title: The P2X(7) receptor from Xenopus laevis: formation of a large pore in Xenopus oocytes.
abstract: The purinergic P2X(7) receptor is an ATP-receptor channel predominantly expressed in immune cells. P2X(7) has been cloned from human, rat and mouse. Here we report cloning of the Xenopus laevis P2X(7) receptor (xP2X(7)). xP2X(7) is only about 50% identical to the mammalian homologues, shows a broad tissue expression pattern, and has the electrophysiological characteristics typical of a P2X(7) receptor: low agonist affinity (EC(50) about 2.6 mM) and a non-desensitizing current. Moreover, expression of xP2X(7) in Xenopus oocytes is sufficient to induce the formation of a large pore, which is permeable to large cations such as NMDG(+). Identification of a non-mammalian P2X(7) receptor may help to identify functionally important parts of the protein.
authors.affiliation: Department of Otolaryngology, Research Group of Sensory Physiology, Röntgenweg 11, D-72076, Tübingen, Germany.
authors.forename: Martin
authors.initials: M
authors.lastname: Paukert
authors.forename: Susanti
authors.initials: S
authors.lastname: Hidayat
authors.forename: Stefan
authors.initials: S
authors.lastname: Gründer
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D003001:Cloning, Molecular; D008969:Molecular Sequence Data; D009865:Oocytes / Q000378:metabolism*; D018408:Patch-Clamp Techniques; D018272:Porins; D012333:RNA, Messenger / Q000378:metabolism; D018048:Receptors, Purinergic P2 / Q000235:genetics / Q000378:metabolism*; D058486:Receptors, Purinergic P2X7; D017386:Sequence Homology, Amino Acid; D014982:Xenopus laevis / Q000235:genetics / Q000378:metabolism*
chemical_list: C546468:P2RX7 protein, human; C546469:P2rx7 protein, mouse; C546470:P2rx7 protein, rat; D018272:Porins; D012333:RNA, Messenger; D018048:Receptors, Purinergic P2; D058486:Receptors, Purinergic P2X7