Enhancement of calcium current in Aplysia neurones by phorbol ester and protein kinase C.
One of the molecular mechanisms capable of regulating the physiological properties of neurones is the phosphorylation of ion channels and other cellular components by cyclic AMP-dependent protein kinase. Another protein kinase present in high concentrations in the mammalian brain is protein kinase C (a calcium/phosphatidylserine/diacylglycerol-dependent protein kinase), but there is no direct evidence, as yet, for the involvement of this enzyme in the control of neuronal excitability. We now present evidence that activation of endogenous protein kinase C by the tumour-promoting phorbol ester TPA (12-O-tetradecanoyl- phorbol-13-acetate), or intracellular injection of the purified enzyme, enhances the voltage-sensitive calcium current in bag cell neurones of the mollusc Aplysia.
DeRiemer
S A
SA
Strong
J A
JA
Albert
K A
KA
Greengard
P
P
Kaczmarek
L K
LK
D000200:Action Potentials / Q000187:drug effects; D000818:Animals; D001048:Aplysia / Q000502:physiology*; D002118:Calcium / Q000378:metabolism*; D004789:Enzyme Activation / Q000187:drug effects; D007473:Ion Channels / Q000502:physiology*; D009474:Neurons / Q000187:drug effects / Q000502:physiology*; D010704:Phorbols / Q000494:pharmacology*; D011188:Potassium / Q000378:metabolism; D011493:Protein Kinase C; D011494:Protein Kinases / Q000494:pharmacology*; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology*
D007473:Ion Channels; D010704:Phorbols; D011494:Protein Kinases; D011493:Protein Kinase C; D013755:Tetradecanoylphorbol Acetate; D011188:Potassium; D002118:Calcium