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Specific binding of α-bungarotoxin to synaptic membranes in rat sympathetic ganglion: Computer best-fit analysis of electron microscope radioautographs
Journal article   Peer reviewed

Specific binding of α-bungarotoxin to synaptic membranes in rat sympathetic ganglion: Computer best-fit analysis of electron microscope radioautographs

Arnold J. Smolen
Brain research, v 289(1), pp 177-188
1983
PMID: 6661642

Abstract

alpha-bungarotoxin cholinergic receptor radioautography sympathetic ganglion
In the rat superior cervical sympathetic ganglion (SCG), α-bungarotoxin (αBT) demonstrates binding that is saturable and inhibited by nicotinic ligands. However, αBT does not inhibit the physiological response of ganglionic neurons to preganglionic stimulation or to exogenously applied acetylcholine. Thus the specificity of αBT for ganglionic nicotinic cholinergic receptors has been questioned. The present study provides a morphological localization of the binding sites of 125I-labelled αBT in the rat SCG using the method of Blackett and Parry on electron microscopic radioautographs. The distribution of grains resulting from specific binding was calculated by substracting the nonspecific distribution (αBT in the presence of d-tubocurarine, a known nicotinic ligand) from the total grain distribution (αBT alone). A hypothetical grain distribution was obtained based on the geometrical properties of the tissue sections. A computer minimizing routine was employed to adjust the relative weights of each of the potential sources of hypothetical grains until a ‘best-fit’ with the real grain distributions occurred. The nonspecific binding of αBT was uniform across all tissue components, with the exception of a significant concentration on the membrane of the ganglion cell body. By contrast, the specific binding of αBT was highly localized to synaptic membranes, and to a lesser extent, to dendritic membranes.

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