TRPV

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.