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5-Hydroxytryptamine Inhibits P2X2 Receptor Channel Pore Mutants
Authors:Ken Nakazawa  Yasuo Ohno
Institution:(1) Division of Pharmacology, National Institute of Health Sciences, 1-18-1 Kamiyoga, Setagaya, Tokyo, 158-8501, Japan
Abstract:1.5-Hydroxytryptamine (10 mgrM) enhanced ionic current mediated through the wild-type P2X2 receptor/channel expressed in Xenopus oocytes.2.5-Hydroxytryptamine (10 mgrM) 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.
Keywords:P2X2 receptor  5-hydroxytryptamine  site-directed mutagenesis  Xenopus oocytes  voltage clamp
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