Am J Physiol Cell Physiol AJP: Regulatory, Integrative and Comparative Physiology
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Am J Physiol Cell Physiol (November 13, 2002). doi:10.1152/ajpcell.00042.2002
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Articles in PresS, published online ahead of print November 13, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00042.2002
Submitted on January 27, 2002
Accepted on November 7, 2002

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

Wolfgang Boldt1, Manuela Klapperstueck1, Cora Buettner2, Sven Sadtler2, Guenther Schmalzing2, and Fritz Markwardt1*

1 JB Inst Physiology, ML Univ, Halle (Saale), Germany
2 Dep Mol Pharmacol, RWTH Aachen, Aachen, Germany

* To whom correspondence should be addressed. E-mail: fritz.markwardt{at}medizin.uni-halle.de.

A glutamate to alanine exchange at amino acid position 496 of the human P2X7 receptor has recently been 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 (1). Here we analyzed the effect of the Glu496 to Ala exchange on the channel properties of the human P2X7 receptor expressed in Xenopus oocytes using the two microelectrode voltage clamp technique. Neither the amplitudes of ATP-induced whole cell currents characteristic of the functional expression, the kinetic properties including the ATP concentration dependency nor the permeation behaviour were 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. Since the function of the P2X7 receptor as an ATP-gated channel for small cations including Ba2+ remains 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.




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