Abstract
TRPV1 channels are non-selective cation channels activated by capsaicin, protons, and heat. We have previously shown that TRPV1 activation is potentiated in vivo by PI(4,5)P2. We are now investigating the mechanism of PI(4,5)P2 potentiation using TRPV1 channels reconstituted in synthetic lipid vesicles studied with patch-clamp electrophysiology. We will present our results exploring the effects of natural PIP2 extracts and di-C16 PI(4,5)P2 incorporated into asolectin giant unilamellar vesicles (GUVs) and synthetic lipid GUVs. We will compare the effects of these non-soluble forms of PIP2 to the effects of the more water soluble di-C8 PIP2 forms used in many cellular electrophysiology experiments.
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