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Related Experiment Videos

P2Z purinoceptors

S E Hickman1, C E Semrad, S C Silverstein

  • 1Department of Physiology, Columbia University, College of Physicians and Surgeons, New York, NY 10032, USA.

Ciba Foundation Symposium
|January 1, 1996
PubMed
Summary
This summary is machine-generated.

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Tetra-anionic ATP4- activates P2Z receptors, creating a non-selective membrane pore permeable to molecules up to 831 Da. This suggests P2Z receptors may involve multiple proteins, potentially including connexin 43.

Area of Science:

  • Cell biology
  • Molecular biology
  • Immunology

Background:

  • P2Z receptors, activated by tetra-anionic ATP (ATP4-), mediate the opening of a non-selective plasma membrane pore.
  • This pore allows passage of ions, nucleotides, and other small molecules typically unable to cross cell membranes.
  • P2Z receptor-induced pores in macrophages are permeable to molecules up to 831 Da.

Purpose of the Study:

  • To investigate the molecular nature of P2Z receptors.
  • To determine if ATP4- binding and pore formation involve a single protein or multiple components.
  • To explore the potential role of connexin 43 in P2Z receptor function.

Main Methods:

  • Expression of P2Z receptor characteristics in Xenopus oocytes by injecting cRNA from a murine macrophage cDNA library.

Related Experiment Videos

  • Treatment of oocytes with ATP4- to induce membrane conductance.
  • Comparison of conductance induced by cRNA versus macrophage mRNA.

    • Main Results:

    • Xenopus oocytes injected with cRNA and treated with ATP4- exhibited non-selective membrane conductance characteristic of P2Z receptors.
    • The conductance induced by cRNA was less than that induced by native macrophage mRNA.
    • ATP4- unresponsive cell lines lacking connexin 43 suggest a link between P2Z receptors and this gap junction protein.

    Conclusions:

    • The findings suggest that P2Z receptors are likely composed of multiple protein subunits.
    • The reduced conductance in oocytes implies a dominant subunit may be present in the cloned cDNA pool.
    • P2Z receptors may induce the opening or surface expression of connexin 43.