摘要
| 原文 | 英語 |
|---|---|
| 頁（從 - 到） | 4414-4418 |
| 頁數 | 5 |
| 期刊 | Journal of Agricultural and Food Chemistry |
| 卷 | 52 |
| 發行號 | 14 |
| DOIs | |
| 出版狀態 | 已發佈 - 七月 14 2004 |
指紋
ASJC Scopus subject areas
- Agricultural and Biological Sciences (miscellaneous)
- Food Science
- Chemistry (miscellaneous)
引用此文
Mechanisms involved in the antiplatelet activity of rutin, a glycoside of the flavonol quercetin, in human platelets. / Sheu, Joen Rong; Hsiao, George; Chou, Po Hsiu; Shen, Ming Yi; Chou, Duen Suey.
於: Journal of Agricultural and Food Chemistry, 卷 52, 編號 14, 14.07.2004, p. 4414-4418.研究成果: 雜誌貢獻 › 文章
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TY - JOUR
T1 - Mechanisms involved in the antiplatelet activity of rutin, a glycoside of the flavonol quercetin, in human platelets
AU - Sheu, Joen Rong
AU - Hsiao, George
AU - Chou, Po Hsiu
AU - Shen, Ming Yi
AU - Chou, Duen Suey
PY - 2004/7/14
Y1 - 2004/7/14
N2 - The aim of this study was to systematically examine the inhibitory mechanisms of rutin, a well-known flavonoid in platelet aggregation. In this study, rutin concentration-dependently (250 and 290 μM) inhibited platelet aggregation in human platelets stimulated by agonists (i.e., collagen). Rutin (250 and 290 μM) did not significantly interfere with the binding of FITC-triflavin to the glycoprotein IIb/IIIa complex in human platelets. Rutin (250 and 290 μM) markedly inhibited intracellular Ca2+ mobilization and thromboxane A2 formation in human platelets stimulated by collagen. Rapid phosphorylation of a platelet protein of M r 47000 (P47), a marker of protein kinase C activation, was triggered by collagen (1 μg/mL). This phosphorylation was markedly inhibited by rutin (250 and 290 μM). On the other hand, rutin (250 and 290 μM) did not significantly increase the formations of cyclic AMP and nitric oxide/cyclic GMP in platelets. In conclusion, these results indicate that the antiplatelet activity of rutin may involve the following pathways: rutin inhibited the activation of phospholipase C, followed by inhibition of protein kinase C activity and thromboxane A2 formation, thereby leading to inhibition of the phosphorylation of P47 and intracellular Ca2+ mobilization, finally resulting in inhibition of platelet aggregation.
AB - The aim of this study was to systematically examine the inhibitory mechanisms of rutin, a well-known flavonoid in platelet aggregation. In this study, rutin concentration-dependently (250 and 290 μM) inhibited platelet aggregation in human platelets stimulated by agonists (i.e., collagen). Rutin (250 and 290 μM) did not significantly interfere with the binding of FITC-triflavin to the glycoprotein IIb/IIIa complex in human platelets. Rutin (250 and 290 μM) markedly inhibited intracellular Ca2+ mobilization and thromboxane A2 formation in human platelets stimulated by collagen. Rapid phosphorylation of a platelet protein of M r 47000 (P47), a marker of protein kinase C activation, was triggered by collagen (1 μg/mL). This phosphorylation was markedly inhibited by rutin (250 and 290 μM). On the other hand, rutin (250 and 290 μM) did not significantly increase the formations of cyclic AMP and nitric oxide/cyclic GMP in platelets. In conclusion, these results indicate that the antiplatelet activity of rutin may involve the following pathways: rutin inhibited the activation of phospholipase C, followed by inhibition of protein kinase C activity and thromboxane A2 formation, thereby leading to inhibition of the phosphorylation of P47 and intracellular Ca2+ mobilization, finally resulting in inhibition of platelet aggregation.
KW - Phospholipase C
KW - Platelet aggregation
KW - Protein kinase C
KW - Rutin
KW - Thromboxane A
UR - http://www.scopus.com/inward/record.url?scp=3142583067&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=3142583067&partnerID=8YFLogxK
U2 - 10.1021/jf040059f
DO - 10.1021/jf040059f
M3 - Article
C2 - 15237945
AN - SCOPUS:3142583067
VL - 52
SP - 4414
EP - 4418
JO - Journal of Agricultural and Food Chemistry
JF - Journal of Agricultural and Food Chemistry
SN - 0021-8561
IS - 14
ER -