Analysis of rare variations reveals roles of amino acid residues in the N-terminal extracellular domain of nicotinic acetylcholine receptor (nAChR) alpha6 subunit in the functional expression of human alpha6*-nAChRs

Table 3 **Parameters for ACh action at WT or variant hα6hβ4*- nAChRs**

¹From Kuryatov et al. (2000).
Potencies [micromolar EC₅₀ values with 95% confidence intervals (CI)], Hill coefficients (n_H ± SE), mean ± SE peak response (I_max in nanoamps) and concentrations (μM) where maximal peak current amplitudes (I_max) achieved are provided for ACh acting at nAChR composed of the indicated subunits and from the indicated number of independent experiments (n) based on studies as shown in Figure 8. ⬆ or ⬇ indicate a significant (p < 0.05) increase or decrease in indicated parameter at the indicated nAChR subtype relative to nAChR containing the same subunits but in the presence of the WT hα6 subunit (i.e., hα6hβ4- vs. variant-hα6hβ4- nAChR; hα6hβ4hβ3- vs. variant-hα6hβ4hβ3- nAChR). ▲ or ▼ indicate a significant (p < 0.05) increase or decrease, respectively, in indicated parameter at the indicated nAChR subtype relative to nAChR containing the same subunits but in the absence WT β3 subunits (i.e., hα6hβ4- vs. hα6hβ4hβ3- nAChR; variant-hα6hβ4- vs. variant-hα6hβ4hβ3- nAChR). ‘-‘ indicates that inconsistent functional responses in two electrode voltage clamp studies precluded determination of the parameter of interest.

ISSN: 1756-6606