The identification and characterization of protein kinase C activity in fetal membranes.
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.
D000650:Amnion / Q000201:enzymology*; D002118:Calcium / Q000494:pharmacology; D003656:Decidua / Q000201:enzymology*; D004075:Diglycerides / Q000494:pharmacology; D005260:Female; D006801:Humans; D010718:Phosphatidylserines / Q000494:pharmacology; D010743:Phospholipids / Q000494:pharmacology; D011247:Pregnancy; D011493:Protein Kinase C; D011494:Protein Kinases / Q000378:metabolism*; D013379:Substrate Specificity
D004075:Diglycerides; D010718:Phosphatidylserines; D010743:Phospholipids; D011494:Protein Kinases; D011493:Protein Kinase C; D002118:Calcium; C013965:diolein