Developmental change in the modulation of acetylcholine receptor channel by protein kinase C activation in Xenopus embryonic muscle cells
Journal
Neuroscience Letters
Journal Volume
164
Journal Issue
1????
Pages
97-100
Date Issued
1993
Author(s)
Lin J.-L.
DOI
3043940
Abstract
Protein phosphorylation is important in synaptic transmission and plasticity. We report here that phorbol 12-myristate 13-acetate (TPA), a protein kinase C (PKC) activator, enhances the postsynaptic response at developing neuromuscular junctions by increasing the open time of embryonic acetylcholine (ACh) channels at earlier stages of cultured myocytes. Compared with day-1 cultures, the effects of TPA declined or disappeared on day-3 cultures. Adenosine 5'-triphosphate (ATP) which is co-stored and co-released with ACh at motor nerve terminals and is reported to enhance spontaneous synaptic currents by the activation of PKC, also shows similar developmental changes in the modulation of embryonic ACh channels in Xenopus embryonic myocytes.
Type
journal article