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PMID: 1436036 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Quantal transmitter secretion from myocytes loaded with acetylcholine.

Nature ·Vol. 359 ·No. 6397 ·1992-10-22 ·Pages 733-6

Dan Y, Poo MM

Abstract

It is well known that transmitter secretion requires specialized secretory organelles, the synaptic vesicles, for the packaging, storage and exocytotic release of the transmitter. Here we report that when acetylcholine (ACh) is loaded into an isolated Xenopus myocyte, there is spontaneous quantal release of ACh from the myocyte which results in activation of its own surface ACh channels and the appearance of membrane currents resembling miniature endplate currents. This myocyte secretion probably reflects Ca(2+)-regulated exocytosis of ACh-filled cytoplasmic compartments. Furthermore, step depolarization of the myocyte membrane triggers evoked ACh release from the myocyte with a weak excitation-secretion coupling. These findings suggest that quantal transmitter secretion does not require secretory pathways unique to neurons and that the essence of presynaptic differentiation may reside in the provision of transmitter supply and modification of the preexisting secretion pathway.

MeSH Terms
Acetylcholine/metabolism Acetylcholinesterase/metabolism Animals Calcium/physiology Cells, Cultured Exocytosis In Vitro Techniques Ion Channel Gating Muscles/cytology,metabolism Receptors, Nicotinic/metabolism Synaptic Vesicles/metabolism Xenopus laevis
Chemicals
Receptors, Nicotinic Acetylcholinesterase Acetylcholine Calcium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Dan Y
Department of Biological Sciences, Columbia University, New York, New York 10027.
Poo M M
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1992-10-22
Pages
733-6
Language
English
Region
England
NLM ID
0410462
Subset
IM
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