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논문 기본 정보

자료유형
학술저널
저자정보
Ryu, Jin-Hyeob (Department of Biomedical Laboratory Science, College of Medical Science, Konyang University) Ro, Ju-Ye (Department of Biomedical Laboratory Science, College of Medical Science, Konyang University) Park, Hwa-Jin (Department of Biomedical Laboratory Science, College of Biomedical Science and Engineering and Regional Research Center, Inje University) Cho, Hyun-Jeong (Department of Biomedical Laboratory Science, College of Medical Science, Konyang University)
저널정보
한국응용생명화학회 Applied Biological Chemistry Applied Biological Chemistry 제57권 제2호
발행연도
2014.1
수록면
221 - 228 (8page)

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초록· 키워드

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Effects of ginkgolide A (GA) from Ginkgo biloba leaves in collagen ($10{\mu}g/mL$)-stimulated platelet aggregation were investigated. Zymographic analysis confirmed that pro-matrix metalloproteinase-9 (MMP-9) (92 kDa) was activated by GA to form an activated MMP-9 (86-kDa) on gelatinolytic activities. GA concentration-dependently inhibited platelet aggregation, intracellular $Ca^{2+}$; mobilization, and thromboxane $A^2$ ($TXA^2$) formation by inhibiting the cyclooxygenase-1 (COX-1) activity in collagen-stimulated platelets. In addition, GA increased the formation of cyclic adenosine monophosphate (cAMP) and cyclic guanosine monophosphate (cGMP), which have an anti-platelet function in both resting and collagen-stimulated platelets. On the other hand, GA did not prolong prothrombin time (PT) and activated partial thromboplastin time (aPTT) associated with the extrinsic and intrinsic coagulation pathways on human plasma, respectively. Therefore, we suggest that the inhibitory effect of GA on platelet aggregation might involve the following pathway. GA may increase the MMP-9 activity and intracellular cAMP and cGMP production, inhibit intracellular $Ca^{2+}$ mobilization, and decrease $TXA^2$ production by down-regulating the COX-1, thereby leading to inhibition of platelet aggregation without cytotoxicity. These results strongly indicate that GA is a potent inhibitor of collagen-stimulated platelet aggregation. It may play an important role as a negative regulator during platelet activation.

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