Indexed on: 03 Sep '19Published on: 28 Apr '19Published in: Methods in molecular biology (Clifton, N.J.)
The family of transient receptor potential (TRPs) channels contains 28 mammalian members, each a unique cellular sensor that responds to a wide variety of external and internal signals. TRP channels are expressed by most mammalian cells, where they are involved in many different physiological functions. Canonical TRP channels (TRPCs) form a family of nonselective cationic channels, although with greater selectivity for Ca. This family is made up of seven members (TRPC1-7), all of which contain a TRP box in the carboxyl terminal and 3-4 ankyrin repeats in the amino terminal. While these channels share some similar properties, they display diverse gating mechanisms and are involved in different signaling pathways (Gees M et al., Compr Physiol, 2012). The activation or inhibition of these channels has been studied using different approaches and techniques. Here, we characterize the activation of the TRPC5 channel expressed in a heterologous system, using calcium imaging and the patch-clamp technique in whole-cell configuration.