P2X7 purinoceptor expression in Xenopus oocytes is not sufficient to produce a pore-forming P2Z-like phenotype

FEBS Lett. 1997 Jul 14;411(2-3):339-45. doi: 10.1016/s0014-5793(97)00700-x.


The purinergic rP2X7 receptor expressed in a number of heterologous systems not only functions as a cation channel but also gives rise to a P2Z-like response, i.e. a reversible membrane permeabilization that allows the passage of molecules with molecular masses of > or = 300 Da. We investigated the properties of rP2X7 receptors expressed in Xenopus oocytes. In two-electrode voltage-clamp experiments, ATP or BzATP caused inward currents that were abolished or greatly diminished when NMDG+ or choline replaced Na+ as the principal external cation. In fluorescent dye experiments, BzATP application did not result in entry of the fluorophore YO-PRO-1(2+). Thus, rP2X7 expression in Xenopus oocytes does not by itself give rise to the pore-forming P2Z phenotype, suggesting that ancillary factors are involved.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphate / analogs & derivatives
  • Adenosine Triphosphate / pharmacology
  • Animals
  • Benzoxazoles
  • Cell Membrane Permeability*
  • Electrophysiology
  • Fluorescent Dyes / metabolism
  • Gene Expression
  • Ion Channels / metabolism*
  • Meglumine / metabolism
  • Microinjections
  • Oocytes
  • Patch-Clamp Techniques
  • Phenotype
  • Quinolinium Compounds
  • RNA, Complementary / genetics
  • Receptors, Purinergic P2 / genetics
  • Receptors, Purinergic P2 / metabolism*
  • Receptors, Purinergic P2X7
  • Recombinant Proteins / metabolism
  • Xenopus


  • Benzoxazoles
  • Fluorescent Dyes
  • Ion Channels
  • Quinolinium Compounds
  • RNA, Complementary
  • Receptors, Purinergic P2
  • Receptors, Purinergic P2X7
  • Recombinant Proteins
  • YO-PRO 1
  • 3'-O-(4-benzoyl)benzoyladenosine 5'-triphosphate
  • Meglumine
  • Adenosine Triphosphate