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

Martin Paukert; Susanti Hidayat; Stefan Gründer

doi:10.1016/S0014-5793(02)02324-4

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

Martin Paukert, Susanti Hidayat, Stefan Gründer

Producción científica: Article › revisión exhaustiva

30 Citas (Scopus)

Resumen

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.

Idioma original	English (US)
Páginas (desde-hasta)	253-258
Número de páginas	6
Publicación	FEBS Letters
Volumen	513
N.º	2-3
DOI	https://doi.org/10.1016/S0014-5793(02)02324-4
Estado	Published - feb 27 2002
Publicado de forma externa	Sí

ASJC Scopus subject areas

Genetics
Molecular Biology
Biophysics
Structural Biology
Biochemistry
Cell Biology

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10.1016/S0014-5793(02)02324-4

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abstract = "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.",

keywords = "Ion channel, Ion selectivity, P2 purinoceptor, Two-electrode voltage-clamp",

author = "Martin Paukert and Susanti Hidayat and Stefan Gr{\"u}nder",

note = "Funding Information: We thank H.-S. Geisler for expert technical assistance. S.H. is student of the T{\"u}bingen Graduate School of Neural and Behavioural Sciences and is supported by a stipend of the Max-Planck-Gesellschaft. S.G. is supported by Grants of the Attempto research group program of the Universit{\"a}tsklinikum T{\"u}bingen (FG 1-0-0) and the DFG (GR1771/3-1).",

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N2 - 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.

AB - 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.

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