The P2X7 receptor from Xenopus laevis: formation of a large pore in Xenopus oocytes

FEBS Letters

Gründer, Stefan¹  Paukert, Martin¹  Hidayat, Susanti¹ 

[1] Department of Otolaryngology, Research Group of Sensory Physiology, Röntgenweg 11, D-72076 Tübingen, Germany

关键词: P2 purinoceptor;    Ion channel;    Two-electrode voltage-clamp;    Ion selectivity;    cDNA;    complementary DNA;    cRNA;    complementary RNA;    BzATP;    3′-O-(4-benzoyl)-benzoyl-ATP;    HMA;    N;    N-hexamethylene amiloride;    KN-62;    1-[N;    O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenylpiperazine;    NMDG;    N-methyl-D-glucamine;   

DOI  :  10.1016/S0014-5793(02)02324-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The purinergic P2X₇ receptor is an ATP-receptor channel predominantly expressed in immune cells. P2X₇ has been cloned from human, rat and mouse. Here we report cloning of the Xenopus laevis P2X₇ receptor (xP2X₇). xP2X₇ is only about 50% identical to the mammalian homologues, shows a broad tissue expression pattern, and has the electrophysiological characteristics typical of a P2X₇ receptor: low agonist affinity (EC₅₀ about 2.6 mM) and a non-desensitizing current. Moreover, expression of xP2X₇ 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 P2X₇ receptor may help to identify functionally important parts of the protein.

【 授权许可】

Unknown