Role of lamellar bodies in the biosynthesis of phosphatidylcholine in mouse lung.
1. A lamellar body-enriched fraction was isolated from whole lung homogenates of mouse lung and its contamination with microsomes, mitochondria, and cytosol protein assessed by marker enzyme analyses. 2. By measuring the activity of cholinephosphotransferase (EC 2.7.8.2) in varying amounts of microsomes in the presence and absence of a fixed quantity of lamellar bodies, it could be demonstrated unequivocally that lamellar bodies of mouse lung lack the capacity to synthesize phosphatidylcholine de novo. 3. A similar approach allowed the conclusion that lamellar bodies of mouse lung do not contain lysophosphatidylcholine acyltransferase (EC 2.3.1.23) and lysophosphatidylcholine:lysophosphatidylcholine acyltransferase (EC 2.3.1.--), enzymes which play a putative role in the formation of pulmonary 1,2-dipalmitoyl-sn-glycerol-3-phosphocholine. The activities of these enzymes observed in lamellar body fractions could be attributed completely to contaminating microsomes and cytosol respectively. 4. Lamellar bodies contributed to the activity of microsomal lysophosphatidylcholine acyltransferase by a cooperative effect. The possible role of this cooperation in the biosynthesis of 1,2-dipalmitoyl-sn-glycero-3-phosphocholine is discussed.
D008243:1-Acylglycerophosphocholine O-Acyltransferase / Q000378:metabolism; D000217:Acyltransferases / Q000378:metabolism; D000818:Animals; D002798:Diacylglycerol Cholinephosphotransferase / Q000378:metabolism; D007700:Kinetics; D008168:Lung / Q000378:metabolism*; D051379:Mice; D009940:Organoids / Q000378:metabolism*; D010713:Phosphatidylcholines / Q000096:biosynthesis*; D013347:Subcellular Fractions / Q000378:metabolism
D010713:Phosphatidylcholines; D000217:Acyltransferases; D008243:1-Acylglycerophosphocholine O-Acyltransferase; D002798:Diacylglycerol Cholinephosphotransferase