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  Glutamate mediates platelet activation through the AMPA receptor

Morrell, C. N., Sun, H., Ikeda, M., Beique, J.-C., Swaim, A. M., Mason, E., et al. (2008). Glutamate mediates platelet activation through the AMPA receptor. The Journal of experimental medicine, 205(3), 575-584. doi:10.1084/jem.20071474.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-002C-080D-1 Version Permalink: https://hdl.handle.net/21.11116/0000-0000-DC2B-9
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 Creators:
Morrell, Craig N., Author
Sun, Hui, Author
Ikeda, Masahiro, Author
Beique, Jean-Claude, Author
Swaim, Anne Marie, Author
Mason, Emily, Author
Martin, Tanika V., Author
Thompson, Laura E., Author
Gozen, Oguz, Author
Ampagoomian, David, Author
Sprengel, Rolf1, Author           
Rothstein, Jeffrey, Author
Faraday, Nauder, Author
Huganir, Richard L., Author
Lowenstein, Charles J., Author
Affiliations:
1Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497704              

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 Abstract: Glutamate is an excitatory neurotransmitter that binds to the kainate receptor, the N-methyl-D-aspartate (NMDA) receptor, and the alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor (AMPAR). Each receptor was first characterized and cloned in the central nervous system (CNS). Glutamate is also present in the periphery, and glutamate receptors have been identified in nonneuronal tissues, including bone, heart, kidney, pancreas, and platelets. Platelets play a central role in normal thrombosis and hemostasis, as well as contributing greatly to diseases such as stroke and myocardial infarction. Despite the presence of glutamate in platelet granules, the role of glutamate during hemostasis is unknown. We now show that activated platelets release glutamate, that platelets express AMPAR subunits, and that glutamate increases agonist-induced platelet activation. Furthermore, we demonstrate that glutamate binding to the AMPAR increases intracellular sodium concentration and depolarizes platelets, which are important steps in platelet activation. In contrast, platelets treated with the AMPAR antagonist CNQX or platelets derived from GluR1 knockout mice are resistant to AMPA effects. Importantly, mice lacking GluR1 have a prolonged time to thrombosis in vivo. Our data identify glutamate as a regulator of platelet activation, and suggest that the AMPA receptor is a novel antithrombotic target.

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Language(s): eng - English
 Dates: 2007-07-172008-01-242008-02-182008-03-17
 Publication Status: Issued
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1084/jem.20071474
URI: http://www.ncbi.nlm.nih.gov/pubmed/18283118
 Degree: -

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Title: The Journal of experimental medicine
  Alternative Title : J Exp Med
Source Genre: Journal
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Publ. Info: New York, NY : Rockefeller Univ. Press
Pages: - Volume / Issue: 205 (3) Sequence Number: - Start / End Page: 575 - 584 Identifier: ISSN: 0022-1007