5-Hydroxytryptamine Inhibits P2X2 Receptor Channel Pore Mutants |
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Authors: | Ken Nakazawa Yasuo Ohno |
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Institution: | (1) Division of Pharmacology, National Institute of Health Sciences, 1-18-1 Kamiyoga, Setagaya, Tokyo, 158-8501, Japan |
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Abstract: | 1.5-Hydroxytryptamine (10 M) enhanced ionic current mediated through the wild-type P2X2 receptor/channel expressed in Xenopus oocytes.2.5-Hydroxytryptamine (10 M) inhibited a current mediated through P2X2 receptor/channel mutants when Thr330 or Asn333 was replaced with Ile (T330I and N333I).3.Our results suggest that neutralization of Thr330 or Asn333 exposes a high-affinity, inhibitory binding site for 5-hydroxytryptamine. This implies that 5-hydroxytryptamine interacts with the P2X2 receptor/channel at their channel pores. |
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Keywords: | P2X2 receptor 5-hydroxytryptamine site-directed mutagenesis Xenopus oocytes voltage clamp |
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