Regulation of human tyrosine hydroxylase activity. Effects of cyclic AMP-dependent protein kinase, calmodulin-dependent protein kinase II and polyanion.

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Okuno S,Kanayama Y,Fujisawa H

doi

10.1016/0014-5793(89)80927-5

subject

Has Abstract

pub_date

1989-08-14 00:00:00

pages

52-4

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(89)80927-5

journal_volume

253

pub_type

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