Open AccessProtein kinase C regulates ionic conductance in hippocampal pyramidal neurons: electrophysiological effects of phorbol esters.
Author(s) -
Jay M. Baraban,
Solomon H. Snyder,
Bradley E. Alger
Publication year - 1985
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.82.8.2538
Subject(s) - protein kinase c , phorbol , protein kinase a , hippocampal formation , chemistry , biochemistry , calcium , hyperpolarization (physics) , microbiology and biotechnology , biology , kinase , biophysics , neuroscience , stereochemistry , organic chemistry , nuclear magnetic resonance spectroscopy
The vertebrate central nervous system contains very high concentrations of protein kinase C, a calcium- and phospholipid-stimulated phosphorylating enzyme. Phorbol esters, compounds with inflammatory and tumor-promoting properties, bind to and activate this enzyme. To clarify the role of protein kinase C in neuronal function, we have localized phorbol ester receptors in the rat hippocampus by autoradiography and examined the electrophysiological effects of phorbol esters on hippocampal pyramidal neurons in vitro. Phorbol esters blocked a calcium-dependent potassium conductance. In addition, phorbol esters blocked the late hyperpolarization elicited by synaptic stimulation even though other synaptic potentials were not affected. The potencies of several phorbol esters in exerting these actions paralleled their affinities for protein kinase C, suggesting that protein kinase C regulates membrane ionic conductance.