J. Lipid Res.
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A more recent version of this article appeared on April 1, 2004

Papers In Press, published online ahead of print January 16, 2004
J. Lipid Res., doi:10.1194/jlr.M300376-JLR200
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Submitted on September 5, 2003
Revised on December 15, 2003
Accepted on January 7, 2004

Protein-bound 4-hydroxy-2-hexenal as a marker of oxidized n-3 polyunsaturated fatty acids

Satoshi Yamada, Tadashi Funada, Noriyuki Shibata, Makio Kobayashi, Yoshichika Kawai, Emi Tatsuda, Atsunori Furuhata, and Koji Uchida

Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, Aichi 464-8601

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

In the present study, to investigate the contribution of n-3 polyunsaturated fatty acids (n-3 PUFAs) in the oxidative modification of protein in vivo, we characterize the covalent binding of 4-hydroxy-2-hexenal (HHE), a potent cytotoxic aldehyde originating from the peroxidation of n-3 PUFAs, to protein and describe the production of this aldehyde in oxidatively modified LDL and in human atherosclerotic lesions. Upon incubation with bovine serum albumin, HHE was rapidly incorporated into the protein and generated the protein-linked carbonyl derivative, a potential marker of oxidatively modified proteins under oxidative stress. To detect the protein-bound HHE in vivo, we raised a monoclonal antibody HHE53 (mAb HHE53) directed to the HHE-modified protein and identified the Michael addition-type HHE-histidine adduct as the major epitope. This antibody reacted with copper-oxidized LDL, suggesting that HHE was produced during the oxidative modification of LDL. In addition, we demonstrated that the materials immunoreactive to mAb HHE53 indeed constituted the atherosclerotic lesions, in which intense positivity was associated primarily with macrophage-derived foam cells. The results of this study suggest that the reaction between oxidized n-3 PUFAs and protein might represent a process common to the formation of degenerative proteins during aging and its related diseases.


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[Abstract] [Full Text] [PDF]


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