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Molecular cloning, functional characterization and possible cooperativity between the murine P2X4 and P2X4a receptors.

Townsend-Nicholson, A, King, B F, Wildman, Scott S.P., Burnstock, G (1999) Molecular cloning, functional characterization and possible cooperativity between the murine P2X4 and P2X4a receptors. Brain research. Molecular brain research, 64 (2). pp. 246-54. ISSN 0169-328X. (doi:10.1016/S0169-328X(98)00328-3) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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Official URL
https://doi.org/10.1016/S0169-328X(98)00328-3

Abstract

We have cloned and functionally characterised the mouse orthologue of the P2X4 receptor, mP2X4, and a splice variant of this receptor, mP2X4a. mP2X4 is 388 amino acids in length and shares 94% and 87% identity with the rat and human P2X4 receptors, respectively, while mP2X4a is 361 amino acids in length and lacks a 27-amino acid region in the extracellular domain corresponding to exon 6 of the known P2X receptor gene structures. When expressed in Xenopus laevis oocytes, mP2X4 produces a rapid inward current in response to ATP with an EC50 of 1.68+/-0.2 microM, consistent with the affinity of the rat and human P2X4 receptors for ATP. This agonist response is potentiated by the P2X receptor antagonists suramin, Reactive blue 2 and, over a limited concentration range, by PPADS. Although mP2X4a forms a poorly functional homomeric receptor, it appears able to interact with the full-length mP2X4 subunit to result in a functional channel with a reduced affinity for ATP. These results suggest a possible role for splice variants of P2X receptors in the formation of functional heteromeric ion channels.

Item Type: Article
DOI/Identification number: 10.1016/S0169-328X(98)00328-3
Subjects: R Medicine > RM Therapeutics. Pharmacology
Divisions: Faculties > Sciences > Medway School of Pharmacy
Depositing User: Scott S.P. Wildman
Date Deposited: 13 Dec 2015 13:52 UTC
Last Modified: 29 May 2019 16:40 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/52962 (The current URI for this page, for reference purposes)
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