Two Studies on Protein Phosphorylation in Synaptic Plasma Membrane
Gardner, Glendon M.
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An essay involving radioactive labeling, gel electrophoresis and autoradiography was used to study protein phosphorylation in synaptic plasma membrane. Protein phosphorylation is a regulatory process found in the body involving the activation or inactivation of ennzymes via the addition of a phosphate group. This group is the -phosphate group of adenosine triphosphate(ATP). It has recently been demonstrated that Ca2+ and calmodulin(CDR), together, stimulate protein phosphorylation. Calmodulin, a calcium binding protein, is present throughout the body and has been shown to play an integral role in the regulatory functions of Ca2+. Two studies of Ca-CDR-dependent protein phosphorylation were begun. The first of these investigated the effects of various neuropeptides on phosphorylation. Neuropeptides are short-chain polypeptides found in the brain with various physiological properties. The preliminary results of this study were interpreted to determine if protein phosphorylation plays a role in the neuropeptides' mechanism of action. A second study was begun involving protein phosphorylation in 17 distinct regions of rat brain. These preliminary results were interpreted to determine if there exist any significant differences among the protein kinases of different brain regions. These two studies serve as a good demonstration of the versatility of the technique employed here.