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  • Title: Phosphatidylglycerol stimulates cholinephosphate cytidylyltransferase activity and phosphatidylcholine synthesis in type II pneumocytes.
    Author: Gilfillan AM, Smart DA, Rooney SA.
    Journal: Biochim Biophys Acta; 1985 Jun 14; 835(1):141-6. PubMed ID: 2988633.
    Abstract:
    Phosphatidylcholine synthesis in type II pneumocytes is stimulated by inclusion of phosphatidylglycerol and other phospholipids in the culture medium (Gilfillan, A.M., Chu, A.J. and Rooney, S.A. (1984) Biochim. Biophys. Acta 794, 269-273). We have now examined the effect of phosphatidylglycerol in the medium on enzymes of de novo phosphatidylcholine synthesis in adult rat type II cells. Activities of choline kinase, cholinephosphate cytidylyltransferase and cholinephosphotransferase in homogenates of whole lung and type II cells were generally similar. Phosphatidate phosphatase activity in type II cells, however, was only 16% that in whole lung. Addition of phosphatidylglycerol (10 microM) to the culture medium had no effect on choline kinase, cholinephosphotransferase or phosphatidate phosphatase activities in type II cells but it increased the activity of cholinephosphate cytidylyltransferase by 56%. Since it is known that cholinephosphate cytidylyltransferase is stimulated in vitro by addition of phospholipids to the assay mixture, we also measured its activity in the presence of sufficient phosphatidylglycerol (1.1 mM) to maximally stimulate in vitro. Even under these conditions cholinephosphate cytidylyltransferase activity in type II cells cultured in the presence of phosphatidylglycerol was 32% greater than in control cells. These data show that the stimulatory effect of phospholipid in the culture medium on phosphatidylcholine synthesis in type II cells is mediated by increased cholinephosphate cytidylyltransferase activity. The mechanism of increased cytidylyltransferase activity remains to be elucidated but it is not due to direct in vitro activation by the phospholipid.
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