RGD Reference Report - beta-Bungarotoxin blocks phorbol ester-stimulated phosphorylation of MARCKS, GAP-43 and synapsin I in rat brain synaptosomes. - Rat Genome Database

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beta-Bungarotoxin blocks phorbol ester-stimulated phosphorylation of MARCKS, GAP-43 and synapsin I in rat brain synaptosomes.

Authors: Ueno, E  Rosenberg, P 
Citation: Ueno E and Rosenberg P, Toxicon. 1995 Jun;33(6):747-62.
RGD ID: 9685336
Pubmed: PMID:7676466   (View Abstract at PubMed)

The phospholipase A2 neurotoxin, beta-bungarotoxin, presynaptically blocks acetylcholine release. Its mechanism of action is unknown; however, our previous studies suggest that it inhibits phosphorylation of synaptosomal proteins, which might be expected to decrease neurotransmitter release. In our present study, we found that 1 nM beta-BuTX blocked phorbol ester-stimulated phosphorylation of GAP-43, MARCKS and synapsin I without affecting their basal phosphorylation. In contrast, a 1 nM concentration of the non-neurotoxic enzyme. Naja naja atra phospholipase A2 did not affect the phorbol ester-stimulated phosphorylation of these proteins but increased the basal phosphorylation of GAP-43 and MARCKS. Although it has been suggested that cytosolic calmodulin is increased by phosphorylation of the protein kinase C substrates, GAP-43 and MARCKS, we found no change in calmodulin levels by phorbol ester or beta-bungarotoxin. The stimulation of phosphorylation by Naja naja atra phospholipase A2 may be due to products liberated as a result of its phospholipase A2 activity. In contrast, the inhibition of phosphorylation by beta-bungarotoxin appears to be due to an action which may be unrelated its relatively weak phospholipase A2 activity. Inhibition of phosphorylation by beta-bungarotoxin is a possible mechanism by which it could block acetylcholine release. Furthermore, beta-bungarotoxin may be a useful tool to study the physiological role of phosphorylation of synaptosomal proteins in neurotransmitter release.

Objects referenced in this article
Gene Marcks myristoylated alanine rich protein kinase C substrate Rattus norvegicus

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