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  • Title: The identification and characterization of protein kinase C activity in fetal membranes.
    Author: Okazaki T, Ban C, Johnston JM.
    Journal: Arch Biochem Biophys; 1984 Feb 15; 229(1):27-32. PubMed ID: 6230994.
    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. Ca2+ 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 Ca2+. 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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