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• W2113921063 endingPage "998" @default.
• W2113921063 startingPage "989" @default.
• W2113921063 abstract "We studied the opening mechanism of Ca²⁺-permeable channels formed with mouse transient receptor potential type 5 (mTRP5) using<i>Xenopus</i> 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 G_q, G₁₁, or both. The mTRP5 channel response was also induced by a direct activation of G proteins with injection of guanosine 5′-3-<i>O</i>-(thio)triphosphate (GTPγS). The ACh- and GTPγS-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 G_q/11 or U73122 but was suppressed by either preinjection of XeC or a peptide mimicking the IP₃ binding domain of <i>Xenopus</i> 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 IP₃receptor-linked opening of mTRP5 channels." @default.
• W2113921063 created "2016-06-24" @default.
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• W2113921063 date "2001-11-01" @default.
• W2113921063 modified "2023-10-12" @default.
• W2113921063 title "Activation of Inositol 1,4,5-Trisphosphate Receptor Is Essential for the Opening of Mouse TRP5 Channels" @default.
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• W2113921063 doi "https://doi.org/10.1124/mol.60.5.989" @default.
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