Voltage-sensitive sodium channels: an evolving molecular view.

R L Barchi; J M Casadei; R D Gordon; R H Roberts

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PubMed · 2436306

Voltage-sensitive sodium channels: an evolving molecular view.

R L Barchi·J M Casadei·R D Gordon·R H Roberts

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Abstract

Sodium channel proteins have now been isolated from a number of nerve and muscle preparations. All are characterized by the presence of a very large glycoprotein subunit of approximately 260 kilodaltons which may contain the structural features required for voltage-dependent channel gating and cation selectivity. These purified proteins have been reconstituted into vesicle systems and planar bilayers and demonstrate the ensemble and single-channel behavior characteristic of the native sodium channel. Although the sodium channel from eel appears to consist of only the 260-kilodalton protein, the channels from rat brain and rat or rabbit skeletal muscle contain one or more smaller subunits of 37-39 kilodaltons. In skeletal muscle, a 38-kilodalton subunit is present in both conventionally purified channel and channel isolated with immunoaffinity techniques. The stoichiometry of the large (alpha) and the small (beta) subunits appears to be 1:1 in skeletal muscle but 1:2 in rat brain. The role of the small subunits in the normal functioning of the sodium channel remains to be defined.

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Animals Carbohydrates Glycoproteins Ion Channels Macromolecular Substances Membrane Potentials Molecular Weight Muscles Rabbits Sodium Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.Review

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R L Barchi, J M Casadei, R D Gordon, R H Roberts. 1987. Voltage-sensitive sodium channels: an evolving molecular view.. https://pubmed.ncbi.nlm.nih.gov/2436306/

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