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 nonmammalian P2X 7 receptor may help to identify functionally important parts of the protein. ß
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