IUPHAR/BPS Guide to Pharmacology CITE
https://doi.org/10.2218/gtopdb/F77/2020.4

P2X receptors (version 2020.4) in the IUPHAR/BPS Guide to Pharmacology Database



Francesco Di Virgilio1, Richard J. Evans2, Simonetta Falzoni1, Samuel J. Fountain3, Michael F. Jarvis4, Charles Kennedy5, Baljit S. Khakh6, Brian F. King7, Annette Nicke8, Patrizia Pellegatti1 and John A. Peters9
  1. University of Ferrara, Italy
  2. University of Leicester, UK
  3. University of East Anglia, UK
  4. AbbVie Pharmaceutical, USA
  5. University of Strathclyde, UK
  6. University of California Los Angeles, USA
  7. University College London, UK
  8. Ludwig-Maximilians-Universität München, Germany
  9. University of Dundee, UK


Abstract

P2X receptors (nomenclature as agreed by the NC-IUPHAR Subcommittee on P2X Receptors [48, 141]) have a trimeric topology [124, 139, 188] with two putative TM domains, gating primarily Na+, K+ and Ca2+, exceptionally Cl-. The Nomenclature Subcommittee has recommended that for P2X receptors, structural criteria should be the initial criteria for nomenclature where possible. X-ray crystallography indicates that functional P2X receptors are trimeric and three agonist molecules are required to bind to a single receptor in order to activate it [139, 93, 101, 170]. Native receptors may occur as either homotrimers (e.g. P2X1 in smooth muscle) or heterotrimers (e.g. P2X2:P2X3 in the nodose ganglion [265], P2X1:P2X5 in mouse cortical astrocytes [155], and P2X2:P2X5 in mouse dorsal root ganglion, spinal cord and mid pons [52, 221]. P2X2, P2X4 and P2X7 receptor activation can also lead to influx of large cationic molecules, such as NMDG, Yo-Pro, ethidium or propidium iodide [200]. The hemi-channel pannexin-1 was initially implicated in the action of P2X7 [201], but not P2X2, receptors [40], but this interpretation is probably misleading. Convincing evidence now supports the view that the activated P2X7 receptor is immediately permeable to large cationic molecules, but influx proceeds at a much slower pace than that of the small cations Na+, K+, and Ca2+ [64].

Contents

This is a citation summary for P2X receptors in the Guide to Pharmacology database (GtoPdb). It exists purely as an adjunct to the database to facilitate the recognition of citations to and from the database by citation analyzers. Readers will almost certainly want to visit the relevant sections of the database which are given here under database links.

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Please note that the database version for the citations given in GtoPdb are to the most recent preceding version in which the family or its subfamilies and targets were substantially changed. The links below are to the current version. If you need to consult the cited version, rather than the most recent version, please contact the GtoPdb curators.

Database links

P2X receptors
http://www.guidetopharmacology.org/GRAC/FamilyDisplayForward?familyId=77
Introduction to P2X receptors
http://www.guidetopharmacology.org/GRAC/FamilyIntroductionForward?familyId=77
    Channels and Subunits
            P2X1
            http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=478
            P2X2
            http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=479
            P2X3
            http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=480
            P2X4
            http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=481
            P2X5
            http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=482
            P2X6
            http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=483
            P2X7
            http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=484

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