Calcium- and lipid-dependent protein phosphorylation in the human ovary.
The cytosol of human ovarian tissues was observed to promote protein phosphorylation in the combined presence of Ca2+, 1,2-diolein, and phosphatidylserine. Ca2+ alone or lipid alone did not produce full activation of this protein kinase(s). The addition of human erythrocyte calmodulin to the assay mixture, in the presence or absence of Ca2+, had no effect on protein kinase activity. Phosphorylation of cytosol proteins ranging in mol wt from 10,000 to 200,000 was selectively increased by Ca2+ plus lipid. This protein kinase activity may play a crucial role in the intracellular transmission of the action of hormones affecting cellular Ca2+ flux and/or phospholipid metabolism.
D002118:Calcium / Q000378:metabolism*; D002147:Calmodulin / Q000494:pharmacology; D004789:Enzyme Activation; D005260:Female; D006801:Humans; D050356:Lipid Metabolism; D008875:Middle Aged; D008970:Molecular Weight; D010053:Ovary / Q000201:enzymology*; D010718:Phosphatidylserines / Q000494:pharmacology; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism*
D002147:Calmodulin; D010718:Phosphatidylserines; D011506:Proteins; D011494:Protein Kinases; D002118:Calcium