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Biochemical studies of the structure, mechanism and differentiation of the voltage-sensitive sodium channel
M Lazdunski1, M Balerna, J Barhanin
1Centre de Biochimie du CNRS, Faculté des Sciences, Parc Valrose, 06034 NICE CEDEX, France.
Neurochemistry International
|May 22, 2010
Abstract:
This paper describes how neurotoxins specific of the Na(+) channel are used to study its function, its structure and its differentiation in a variety of excitable and non-impulsive cells.
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Generally, all voltage-gated ion channels have a 'voltage-sensing domain' that spans the lipid bilayer. The charged residues in the sensor move in response to the membrane potential changes that open the channel allowing ions movement. There are several types of...
Generally, all voltage-gated ion channels have a 'voltage-sensing domain' that spans the lipid bilayer. The charged residues in the sensor move in response to the membrane potential changes that open the channel allowing ions movement. There are several types of...
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Voltage-gated ion channels are transmembrane proteins that open and close in response to changes in the membrane potential. They are present on the membranes of all electrically excitable cells such as neurons, heart, and muscle cells.
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Sometimes a single EPSP is strong enough to induce an action potential in the postsynaptic neuron. However, multiple presynaptic inputs must often create EPSPs around the same time for the postsynaptic neuron to be sufficiently depolarized to fire an action potential.
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