[Aqueous pores of the protein globule in the sodium channel associated with its gating mechanism].
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Biomedical subjects
Publications and source records attributed to Z A Sorokina.
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The paper summarizes the results obtained from the 10-12 years studies on the mechanism of action of blocking toxins--tetrodotoxin (TTX) and saxitoxin (STX)--on voltage-operated sodium channels. Experimental data can be interpreted on the basis of two models of blocking action of toxins: channel blockade, when guanidine group of toxins penetrates into the channel and causes its blockade and allosteric action on sodium conductance. Special attention is devoted to peculiarities of cooperative interaction between the blockers and channels. The analysis of experimental findings permits a better understanding of functional organization of sodium channels, in particular, the interrelation between the receptor of blocking toxins and its other structural elements.
The temperature dependence of the effect of transmembrane osmotic pressure on sodium TTX-sensitive inward current was studied on isolated neurons of rat dorsal root ganglia using intracellular perfusion under voltage clamp conditions. It was found that the effect of transmembrane osmotic pressure on the kinetic parameters of sodium current does not depend on temperature in a wide range (from 8 to 40 degrees C). The apparent values of activation energies for the activation and inactivation processes do not depend on osmolality. The overall results indicate that the most satisfactory way to account for the present observations is to postulate that the effect of transmembrane osmotic pressure is determined by the water flux crossing the membrane. It is supposed that this flux takes place within the protein molecule which forms the sodium channel. The molecular mechanisms of interaction between water pathways and gating are discussed.
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