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Journal of Neuroscience, Vol 3, 260-271, Copyright © 1983 by Society for Neuroscience
The ultrastructural localization of alpha-bungarotoxin binding sites in relation to synapses on chick ciliary ganglion neurons
MH Jacob and DK Berg
The distribution of alpha-bungarotoxin binding sites on chick ciliary
ganglion neurons was examined at the ultrastructural level by incubating
ganglia with horseradish peroxidase-conjugated toxin and examining the
peroxidase-stained and thin-sectioned ganglia with the electron microscope.
Both in embryonic and in adult ganglia heavy labeling was restricted to the
surface membrane of short processes emerging from the ciliary and choroid
cell somata in the region of preganglionic innervation. Less dense labeling
occasionally was present on the smooth surface membrane of the soma in the
same region. In contrast, the pre- and postsynaptic membranes of most
synapses were clearly not labeled even in the immediate vicinity of heavily
labeled processes. The labeling represented specific binding of the toxin
conjugate since it could be prevented by d-tubocurarine and hexamethonium
or by unconjugated toxin. The conjugated toxin was not excluded from the
synaptic cleft on the basis of size because a substantially larger protein
conjugate, a horseradish peroxidase- labeled monoclonal antibody, was able
to enter the cleft and heavily label synaptic membranes as well as soma
membranes. Even neurons in adult ganglia had very little synaptic labeling
after exposure to the conjugated toxin. These results strongly suggest that
the high affinity alpha-bungarotoxin binding sites on chick ciliary
ganglion neurons are different from the synaptic ACh receptors which would
be expected to be concentrated in the postsynaptic membrane. Clustering of
the alpha- bungarotoxin binding sites in the vicinity of synapses, however,
may reflect a related synaptic function.
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