Cloning and tissue distribution of a novel P2X receptor from rat brain

Florentina Soto; Miguel Garcia-Guzman; Christine Karschin; Walter Stühmer

doi:10.1006/bbrc.1996.0915

Cloning and tissue distribution of a novel P2X receptor from rat brain

Florentina Soto, Miguel Garcia-Guzman, Christine Karschin, Walter Stühmer

Department of Ophthalmology and Visual Sciences

Research output: Contribution to journal › Article › peer-review

83 Scopus citations

Abstract

We have isolated the cDNA for a novel member (P2X₆) of the ATP-gated ion channel family. The rat P2X₆ nucleotide sequence encodes a 379 amino acid protein that conserves all the structural features of previously cloned P2X receptors, including the two putative transmembrane domains predicted by hydrophobicity plots. In situ hybridization analysis of rat brain sections showed a wide pattern of mRNA expression that is virtually identical to that already described for P2X₄. Injection of P2X₆ cRNA in Xenopus oocytes did not give rise to ATP-activated channels. Coexpression of P2X₆ with P2X₄ subunits produced currents which were not discernibly different from those of P2X₄ expressed alone.

Original language	English
Pages (from-to)	456-460
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	223
Issue number	2
DOIs	https://doi.org/10.1006/bbrc.1996.0915
State	Published - Jun 14 1996

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title = "Cloning and tissue distribution of a novel P2X receptor from rat brain",

abstract = "We have isolated the cDNA for a novel member (P2X6) of the ATP-gated ion channel family. The rat P2X6 nucleotide sequence encodes a 379 amino acid protein that conserves all the structural features of previously cloned P2X receptors, including the two putative transmembrane domains predicted by hydrophobicity plots. In situ hybridization analysis of rat brain sections showed a wide pattern of mRNA expression that is virtually identical to that already described for P2X4. Injection of P2X6 cRNA in Xenopus oocytes did not give rise to ATP-activated channels. Coexpression of P2X6 with P2X4 subunits produced currents which were not discernibly different from those of P2X4 expressed alone.",

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AU - Soto, Florentina

AU - Garcia-Guzman, Miguel

AU - Karschin, Christine

AU - Stühmer, Walter

PY - 1996/6/14

Y1 - 1996/6/14

N2 - We have isolated the cDNA for a novel member (P2X6) of the ATP-gated ion channel family. The rat P2X6 nucleotide sequence encodes a 379 amino acid protein that conserves all the structural features of previously cloned P2X receptors, including the two putative transmembrane domains predicted by hydrophobicity plots. In situ hybridization analysis of rat brain sections showed a wide pattern of mRNA expression that is virtually identical to that already described for P2X4. Injection of P2X6 cRNA in Xenopus oocytes did not give rise to ATP-activated channels. Coexpression of P2X6 with P2X4 subunits produced currents which were not discernibly different from those of P2X4 expressed alone.

AB - We have isolated the cDNA for a novel member (P2X6) of the ATP-gated ion channel family. The rat P2X6 nucleotide sequence encodes a 379 amino acid protein that conserves all the structural features of previously cloned P2X receptors, including the two putative transmembrane domains predicted by hydrophobicity plots. In situ hybridization analysis of rat brain sections showed a wide pattern of mRNA expression that is virtually identical to that already described for P2X4. Injection of P2X6 cRNA in Xenopus oocytes did not give rise to ATP-activated channels. Coexpression of P2X6 with P2X4 subunits produced currents which were not discernibly different from those of P2X4 expressed alone.

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JO - Biochemical and Biophysical Research Communications

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Cloning and tissue distribution of a novel P2X receptor from rat brain

Abstract

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