期刊
CURRENT OPINION IN PHARMACOLOGY
卷 12, 期 6, 页码 696-703出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.coph.2012.07.007
关键词
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资金
- Institut National de la Sante et de la Recherche Medicale
- University of Toulouse III
- Institut Claudius Regaud
- Fondation de France
- Institut National du Cancer
- Agence Nationale de la Recherche (RPIB)
- le 'Groupe d'etude des Tumeurs Endocrines'
- Conseil Regional de Midi-Pyrenees et d'Aquitaine
Cholesterol epoxide hydrolase (ChEH) catalyzes the hydration of cholesterol-5,6-epoxides (5,6-EC) into cholestane-3 beta,5 alpha,6 beta-triol. ChEH is a hetero-oligomeric complex called the anti-estrogen binding site (AEBS) comprising 3 beta-hydroxysterol-Delta(8)-Delta(7)-isomerase (D8D7I) and 3 beta-hydroxysterol-Delta(7)-reductase (DHCR7). D8D7I and DHCR7 regulate cholesterol biosynthesis, fetal development and growth, tumor cell differentiation and death. The un-reactivity of 5,6-EC toward nucleophiles has recently been demonstrated indicating that 5,6-EC are not alkylating and carcinogenic agents as first postulated. Here we discuss recent advances in the molecular characterization of ChEH, its potential role in cancer progression and resistance as well as the interest of inhibiting ChEH and to accumulate 5,6-EC which may contribute to the anti-tumor and chemopreventive action of ChEH inhibitors used in the clinic such as tamoxifen.
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