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Regulation of hepatic cholesterol biosynthesis by fatty acids effect of feeding olive oil on cytoplasmic acetoacetyl coenzyme a thiolase beta hydroxy beta methylglutaryl coenzyme a synthase and acetoacetyl coenzyme a ligase


, : Regulation of hepatic cholesterol biosynthesis by fatty acids effect of feeding olive oil on cytoplasmic acetoacetyl coenzyme a thiolase beta hydroxy beta methylglutaryl coenzyme a synthase and acetoacetyl coenzyme a ligase. Biochemical & Biophysical Research Communications 153(1): 422-427

We reported previously that, in the perfused rat liver, oleic acid increased the specific activity of cytosolic enzymes of cholesterol biosynthesis. In this study, we examined the effects of oral administration of olive oil on the activities of HMG-CoA synthase, AcAc-CoA thiolase, AcAc-Coa ligase and HMG-CoA reductase. Olive oil feeding increased the specific activity of hepatic HMG-CoA synthase by 50%, AcAc-Coa thiolase by 2-fold, and AcAc-CoA ligase by 3-fold. Olive oil had no effect on HMG-CoA reductase activity. These data suggest that the enzymes that supply the HMG-CoA required for hepatic cholesterogenesis are regulated in parallel by a physiological substrate, fatty acid, independent of HMG-CoA reductase under these conditions.

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Salam, W.H.; Cagen, L.M.; Heimberg, M., 1988: Regulation of hepatic cholesterol biosynthesis by fatty acids: effect of feeding olive oil on cytoplasmic acetoacetyl-coenzyme A thiolase, beta-hydroxy-beta-methylglutaryl-CoA synthase, and acetoacetyl-coenzyme A ligase. We reported previously that, in the perfused rat liver, oleic acid increased the specific activity of cytosolic enzymes of cholesterol biosynthesis. In this study, we examined the effects of oral administration of olive oil on the activities of HM...

Salam W.H.; Wilcox H.G.; Cagen L.M.; Heimberg M., 1989: Stimulation of hepatic cholesterol biosynthesis by fatty acids effects of oleate on cytoplasmic acetoacetyl coenzyme a thiolase acetoacetyl coenzyme a synthetase and hydroxymethylglutaryl coenzyme a synthase. The effects of oleic acid on the activities of cytosolic HMG-CoA (3-hydroxy-3-methylglutaryl-CoA) synthase, AcAc-CoA (acetoacetyl-CoA) thiolase and AcAc-CoA synthetase, as well as microsomal HMG-CoA reductase, all enzymes in the pathway of cholest...

Heimberg M., 1986: Oleic acid stimulates activities of cytosolic acetoacetyl coenzyme a synthetase acetoacetyl coenzyme a thiolase and beta hydroxy beta methylglutaryl coenzyme a synthase in the perfused liver. Federation Proceedings: 1483

Honda, A.; Salen, G.; Nguyen, L.B.; Xu, G.; Tint, G.S.; Batta, A.K.; Shefer, S., 1998: Regulation of early cholesterol biosynthesis in rat liver: effects of sterols, bile acids, lovastatin, and BM 15.766 on 3-hydroxy-3-methylglutaryl coenzyme A synthase and acetoacetyl coenzyme A thiolase activities. Cytosolic 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) synthase catalyzes the formation of HMG-CoA, the substrate for the rate-controlling enzyme in the cholesterol biosynthetic pathway. To explore the regulation in liver, we developed a new, a...

Chang, T.Y.; Limanek, J.S., 1980: Regulation of cytosolic acetoacetyl coenzyme A thiolase, 3-hydroxy-3-methylglutaryl coenzyme A synthase, 3-hydroxy-3-methylglutaryl coenzyme A reductase, and mevalonate kinase by low density lipoprotein and by 25-hydroxycholesterol in Chinese hamster ovary cells. Journal of Biological Chemistry 255(16): 7787-7795

Rudney, H.; Ferguson, J.J., 1959: The biosynthesis of beta-hydroxy-beta-methylglutaryl coenzyme A in yeast. II. The formation of hydroxymethylglutaryl coenzyme A via the condensation of acetyl coenzyme A and acetoacetyl coenzyme A. Journal of Biological Chemistry 234(5): 1076-1080

Hedl, M.; Sutherlin, A.; Wilding, E.Imogen.; Mazzulla, M.; McDevitt, D.; Lane, P.; Burgner, J.W.; Lehnbeuter, K.R.; Stauffacher, C.V.; Gwynn, M.N.; Rodwell, V.W., 2002: Enterococcus faecalis acetoacetyl-coenzyme A thiolase/3-hydroxy-3-methylglutaryl-coenzyme A reductase, a dual-function protein of isopentenyl diphosphate biosynthesis. Many bacteria employ the nonmevalonate pathway for synthesis of isopentenyl diphosphate, the monomer unit for isoprenoid biosynthesis. However, gram-positive cocci exclusively use the mevalonate pathway, which is essential for their growth (E. I....

Salam, W.H.; Wilcox, H.G.; Cagen, L.M.; Heimberg, M., 1989: Stimulation of hepatic cholesterol biosynthesis by fatty acids. Effects of oleate on cytoplasmic acetoacetyl-CoA thiolase, acetoacetyl-CoA synthetase and hydroxymethylglutaryl-CoA synthase. The effects of oleic acid on the activities of cytosolic 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) synthase (EC 4.1.3.5), acetoacetyl-CoA (AcAc-CoA) thiolase (EC 2.3.1.9) and AcAc-CoA synthetase (EC 6.2.1.16), as well as microsomal HMG-CoA reductas...

Van-Der-Heijden, R.; Verpoorte, R.; Duine, J., A., 1994: Biosynthesis of 3S-hydroxy-3-methylglutaryl-coenzyme A in Catharanthus roseus: Acetoacetyl-CoA thiolase and HMG-CoA synthase show similar chromatographic behaviour. In eukaryotic terpenoid/sterol biosynthesis, 3S-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) is an important intermediate. In yeast and animal cells, two enzymes, acetoacetyl-CoA thiolase (AACT, EC 2.3.1.9) and HMG-CoA synthase (HMGS, EC 4.1.3.5)...

Jordan, P.M.; Gibbs, P.N., 1983: Mechanism of action of beta oxoacyl coenzyme a thiolase ec 2.3.1.9 from rat liver cytosol direct evidence for the order of addition of the 2 acetyl coenzyme a molecules during the formation of acetoacetyl coenzyme a. Single-turnover enzyme reactions were employed with .beta.-oxoacyl-CoA thiolase purified from rat liver cytosol to determine the order of binding of the 2 acetyl-CoA molecules to the enzyme during the formation of acetoacetyl-CoA. Equimolar quanti...