| First Author | Gustafsson AJ | Year | 2011 |
| Journal | Mol Cell Endocrinol | Volume | 333 |
| Issue | 1 | Pages | 8-19 |
| PubMed ID | 21094205 | Mgi Jnum | J:168615 |
| Mgi Id | MGI:4889131 | Doi | 10.1016/j.mce.2010.11.004 |
| Citation | Gustafsson AJ, et al. (2011) ADP ribose is an endogenous ligand for the purinergic P2Y1 receptor. Mol Cell Endocrinol 333(1):8-19 |
| abstractText | The mechanism by which extracellular ADP ribose (ADPr) increases intracellular free Ca(2+) concentration ([Ca(2+)](i)) remains unknown. We measured [Ca(2+)](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 [Ca(2+)](i) in the form of a peak followed by a plateau dependent on extracellular Ca(2+). NAD(+), cADPr, PADPr, 8Br-ADPr or breakdown products of ADPr did not increase [Ca(2+)](i). The ADPr-induced [Ca(2+)](i) increase was not affected by inhibitors of TRPM2, but was abolished by thapsigargin and inhibited when phospholipase C and IP(3) receptors were inhibited. MRS 2179 and MRS 2279, specific inhibitors of the purinergic receptor P2Y1, completely blocked the ADPr-induced [Ca(2+)](i) increase. ADPr increased [Ca(2+)](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. |
