Abstract
We have previously shown that protein kinase C (PKC) has a pivotal role in activating diverse TRPC SOCs in vascular myocytes (Albert & Large, 2002; Saleh et al, 2008). The present work investigated mechanisms involved in linking PKC activity with gating of SOCs and provides evidence that PIP2 is an obligatory molecule in this process.Bath application of PIP2 to quiescent inside‐out patches from rabbit portal vein myocytes activated SOC activity, which was inhibited by anti‐TRPC1 antibodies (Albert & Large, 2003; Saleh et al, 2008). Cyclopiazonic acid (CPA)‐, BAPTA‐AM‐ and phorbol esters (PDBu)‐induced SOC activity was inhibited by an anti‐PIP2 antibody and by pre‐treatment with agents that deplete tissue PIP2 levels. Pre‐treatment with PDBu and the PKC inhibitor, chelerythrine, enhanced and decreased SOC stimulation by PIP2. Co‐immunoprecipiation experiments showed association between PIP2 and TRPC1 at rest and moreover that PKC‐dependent phosphorylation of TRPC1 was increased by CPA and PDBu and decreased by chelerythrine.These data clearly indicate that PIP2 activates SOCs and that PIP2 is obligatory for stimulation of SOCs via PKC‐dependent phosphorylation of TRPC1.Albert & Large (2002) J Physiol 544 113‐25; Saleh et al (2008) J Physiol 566 2463‐76
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