@article{oai:dmu.repo.nii.ac.jp:00005255,
 author = {Ando, Hiromi and Shinohara, Yasutake and Arai, Maki and Yamashita, Satoko and Sugimoto, Hiroyuki},
 issue = {3},
 journal = {Dokkyo Medical Journal},
 month = {Sep},
 note = {Phosphatidylethanolamine (PE) and cholesterol are major lipid components of mammalian cell membranes. The rate limiting enzymes for the synthesis of PE and cholesterol are CTP: phosphoethanolamine cytidylyltransferase (Pcyt2) and 3-hydroxy-3-methylglutaryl-CoA reductase (Hmgcr), respectively. The transcription and activity of these enzymes in NIH3T3 cells are suppressed by fetal bovine serum (FBS) and hydroxylated cholesterol (oxysterols) in similar dose-dependent manners. These results suggested that the intrinsic oxysterol concentration in cells is important for maintaining membrane lipid components, leading us to investigate the regulation of oxysterol-producing enzyme activity in cells. Using NIH3T3 cells, we found that of all oxysterol-producing enzymes, only the 24S-hydroxycholesterol producing enzyme cytochrome P450 46A1 (Cyp46A1) is expressed. Transcription of Cyp46A1 is suppressed by FBS, and we identified insulin-like growth factor II (IGF-II) in FBS as the factor suppressing Cyp46A1 transcription. The oxysterol level in NIH3T3 cells is also suppressed by IGF-II. These results suggested that the classical hormone IGF-II regulates the oxysterol content in cells and transduces cellular signals.},
 pages = {157--166},
 title = {Regulation of Glycerophospholipid and Cholesterol Synthesis in Cells by Hydroxylated Cholesterols (Oxysterols)},
 volume = {1},
 year = {2022}
}