Characterization of acrolein-induced protein cross-links |
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Authors: | Ishii Takeshi Yamada Tomoe Mori Taiki Kumazawa Shigenori Uchida Koji Nakayama Tsutomu |
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Institution: |
a Department of Food and Nutritional Sciences, and Global COE Program, University of Shizuoka, Suruga-ku Shizuoka, Japan
b Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa-ku, Nagoya, Japan |
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Abstract: | Lipid peroxidation products contribute to protein aggregation that occurs during oxidative stress in a number of degenerative disorders. Acrolein (ACR), a highly toxic lipid peroxidation aldehyde, is a strong cross-linking agent of cellular components such as proteins. To understand the mechanisms of oxidative stress-induced protein aggregation, this study characterized the ACR modification of chain B from bovine insulin by mass spectrometry. To identify the cross-linking sites, the ACR-treated peptide was digested with a protease and the resulting peptides were analysed by liquid chromatography-tandem mass spectrometry. Inter- and intra-molecular cross-linking adducts were identified between amino groups and the side chain of histidine in the peptide. These results indicated that the ACR-induced cross-links were accompanied by two reactions, namely Michael addition and Schiff base formation. In conclusion, the use of mass spectrometric techniques provided chemical evidence for protein cross-linking with ACR. |
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Keywords: | Acrolein cross-link lipid peroxidation mass spectrometry protein modification |
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