ADP ribose is an endogenous ligand for the purinergic P2Y1 receptor

A.J. Gustafsson, L. Muraro, C. Dahlberg, Marie Migaud, Olivier Chevallier, H.N. Khanh, K. Krishnan, Xiaolin Li, Barira Islam

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19 Citations (Scopus)


The mechanism by which extracellular ADP ribose (ADPr) increases intracellular free Ca2+ concentration ([Ca2+](i)) remains unknown. We measured [Ca2+](i) changes in fura-2 loaded rat insulinoma INS-1E cells, and in primary beta-cells from rat and human. A phosphonate analogue of ADPr (PADPr) and 8-Bromo-ADPr (8Br-ADPr) were synthesized. ADPr increased [Ca2+](i) in the form of a peak followed by a plateau dependent on extracellular Ca2+. NAD(+), cADPr, PADPr, 8Br-ADPr or breakdown products of ADPr did not increase [Ca2+](i). The ADPr-induced [Ca2+](i) increase was not affected by inhibitors of TRPM2, but was abolished by thapsigargin and inhibited when phospholipase C and IP3 receptors were inhibited. MRS 2179 and MRS 2279, specific inhibitors of the purinergic receptor P2Y1, completely blocked the ADPrinduced [Ca2+](i) increase. ADPr increased [Ca2+](i) in transfected human astrocytoma cells (1321N1) that express human P2Y1 receptors, but not in untransfected astrocytoma cells. We conclude that ADPr is a specific agonist of P2Y1 receptors. (c) 2010 Elsevier Ireland Ltd. All rights reserved.
Original languageEnglish
Pages (from-to)8-19
Number of pages12
JournalMolecular and Cellular Endocrinology
Issue number1
Publication statusPublished - 10 Feb 2011

ASJC Scopus subject areas

  • Endocrinology
  • Molecular Biology
  • Biochemistry


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