Abstract
Fibroblast-pneumonocyte factor (FPF) was purified from cortisol-treated fetal lung fibroblast conditioned medium by gel filtration and affinity chromatography. Based on bioactivity (choline incorporation into saturated phosphatidylcholine (SPC) by fetal type II cells), a 3,000-fold purification was obtained. Maximal stimulation by FPF was observed after 60 min of incubation. This finding suggests that the effect of FPF on SPC formation by fetal type II cells is not due to new protein synthesis but rather to an activation of enzymes involved in SPC production. A pulse-chase study on the metabolism of choline in fetal type II cells revealed that the presence of FPF in the chase medium increased the rate of disappearance of label from choline-phosphate and the rate of appearance in phosphatidylcholine. The radioactivity in CDPcholine was not significantly affected. This result indicates that FPF stimulates the activity of choline-phosphate cytidylyltransferase, the rate-controlling enzyme in the formation of phosphatidylcholine by fetal type II cells.
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Post, M., Smith, B. FIBROBLAST-PNEUMONOCYTE FACTOR PURIFIED WITH THE AID 0F MONOCLONAL ANTIBODIES STIMULATES CHOLINEPHOSPHATE CYTIDYLYLTRANSFERASE ACTIVITY IN FETAL TYPE II CELLS. Pediatr Res 18 (Suppl 4), 401 (1984). https://doi.org/10.1203/00006450-198404001-01849
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DOI: https://doi.org/10.1203/00006450-198404001-01849