Abstract
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
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenosine Triphosphate / analogs & derivatives
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Adenosine Triphosphate / pharmacology
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Animals
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Benzoxazoles
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Cell Membrane Permeability*
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Electrophysiology
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Fluorescent Dyes / metabolism
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Gene Expression
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Ion Channels / metabolism*
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Meglumine / metabolism
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Microinjections
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Oocytes
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Patch-Clamp Techniques
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Phenotype
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Quinolinium Compounds
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RNA, Complementary / genetics
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Receptors, Purinergic P2 / genetics
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Receptors, Purinergic P2 / metabolism*
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Receptors, Purinergic P2X7
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Recombinant Proteins / metabolism
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Xenopus
Substances
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Benzoxazoles
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Fluorescent Dyes
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Ion Channels
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Quinolinium Compounds
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RNA, Complementary
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Receptors, Purinergic P2
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Receptors, Purinergic P2X7
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Recombinant Proteins
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YO-PRO 1
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3'-O-(4-benzoyl)benzoyladenosine 5'-triphosphate
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Meglumine
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Adenosine Triphosphate