Skip to main content
PMC home page
The Journal of Physiology logoLink to The Journal of Physiology
. 1997 Jan 1;498(Pt 1):143–151. doi: 10.1113/jphysiol.1997.sp021847

Purinoceptor-operated cationic channels in human B lymphocytes.

F Markwardt 1, M Löhn 1, T Böhm 1, M Klapperstück 1
PMCID: PMC1159240  PMID: 9023774

Abstract

1. Using the patch clamp method in the outside-out configuration, purinoceptor-dependent unitary currents were measured in tonsillar and transformed tonsillar human B lymphocytes. 2. Single channel currents were evoked by ATP4-, the free-acid form of ATP, and by 2',3' O-benzoyl-4-benzoyl-ATP (BzATP) in the micromolar concentration range, but not by 10 mM ADP3- or 0.5 mM Mg(2+)-bound ATP. 3. The channels could be activated and deactivated several times for as long as 30 min even in the absence of intracellular ATP, GTP, or glucose. 4. The channels were selective for small cations and had a conductance of 9 pS with Cs+ as the intracellular and Na+ as the extracellular monovalent cation. 5. The half-maximal activation of the channels was obtained by 114 microM ATP4- and by 16 microM BzATP. The increase in the open probability after raising the ATP4- concentration was mainly due to a decrease in the times the channels spend in the closed state. 6. It is concluded that human B lymphocytes possess cationic channels directly gated by extracellular ATP4-. Their agonist binding characteristics are typical for P2z purinoceptors, but their permeation behaviour is different from the large non-specific pores formed by ATP4- in fibroblasts, macrophages and mast cells.

