title: Calcium-dependent phosphorylation of the amphibian oocyte plasma membrane: an early event in initiating the meiotic divisions.
abstract: Plasma membranes isolated from Rana oocytes showed a 7-10 fold increase in the Ca2+-dependent phosphorylation of endogenous protein following exposure to meiotic stimuli (progesterone, insulin) either in vivo or in-vitro. Exogenous phosphatidylmonomethylethanolamine (PME) was effective in stimulating Ca2+-dependent membrane phosphorylation and also induced meiosis. Induction of phosphorylation was blocked by the protease inhibitor leupeptin, as are all other responses to meiotic stimuli. Phosphatidylserine was inactive when added to intact oocytes, but stimulated membrane phosphorylation nearly 15-fold when added to isolated membranes. The results indicate a link between phospholipid methylation and protein kinase C activation.
mesh_terms: D000818:Animals; D002118:Calcium / Q000494:pharmacology*; D002462:Cell Membrane / Q000378:metabolism; D004789:Enzyme Activation / Q000187:drug effects; D005260:Female; D008540:Meiosis; D008565:Membrane Proteins / Q000378:metabolism*; D009865:Oocytes / Q000166:cytology / Q000187:drug effects / Q000378:metabolism*; D010714:Phosphatidylethanolamines / Q000494:pharmacology; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D011374:Progesterone / Q000494:pharmacology; D011493:Protein Kinase C / Q000378:metabolism*; D011894:Rana pipiens; D014817:Vitelline Membrane / Q000187:drug effects / Q000378:metabolism
chemical_list: D008565:Membrane Proteins; D010714:Phosphatidylethanolamines; D010750:Phosphoproteins; C032000:phosphatidyl-N-monomethylaminoethanol; D011374:Progesterone; D011493:Protein Kinase C; D002118:Calcium