Fig. 2: The purified human TRPA1 without its N-terminal ankyrin repeat domain (Δ1–688 hTRPA1) is both cold- and heat sensitive. | Nature Communications

Fig. 2: The purified human TRPA1 without its N-terminal ankyrin repeat domain (Δ1–688 hTRPA1) is both cold- and heat sensitive.

From: The human TRPA1 intrinsic cold and heat sensitivity involves separate channel structures beyond the N-ARD domain

Fig. 2

Purified Δ1–688 hTRPA1 was reconstituted into planar lipid bilayers and single-channel currents were recorded with the patch-clamp technique in a symmetrical K+ solution at a holding potential of +60 mV. a, b As shown by representative traces and corresponding histograms, exposure to various temperatures evoked outward single-channel currents. c The graph shows single-channel mean open probability (Po) values as a function of different temperatures. Data are represented as the mean ± SEM of separate experiments (shown within parentheses). Data points marked with asterisk were published previously (ref. 7). d The selective TRPA1 antagonist HC030031 inhibited heat responses (n = 3). Black dashed line shows zero channel current level (c indicates the closed channel state) and upward deflections are channel openings. Q10 cold = 0.018 (ref. 7); Q10 heat = 29 (T1 = 20 °C and T2 = 30 °C, and corresponding Po values in Supplementary Table 1; Eq. (1)). Source data are provided as a Source Data file.

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