Abstract
The base exchange enzymes catalyze the incorporation of L-serine, ethanolamine and choline into their corresponding phospholipids. The L-serine base enzyme activity was increased 120% by 0.1 mM sphingosine. There was a modest increase of the ethanolamine base exchange enzyme activity but the choline base exchange enzyme activity was unaffected. Na-arachadonate, Na-oleate and Na-linolenate at 0.2 mM concentration increased the activity of the L-serine and ethanolamine base exchange enzymes but inhibited the choline base exchange enzyme activity. A model is proposed suggesting that modulations of the L-serine base exchange enzyme may participate in the regulation of the calcium phospholipid-dependent protein kinase C.