Reversible translocation of CTP:phosphocholine cytidylyltransferase from cytosol to membranes in the adult bovine liver around parturition

Abstract

The key regulatory enzyme of phosphatidylcholine (PC) synthesis, CTP:phosphocholine cytidylyltransferase (CT), is known to be activated in vitro by translocation from soluble to particulate fractions of the cell. In the present study the periparturient cow was chosen as a model to investigate whether translocation of CT can contribute to the regulation of PC synthesis in vivo. Between parturition and 1.5 weeks post-partum, the cytosolic CT activity in the liver of the adult animal decreased 1.9-fold, and this correlated with a 1.8-fold increase in microsomal CT activity. At that time, microsomal CT activity started to decline again whereas the cytosolic activity rose concomitantly until both activities reached their pre-partum values at 8 weeks post-partum. The activities of soluble and membrane-bound CTP:phosphoethanolamine cytidylyltransferase (ET), the analogous enzyme in the CDP-ethanolamine pathway, did not change significantly throughout this period. Whereas hepatic PC concentrations declined until about 2 weeks post-partum and thereafter gradually returned to pre-partum levels, the PC levels in very-low-density-lipoproteins, started to rise 2 weeks after the partus reaching a maximum of 219% of the original value at 8 weeks post-partum. These results strongly suggest that there is a reversible redistribution of CT between cytosol and membranes in a physiologically relevant animal model, supporting the concept that translocation of CT is occurring in vivo.