TRPV1
TRPV1 (transient receptor potential cation channel subfamily V member 1, also known as VR1) is a non-selective, calcium-permeant cation channel that detects noxious chemical and thermal stimuli. It is the receptor for capsaicin, the pungent compound in hot chilli peppers. Browse Assay Genie's current range of TRPV1 research reagents below, or read on for the biology behind the target.
TRPV1 is a non-selective cation channel that is permeable to calcium and is involved in the detection of noxious chemical and thermal stimuli. It is activated by vanilloids such as capsaicin and by temperatures above 42 degrees Celsius. Mild extracellular acidity (pH 6.5) potentiates activation by noxious heat and vanilloids, whereas stronger acidic conditions (pH below 6) activate the channel directly. Endogenous compounds, including 12-hydroperoxytetraenoic acid and bradykinin, can also activate it. Following activation, the channel shows time- and calcium-dependent outward rectification and then enters a long-lasting refractory state.
The channel is sensitised by a phosphatidylinositol second messenger system that is engaged by receptor tyrosine kinases and involves PKC isozymes and PCL. TRPV1 appears to mediate proton influx and may contribute to intracellular acidosis in nociceptive neurons. It is involved in mediating inflammatory pain and hyperalgesia. Capsaicin selectively activates sensory neurons that relay information about noxious stimuli to the central nervous system, and the receptor is thought to act as a transducer of painful thermal stimuli in vivo. UniProt also describes TRPV1 as an ionotropic endocannabinoid receptor with central neuromodulatory effects. It triggers a form of long-term depression, TRPV1-LTD, mediated by the endocannabinoid anandamide in the hippocampus and nucleus accumbens, by affecting AMPA receptor endocytosis.
The TRPV1 gene belongs to the transient receptor family (TC 1.A.4), TrpV subfamily, and HGNC places it in the ankyrin repeat domain containing group and the TRPV subfamily. It was previously named vanilloid receptor subtype 1, hence the alias VR1. Four transcript variants encode the same protein and differ only in their 5' UTR sequence. Mouse and rat both carry a Trpv1 ortholog. TRPV1 is localised to the postsynaptic cell membrane and dendritic spine membrane.
TRPV1 transduces noxious chemical and thermal stimuli in sensory neurons and is involved in mediating inflammatory pain and hyperalgesia.
The channel is activated by temperatures above 42 degrees Celsius, making it a reference point for studying how noxious heat is detected.
TRPV1 acts as an ionotropic endocannabinoid receptor and triggers anandamide-mediated long-term depression in the hippocampus and nucleus accumbens.
Capsaicin and other vanilloids, protons, bradykinin and lipid mediators gate the channel, which is also sensitised through PKC-linked signalling.
TRPV1 is a non-selective, calcium-permeant cation channel that detects noxious chemical and thermal stimuli. It is activated by capsaicin, by temperatures above 42 degrees Celsius and by strongly acidic conditions, and it is involved in inflammatory pain and hyperalgesia.
VR1 derives from the previous name vanilloid receptor subtype 1, reflecting activation by vanilloids such as capsaicin. The current HGNC name is transient receptor potential cation channel subfamily V member 1. Four transcript variants differ in their 5' UTR but encode the same protein.
Yes. Mouse and rat each have a Trpv1 ortholog, so the channel can be studied in common rodent models of pain and thermosensation. As with any reagent, check the datasheet of any product for its validated reactivity.
Other TRPV subfamily ion channels involved in sensory and cellular signalling.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q8NER1; product specifications from Assay Genie datasheets.