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Antiplatelet activity of chrysin via inhibiting platelet αIIbβ3‐mediated signaling pathway
Author(s) -
Liu Gang,
Xie Wen,
He AoDi,
Da XingWen,
Liang MingLu,
Yao Guangqiang,
Xiang JiZhou,
Gao Cunji,
Ming ZhangYin
Publication year - 2016
Publication title -
molecular nutrition and food research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.495
H-Index - 131
eISSN - 1613-4133
pISSN - 1613-4125
DOI - 10.1002/mnfr.201500801
Subject(s) - chrysin , chemistry , platelet , phosphorylation , protein kinase b , platelet activation , pharmacology , clot retraction , signal transduction , microbiology and biotechnology , biochemistry , thrombin , immunology , biology , flavonoid , antioxidant
Scope Propolis is thought to help prevent thrombotic and related cardiovascular diseases in humans. Chrysin, a bioflavonoids compound found in high levels in propolis and in honey, has been reported to possess antiplatelet activity. However, the mechanism by which it inhibits platelet function is unclear. Methods and results The effects of chrysin on agonist‐activated platelet‐aggregation, granule‐secretion, and integrin αIIbβ3 activation were examined. Its effects on the phosphorylation of Akt, GSK3β, MAPKs, and several proteins of the glycoprotein VI (GPVI) signaling pathway were also studied on collaged‐activated platelets. In addition, human platelet spreading on immobilized fibrinogen was also tested. We found that chrysin dose dependently inhibited platelet aggregation and granule secretion induced by collagen, as well as platelet aggregation induced by ADP, thrombin, and U46619. Chrysin also markedly reduced the number of adherent platelets and the single platelet spreading area on immobilized fibrinogen. Biochemical analysis revealed that chrysin inhibited collagen‐induced activation of Syk, PLCγ2, PKC, as well as the phosphorylation of Akt and ERK1/2. Additionally, chrysin attenuated phosphorylation of molecules such as FcγRIIa, FAK, Akt, and GSK3β in platelet spreading on immobilized fibrinogen. Conclusions Our findings indicate that chrysin suppresses not only integrin αIIbβ3‐mediated “inside‐out” signaling, but also the “outside‐in” signal transmission. This implies that chrysin may represent a potential candidate for an antiplatelet agent.