Contribution of TRPC3-mediated Ca²⁺ entry to taste transduction

The current concept of taste transduction implicates the TASR/PLCβ2/IP₃R3/TRPM5 axis in mediating chemo-electrical coupling in taste cells of the type II. While generation of IP₃ has been verified as an obligatory step, DAG appears to be a byproduct of PIP₂ cleavage by PLCβ2. Here, we provide evidence that DAG-signaling could play a significant and not yet recognized role in taste transduction. In particular, we found that DAG-gated channels are functional in type II cells but not in type I and type III cells. The DAG-gated current presumably constitutes a fraction of the generator current triggered by taste stimulation in type II cells. Bitter stimuli and DAG analogs produced Ca²⁺ transients in type II cells, which were greatly decreased at low bath Ca²⁺, indicating their dependence on Ca²⁺ influx. Among DAG-gated channels, transcripts solely for TRPC3 were detected in the taste tissue, thus implicating this channel in mediating DAG-regulated Ca²⁺ entry. Release of the afferent neurotransmitter ATP from CV papillae was monitored online by using the luciferin/luciferase method and Ussing-like chamber. It was shown that ATP secretion initiated by bitter stimuli and DAG analogs strongly depended on mucosal Ca²⁺. Based on the overall findings, we speculate that in taste transduction, IP₃-driven Ca²⁺ release is transient and mainly responsible for rapid activation of Ca²⁺-gated TRPM5 channels, thus forming the initial phase of receptor potential. DAG-regulated Ca²⁺ entry through apically situated TRPC3 channels extends the primary Ca²⁺ signal and preserves TRPM5 activity, providing a needful prolongation of the receptor potential.