Cholinephosphotransferase from rabbit lung microsomes. An improved assay and specificity towards exogenous diacylglycerols

  title={Cholinephosphotransferase from rabbit lung microsomes. An improved assay and specificity towards exogenous diacylglycerols},
  author={Seamus A. Rooney and T S Wai-lee},
Cholinephosphotransferase is an important enzyme in the synthesis of pulmonary surfactant, the major surface-active component of which is dipalmitoylglycerophosphocholine. Cholinephosphotransferase from rabbit lung microsomes was assayed using a variety of exogenous diacylglycerols as substrate. The enzyme exhibited a preference for unsaturated diacylglycerols, which is in keeping with other evidence that the bulk of pulmonary dipalmitoylglycerophosphocholine is not synthesized de novo. However… 
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Synthesis of disaturated phosphatidylcholine by cholinephosphotransferase in rat lung microsomes.
The results support the conclusion that disaturated phosphatidylcholine in lung can be formed by direct utilization of disaturated diacylglycerol and is not produced exclusively via remodelling of de novo synthesized unsaturated species.
Chapter 22 – Lung Lipid Composition and Surfactant Biology
This chapter considers the lipid composition and metabolism of the lung, the lung surfactant, the Lung alveolar epithelial cells (type II) as the source of surfactan, and the lung lamellar bodies, the surfactants storage organelle.
Perspectives on fetal lung development
This review addresses salient features of lung development in a multidisciplinary fashion with emphasis on recent biochemical observations and their implications.


Selective utilization of endogenous unsaturated phosphatidylcholines and diacylglycerols by cholinephosphotransferase of mouse lung microsomes.
In the presence of CMP, cholinephosphotransferase of mouse lung microsomes catalyzes the conversion of endogenous phosphatidylcholines into 1,2-diacyl-sn-glycerols and CDPcholine, which shows a distinct preference for those molecular species of phosphate which contain an unsaturated fatty acid.
Utilization of diacylglycerol species by cholinephospho-transferase, ethanolaminephosphotransferase and diacylglycerol acyltransferase in rat liver microsomes
Abstract 1. 1. Several mixtures of 3H- and 14C-labelled diacylglycerols at varying degrees of unsaturation were incubated in the simultaneous presence of CDP-choline and CDP-ethanolamine with
Substrate-selectivity of rat liver microsomal 1,2-diacylglycerol: CDP-choline(ethanolamine) choline(ethanolamine)phosphotransferase in utilizing endogenous substrates.
Rat liver microsomes containing 1,2-diacylglycerols formed from the endogenous phosphatidycholines by the action of 1,2-diacylglycerol: CDPcholine cholinephosphotransferase (E.C. were used
Utilization of endogenous phospholipids by the backreaction of CDP-choline (-ethanolamine): 1,2-diglyceride choline (ethanolamine)-phosphotransferase in rat liver microsomes
Abstract Rats were injected intraperitoneally or intraportally with various radioactive precursors for the synthesis of lecithins and phosphatidylethanolamines. After 30 min the animals were killed
Some studies on the biosynthesis of the molecular species of phosphatidylcholine from rat lung and phosphatidylcholine and phosphatidylethanolamine from rat liver.
The results indicate that, in liver, a de novo synthesis is primarily operating in the biosynthesis of linoleic acid-containing molecules of lecithin and of the hexaenoic molecular species of phosphatidylethanolamine and, in lung, an acylation of monoacyl derivatives of these phospholipids is suggested to play an important role particularly in the formation of arachidonic acid containing molecular Species of theseospholipid.
Biosynthesis of lecithins and phosphatidyl ethanolamines from various radioactive 1,2-diglycerides in rat liver microsomes
Abstract Various species of 1,2-diglycerides labeled with 2- 3 H]glycerol or with [1- 14 C]-glycerol were obtained from biosynthetically labeled rat liver lecithins. The modes of utilization of the
The Enzymes of Lecithin Biosynthesis in Human Newborn Lungs. III. Phosphorylcholine Glyceride Transferase
  • R. Zachman
  • Chemistry, Medicine
    Pediatric Research
  • 1973
The difference in enzyme activity between premature infants and infants of longer gestation periods is statistically significant at the 95% confidence limit and could play a significant role in the relation between lung lecithin biosynthesis and respiratory distress syndrome of the human neonate.
Activity and properties of CTP: cholinephosphate cytidylyltransferase in adult and fetal rat lung.
There is an inverse relationship between the concentration of phospholipid in the fetal lung supernatant and the degree of lipid stimulation, and the activity of cytidylyltransferase in fetal lung increases 5- to 6-fold within 12 h after birth, to values higher than in the adult.
Stimulation of phosphorylcholine-glyceride transferase activity by unsaturated fatty acids.
A number of unsaturated fatty acids markedly stimulate chicken liver microsomal phosphorylcholine–glyceride transferase (CDP-choline:1,2-diglyceride cholinephosphotransferase, EC, while diglyceride O-acyltransferase activity is inhibited to a small extent.
Activity of cholinephosphotransferase, lysolecithin: lysolecithin acyltransferase and lysolecithin acyltransferase in the developing mouse lung.
The specific activity of cholinephosphotransferase, a key enzyme in the de novo synthesis of phosphatidylcholine, increases during the later stages of fetal development until it reaches a maximal value at a gestational age of 17 days, i.e. 2 days before term.