5-Hydroxytryptamine inhibits P2X2 receptor channel pore mutants.
1. 5-Hydroxytryptamine (10 microM) enhanced ionic current mediated through the wild-type P2X2 receptor/channel expressed in Xenopus oocytes. 2. 5-Hydroxytryptamine (10 microM) 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.
Nakazawa
K
K
Division of Pharmacology, National Institute of Health Sciences, Tokyo, Japan. nakazawa@nihs.go.jp
Ohno
Y
Y
D000200:Action Potentials / Q000187:drug effects*; D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D004298:Dopamine / Q000494:pharmacology; D009154:Mutation; D018048:Receptors, Purinergic P2 / Q000187:drug effects* / Q000235:genetics; D058476:Receptors, Purinergic P2X2; D012701:Serotonin / Q000494:pharmacology*; D014981:Xenopus
D018048:Receptors, Purinergic P2; D058476:Receptors, Purinergic P2X2; D012701:Serotonin; D000255:Adenosine Triphosphate; D004298:Dopamine