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Abstract
The phosphorylcholine cytidyltransferase activity of the cytosol fractions of rat intestinal crypt and villus cells was observed to be stimulated by addition of 3- sn-lysophosphatidylcholine. A 15- to 20-fold increase in activity was seen following a prior removal of phospholipids with acetone and butanol. 3- sn-Lysophosphatidylcholines of C 16 and C 18 carbon fatty acids were three to four times more effective than those with fatty chains of shorter length. The 3- sn-phosphatidyl and 3- sn-lysophosphatidyl ethanolamine, inositol, and serine were ineffective. 3- sn-Lysophosphatidic acid and 3- sn-glycerophosphorylcholine did not stimulate the transferase activity indicating that both fatty acyl and phosphorylcholine moieties of the 3- sn-lysophosphatidylcholine molecule were required for the observed effect. Addition of the enantiomeric 1- sn-lysophosphatidylcholine had an effect comparable to that of 3- sn-lysophosphatidylcholine on the phosphorylcholine cytidyltransferase activity when assayed in rat intestinal mucosa and in pigeon liver. It is suggested that the stimulatory effect of lysophosphatidylcholine may be related to a specific detergent property dependent upon the peculiar balance of hydrophilic and hydrophobic components in the molecule.
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