Journal of Lipid Research, Vol 28, 216-220, Copyright © 1987 by Lipid Research, Inc.
Relation of lung fatty acid binding protein to the biosynthesis of pulmonary phosphatidic acid and phosphatidylcholine
RU Haq, F Tsao and E Shrago
The activities of glycerophosphate and lysophosphatidylcholine (LPC)
acyltransferases were determined using lung microsomes in the presence of
lung fatty acid binding protein (FABP). The synthesis of phosphatidic acid
(PA) was increased two- to fourfold in the presence of FABP as compared to
albumin. Lung FABP did not increase the incorporation of palmitoyl CoA into
phosphatidylcholine. The results indicate that FABP-bound fatty acyl CoA
may be a preferred substrate for glycerophosphate acyltransferase.