Relationship between activation and phosphorylation of tyrosine hydroxylase by 56 mm K+ in PC12 cells in culture.
Incubation of rat pheochromocytoma PC12 cells with 56 mM K+ is associated with increased activity and enhanced phosphorylation of tyrosine hydroxylase in the cells. The increase in the phosphorylation of tyrosine hydroxylase is observed after 30 sec of incubation with 56 mM K+; maximal phosphorylation is observed after 1 min of incubation. In contrast, although a significant increase in the activity of tyrosine hydroxylase is demonstrable after 30 sec of incubation with 56 mM K+, maximal activation is not attained until 3 min of incubation. Both the activation and increased phosphorylation of tyrosine hydroxylase exhibit a similar dependence upon potassium concentration in the incubation medium and are dependent on the presence of extracellular calcium. These results suggest that, although there is a relationship between activation and phosphorylation of tyrosine hydroxylase after potassium-evoked depolarization of rat pheochromocytoma PC12 cells in culture, this relationship may be complex.
D000310:Adrenal Gland Neoplasms / Q000201:enzymology*; D000818:Animals; D002460:Cell Line; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D007700:Kinetics; D008970:Molecular Weight; D009994:Osmolar Concentration; D010673:Pheochromocytoma / Q000201:enzymology*; D010766:Phosphorylation; D011188:Potassium / Q000494:pharmacology*; D051381:Rats; D014446:Tyrosine 3-Monooxygenase / Q000302:isolation & purification / Q000378:metabolism*
D014446:Tyrosine 3-Monooxygenase; D011188:Potassium