Abstract
Mammalian cells poorly express rNa(v)1.8 channels. In contrast, rNa(v)1.7 dorsal root ganglion channels have 90-fold higher peak Na(+) current densities. We investigated the role of rNa(v)1.7 and rNa(v)1.8 carboxy-termini in modulating the expression of rNa(v)1.7 and rNa(v)1.8 channels in tsA201 cells. Mutations in the ubiquitination site of the C-terminus did not improve rNa(v)1.8 current levels. However, rNa(v)1.8 chimeras containing the entire or the proximal portion of the rNa(v)1.7 C-terminus expressed 3.2-fold and 4.8-fold higher peak current densities, respectively, than parent rNa(v)1.8 channels. We conclude that the two Na(+) channels may have different endoplasmic reticulum processing signals.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence / physiology
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Animals
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Cell Line
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Electrophysiology
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Mutation
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NAV1.7 Voltage-Gated Sodium Channel
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NAV1.8 Voltage-Gated Sodium Channel
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Nerve Tissue Proteins / genetics
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Nerve Tissue Proteins / metabolism*
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Nerve Tissue Proteins / physiology
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Patch-Clamp Techniques
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Protein Transport
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Rats
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Sodium Channels / genetics
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Sodium Channels / metabolism*
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Sodium Channels / physiology
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Transfection
Substances
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NAV1.7 Voltage-Gated Sodium Channel
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NAV1.8 Voltage-Gated Sodium Channel
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Nerve Tissue Proteins
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Recombinant Fusion Proteins
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Scn10a protein, rat
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Scn9a protein, rat
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Sodium Channels