The incorporation of hydrophobic protein receptors and artificial lipid membranes.
The mechanism of chemical synaptic transmission implies: 1) the existence of a specific protein receptor at the postsynaptic membrane, and 2) the interaction between the transmitter released and the receptor, thus producing a change in ionic permeability. Previous studies from our laboratory have shown that special hydrophobic proteins extracted from postsynpatic membranes of different tissues showed a high affinity binding for the different pharmacological agents. The present paper describes experiments in which different hydrophobic protein binding acetylcholine, noradrenaline, gamma-aminobutyric acid, and glutamate were incorporated into artificial lipid membranes, similar to those first described by Mueller et al. (19). The effect of the different pharmacological agents was tested under experimental conditions of voltage clamp and the d.c. current changes measured. The results were then compared for the different lipid-protein membranes employed during the steady state and during transient conductance changes. The specificity of the responses indicate that artificial lipid membranes containing these hydrophobic proteins from electroplax, myocardium, spleen capsule and shrimp muscle can be used as a model to study pharmacologic receptors.
D000109:Acetylcholine / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D001667:Binding, Competitive; D004553:Electric Conductivity; D004557:Electric Organ / Q000378:metabolism; D005399:Fishes; D007700:Kinetics; D008074:Lipoproteins; D008567:Membranes, Artificial; D008954:Models, Biological; D009419:Nerve Tissue Proteins / Q000378:metabolism; D010713:Phosphatidylcholines; D011485:Protein Binding; D011950:Receptors, Cholinergic; D012997:Solvents
D008074:Lipoproteins; D008567:Membranes, Artificial; D009419:Nerve Tissue Proteins; D010713:Phosphatidylcholines; D011950:Receptors, Cholinergic; D012997:Solvents; D000109:Acetylcholine