Regulation of human tyrosine hydroxylase activity. Effects of cyclic AMP-dependent protein kinase, calmodulin-dependent protein kinase II and polyanion.
To determine the regulatory mechanism for human tyrosine hydroxylase, we examined modulations of the activity of the enzyme from human pheochromocytoma by cyclic AMP-dependent protein kinase, calmodulin-dependent protein kinase II and polyanion. The most remarkable activation was observed when the enzyme was assayed at physiological pH (pH 7) after being subjected to phosphorylation by cyclic AMP-dependent protein kinase. Calmodulin-dependent protein kinase II and polyanion also modulated the enzyme activity. The results suggest that tyrosine hydroxylase may be regulated similarly in both human and rat.
Okuno
S
S
Department of Biochemistry, Asahikawa Medical College, Japan.
Kanayama
Y
Y
Fujisawa
H
H
D000818:Animals; D016264:Dextran Sulfate; D003911:Dextrans / Q000494:pharmacology; D006801:Humans; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D010673:Pheochromocytoma; D000071228:Polyelectrolytes; D011108:Polymers / Q000494:pharmacology*; D011494:Protein Kinases / Q000502:physiology*; D051381:Rats; D014407:Tumor Cells, Cultured; D014446:Tyrosine 3-Monooxygenase / Q000378:metabolism*
D016264:Dextran Sulfate; D003911:Dextrans; D000071228:Polyelectrolytes; D011108:Polymers; D011494:Protein Kinases; D014446:Tyrosine 3-Monooxygenase