Protein Kinase C Enhances Exocytosis from Chromaffin Cells by Increasing the 
Size of the Readily Releasable Pool of Secretory Granules

Gillis, K. D.; Mossner, R.; Neher, E.

doi:10.1016/S0896-6273(00)80147-6

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Protein Kinase C Enhances Exocytosis from Chromaffin Cells by Increasing the Size of the Readily Releasable Pool of Secretory Granules

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Gillis, K. D.
Department of Membrane Biophysics, MPI for biophysical chemistry, Max Planck Society;

Mossner, R.
Department of Membrane Biophysics, MPI for biophysical chemistry, Max Planck Society;

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Neher, E.
Department of Membrane Biophysics, MPI for biophysical chemistry, Max Planck Society;

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Citation

Gillis, K. D., Mossner, R., & Neher, E. (1996). Protein Kinase C Enhances Exocytosis from Chromaffin Cells by Increasing the Size of the Readily Releasable Pool of Secretory Granules. Neuron, 16(6), 1209-1220. doi:10.1016/S0896-6273(00)80147-6.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0013-0169-A

Abstract

We have used membrane capacitance measurements to assay Ca2+-triggered exocytosis in single bovine adrenal chromaffin cells. Brief application of phorbol ester (PMA) enhances depolarization-evoked exocytosis severalfold while actually decreasing the Ca2+ current. Ca2+ metabolism is unchanged. Three different protocols were used to show that PMA increases the size of the readily releasable pool of secretory granules. PMA treatment leads to a large increase in amplitude, but little change in the time course of the exocytic burst that results from rapid elevation of [Ca2+]i upon photolysis of DM-Nitrophen. Thus, PKC appears to affect a late step in secretion but not the Ca2+ sensitivity of the final step.