P2Z Purinoceptors

  1. Derek J. Chadwick Organizer and
  2. Jamie A. Goode
  1. S. E. Hickman1,
  2. C. E. Semrad2 and
  3. S. C. Silverstein2

Published Online: 28 SEP 2007

DOI: 10.1002/9780470514900.ch4

Ciba Foundation Symposium 198 - P2 Purinoceptors: Localization, Function and Transduction Mechanisms

Ciba Foundation Symposium 198 - P2 Purinoceptors: Localization, Function and Transduction Mechanisms

How to Cite

Hickman, S. E., Semrad, C. E. and Silverstein, S. C. (2007) P2Z Purinoceptors, in Ciba Foundation Symposium 198 - P2 Purinoceptors: Localization, Function and Transduction Mechanisms (eds D. J. Chadwick and J. A. Goode), John Wiley & Sons, Ltd., Chichester, UK. doi: 10.1002/9780470514900.ch4

Author Information

  1. 1

    The Rover Laboratory of Physiology, Department of Physiology and Cellular Biophysics, Columbia University, College of Physicians and Surgeons, 630 West 168th Street, New York, NY 10032, USA

  2. 2

    Departments of Physiology and Medicine, Columbia University, College of Physicians and Surgeons, 630 West 168th Street, New York, NY 10032, USA

Publication History

  1. Published Online: 28 SEP 2007

ISBN Information

Print ISBN: 9780471961253

Online ISBN: 9780470514900

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Keywords:

  • P2Z purinoceptors;
  • human culture-matured macrophages;
  • xenopus oocytes;
  • murine transformed cell lines;
  • pharmacology

Summary

In response to tetra-anionic ATP4−, P2Z receptors signal opening of a non-selective plasma membrane pore which permits passage across cell membranes of ions, nucleotides and other small molecules that are usually membrane impermeant. P2Z receptor-induced pores on murine macrophages, macrophage-like cell lines and human culture-matured macrophages are permeable to molecules of up to 831 Da. The function of P2Z receptors is unknown. Also unknown is whether the binding site for ATP4− and the transmembrane pore, the properties that characterize P2Z receptors, reside on a single protein or reflect the activities of two or more proteins. That ATP4−-unresponsive cell lines do not express connexin 43 has led Beyer and Steinberg to suggest that opening or surface expression of this gap junction protein is induced by P2Z receptors. Xenopus oocytes, injected with cRNA transcribed from a pool of 100 cDNA clones isolated from a murine macrophage-derived cDNA library, and treated with ATP4−, express a non-selective membrane conductance characteristic of P2Z receptors. The conductance induced with cRNA is smaller than that induced by mRNA from macrophages, suggesting the presence of a dominant subunit of a multicomponent receptor in this pool of 100 cDNA clones.