The incorporation of labelled glycerophosphoric acid into the lipids of rat brain preparations. 3. On the biosynthesis of phosphatidyl glycerol.
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F Possmayer
Publications and source records attributed to F Possmayer.
Characterization of the pulmonary N-ethylmaleimide-insensitive phosphatidate phosphohydrolase.
Phosphatidate phosphohydrolase (PAPase) is a key enzyme involved in glycerolipid synthesis where it converts phosphatidic acid to diacylglycerol. Previous studies performed in lung have demonstrated the existence of 2 different forms of PAPases, namely PAP-1 and PAP-2. The former pulmonary Mg+2-dependent enzyme is N-ethylmaleimide (NEM)-sensitive, heat labile, and is involved in phospholipid biosynthesis. However, the function of the latter lung isozyme is unknown. PAP-2 activity was selectively assayed using NEM in the absence of Mg+2. Studies employing this assay and adult rat lung microsomal preparations demonstrated that PAP-2 activity was inhibited by amphiphilic amines, sphingoid bases, products of the PAP-2 reaction (monoacylglycerol [MAG] and diacylglycerol [DAG]), and substrate analogs such as lysophosphatidic acid (lyso-PA), ceramide-1-phosphate, and to a lesser extent, sphingosine-1-phosphate. Purified lung plasma membranes, prepared using discontinuous sucrose and Percoll gradients, showed that PAP-2 activity was enriched 6.9 +/- 1.6-fold over the whole homogenate and was between the enrichment for plasma membrane markers, 5'-nucleotidase (14.7 +/- 0.3) and Na+, K(+)-ATPase (4.0 +/- 0.2). Both phosphatidic acid and lysophosphatidic acid were good substrates for PAP-2 activity in this purified plasma membrane fraction. In contrast, sphingosine-1-phosphate was a relatively poor substrate. PAP-2 activity was slightly enriched in isolated type II cells and low in isolated rat lung fibroblasts. This study shows lung contains PAP-2 activity in plasma membranes and type II cells where it could play a role in signal transduction.
Animals↗
Cellular distribution of enzymes involved in phosphatidylcholine synthesis in developing rat lung.
The incorporation of radioactive choline into phosphatidylcholine and disaturated phosphatidylcholine in rat lung slices increased markedly before term and peaked after birth. The specific activity of cholinephosphate cytidylyltransferase in the microsomal fraction increased before birth but fell after delivery. The specific activity of this enzyme in the cytosol showed a marked increased at birth. The developmental profile for the total cytosolic activity per gram lung was similar to the pattern observed with choline incorporation. Although the specific activity of cholinephosphotransferase in the whole homogenate remained relatively constant throughout pulmonary maturation, there was a marked increase in the specific activity of this enzyme in the microsomal fraction at term. Similar findings were obtained with the microsomal marker NADPH-cytochrome c reductase. The basis of this disparity in specific activity profiles is being investigated further. The specific activity of lysophosphatidylcholine:lysophosphatidylcholine transacylase in rat lung homogenates increased during gestation but rose a further 10-fold between day 3 after birth and the adult. The specific activity of lysophosphatidylcholine:palmitoyl-CoA acyltransferase remained relatively constant throughout development. At term, the specific activity of the acylation enzyme was 10- to 15-fold greater than the specific activity of the transacylation enzyme. These observations are consistent with previous studies indicating that the accumulation of phosphatidylcholine and dipalmitoyl phosphatidylcholine during the perinatal period may be due to alterations in the activity of cholinephosphate cytidylyltransferase. Cholinephosphotransferase could also play a regulatory role. The formation of dipalmitoyl phosphatidylcholine appears to occur via the acylation, rather than the transacylation pathway.
1-Acylglycerophosphocholine O-Acyltransferase↗