Abstract
Pulmonary surfactant phosphatidylcholine (PC) formation increases as alveolar type II cells mature and arrest in G0/G1 state of the cell cycle at late fetal gestation. To determine whether this G0/G1 arrest is responsible for the increase in PC synthesis, we investigated the rates of PC synthesis and the activity, phosphorylation, intracellular distribution, synthesis, and degradation of a key enzyme of PC synthesis, cytidine triphosphate (CTP):phosphocholine cytidylyltransferase (CCTalpha). In synchronized mouse lung epithelial (MLE)-15 cells, PC production and CCTalpha activity peaked at G0/G1, declined during transition to G1/S, and remained low during S and G2/M. The changes in CCTalpha activity were not due to alterations in CCTalpha gene and protein expression. CCTalpha protein degradation also did not change during the cell cycle. Indirect immunofluorescence and immunogold electron microscopy revealed that CCTalpha localized to the cytoplasmic compartment and that its cytosolic localization did not change with the cell cycle. Although immunoblotting suggested no major redistribution of CCTalpha mass from cytosol to endoplasmic reticulum, activity measurements revealed that the ratio of particulate/soluble CCTalpha activi...Continue Reading
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