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Departments of 1 Biochemistry and Molecular Biophysics, 3 Microbiology and Immunology, and 2 Medicine-Gastroenterology, Medical College of Virginia, Virginia Commonwealth University, Richmond, Virginia 23298
To understand molecular events in regulation of hepatic neutral cholesteryl ester hydrolase (EC3.1.1.13; CEH), catalytic activity, protein mass, and mRNA levels were measured in rats with various perturbations of hepatic cholesterol metabolism. Cholesterol feeding decreased activity (56 ± 2%), mass (44 ± 2%), and mRNA (14 ± 3%). The cholesterol precursor mevalonate also decreased activity (42 ± 6%), mass (76 ± 3%), and mRNA (23 ± 16%). Inhibition of cholesterol biosynthesis by lovastatin increased activity (65 ± 12%) and mRNA (31 ± 24%). Stimulation of cholesterol efflux by chronic biliary diversion increased activity (138 ± 34%), mass (29 ± 7%), and mRNA (146 ± 28%). Chenodeoxycholate feeding decreased activity (46 ± 6%) and mRNA (26 ± 12%). These data suggest rational regulation of CEH in response to changes in cholesterol flux through the liver. In primary hepatocytes, steady-state mRNA markedly decreased during 72-h cultures and addition of L-thyroxine and dexamethasone synergistically maintained mRNA levels near control values. Lovastatin increased mRNA levels by 103 ± 15%. Taurocholate and phorbol 12-myristate 13-acetate suppressed mRNA (61 ± 4% and 49 ± 13%, respectively), suggesting that protein kinase C mediated effects of bile acids on CEH mRNA levels. These data suggest regulation of CEH by hormones and signal transduction in addition to changes in cholesterol flux.
regulation in vivo and in vitro; role of signal transduction pathways
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