Effect of Cordycepin-Enriched WIB801C from Cordyceps militaris Suppressing Fibrinogen Binding to Glycoprotein IIb/IIIa
Biomolecules & Therapeutics
; : 60-70, 2015.
Article
de En
| WPRIM
| ID: wpr-202118
Bibliothèque responsable:
WPRO
ABSTRACT
In this study, we investigated the effects of cordycepin-enriched (CE)-WIB801C, a n-butanol extract of Cordyceps militaris-hypha on collagen-stimulated platelet aggregation. CE-WIB801C dose dependently inhibited collagen-induced platelet aggregation, and had a synergistic effect together with cordycepin (W-cordycepin) from CE-WIB801C on the inhibition of collagen-induced platelet aggregation. CE-WIB801C and cordycepin stimulated the phosphorylation of VASP (Ser157) and the dephosphorylation of PI3K and Akt, and inhibited the binding of fibrinogen to glycoprotein IIb/IIIa (alphaIIb/beta3) and the release of ATP and serotonin in collagen-induced platelet aggregation. A-kinase inhibitor Rp-8-Br-cAMPS reduced CE-WIB801C-, and cordycepin-increased VASP (Ser157) phosphorylation, and increased CE-WIB801C-, and cordycepin-inhibited the fibrinogen binding to alphaIIb/beta3. Therefore, we demonstrate that CE-WIB801C-, and cordycepin-inhibited fibrinogen binding to alphaIIb/beta3 are due to stimulation of cAMP-dependent phosphorylation of VASP (Ser157), and inhibition of PI3K/Akt phosphorylation. These results strongly indicate that CE-WIB801C and cordycepin may have preventive or therapeutic potential for platelet aggregation-mediated diseases, such as thrombosis, myocardial infarction, atherosclerosis, and ischemic cerebrovascular disease.
Mots clés
Texte intégral:
1
Indice:
WPRIM
Sujet Principal:
Phosphorylation
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Thrombose
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Plaquettes
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Fibrinogène
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Glycoprotéines
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Sérotonine
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Adénosine triphosphate
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Agrégation plaquettaire
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Butan-1-ol
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Cordyceps
langue:
En
Texte intégral:
Biomolecules & Therapeutics
Année:
2015
Type:
Article