Showing papers on "Acyl-CoA published in 1978"
TL;DR: It is suggested that the conversion of carn itine to acyl carnitine during the onset of ischemia may play an important role, by virtue of its effect on these enzymes, in the regulation of metabolism during the early or reversible phase of isChemia.
239 citations
72 citations
TL;DR: Inhibition of the adenine nucleotide translocase by long chain fatty acyl CoA esters demonstrated in vitro may also occur in vivo when the complete oxidation of fatty acids by the myocardium has been compromised during ischemia.
35 citations
TL;DR: Variation in intracellular concentrations of fatty acyl-CoA thioesters may significantly alter cholesterol synthesis, and inhibition of in vitro cholesterol synthesis is due to inhibition of hydroxymethylglutaryl- CoA reductase activity.
14 citations
TL;DR: The goat mammary gland fatty acid synthetase hydrolysed both medium and long chain length acyl CoA esters, and the medium chain acyl-thioester hydrolase activity was much less sensitive to inhibition by phenylmethanesulfonyl-fluorid than the long chain acyll CoA hydrolases activity.
11 citations
TL;DR: The existence of a very active long-chain fatty acyl-CoA hydrolase in homogenates of human blood platelets is reported and the highest activity was found with palmitoyl- CoA as the substrate.
Abstract: The existence of a very active long-chain fatty acyl-CoA hydrolase in homogenates of human blood platelets is reported. The highest activity was found with palmitoyl-CoA as the substrate. Palmitoyl-CoA hydrolase activity was not found in intact platelets indicating that the enzyme is localized within the platelet membrane. No palmitoyl-CoA hydrolase activity was found in fasting plasma. Mg2+, Mn2+, Ca2+ and Triton X-100 inhibited the palmitoyl-CoA hydrolase activity. Sulphydryl reagents had no effect, whereas high concentrations of D- and L-carnitine inhibited the activity. Carnitine palmitoyltransferase did not interfere with the assay of palmitoyl-CoA hydrolysis as the activity of carnitine-palmitoyl hydrolase was less than 1% of the palmitoyl-CoA hydrolase activity.
10 citations
TL;DR: Preliminary data suggest that there is also a decrease in cholesterol affinity for its cytosolic binding protein in Morris hepatomas, raising the intriguing possibility that the common denominator for these metabolic defects in hepatomas resides in the abnormal metabolism of a family of cytosol binding proteins.
Abstract: It is well established that fatty acid and cholesterol synthesis are not inhibited in Morris hepatomas during the fasting state in contradistinction to normal liver. The constitutive enzymes of these pathways in hepatomas appear to be normal. We observed that the tumor content of the feedback inhibitor of lipo-genesis, long chain fatty acyl CoA and its cytoplasmic binding protein, Z protein, were both low and did not increase significantly during fasting. We proposed that the basic defect could be defective net production of Z protein. Preliminary data suggest that there is also a decrease in cholesterol affinity for its cytosolic binding protein in Morris hepatomas. This raises the intriguing possibility that the common denominator for these metabolic defects in hepatomas resides in the abnormal metabolism of a family of cytosolic binding proteins.
10 citations
01 Jan 1978
TL;DR: It is concluded that acyl transfer reactions may be an important mechanism for regulating the fatty acid profile of CDP-diacylglycerol.
Abstract: SUMMARY: Cytidine diphosphate diacylglycerol of rat liver, like phosphatidylinositol, contains stearate and arachidonate as the major fatty acids, whereas palmitate and oleate predominate in phosphatidic acid. Following the intrajugular injection of 3 H-glycerol the distribution of radioactivity in the polyenoic species (≥ Δ 3) of CDP-diacylglycerol is significantly enriched over that in phosphatidic acid, suggestive of a selective process occurring. In vitro conversion of 3 H-labeled phosphatidic acid to CDP-diacylglycerol by rat liver microsomes indicates that the de novo pathway is not selective enough to account for the high arachidonate content of the liponucleotide. However, CDP-monoacylglycerol is readily acylated by microsomes with a marked preference shown for unsaturated over saturated acyl CoA thioesters and under certain incubation conditions, with selectivity for arachidonoyl CoA. It is concluded that acyl transfer reactions may be an important mechanism for regulating the fatty acid profile of CDP-diacylglycerol.