Cationic amphiphilic drugs inhibit the synthesis of long-chain fatty acyl coenzyme A in rat brain microsomes.
The effect of cationic amphiphilic drugs (CAD) on the synthesis of thiol esters of coenzyme A with long-chain fatty acids was studied in microsomes of rat brain in vitro. The results indicate that propranolol, tetracaine and to a lesser extent, chloroquine, inhibit enzyme activity. Procaine and lidocaine did not inhibit enzyme activity in concentrations up to 0.8 mM. This inhibition seems to be directed primarily to the synthesis of polyunsaturated fatty acyl coenzyme A. The results also suggest that this inhibition may be due to the action of CAD on the microsomal membrane and not to an interaction of these drugs with the fatty acid substrates.
D000214:Acyl Coenzyme A / Q000096:biosynthesis*; D000779:Anesthetics, Local / Q000494:pharmacology*; D000818:Animals; D001921:Brain / Q000187:drug effects / Q000648:ultrastructure*; D002738:Chloroquine / Q000494:pharmacology*; D008012:Lidocaine / Q000494:pharmacology; D008861:Microsomes / Q000187:drug effects / Q000378:metabolism*; D011433:Propranolol / Q000494:pharmacology*; D051381:Rats; D013748:Tetracaine / Q000494:pharmacology
D000214:Acyl Coenzyme A; D000779:Anesthetics, Local; D013748:Tetracaine; D002738:Chloroquine; D008012:Lidocaine; D011433:Propranolol