Transient receptor potenital (TRP) is a large family of non-selective cation channels located on the cell membrane. One type of channel can be activated by Vanillic acid compounds, so this type of channel is called the TRPV subfamily. Mutations in TRPV are associated with neurodegenerative diseases, skeletal dysplasia, kidney disease and cancer and TRPV is an important therapeutic target for these diseases.

1. TRPV
Transient receptor potenital (TRP) is a large family of non-selective cation channels
located on the cell membrane. One type of channel can be activated by Vanillic acid
compounds, so this type of channel is called the TRPV subfamily. Mutations in TRPV
are associated with neurodegenerative diseases, skeletal dysplasia, kidney disease
and cancer and TRPV is an important therapeutic target for these diseases. The role
of TRPV1, TRPV2 and TRPV3 as thermoreceptors and the role of TRPV4 as a
mechanoreceptor have important clinical implications; reducing the sensitivity to
stimuli by targeting ion channels involved in thermal, chemical and mechanical
sensations can alleviate chronic pain. For example, the use of a TRPV1 agonist may
inhibit nociception at TRPV1, particularly in pancreatic tissue with high expression of
TRPV1. The TRPV1 agonist capsaicin found in pepper has been shown to alleviate
neuropathic pain, and TRPV1 agonists can inhibit noxious analgesia. So now the
study of the TRPV family is of great significance.
Six family members of the TRPV family (TRPV1-6) are now found. Functional TRPV ion
channels are structurally homotetramers or heterotetramers, and the four subunits
are symmetrically arranged around the ion conducting holes. Although the degree of
heteromorphism has been the subject of some debates, recent research in this field
suggests that all four thermosensitive TRPVs (1-4) can form isomers with each other.
This result is consistent with the general observation that TRP co-assembly tends to
occur between subunits with high sequence similarity. How the TRP subunit
recognizes and interacts is unclear. The TRPV channel monomer subunit components
each comprise six transmembrane (TM) domains (designated S1-S6) with a pore
domain between the fifth (S5) and sixth (S6) regions. The TRPV subunit contains
three to five N-terminal ankyrin repeats.