Abstract
Synaptoneurosomes (1–3 µm in diameter), prepared from rat brain stem or brain cortex, were fused with liposomes, producing a high yield of giant synaptosomes (10–60 µm in diameter). Single channel currents were measured by using the cell-attach patch-clamp technique. The membrane of the majority of these giant synaptosomes retained the cell membrane selective permeability. However, nonpermeating molecules, such as guanine nucleotides and antibodies directed against GTP-binding region in the α-subunit of trimeric GTP-binding proteins, were trapped in the giant synaptosomes during their preparation. Activation of Go proteins was assayed in high [K+]-depolarized giant synaptosomes, indicating the advantage of this preparation for tracing signal-transduction mechanisms in stimulated synaptic membranes. Stimulation-induced interactions between membrane proteins, either native or reconstituted, can be studied in the giant synaptosomes.
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Dekel, N., Visochek, L., Anis, Y. et al. Stimulation-induced modifications in go proteins examined in giant fused synaptosomes. J Mol Neurosci 20, 73–80 (2003). https://doi.org/10.1385/JMN:20:1:73
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DOI: https://doi.org/10.1385/JMN:20:1:73