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Resolvin E1 regulates adenosine diphosphate activation of human platelets
Gabrielle Fredman1, Thomas E Van Dyke, Charles N Serhan
1Department of Anesthesiology, Perioperative, and Pain Medicine, Brigham and Women's Hospital and Harvard Medical School, Center for Experimental Therapeutics and Reperfusion Injury, Boston, Mass 02115, USA.
Arteriosclerosis, Thrombosis, and Vascular Biology
|August 13, 2010
Summary
Resolvin E1 (RvE1) inhibits adenosine diphosphate (ADP)-activated platelet aggregation by interacting with the human ChemR23 receptor. This finding reveals a new mechanism for how omega-3 fatty acids resolve vascular inflammation and impact pathological cardiovascular events.
Area of Science:
- Biochemistry
- Molecular Biology
- Cardiovascular Research
Background:
- Resolvin E1 (RvE1) is a specialized proresolving mediator derived from eicosapentaenoic acid.
- RvE1 demonstrates organ-protective effects and interacts with various cell types, including platelets.
- Previous studies indicated RvE1 reduces platelet aggregation induced by certain agonists like ADP.
Purpose of the Study:
- To investigate how RvE1 regulates adenosine diphosphate (ADP)-mediated platelet activation.
- To determine the specific receptors involved in RvE1's effect on platelet aggregation.
- To elucidate the role of RvE1 in ADP-dependent platelet activation and vascular inflammation.
Main Methods:
- Incubation of human platelets with varying concentrations of RvE1.
- Assessment of ADP-stimulated P-selectin mobilization and polymerized actin content.
- Utilizing a P2Y(12)-β-arrestin-coupled cell system and recombinant P2Y(12)-expressing cells transfected with human ChemR23.
Main Results:
- RvE1 significantly reduced ADP-stimulated P-selectin mobilization and actin polymerization in platelets.
- RvE1 did not directly stimulate or block intracellular calcium mobilization via P2Y(12) receptors.
- RvE1 blocked ADP-induced P2Y(12) signals in cells co-expressing P2Y(12) and the RvE1 receptor, human ChemR23.
Conclusions:
- RvE1's inhibitory effects on platelet activation are dependent on the human ChemR23 receptor.
- RvE1 selectively targets ADP-activated platelets, revealing a novel cellular mechanism.
- These findings link omega-3 fatty acid metabolism to the resolution of vascular inflammation and modulation of pathological cardiovascular events.
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