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Vol. 60, Issue 5, 989-998, November 2001
Departments of Neuropharmacology (H.K., M.K., S.K.), Pharmacology
(A.A.), and Molecular Pharmacology (M.S.), Graduate School of
Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto, Japan; and
Center for Integrative Bioscience (Y.M.), Okazaki National Research
Institutes, Okazaki, Japan
We studied the opening mechanism of Ca2+-permeable channels
formed with mouse transient receptor potential type 5 (mTRP5) using Xenopus oocytes. After stimulation of coexpressed
muscarinic M1 receptors with acetylcholine (ACh) in a
Ca2+-free solution, switching to 2 mM
Ca2+-containing solution evoked a large Cl
current, which reflects the opening of endogenous
Ca2+-dependent Cl channels following
Ca2+ entry through the expressed channels. The ACh-evoked
response was not affected by a depletion of Ca2+ store with
thapsigargin but was inhibited by preinjection of antisense
oligodeoxynucleotides (ODNs) to Gq, G11, or
both. The mTRP5 channel response was also induced by a direct
activation of G proteins with injection of guanosine
5'-3-O-(thio)triphosphate (GTP
S). The ACh- and
GTPS-evoked responses were inhibited by either pretreatment with a
phospholipase C inhibitor, U73122, or an inositol-1,4,5-trisphosphate
(IP3) receptor inhibitor, xestospongin C (XeC). An
activation of IP3 receptors with injection of adenophostin A (AdA) evoked the mTRP5 channel response in a dose-dependent manner.
The AdA-evoked response was not suppressed by preinjection of antisense
ODNs to Gq/11 or U73122 but was suppressed by either
preinjection of XeC or a peptide mimicking the IP3 binding domain of Xenopus IP3 receptor. These
findings suggest that the activation of IP3 receptor is
essential for the opening of mTRP5 channels, and that neither G
proteins, phosphoinositide metabolism, nor depletion of the
Ca2+ store directly modifies the IP3
receptor-linked opening of mTRP5 channels.
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