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Benzo[a]pyrene sensitizes mouse aortic endothelial cells to oxidized lipids
Author(s) -
Jules George,
Zhou LiChun,
Yang Hong,
Guo ZhongMao
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.1_supplement.1128.22
Subject(s) - lysophosphatidylcholine , catalase , reactive oxygen species , phospholipase a2 , chemistry , programmed cell death , benzo(a)pyrene , phospholipase , biochemistry , superoxide , viability assay , endothelial stem cell , microbiology and biotechnology , apoptosis , oxidative stress , enzyme , biology , phospholipid , phosphatidylcholine , in vitro , carcinogen , membrane
Benzo[a]pyrene (BaP) is a ubiquitous environmental pollutant arising from the incomplete combustion of organic substances, and is known to cause many diseases including atherosclerosis. It has also been shown that BaP activates phospholipase A2, an enzyme necessary for the synthesis of lysophosphatidylcholine (LPC), an oxidized lipid known to promote atherosclerosis. Several studies have shown that both LPC and BaP promote endothelial cell (EC) death through the production of reactive oxygen species such as hydrogen peroxide, a relatively stable molecule. However, the mechanism by which both LPC and BaP promote EC death is not well defined. Preliminary data from our laboratory shows that BaP increases sensitivity of mouse aortic endothelial cell (MAECs) to LPC. Therefore the central hypothesis to be tested in this study is that BaP increases lysophosphatidylcholine (LPC) induced cell death in mouse aortic endothelial cells (MAECs) through the production of reactive oxygen species such as hydrogen peroxide. To test this hypothesis, cell viability, membrane integrity, and apoptotic cell markers will be measured in MAECs obtained from wild‐type mice and mice overexpressing the human catalase gene (hCatTg +/0 ). Furthermore, phospholipase A2 enzyme activity will be examined in hCatTg +/0 and wild‐type ECs based on protein level, and the phosphorylation status of the protein. Since catalase is an antioxidant that converts H 2 O 2 to water and oxygen, I expect to find cell death as well as phospholipase A2 activity to be decreased in hCatTg +/0 ECs compared to wild‐type cells.