Summary |
Neurotransmitter release occurs when depolarization of the membrane of presynaptic nerve terminals opens voltage-sensitive calcium channels, and allows calcium influx and diffusion into the cell. The rise in intracellular calcium binds intracellular receptor proteins that mediate the fusion of synaptic vesicles with the presynaptic plasma membrane resulting in the release of vesicle contents (quanta) to postsynaptic receptors. There are many stages involved that prepare a nerve terminal that is at rest (polarized plasma membrane) for exocytosis and subsequent reactivation in response to subsequent action potentials. In order for neurons to respond to constant or repeated stimuli, neurons have networked many regulatory pathways to modulate signal transduction and synaptic vesicle recycling. Surface receptors are coupled to cytosolic regulatory molecules through four major second messenger pathways mediated by cyclic adenosine monophosphate (cAMP), cyclic guanosine monophosphate (cGMP), calcium and the hydrolysis products of phosphatidylinositol. These second messengers catalyze the transfer of the r-phosphate from ATP to proteins that cause a conformational change which can regulate their function. Much attention has been focused on protein kinase C (PKC) as a possible mechanism in the phosphorylation of signal transduction cascades to facilitate glutamate exocytosis. This study attempts to elucidate the effect PKC activation has on the cascade of events modulating exocytosis. Specifically, examining the activation of PKC through the use of phorbol esters and its effects on K'^-evoked release of glutamate from hippocampal mossy fiber synaptosomes. |
General note | Submitted to the faculty of the Department of Biology. |
General note | Advisor: David M. Terrian |
Dissertation note | M.S. East Carolina University 1994 |
Bibliography note | Includes bibliographical references (leaves 124-134). |
Genre/form | Academic theses. |
Genre/form | Academic theses. |
Genre/form | Thèses et écrits académiques. |