Publication Type:
Journal ArticleSource:
FEBS Lett, Volume 559, Issue 1-3, p.39-44 (2004)Keywords:
Amino Acid Sequence, Animals, Cell Line, Electrophysiology, Mutation, NAV1.7 Voltage-Gated Sodium Channel, NAV1.8 Voltage-Gated Sodium Channel, Nerve Tissue Proteins, Patch-Clamp Techniques, Protein Transport, Rats, Recombinant Fusion Proteins, Sodium Channels, TransfectionAbstract:
<p>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.</p>