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Am J Physiol Cell Physiol 284: C749-C756, 2003. First published November 13, 2002; doi:10.1152/ajpcell.00042.2002
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Vol. 284, Issue 3, C749-C756, March 2003

Glu496Ala polymorphism of human P2X7 receptor does not affect its electrophysiological phenotype

Wolfgang Boldt1, Manuela Klapperstück1, Cora Büttner2, Sven Sadtler2, Günther Schmalzing2, and Fritz Markwardt1

1 Julius-Bernstein-Institut für Physiologie, Martin-Luther-Universität Halle-Wittenberg, D-06097 Halle/Saale; and 2 Abteilung für Molekulare Pharmakologie, Rheinisch-Westfälische Technische Hochschule Aachen, D-52074 Aachen, Germany

A glutamate to alanine exchange at amino acid position 496 of the human P2X7 receptor was recently shown to be associated with a loss of function in human B lymphocytes in terms of ATP-induced ethidium+ uptake, Ba2+ influx, and induction of apoptosis (Gu BJ, Zhang WY, Worthington RA, Sluyter R, Dao-Ung P, Petrou S, Barden JA, and Wiley JS. J Biol Chem 276: 11135-11142, 2001). Here we analyzed the effect of the Glu496 to Ala exchange on the channel properties of the human P2X7 receptor expressed in Xenopus oocytes with the two-microelectrode voltage-clamp technique. The amplitudes of ATP-induced whole cell currents characteristic of functional expression, kinetic properties including ATP concentration dependence, and permeation behavior were not altered by this amino acid exchange. Also in HEK293 cells, the Ala496 mutant mediated typical P2X7 receptor-dependent currents like the parent Glu496 hP2X7 receptor. Because the function of the P2X7 receptor as an ATP-gated channel for small cations including Ba2+ remained unaffected by this mutation, we conclude that Glu496 plays a critical role in pore formation but does not determine the ion channel properties of the human P2X7 receptor.

Xenopus oocytes; whole cell current; permeation; kinetics; HEK293 cells


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