The synaptophysin (p38), a transmembrane glycoprotein of synaptic vesicles, has been used as a marker in order to study the membrane events that take place during transmitter release at the mouse neuromuscular junction (NMJ). p38 has been labelled by immunofluorescence using a monoclonal anti-p38 antibody and fluorescein-conjugated IgG on dissociated muscle fibres (biceps brachialis m.). Its localization has been compared to that of the acetylcholine (ACh) receptors labelled with rhodaminated alpha-bungarotoxin. A weak labelling was obtained in nerve-muscle preparations at rest only when the muscle fibres were permeabilized with Triton X-100. By contrast, an intense immunofluorescence of the NMJ was observed after an exhaustive ACh release induced by Cd2+ in Ca(2+)-free medium, which leads to a synaptic vesicle depletion and an increase in the membranous structures in nerve terminals. Treatment with Cd2+ in Ca(2+)-free solution leads to both synaptic vesicle depletion and p38 immunolabelling, which is in favour of synaptic vesicle fusion and incorporation into the axolemma.
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