Journal
MOLECULAR AND CELLULAR ENDOCRINOLOGY
Volume 333, Issue 1, Pages 8-19Publisher
ELSEVIER IRELAND LTD
DOI: 10.1016/j.mce.2010.11.004
Keywords
Calcium; Cell signaling; ADPr; Purinergic receptors; TRPM2
Categories
Funding
- Swedish Research Council [K2006-72X-10159-01-3]
- Karolinska Institutet
- Swedish Medical Society
- Swedish Research Council
- Swedish Heart-Lung Foundation
- Stiftelsen Irma och Arvid Larsson-Rosts minne
- Stiftelsen Goljes minne
- Svenska Diabetesstiftelsen
- Leonardo da Vinci project
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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.
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