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- W2023709977 abstract "Agonist activation of the hP2Y1 receptor expressed in Xenopus oocytes stimulated an endogenous voltage-gated ion channel, previously identified as the transient inward (Tin) channel. When human P2Y1 (hP2Y1) and skate P2Y (sP2Y) receptors were expressed in Xenopus oocytes, time-to-peak values (a measure of the response to membrane hyperpolarization) of the Tin channel were significantly reduced compared to oocytes expressing the hB1-bradykinin receptor or the rat M1-muscarinic (rM1) receptor. Differences in activation were also observed in the Tin currents elicited by various P2Y receptor subtypes. The time-to-peak values of the Tin channel in oocytes expressing the hP2Y4, hP2Y11, or hB1-bradykinin receptors were similar, whereas the channel had significantly shorter time-to-peak values in oocytes expressing either the hP2Y1 or sP2Y receptor. Amino acid substitutions at His-132, located in the third transmembrane domain (TM3) of the hP2Y1 receptor, delayed the onset of channel opening, but not the kinetics of the activation process. In addition, Zn2+ sensitivity was also dependent on the subtype of P2Y receptor expressed. Replacement of His-132 in the hP2Y1 receptor with either Ala or Phe increased Zn2+ sensitivity of the Tin current. In contrast, truncation of the C-terminal region of the hP2Y1 receptor had no affect on activation or Zn2+ sensitivity of the Tin channel. These results suggested that TM3 in the hP2Y1 receptor was involved in modulating ion channel function and blocker pharmacology of the Tin channel." @default.
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- W2023709977 date "2004-12-01" @default.
- W2023709977 modified "2023-09-26" @default.
- W2023709977 title "P2Y1 receptor modulation of endogenous ion channel function in Xenopus oocytes: Involvement of transmembrane domains" @default.
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- W2023709977 doi "https://doi.org/10.1007/s11302-004-4744-5" @default.
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