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  • Title: Inhibition of nicotinic receptor mediated ion fluxes in rat sympathetic ganglia by BGT II-S1 a potent phospholipase.
    Author: Quik M.
    Journal: Brain Res; 1985 Jan 28; 325(1-2):79-88. PubMed ID: 3978435.
    Abstract:
    The mechanism of action of the bungarotoxin fraction II-S1 (BGT II-S1), which copurifies with alpha-bungarotoxin (alpha-BGT) and inhibits nicotinic transmission, has been further characterized. BGT II-S1 (1 microM) inhibited the carbachol (100 microM) or nicotine (50 microM) stimulated uptake of [3H]agmatine into rat sympathetic ganglia by 73% and 52%, respectively. These responses were inhibited 90% by D-tubocurarine (100 microM), but unaffected by alpha-BGT (1 microM) or atropine (10 microM), suggesting that BGT II-S1 affects nicotinic function at a postsynaptic site. Binding of physiologically active [125I]BGT II-S1 could be demonstrated to intact sympathetic ganglia; however, the binding could not be displaced by nicotinic agents, suggesting that BGT II-S1 is not interacting at the receptor. Because some neurotoxins produce their effect at the synapse through a phospholytic action, the phospholipase activity of BGT II-S1 was determined. The results demonstrate that BGT II-S1 is a very potent calcium dependent phospholipase. In addition, conditions which abolished the toxin's phospholytic activity prevented its effects on nicotinic transmission and on nicotinic receptor mediated ion fluxes. These include irreversible inhibition of enzymic activity by treatment of BGT II-S1 with p-bromophenacylbromide, as well as reversible inhibition of the phospholipase by substitution of Ba2+ or Sr2+ ions for Ca2+ ions in the physiological medium. Thus, in rat sympathetic ganglia, BGT II-S1 blocks the nicotinic receptor mediated movement of ions across the membrane. This is probably not due to a direct interaction at the nicotinic acetylcholine recognition site; rather, it may be an ion channel associated effect which is mediated by alterations in the phospholipid environment of the receptor complex or of the membrane. Although BGT II-S1 also has presynaptic actions, in a cultured system of postsynaptic cells, it could prove a useful tool to study the role of phospholipids in neuronal nicotinic receptor regulation.
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