The Diverse Series of Recombinant P2Y Purinoceptors

  1. Derek J. Chadwick Organizer and
  2. Jamie A. Goode
  1. E. A. Barnard1,
  2. T. E. Webb1,
  3. J. Simon1 and
  4. S. P. Kunapuli2

Published Online: 28 SEP 2007

DOI: 10.1002/9780470514900.ch10

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

Barnard, E. A., Webb, T. E., Simon, J. and Kunapuli, S. P. (2007) The Diverse Series of Recombinant P2Y 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.ch10

Author Information

  1. 1

    Molecular Neurobiology Unit, Division of Basic Medical Sciences, Royal Free Hospital School of Medicine, Rowland Hill Street, London NW3 2PF, UK

  2. 2

    Department of Physiology, Temple University Medical School, Philadelphia, PA 19140, USA

Publication History

  1. Published Online: 28 SEP 2007

ISBN Information

Print ISBN: 9780471961253

Online ISBN: 9780470514900

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Keywords:

  • diverse series;
  • recombinant P2Y purinoceptors;
  • cDNA encoding;
  • G protein-coupled receptor;
  • P2Y1 receptor

Summary

A cDNA encoding a P2Y purinoceptor was originally cloned from chick brain and the bovine and human homologues have recently been obtained. These are seven-transmembrane-domain polypetides, i.e. G protein-coupled receptors. When activated by agonists, this P2Y receptor mobilizes intracellular Ca2+ and has been shown to be coupled to inositol-1,4,5-trisphosphate formation. Its pharmacology has been established in several expression systems, using both ligand binding and functional responses: 2-methylthioATP has the highest potency of nucleotides and derivatives tested, while UTP and α,β-methylene ATP are inactive. This was hence assigned as a new subtype of the pharmacologically defined P2Y receptors, P2Y1. P2Y1 receptors are exceptionally abundant in the brain. A P2U receptor reported by others can be designated P2Y2. Another P2 receptor subtype, P2Y3, now cloned as a cDNA from the brain and expressed in oocytes and in transfected cells, shows a quite different ligand potency profile to the first two. A fourth subtype is expressed primarily in certain haemopoietic cells and in cardiac muscle. A putative fifth subtype is expressed only in T lymphocytes, upon activation. Yet other P2Y subtypes are indicated by recent cloning studies. The amino acid sequences of all of these P2 receptors, while displaying some homology, are strikingly diverse: they form a separate and unusual new family in the G protein-coupled receptor main superfamily.