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(A) Increase of Nav 1.8 currents caused by BmK I was blocked in the presence of A-803467.
Open image in new window Figure 5 Increase of Nav 1.8 currents caused by BmK I was blocked in the presence of A-803467 (5 μmol/L).
Leak and background conductances, identified by blocking Nav channels with tetrodotoxin, were subtracted for all of the Nav channel-mediated currents.
We are particularly interested in the structure and function of the Nav β3 subunit (19– 22).
While related to members of the Nav superfamily, NsvBa is nonselective among cations.
Currently, no high-resolution structures exist for any of the Nav β-subunit Ig domains.
Thus, pH and temperature-induced increases of the peak current and reduction of the voltage-dependence of activation are distinct from eukaryotic Nav channels.
However, at least some of the CAM-like behavior shown by the Nav β subunits is likely to be independent of any effects they have on Nav α subunits (3).
Knockdown of FGF14 did not affect NaV current density compared to the NaV current density recorded in neurons transfected with a control shRNA.
The FGF14bR/A mutant that prevents interaction with the NaV C-terminus cannot rescue NaV kinetic effects of FGF14 knockdown.
The DIII lysine in the Nav selectivity filter is also integral to the binding of TTX [20].
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