期刊
BIOCHEMICAL PHARMACOLOGY
卷 65, 期 10, 页码 1603-1610出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/S0006-2952(03)00151-5
关键词
quercetin; flavonoids; peroxidative metabolism; covalent binding; DNA and protein; Caco-2 cells; Hep G2 cells
资金
- NIGMS NIH HHS [GM 55561] Funding Source: Medline
Quercetin-rich foods have the potential to prevent human disease. However, knowledge of its biological fate and mechanism of action is limited. This study extends previous observations of the oxidation of quercetin by peroxidases to quinone/quinone methide intermediates and. for the first time. demonstrates covalent binding of [C-14]quercetin to macromolecules. This was first demonstrated using horseradish peroxidase and hydrogen peroxide with human liver microsomal protein to trap the intermediates. To extend this observation to the cellular level. human intestinal Caco-2 cells and hepatic Hep G2 cells were incubated for up to 2 hr with [C-14]quercetin, and cellular DNA and protein were isolated. The cellular uptake of [C-14]quercetin was rapid, and the covalent binding of [C-14]quercetin to DNA and protein was determined by liquid scintillation spectrometry after extensive purification. Both cell types demonstrated DNA binding with a maximum level of 5-15 pmol/mg DNA. The level of covalent binding to protein was considerably higher in both cell types, 75-125 pmol/mg protein. To determine potential specificity in the protein binding, Hep G2 cells were treated with [C-14]quercetin, and the cell lysate was subjected to SDS-PAGE followed by staining and autoradiography. Several distinct radiolabeled protein bands did not correspond to the major Coomassie blue stained cellular proteins. We propose that this specific binding may mediate part of the antiproliferative and other cellular actions of quercetin. (C) 2003 Elsevier Science Inc. All rights reserved.
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