ArticlePurinergic signalling2004
P2Y(1) receptor modulation of endogenous ion channel function in Xenopus oocytes: Involvement of transmembrane domains.
Article in Purinergic signalling, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
1 citing paper in PubMed, 1 citations in OpenAlex.
- Human P2YFrontiers in immunology · 2018Article
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 2 countries.
Funding
Abstract
Agonist activation of the hP2Y(1) receptor expressed in Xenopus oocytes stimulated an endogenous voltage-gated ion channel, previously identified as the transient inward (T(in)) channel. When human P2Y(1) (hP2Y(1)) and skate P2Y (sP2Y) receptors were expressed in Xenopus oocytes, time-to-peak values (a measure of the response to membrane hyperpolarization) of the T(in) channel were significantly reduced compared to oocytes expressing the hB(1)-bradykinin receptor or the rat M(1)-muscarinic (rM(1)) receptor. Differences in activation were also observed in the T(in) currents elicited by various P2Y receptor subtypes. The time-to-peak values of the T(in) channel in oocytes expressing the hP2Y(4), hP2Y(11), or hB(1)-bradykinin receptors were similar, whereas the channel had significantly shorter time-to-peak values in oocytes expressing either the hP2Y(1) or sP2Y receptor. Amino acid substitutions at His-132, located in the third transmembrane domain (TM3) of the hP2Y(1) receptor, delayed the onset of channel opening, but not the kinetics of the activation process. In addition, Zn(2+) sensitivity was also dependent on the subtype of P2Y receptor expressed. Replacement of His-132 in the hP2Y(1) receptor with either Ala or Phe increased Zn(2+) sensitivity of the T(in) current. In contrast, truncation of the C-terminal region of the hP2Y(1) receptor had no affect on activation or Zn(2+) sensitivity of the T(in) channel. These results suggested that TM3 in the hP2Y(1) receptor was involved in modulating ion channel function and blocker pharmacology of the T(in) channel.
Identifiers
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.