Relation of lung fatty acid binding protein to the biosynthesis of pulmonary phosphatidic acid and phosphatidylcholine.
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.
D008243:1-Acylglycerophosphocholine O-Acyltransferase / Q000378:metabolism; D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism*; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D005992:Glycerol-3-Phosphate O-Acyltransferase / Q000378:metabolism; D066298:In Vitro Techniques; D008168:Lung / Q000378:metabolism*; D008297:Male; D008861:Microsomes / Q000378:metabolism; D009363:Neoplasm Proteins; D009419:Nerve Tissue Proteins; D010712:Phosphatidic Acids / Q000096:biosynthesis*; D010713:Phosphatidylcholines / Q000096:biosynthesis*; D051381:Rats; D011919:Rats, Inbred Strains
D002352:Carrier Proteins; C490174:Fabp7 protein, rat; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D009363:Neoplasm Proteins; D009419:Nerve Tissue Proteins; D010712:Phosphatidic Acids; D010713:Phosphatidylcholines; D005992:Glycerol-3-Phosphate O-Acyltransferase; D008243:1-Acylglycerophosphocholine O-Acyltransferase