Nutrition Guide

Transient receptor potential cation channel, subfamily C, member 3, also known as TRPC3, is a human gene encoding a protein of the same name.

Transient receptor potential cation channel, subfamily C, member 2, also known as TRPC2, is a human gene encoding a protein of the same name.

Transient receptor potential cation channel, subfamily C, member 1, also known as TRPC1, is a human gene encoding a protein of the same name.

TRPC is a family of transient receptor potential cation channels in animals.

TRPC channels form the subfamily of channels in human most closely related to drosophila TRP channels. Structurally, this family shares a number of similar characteristics. At the proximal C-terminus of this sub-family is a TRP box motif containing the invariant EWKFAR sequence and between 3 and 4 ankyrin repeats near the N-terminus. These channels are non-selectively permeable to cations, with a selectivity of calcium over sodium variable among the different members. Many of TRPC channel subunits are able to coassemble.[1]

In general, TRPC channels can be activated by phospholipase C stimulation, with some members also activated by diacylglycerol. There is one at least one report that TRPC1 is also activated by stretching of the membrane and TRPC5 channels are activated by extracellular reduced thioredoxin. [2]

It has long been proposed that TRPC channels underlie the store-operated channels (SOC) observed in many cell types. These channels open due to the depletion of intracellular calcium stores. Two other proteins, stromal interaction molecules (STIMs) and the ORAIs, however, have more recently been implicated in this process. It should be noted that STIM1 and TRPC1 can coassemble, complicating the understanding of this phenomenon.[1]

TRPC6 and TRPC4 have been implicated in late onset Alzheimer’s disease.[3][4][5]

TRPA is a family of transient receptor potential ion channels.

The sole member of the TRPA sub-family, TRPA1, contains 14 N-terminal ankyrin repeats and is believed to function as a mechanical stress sensor. It is expressed in the dorsal root ganglion, trigeminal ganglion, and hair cells. The temperature sensitivity of TRPA1 is highly disputed, with some reports claiming that it is activated by noxiously cold stimuli and others disputing such a claim. TRPA1 is known to be activated by isothiocyanates, which are the pungent chemicals in substances such as mustard oil and wasabi, methyl salicylate in winter green oil, and cinnamaldehyde in cinnamon, amongst numerous other substances.

Two pore segment channel 2 (TPC2) is a human protein encoded by the TPCN2 is a human gene. TPC2 is is an ion channel, however, in contrast to other calcium and sodium channels which have four homologous domains, each containing 6 transmembrane segments (S1 to S6), TPCN1 only contains two domain (each containing segments S1 to S6)

Two pore segment channel 1 (TPC1) is a human protein encoded by the TPCN1 is a human gene. The protein encoded by this gene is an ion channel. In contrast to other calcium and sodium channels which have four homologous domains, each containing 6 transmembrane segments (S1 to S6), TPCN1 only contains two domain (each containing segments S1 to S6).

Such channels are of use in the initial formation of an action potential from a mechanical stimulus, for example by the mechanoreceptors in an animal’s vibrissae (whiskers).

A possible role in myoblast development has been described.[2]

Though little is known about these channels, they may be linked to molecules in the cytoskeleton, which may open them by transmitting physical forces of stretch or pressure to the channels, causing them to undergo a conformational change.[1] The channels may also be pulled open due to tension on the membrane itself.[1] Opening the channels allows ions to which they are permeable to flow down their electrochemical gradients into or out of the cell, causing a change in membrane potential.

This can also be referred to as the Stress-activated gate because the gate (protein receptor) responds to pressure or stress.

Stretch-activated or stretch-gated ion channels are ion channels which open their pores in response to mechanical deformation of a neuron’s plasma membrane.