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The present studies were carried out to determine if tyrosine hydroxylase phosphorylation in rat brain striatal synaptosomes is activated by dibutyryl cyclic AMP treatment. Incubation of synaptosomes with [32P]orthophosphate, followed by immunoprecipitation and sodium dodecyl sulfate polyacrylamide gel electrophoresis, produced a band of radioactivity associated with a 62 kDa polypeptide. Treatment with the catecholamine neurotoxin, 6-hydroxydopamine, produced parallel losses of: (1) tyrosine hydroxylase enzyme activity, (2) dopamine content, and (3) the 62 kDa band of radioactivity. These data support the identification of this band as a tyrosine hydroxylase-derived polypeptide. Incubation with dibutyryl cyclic AMP produced an increase in soluble tyrosine hydroxylase activity and phosphorylation. These results suggest that the increase in synaptosomal catecholamine synthesis produced by dibutyryl cyclic AMP is mediated by an increase in tyrosine hydroxylase phosphorylation.
K A Colby, and
T L Thompson, and
R L Patrick
October 1976,
Biochemical pharmacology,
K A Colby, and
T L Thompson, and
R L Patrick
May 1994,
Neurochemical research,
K A Colby, and
T L Thompson, and
R L Patrick
September 1992,
Journal of neurochemistry,
K A Colby, and
T L Thompson, and
R L Patrick
March 1991,
The Journal of biological chemistry,
K A Colby, and
T L Thompson, and
R L Patrick
July 1980,
Molecular pharmacology,
K A Colby, and
T L Thompson, and
R L Patrick
January 1994,
Journal of neural transmission. General section,
K A Colby, and
T L Thompson, and
R L Patrick
January 2008,
Neuroreport,
K A Colby, and
T L Thompson, and
R L Patrick
May 1989,
Journal of neurochemistry,
K A Colby, and
T L Thompson, and
R L Patrick
January 1983,
Neurochemistry international,
K A Colby, and
T L Thompson, and
R L Patrick
July 1988,
Brain research,
