Journal of Cell Science, Vol 106, Issue 3 731-740, Copyright © 1993 by Company of Biologists

JOURNAL ARTICLES

Regulated and constitutive secretion of distinct molecular forms of acetylcholinesterase from PC12 cells

ES Schweitzer
Department of Anatomy and Cell Biology, UCLA Medical School.

PC12 cells secrete the enzyme acetylcholinesterase (AChE) while at rest, and increase the overall rate of this secretion 2-fold upon depolarization. This behavior is different from the release of other markers by the constitutive or regulated secretory pathways in PC12 cells. Both the resting and stimulated release of AChE are unchanged after treatment with a membrane-impermeable esterase inhibitor, demonstrating that it represents true secretion and not shedding from the cell surface. The stimulation release of AChE is Ca(2+)-dependent, while the unstimulated release is not. Analysis of the molecular forms of AChE secreted by PC12 cells indicates that the release of AChE actually involves two concurrent but independent secretory processes, and that the G4 form of the enzyme is secreted constitutively, while both the G2 and G4 forms are secreted in a regulated manner, presumably from regulated secretory vesicles. Compared with other regulated secretory proteins, a much smaller fraction of cellular AChE is secreted, and the intracellular localization of this enzyme differs from that of other regulated secretory proteins. The demonstration that a cell line that exhibits regulated secretion of acetylcholine (ACh) is also capable of regulated secretion of AChE provides additional evidence for the existence of multiple regulated secretory pathways within a single cell. Moreover, there appears to be a selective packaging of different molecular forms of AChE into the regulated versus the constitutive secretory pathway. Both the specificity of sorting of AChE and the regulation of its secretion suggest that AChE may play a more dynamic role in synaptic function than has been recognized previously.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    Twitter    What's this?

This article has been cited by other articles:

				G. Li, L. Han, T.-C. Chou, Y. Fujita, L. Arunachalam, A. Xu, A. Wong, S.-K. Chiew, Q. Wan, L. Wang, et al. RalA and RalB Function as the Critical GTP Sensors for GTP-Dependent Exocytosis J. Neurosci., January 3, 2007; 27(1): 190 - 202. [Abstract] [Full Text] [PDF]

				A Balogh, S Cadel, T Foulon, R Picart, A Der Garabedian, A Rousselet, C Tougard, and P Cohen Aminopeptidase B: a processing enzyme secreted and associated with the plasma membrane of rat pheochromocytoma (PC12) cells J. Cell Sci., January 1, 1998; 111(2): 161 - 169. [Abstract] [PDF]

				M. Passafaro, P. Rosa, C. Sala, F. Clementi, and E. Sher N-type Ca2+ Channels Are Present in Secretory Granules and Are Transiently Translocated to the Plasma Membrane during Regulated Exocytosis J. Biol. Chem., November 22, 1996; 271(47): 30096 - 30104. [Abstract] [Full Text] [PDF]

				E. Schweitzer, M. Sanderson, and C. Wasterlain Inhibition of regulated catecholamine secretion from PC12 cells by the Ca2+/calmodulin kinase II inhibitor KN-62 J. Cell Sci., January 7, 1995; 108(7): 2619 - 2628. [Abstract] [PDF]