Transient Receptor Potential (TRP) cation channels participate in various fundamental processes in cell- andorganism-physiology in unicellular eukaryotes, invertebrates and vertebrates. Interestingly, many TRP channels functionas detectors of sensory stimuli. The TRPV1 (vanilloid 1) channel serves as an integrator of noxious chemical and physicalstimuli known to cause irritation and pain, such as elevated temperatures, acids, and irritant chemical compounds, and itsactivation has been linked to acute nociceptive pain and neurogenic inflammation. The mechanisms by which the channeldetects incoming stimuli, how the sensing domains are coupled to channel gating and how these processes are connectedto specific structural regions in the channel are not fully understood, but valuable information is available. Many sites involvedin agonist detection have been characterized and gating models that describe many features of the channel’s behaviorhave been put forward. Structural and functional information indicates TRP channels are similar to voltage-activatedpotassium channels, with a tetrameric organization and six-transmembrane-region subunits, a pore domain with multi-ionbinding properties and an intracellular S6 gate that seems to be the point of convergence of the many activation modalitiesleading to the opening of the ion conduction pathway. Furthermore, TRPV1 expression is altered in various disease statesand TRPV1 gene polymorphism was speculated to play a role in pain sensation. The complex activation and regulation ofTRPV1 may have important implications for drug development
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