Andres Jara-Oseguera

TL;DR: It is established that TRPV1 is activated by pungent extracts from onion and garlic, as well as by allicin, the active compound in these preparations, and participates together with TRPA1 in the pain-related behavior induced by this compound.

TL;DR: In this paper, the authors show that LPA directly interacts with the C terminus of the TRPV1 ion channel, which is a direct molecular target of the pain-producing molecule LPA.

TL;DR: A general picture of the physiological and pathophysiological roles of the TRPV1 channel and of its structural, pharmacological and biophysical properties is provided.

TL;DR: Measurements of capsaicin-activated currents in excised patches from TRPV1-expressing HEK cells show that enrichment with cholesterol, but not its diastereoisomer epicholesterol, markedly decreased wild-type rat TRpV1 currents, suggesting that there is a cholesterol-binding site in TRPv1 and that the functions of TRP V1 depend on the genetic variant and membrane cholesterol content.

TL;DR: It is shown that access to the pore of TRPV1 is gated by S6 in response to both capsaicin binding and increases in temperature, and that two constrictions are present inThe pore: one that impedes the access of large molecules and the other that hampers theAccess of smaller ions and constitutes an activation gate of these channels.