Effect of Cordycepin-Enriched WIB801C from Cordyceps militaris Suppressing Fibrinogen Binding to Glycoprotein IIb/IIIa.
10.4062/biomolther.2014.086
- Author:
Dong Ha LEE
1
;
Hyun Hong KIM
;
Deok Hwi LIM
;
Jong Lae KIM
;
Hwa Jin PARK
Author Information
1. Department of Biomedical Laboratory Science, College of Biomedical Science and Engineering, Inje University, Gimhae 621-749, Republic of Korea. mlsjpark@inje.ac.kr
- Publication Type:Original Article
- Keywords:
CE-WIB801C;
Cordycepin;
VASP (Ser157);
PI3K/Akt;
Fibrinogen binding
- MeSH:
1-Butanol;
Adenosine Triphosphate;
Atherosclerosis;
Blood Platelets;
Cordyceps*;
Fibrinogen*;
Glycoproteins*;
Myocardial Infarction;
Phosphorylation;
Platelet Aggregation;
Serotonin;
Thrombosis
- From:Biomolecules & Therapeutics
2015;23(1):60-70
- CountryRepublic of Korea
- Language:English
-
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.
