Abstract
Previously we showed that the activity of the gamma-aminobutyric acid-synthesizing enzyme L-glutamate decarboxylase (GAD) in crude brain extract is inhibited by ATP and protein phosphatase inhibitors. We suggested that GAD activity is regulated by protein phosphorylation. In this paper we further present evidence to support our hypothesis that protein kinase A and calcineurin may be involved in regulation of GAD activity through phosphorylation and dephosphorylation fo GAD, respectively. In addition, the effect of neuronal stimulation on GAD activity in cultured neurons is also included. A model to link neuronal excitation and activation of GAD by Ca(2+)-dependent phosphatase is proposed.
Highlights
From the fI]epartment of Physiology and Cell Biology, University ofKansas, Lawrence, Kansas 66045 and the "Institute of Biomedical Sciences, Academia Sinica, Taipei, 11529, Taiwan
We suggested that glutamate decarboxylase (GAD) activity is regulated by protein phosphorylation
In this paper we further present evidence to support our hypothesis that protein kinase A and calcineurin may be involved in regulation of GAD activity through phosphorylation and dephosphorylation of GAD, respectively
Summary
Dept. of Physiology and Cell Biology, University of Kansas, Haworth Hall, Lawrence, KS 66045. Based on the results presented in this paper and those reported in the literature, a model is proposed to link neuronal excitation to activation of GAD through Ca2 + -depsndent dephosphorylation
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