Topic
Acyl-CoA
About: Acyl-CoA is a research topic. Over the lifetime, 527 publications have been published within this topic receiving 25134 citations. The topic is also known as: Acyl Coenzyme A.
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TL;DR: Results indicate that under abnormal pathophysiological conditions such as ischemia, FABP may protect acyl CoA monoacylglyceroph phosphorylcholine acyl transferase as well as stimulate glycerophosphate acyltransferase to limit the loss of membrane phospholipid biosynthesis.
Abstract: Accumulation of free fatty acids and their esters resulting from the degradation of membrane phospholipids is one of the major causes for the myocardial dysfunction during ischemia and reperfusion. In this communication, we have studied the possible physiological role played by fatty acid binding protein (FABP) in stimulating key enzymes involved in phospholipid biosynthesis. Purified rat heart FABP bound a maximum of either 2 mol of [1- 14C]palmitoyl coenzyme A (CoA), oleoyl CoA, or oleic acid per mol of FABP as observed by Scatchard analysis. FABP caused a threefold increase in the incorporation of [1- 14C]palmitoyl CoA into phosphatidic acid as compared to only a 1.5-fold increase by bovine serum albumin (BSA). Myocardial FABP also enhanced acyl CoA monoacylglycerophosphorylcholine acyl transferase minimally at a substrate concentration (greater than 200 microM), the activity of this enzyme was enhanced 4.5- and 2-fold by FABP and BSA, respectively. The maximum stimulation of the enzyme activity took place at the fatty acyl CoA concentration where inhibition of the enzyme activity is usually observed due to the surfactive property of acyl CoAs. These results thus indicate that under abnormal pathophysiological conditions such as ischemia, when acyl CoA concentration increases, FABP may protect acyl CoA monoacylglycerophosphorylcholine acyl transferase as well as stimulate glycerophosphate acyl transferase to limit the loss of membrane phospholipids, suggesting a possible role of FABP in phospholipid biosynthesis.
10 citations
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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
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TL;DR: Glutathione peroxidase has been found to be extremely sensitive to inhibition by CoA, and blocking the SH group of coenzyme A reduces the inhibitory effectiveness about 6-fold, suggesting that GSH peroxIDase activity is regulated in vivo by the CoA/acyl CoA ratio.
10 citations
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10 citations
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TL;DR: It is proposed that cis-parinaric acid, like fatty acids normally found in brain, is incorporated into membrane phospholipids by an acyl-CoA acyltransferase, and the presence of this enzyme in nervous tissue may make it possible to easily introduce fluorescent fatty acid probes into membrane phosphate membranes and to thereby facilitate study of membrane-mediated processes.
10 citations