Full text

PDF
143

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bean B. P. Pharmacology and electrophysiology of ATP-activated ion channels. Trends Pharmacol Sci. 1992 Mar;13(3):87–90. doi: 10.1016/0165-6147(92)90032-2. [DOI] [PubMed] [Google Scholar]
  2. Brake A. J., Wagenbach M. J., Julius D. New structural motif for ligand-gated ion channels defined by an ionotropic ATP receptor. Nature. 1994 Oct 6;371(6497):519–523. doi: 10.1038/371519a0. [DOI] [PubMed] [Google Scholar]
  3. Bretschneider F., Klapperstück M., Löhn M., Markwardt F. Nonselective cationic currents elicited by extracellular ATP in human B-lymphocytes. Pflugers Arch. 1995 Mar;429(5):691–698. doi: 10.1007/BF00373990. [DOI] [PubMed] [Google Scholar]
  4. Brière F., Servet-Delprat C., Bridon J. M., Saint-Remy J. M., Banchereau J. Human interleukin 10 induces naive surface immunoglobulin D+ (sIgD+) B cells to secrete IgG1 and IgG3. J Exp Med. 1994 Feb 1;179(2):757–762. doi: 10.1084/jem.179.2.757. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Chen C. C., Akopian A. N., Sivilotti L., Colquhoun D., Burnstock G., Wood J. N. A P2X purinoceptor expressed by a subset of sensory neurons. Nature. 1995 Oct 5;377(6548):428–431. doi: 10.1038/377428a0. [DOI] [PubMed] [Google Scholar]
  6. Di Virgilio F. The P2Z purinoceptor: an intriguing role in immunity, inflammation and cell death. Immunol Today. 1995 Nov;16(11):524–528. doi: 10.1016/0167-5699(95)80045-X. [DOI] [PubMed] [Google Scholar]
  7. Dubyak G. R., el-Moatassim C. Signal transduction via P2-purinergic receptors for extracellular ATP and other nucleotides. Am J Physiol. 1993 Sep;265(3 Pt 1):C577–C606. doi: 10.1152/ajpcell.1993.265.3.C577. [DOI] [PubMed] [Google Scholar]
  8. Harden T. K., Boyer J. L., Nicholas R. A. P2-purinergic receptors: subtype-associated signaling responses and structure. Annu Rev Pharmacol Toxicol. 1995;35:541–579. doi: 10.1146/annurev.pa.35.040195.002545. [DOI] [PubMed] [Google Scholar]
  9. Honoré E., Martin C., Mironneau C., Mironneau J. An ATP-sensitive conductance in cultured smooth muscle cells from pregnant rat myometrium. Am J Physiol. 1989 Aug;257(2 Pt 1):C297–C305. doi: 10.1152/ajpcell.1989.257.2.C297. [DOI] [PubMed] [Google Scholar]
  10. Markwardt F., Isenberg G. Gating of maxi K+ channels studied by Ca2+ concentration jumps in excised inside-out multi-channel patches (myocytes from guinea pig urinary bladder). J Gen Physiol. 1992 Jun;99(6):841–862. doi: 10.1085/jgp.99.6.841. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Naumov A. P., Kaznacheyeva E. V., Kiselyov K. I., Kuryshev Y. A., Mamin A. G., Mozhayeva G. N. ATP-activated inward current and calcium-permeable channels in rat macrophage plasma membranes. J Physiol. 1995 Jul 15;486(Pt 2):323–337. doi: 10.1113/jphysiol.1995.sp020815. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Naumov A. P., Kiselyov K. I., Mamin A. G., Kaznacheyeva E. V., Kuryshev Y. A., Mozhayeva G. N. ATP-operated calcium-permeable channels activated via a guanine nucleotide-dependent mechanism in rat macrophages. J Physiol. 1995 Jul 15;486(Pt 2):339–347. doi: 10.1113/jphysiol.1995.sp020816. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Neher E. Correction for liquid junction potentials in patch clamp experiments. Methods Enzymol. 1992;207:123–131. doi: 10.1016/0076-6879(92)07008-c. [DOI] [PubMed] [Google Scholar]
  14. Nuttle L. C., Dubyak G. R. Differential activation of cation channels and non-selective pores by macrophage P2z purinergic receptors expressed in Xenopus oocytes. J Biol Chem. 1994 May 13;269(19):13988–13996. [PubMed] [Google Scholar]
  15. Pizzo P., Zanovello P., Bronte V., Di Virgilio F. Extracellular ATP causes lysis of mouse thymocytes and activates a plasma membrane ion channel. Biochem J. 1991 Feb 15;274(Pt 1):139–144. doi: 10.1042/bj2740139. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Saribaş A. S., Lustig K. D., Zhang X., Weisman G. A. Extracellular ATP reversibly increases the plasma membrane permeability of transformed mouse fibroblasts to large macromolecules. Anal Biochem. 1993 Feb 15;209(1):45–52. doi: 10.1006/abio.1993.1080. [DOI] [PubMed] [Google Scholar]
  17. Soto F., Garcia-Guzman M., Gomez-Hernandez J. M., Hollmann M., Karschin C., Stühmer W. P2X4: an ATP-activated ionotropic receptor cloned from rat brain. Proc Natl Acad Sci U S A. 1996 Apr 16;93(8):3684–3688. doi: 10.1073/pnas.93.8.3684. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Surprenant A., Rassendren F., Kawashima E., North R. A., Buell G. The cytolytic P2Z receptor for extracellular ATP identified as a P2X receptor (P2X7). Science. 1996 May 3;272(5262):735–738. doi: 10.1126/science.272.5262.735. [DOI] [PubMed] [Google Scholar]
  19. Tatham P. E., Lindau M. ATP-induced pore formation in the plasma membrane of rat peritoneal mast cells. J Gen Physiol. 1990 Mar;95(3):459–476. doi: 10.1085/jgp.95.3.459. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Valera S., Hussy N., Evans R. J., Adami N., North R. A., Surprenant A., Buell G. A new class of ligand-gated ion channel defined by P2x receptor for extracellular ATP. Nature. 1994 Oct 6;371(6497):516–519. doi: 10.1038/371516a0. [DOI] [PubMed] [Google Scholar]
  21. Wiley J. S., Chen R., Jamieson G. P. The ATP4- receptor-operated channel (P2Z class) of human lymphocytes allows Ba2+ and ethidium+ uptake: inhibition of fluxes by suramin. Arch Biochem Biophys. 1993 Aug 15;305(1):54–60. doi: 10.1006/abbi.1993.1392. [DOI] [PubMed] [Google Scholar]
  22. Wiley J. S., Chen R., Wiley M. J., Jamieson G. P. The ATP4- receptor-operated ion channel of human lymphocytes: inhibition of ion fluxes by amiloride analogs and by extracellular sodium ions. Arch Biochem Biophys. 1992 Feb 1;292(2):411–418. doi: 10.1016/0003-9861(92)90010-t. [DOI] [PubMed] [Google Scholar]
  23. Wiley J. S., Jamieson G. P., Mayger W., Cragoe E. J., Jr, Jopson M. Extracellular ATP stimulates an amiloride-sensitive sodium influx in human lymphocytes. Arch Biochem Biophys. 1990 Aug 1;280(2):263–268. doi: 10.1016/0003-9861(90)90328-v. [DOI] [PubMed] [Google Scholar]
  24. el-Moatassim C., Maurice T., Mani J. C., Dornand J. The [Ca2+]i increase induced in murine thymocytes by extracellular ATP does not involve ATP hydrolysis and is not related to phosphoinositide metabolism. FEBS Lett. 1989 Jan 2;242(2):391–396. doi: 10.1016/0014-5793(89)80508-3. [DOI] [PubMed] [Google Scholar]

Articles from The Journal of Physiology are provided here courtesy of The Physiological Society

RESOURCES