Abstract
Protein kinase C activity was demonstrated in cytosolic fractions prepared from human amnion and decidua vera tissues. The enzyme has been partially purified and was found to be glycerophospholipid-dependent. Phosphatidylserine was most active in the stimulation of protein kinase C. Ca 2+ was also required for the expression of the enzyme activity. In the presence of unsaturated diacylglycerols, maximum activation of protein kinase C was observed at suboptimal concentrations of Ca 2+. A possible role of phospholipid-dependent protein kinase C in the regulation of arachidonic acid release in this tissue is discussed.
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