Open AccessDopamine and depolarizing agents regulate the state of phosphorylation of protein I in the mammalian superior cervical sympathetic ganglion.
Author(s) -
Eric J. Nestler,
Paul Greengard
Publication year - 1980
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.77.12.7479
Subject(s) - superior cervical ganglion , dopamine , protein kinase a , phosphorylation , veratridine , depolarization , protein phosphorylation , chemistry , ganglion , medicine , endocrinology , biology , biophysics , microbiology and biotechnology , biochemistry , neuroscience , sodium , sodium channel , organic chemistry
The regulation of the state of phosphorylation of protein I, a specific neuronal protein that appears to be associated predominantly with synaptic vesicles, has been studied in intact sections of bovine superior cervical ganglion. For this purpose, a technique was developed that made possible the quantitation of the state of phosphorylation of as little as 5 fmol of protein I. Incubation of ganglion sections in the presence of dopamine, 8-bromo-cyclic AMP, or depolarizing agents (i.e., high K+ concentration or veratridine) increased the state of phosphorylation of protein I relative to that of control ganglion sections. Other results indicated that the effect of dopamine is probably mediated via the activation of a cyclic AMP-dependent protein kinase and that the effect of high K+ concentration is probably mediated via the activation of a calcium-dependent protein kinase.