Fig. 8: Δ1–688 hTRPA1 and Δ1–854 hTRPA1 heat and cold sensitivity are dependent on the channel redox state. | Nature Communications

Fig. 8: Δ1–688 hTRPA1 and Δ1–854 hTRPA1 heat and cold sensitivity are dependent on the channel redox state.

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

Fig. 8

Purified Δ1–688 hTRPA1 and Δ1–854 hTRPA1 were 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. As shown by traces, the thiol reducing agent TCEP eliminated the channel activity of Δ1–688 hTRPA1 evoked by heat (n = 6) and Δ1–854 hTRPA1 evoked by cold (n = 5). Black dashed line shows zero channel current level (c indicates the closed channel state) and upward deflections are channel openings.

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