Elsevier

Brain Research Bulletin

Volume 19, Issue 6, December 1987, Pages 619-622
Brain Research Bulletin

Article
Stimulation-Dependent phosphorylation of tyrosine hydroxylase in rat corpus striatum

https://doi.org/10.1016/0361-9230(87)90046-3Get rights and content

Abstract

Incubation of rat corpus striatal synaptosomes with 32PO4 led to a time-dependent incorporation of 322P into tyrosine hydroxylase. Depolarization of the synaptosomes with elevated [K+]0 increased 32P incorporation into tyrosine hydroxylase. The depolarization-dependent increase in 32P incorporation into tyrosine hydroxylase occurred rapidly (<15 sec), persisted in the presence of elevated [K+]0 (up to 120 sec), required the presence of [Ca++]0, and was associated with serine (but not threonine or tyrosine) residues. After limit tryptic digestion of the 32P-tyrosine hydroxylase, several phosphopeptides were separated by HPLC, and elevated [K-]0 increased 32P incorporation into two of these phosphopeptides. Thus, depolarization of dopaminergic terminals from the rat corpus striatum increased the phosphorylation of tyrosine hydroxylase, and the increase in phosphorylation appeared to occur at multiple sites. Multiple-site phosphorylation of tyrosine hydroxylase has been previously shown in peripheral catecholaminergic tissues. However, substantial differences in the elution profiles of tyrosine hydroxylase phosphopeptides from striatal synaptosomes and from bovine adrenal chromaffin cells were observed. Thus, qualitative differences in the regulation of tyrosine hydroxylase may exist among the many catecholaminergic systems.

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