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Vasoactive Intestinal Peptide Stimulates Catecholamine Biosynthesis in Isolated Adrenal Chromaffin Cells: Evidence for a Cyclic AMP‐Dependent Phosphorylation and Activation of Tyrosine Hydroxylase
Author(s) -
Waymire J. C.,
Craviso G. L.,
Lichteig K.,
Johnston J. P.,
Baldwin C.,
Zigmond R. E.
Publication year - 1991
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1991.tb08296.x
Subject(s) - vasoactive intestinal peptide , forskolin , tyrosine hydroxylase , phosphorylation , medicine , catecholamine , endocrinology , biosynthesis , biology , tyrosine , protein kinase a , tyrosine phosphorylation , protein phosphorylation , protein kinase c , tyrosine 3 monooxygenase , chemistry , biochemistry , dopamine , enzyme , neuropeptide , stimulation , receptor
Vasoactive intestinal peptide (VIP) increased catecholamine biosynthesis in bovine adrenal chromaffin cells by 50–200%. Six related peptides produced no effects. In addition, VIP increased tyrosine hydroxylase (TH) activity measured in gel‐filtered supernatants prepared from homogenates of treated cells. The hypothesis that cyclic AMP is the second messenger involved in these effects of VIP was also evaluated. VIP led to an elevation of cyclic AMP levels, and this increase occurred over a similar concentration range and time course as the activation of TH and the increase in catecholamine biosynthesis. Each measure reached maximal levels at 10–20 γ M VIP within 1 min and remained elevated for at least 16 min. These changes produced by VIP were paralleled by enhanced phosphorylation of TH, and this phosphorylation occurred on a single tryptic peptide that was the same peptide whose phosphorylation has been previously shown to be stimulated by forskolin. In contrast to VIP and forskolin, 12‐ O ‐tetradecanoylphorbol 13‐acetate, a phorbol ester known to activate protein kinase C, increased the phosphorylation on a total of three tryptic peptides of TH. Our results indicate that VIP stimulates catecholamine biosynthesis in chromaffin cells through the phosphorylation and activation of TH and support the conclusion that a cyclic AMP‐dependent phosphorylation of TH is responsible for these effects.