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New insights on P2X purinoceptors

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Abstract

Significant advances in understanding of P2X purinoceptor pharmacology have been made in the last few years. The limitations of nucleotide agonists as drug tools have now been amply demonstrated. Fortunately, inhibitors of the degrading ecto-ATPase enzymes are becoming available and it has become apparent that the complete removal of all divalent cations can be used experimentally in some systems to prevent nucleotide breakdown. Despite these issues, convincing evidence for P2X receptor heterogeneity, from data with agonists, has recently been reported.

A number of new antagonists at P2X purinoceptors have also recently been described which to some degree appear to be more specific and useful than earlier antagonists like suramin. It is now apparent that suramin is a poor antagonist of ATP in many tissues because it potently inhibits ATPase activity at similar concentrations to those at which it blocks the P2X purinoceptor.

Advances in the use of radiolabelled nucleotides as radioligands for binding studies has allowed the demonstration of P2X purinoceptors in a variety of tissues throughout the body including the brain. These studies have also provided evidence for receptor heterogeneity. Excitingly, two P2X purinoceptor genes have been cloned but operational studies suggest that more than two types exist. The cloning studies have also demonstrated a unique structure for the P2X purinoceptor which differentiates it from all other ligand-gated ion channel receptors. Further studies on P2X purinoceptor operation and structure are needed to help resolve controversies alluded to regarding the characterization and classification of nucleotide receptors. Hopefully such studies will also lead to a better understanding of the physiological and pathological importance of ATP and its activation of P2X purinoceptors. This will require the identification of better drug tools, in particular antagonists which may also provide the basis for novel therapeutic agents.

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Authors and Affiliations

  1. Glaxo Institute of Applied Pharmacology, Department of Pharmacology, University of Cambridge, CB2 1QJ, Tennis Court Road, Cambridge, UK

    Patrick P. A. Humphrey, Ian Kennedy, Baljit S. Khakh, Anton D. Michel & Derek J. Trezise

  2. Glaxo Institute for Molecular Biology, 14 chemin des Aulx, CH-1228, Plan-les-Ouates, Geneva, Switzerland

    Gary Buell & Annmarie Surprenant

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  1. Patrick P. A. Humphrey
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  2. Gary Buell
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  3. Ian Kennedy
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Humphrey, P.P.A., Buell, G., Kennedy, I. et al. New insights on P2X purinoceptors. Naunyn-Schmiedeberg's Arch Pharmacol 352, 585–596 (1995). https://doi.org/10.1007/BF00171316

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