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alpha-Bungarotoxin binding and cholinergic receptor function on a rat sympathetic nerve line
The Journal of Biological Chemistry
|December 10, 1977
Summary
PC12 cells bind alpha-bungarotoxin reversibly, unlike muscle cells. Cholinergic ligands affect PC12 cell function differently than they inhibit toxin binding, indicating distinct binding sites.
Area of Science:
- Neuroscience
- Cell Biology
- Pharmacology
Background:
- The PC12 cell line, derived from rat sympathetic neurons, is a model for studying neuronal function.
- Alpha-bungarotoxin is a known ligand for nicotinic acetylcholine receptors.
Purpose of the Study:
- To characterize the binding of alpha-bungarotoxin to PC12 cells.
- To investigate the relationship between cholinergic ligand binding and functional effects on PC12 cells.
Main Methods:
- Radioligand binding assays using iodinated alpha-bungarotoxin.
- Measurement of agonist-induced sodium ion permeability.
- Sucrose gradient centrifugation in the presence of Triton X-100.
Main Results:
- PC12 cells exhibit saturable and reversible binding of alpha-bungarotoxin.
- The binding component is an integral membrane protein with a sedimentation coefficient of 10.5 S.
- No correlation was found between the ability of cholinergic ligands to affect receptor function and inhibit alpha-bungarotoxin binding.
Conclusions:
- PC12 cells possess a distinct binding site for alpha-bungarotoxin.
- Cholinergic ligands interact with at least two different sites on PC12 cells: one mediating functional responses and another for toxin binding.