Characteristics of ATP-Induced Current Through P2X7 Receptor in NG108-15 Cells: Unique Antagonist Sensitivity and Lack of Pore Formation
| Autor: | Isao Matsuoka, Tomokazu Watano, Junko Kimura |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
Cell Membrane Permeability
Patch-Clamp Techniques Membrane permeability Suramin P2 receptor Pharmacology Mice chemistry.chemical_compound Adenosine Triphosphate 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine Cations Purinergic P2 Receptor Antagonists Tumor Cells Cultured medicine Animals PPADS Receptor Fluorescent Dyes Benzoxazoles Receptors Purinergic P2 Triazines Chemistry Quinolinium Compounds Antagonist Blocking effect Rats Competitive antagonist Pyridoxal Phosphate Biophysics Receptors Purinergic P2X7 medicine.drug |
| Zdroj: | Japanese Journal of Pharmacology. 88:428-435 |
| ISSN: | 0021-5198 |
| DOI: | 10.1254/jjp.88.428 |
| Popis: | ATP activates the mouse P2X7 receptor and induces a nonselective-cation current in NG108-15 cells. We investigated the effects of five receptor antagonists on the ATP-induced nonselective-cation current through P2X7 receptor (I(NS.P2X7)) in NG108-15 cells. Nonselective P2 receptor antagonists, RB-2, PPADS and suramin inhibited the I(NS.P2X7) with IC50 values of 4.3, 53 and 40 microM, respectively. However, KN-04, which is a potent antagonist of human P2X7 receptors but is not that of rat P2X7 receptors, had only a weak blocking effect. Furthermore, oxidized-ATP (300 microM), an antagonist of the P2X7 receptor-mediated pore-formation, did not affect the I(NS.P2X7). Prolonged ATP application did not increase the membrane permeability to large molecules, N-methyl-D-glucamine or Yo-Pro-1, indicating that pore-formation was not promoted by the P2X7 receptor activation in NG108-15 cells. These results suggest that antagonist sensitivities and pore-forming properties of the P2X7 receptors in NG108-15 cells are different from those of other cells types. |
| Databáze: | OpenAIRE |
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