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Am J Physiol Cell Physiol (May 21, 2008). doi:10.1152/ajpcell.00023.2008
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Submitted on January 18, 2008
Revised on May 15, 2008
Accepted on May 15, 2008

Inhibition of Transient Receptor Potential A1 by Phosphatidylinositol-4,5-bisphosphate

Donghee Kim1*, Eric Cavanaugh1, and Dina Simkin1

1 Rosalind Franklin Univ of Med & Sci

* To whom correspondence should be addressed. E-mail: donghee.kim{at}rosalindfranklin.edu.

Membrane phosphatidylinositol-4,5-bisphosphate (PIP2) is critical for the function of many transient receptor potential (TRP) ion channels. The role of PIP2 in TRPA1 function is not well known. The effect of PIP2 on TRPA1 was investigated by direct application of PIP2, and by using polylysine and PIP2 antibody that sequester PIP2. In inside-out patches from HeLa cells expressing mouse TRPA1, polytriphosphate (PPPi) was added to the bath solution to keep TRPA1 sensitive to allyl isothiocyanate (AITC; mustard oil). Direct application of PIP2 (10 µM) to inside-out patches did not activate TRPA1, but AITC and {Delta}9-tetrahydrocannabinol (THC) produced strong activation. In inside-out patches in which TRPA1 was first activated with AITC (in the presence of PPPi), further addition of PIP2 produced a concentration-dependent inhibition of TRPA1 (K1/2, 2.8 µM). Consistent with the inhibition of TRPA1 by PIP2, AITC activated a large whole-cell current when polylysine or PIP2 antibody was added to the pipette, but a markedly diminished current when PIP2 was added to the pipette. In inside-out patches with PPPi in the bath solution, application of PIP2 antibody or polylysine caused activation of TRPA1, and this was blocked by PIP2. However, TRPA1 was not activated by polylysine and PIP2 antibody under whole-cell conditions, suggesting a more complex regulation of TRPA1 by PIP2 in intact cells. The results of this study show that PIP2 inhibits TRPA1 and reduces the sensitivity of TRPA1 to AITC.




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