The acylation of 1-acyl-sn-glycero-3-phosphorylcholine by glial and neuronal nuclei and derived neuronal nuclear envelopes: a comparison of nuclear and microsomal membranes.

A neuronal nuclear fraction (N1), a glial nuclear fraction (N2) and a fraction containing microsomal membranes (P3) were isolated from homogenates of cerebral cortices of 15-day-old rabbits. A nuclear envelope fraction (E) was prepared from fraction N1. In comparison with the parent fraction N1, fraction E had a much lower yield of protein (0.077 mg/g cerebral cortex), a low specific DNA content, an eightfold higher specific phospholipid content (0.85 mumol phospholipid phosphate/mg protein) and a very similar phospholipid distribution profile. Using 100, 50, and 25 microM 1-acyl-sn-glycero-3-phosphorylcholine (labelled with [3H]palmitate) and 100 microM oleoyl CoA, the activity of acyl-CoA:1-acyl-sn-glycero-3-phosphorylcholine acyltransferase was studied in vitro. Fractions N1 and N2 had specific activities which were two to three times the specific activities shown for fraction P3. Fraction E was particularly enriched in this acylation activity and had specific activities which were 6 times those of fraction N1 and 11-19 times those of fraction P3. The existence of nuclear acyl-CoA:1-acyl-sn-glycero-3-phosphorylcholine acyltransferase activity was indicated as was a particularly high concentration of this enzyme within the nuclear envelope. In assays of lysolecithin-lysolecithin transacylase activities, fraction N2 (glial nuclei) showed the highest specific activities, being three to four times those of fractions N1 or P3. This transacylase activity (N2) was as high as 40% of the corresponding acyltransferase activity measured in this fraction using oleoyl CoA as acyl donor.