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 e...

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Bibliographic Details
Published in:FEBS letters 1989-08, Vol.253 (1), p.52-54
Main Authors: Okuno, Sachiko, Kanayama, Yoshiharu, Fujisawa, Hitoshi
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Dextran Sulfate
Dextrans - pharmacology
dopa, 3,4-dihydroxyphenylalanine
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Hepes, 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid
Human pheochromocytoma
Humans
Hydrogen-Ion Concentration
In Vitro Techniques
man
Mes, 2-(N-morpholino)ethanesulfonic acid
Oxidoreductases
Pheochromocytoma
Polyanion
polyanions
Polymers - pharmacology
protein kinase
protein kinase II
Protein kinase II, calmodulin-dependent
Protein kinase, cyclic AMP-dependent
Protein Kinases - physiology
Rats
Tumor Cells, Cultured
Tyrosine 3-Monooxygenase - metabolism
Tyrosine hydroxylase
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(89)80927-5