Fatty acid synthesizing enzymes intrinsic to myelin

A recent study showing incorporation of acetyl groups from neuronal N-acetylaspartate into myelin lipids suggested the presence of fatty acid synthesizing enzymes in myelin that utilize the acetyl groups liberated by myelin-associated aspartoacylase [J. Neurochem. 78 (2001) 736]. We report here detection of the fatty acid synthase (FAS) complex and acetyl-CoA carboxylase (ACC) in purified myelin. The activity of myelin FAS was approximately half that of cytosolic FAS and, unlike the latter, required detergent for activation. Intrinsic association of FAS with myelin was indicated by failure to remove the activity with NaCl or Na-taurocholate. Myelin-associated ACC was approximately 10% of cytosolic ACC in myelin isolated by gradient centrifugation, and this was reduced by half following osmotic shock; this suggested bimodal distribution of myelin ACC, some being loosely associated within inter-lamellar cytoplasmic spaces and the remainder more firmly associated in a manner that resists NaCl/Na-taurocholate treatments. These results, in combination with earlier findings, provide a possible mechanism for the observed incorporation of neuronal NAA acetyl groups into myelin lipids.