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J Physiol Volume 510, Number 1, 27-35, July 1, 1998
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The Journal of Physiology (1998), 510.1, pp. 27-35
© Copyright 1998 The Physiological Society

Calcium permeability and block at homomeric and heteromeric P2X2 and P2X3 receptors, and P2X receptors in rat nodose neurones

Caterina Virginio, R. A. North and Annmarie Surprenant

Geneva Biomedical Research Institute, Glaxo Wellcome Research and Development, 14 chemin des Aulx, 1228 Plan-les-Ouates, Geneva, Switzerland

  1. Whole-cell recordings were made from HEK 293 (human embryonic kidney) cells stably transfected with cDNAs encoding P2X2, P2X3 or both receptors (P2X2/3) and from cultured rat nodose neurones. Nodose neurones all showed immunoreactivity for both P2X2 and P2X3, but not P2X1, receptors.

  2. Reversal potentials were measured in extracellular sodium, N-methyl-D-glucamine (NMDG) and NMDG containing 5 mM Ca2+; the values were used to compute relative permeabilities (PNMDG/PNa and PCa/PNa). PNMDG/PNa was not different for P2X2, P2X2/3 and nodose neurones (0·03) but was significantly higher (0·07) for P2X3 receptors. PCa/PNa was not different among P2X3, P2X2/3 and nodose neurones (1·2-1·5) but was significantly higher (2·5) for P2X2 receptors.

  3. External Ca2+ inhibited purinoceptor currents with half-maximal concentrations of 5 mM at the P2X2 receptor, 89 mM at the P2X3 receptor and 15 mM at both the P2X2/3 heteromeric receptor and nodose neurones. In each case, the inhibition was voltage independent and was overcome by increasing concentrations of agonist.

  4. These results may indicate that Ca2+ permeability of the heteromeric (P2X2/3) channel is dominated by that of the P2X3 subunit, while Ca2+ block of the receptor involves both P2X2 and P2X3 subunits. The correspondence in properties between P2X2/3 receptors and nodose ganglion neurones further supports the conclusion that the native alpha,beta-methylene ATP-sensitive receptor is a P2X2/3 heteromultimer.




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