived protein modification
J. Lipid Res., July 1, 2006; 47(7): 1386 - 1398.
[Abstract] [Full Text] [PDF]


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