title: An asparagine residue regulating conductance through P2X2 receptor/channels.
abstract: Single channel currents were recorded from Xenopus oocytes expressing wild-type and mutated P2X2 receptors. When 100 mM Na+ was used as the permeant cation, unitary currents of about 80 pS were recorded from the oocyte expressing the wild-type channels. The single channel conductance was roughly halved when Asn333 was replaced by Ile (N333I). A similar decrease in single channel currents was also observed when 100 mM Li+ or Cs+ was used as the permeant cation. With two other mutants, in which Asp315 was replaced by Val (D315V) or Tyr330 was replaced by lie (T333I), single channel conductance was almost the same as that of the wild-type channels. The results suggest that Asn333, which is believed to be involved in the channel pore, plays an essential role in ion transport through P2X2 receptor/channels.
authors.affiliation: Division of Pharmacology, National Institute of Health Science, Setagaya, Tokyo, Japan. nakazawa@nihs.go.jp
authors.forename: K
authors.initials: K
authors.lastname: Nakazawa
authors.forename: K
authors.initials: K
authors.lastname: Inoue
authors.forename: Y
authors.initials: Y
authors.lastname: Ohno
mesh_terms: D000818:Animals; D001216:Asparagine / Q000502:physiology*; D001665:Binding Sites; D002118:Calcium / Q000502:physiology; D002412:Cations; D002586:Cesium / Q000502:physiology; D007473:Ion Channels / Q000502:physiology; D008094:Lithium / Q000502:physiology; D008274:Magnesium / Q000502:physiology; D016297:Mutagenesis, Site-Directed; D018048:Receptors, Purinergic P2 / Q000502:physiology*; D058476:Receptors, Purinergic P2X2; D012964:Sodium / Q000502:physiology; D014981:Xenopus
chemical_list: D002412:Cations; D007473:Ion Channels; D018048:Receptors, Purinergic P2; D058476:Receptors, Purinergic P2X2; D002586:Cesium; D001216:Asparagine; D008094:Lithium; D012964:Sodium; D008274:Magnesium; D002118:Calcium