Differential modulation of protein kinase C by bryostatin 1 and phorbol ester.
Bryostatin 1, a macrocyclic lactone, activated protein kinase C purified from mouse brain in a dose-dependent fashion to the same degree as phorbol 12-myristate 13-acetate (PMA). There was no significant difference in calcium and phosphatidylserine requirements for activation of protein kinase C between bryostatin 1 and PMA. We also found no significant difference in the inhibitory effect between staurosporine and H-7 known to be potent inhibitors of protein kinase C. These data suggest that bryostatin 1 and PMA activate protein kinase C in a similar way. We found, however, that negative modulation of protein kinase C with bryostatin 1 was weaker than that with PMA. The reason of this difference was unclear. It may possibly suggest that there is some difference in configuration of protein kinase C after binding between these activators.
Sako
T
T
Department of Pediatrics, Mie University School of Medicine, Tsu.
Ohshima
S
S
Yoshizumi
T
T
Sakurai
M
M
D000818:Animals; D001921:Brain / Q000187:drug effects / Q000201:enzymology*; D001923:Brain Chemistry / Q000187:drug effects*; D054713:Bryostatins; D002118:Calcium / Q000494:pharmacology; D004791:Enzyme Inhibitors / Q000494:pharmacology; D007783:Lactones / Q000494:pharmacology*; D018942:Macrolides; D051379:Mice; D010718:Phosphatidylserines / Q000494:pharmacology; D011493:Protein Kinase C / Q000378:metabolism*; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology*
D054713:Bryostatins; D004791:Enzyme Inhibitors; D007783:Lactones; D018942:Macrolides; D010718:Phosphatidylserines; C046785:bryostatin 1; D011493:Protein Kinase C; D013755:Tetradecanoylphorbol Acetate; D002118:Calcium