Protective Mechanisms of Inosine in Platelet Activation and Cerebral Ischemic Damage.

English | 正體中文 | 简体中文 | 全文笔数/总笔数 : 45422/58598 (78%)
造访人次 : 2522595 在线人数 : 179

RC Version 7.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.

Home ‧ Login ‧ Upload ‧ Help ‧ About ‧ Administer

Taipei Medical University Institutional Repository > 醫學院 > 醫學系 > 藥理學科 > 期刊論文 > Item 987654321/8937

Please use this identifier to cite or link to this item: http://libir.tmu.edu.tw/handle/987654321/8937

Title:	Protective Mechanisms of Inosine in Platelet Activation and Cerebral Ischemic Damage.
Authors:	周敦穗;蕭哲志 Hsiao G;Lin KH;Chang Y;Chen TL;Tzu NH;Chou DS;Sheu JR
Contributors:	醫學院藥理學系
Date:	2005
Issue Date:	2009-10-07 14:55:24 (UTC+8)
Abstract:	Objective--Inosine is a naturally occurring nucleoside degraded from adenosine. Recent studies have demonstrated that inosine has potent immunomodulatory and neuroprotective effects. In the present study, we further investigated the inhibitory effects of inosine on platelet activation in vitro and in vivo, as well as in attenuating middle cerebral artery occlusion (MCAO)-induced focal cerebral ischemia in rats. Methods and Results--Inosine concentration-dependently (0.5 to 6.0 mmol/L) inhibited platelet aggregation stimulated by agonists. Inosine (1.5 and 3.0 mmol/L) inhibited phosphoinositide breakdown, [Ca+2]i, and TxA2 formation in human platelets stimulated by collagen (1 µg/mL). In addition, inosine (1.5 and 3.0 mmol/L) markedly increased levels of cyclic GMP and cyclic GMP-induced vasodilator-stimulated phosphoprotein Ser157 phosphorylation. Rapid phosphorylation of a platelet protein of Mr. 47 000 (P47), a marker of protein kinase C activation, was triggered by collagen (1 µg/mL). This phosphorylation was markedly inhibited by inosine (3.0 mmol/L). Inosine (1.5 and 3.0 mmol/L) markedly reduced hydroxyl radical in collagen (1 µg/mL)-activated platelets. In in vivo studies, inosine (400 mg/kg) significantly prolonged the latency period of inducing platelet plug formation in mesenteric venules of mice, and administration of 2 doses (100 mg/kg) or a single dose (150 mg/kg) of inosine significantly attenuated MCAO-induced focal cerebral ischemia in rats. Conclusions--Platelet aggregation contributes significantly to MCAO-induced focal cerebral ischemia. The most important findings of this study suggest that inosine markedly inhibited platelet activation in vitro and in vivo, as well as cerebral ischemia. Thus, inosine treatment may represent a novel approach to lowering the risk of or improving function in thromboembolic-related disorders and ischemia-reperfusion brain injury.
Relation:	Arterioscler Thromb Vasc Biol.(25):1998-2004
Data Type:	article
Appears in Collections:	[藥理學科] 期刊論文

Files in This Item:

File	Description	Size	Format
21-3.pdf		464Kb	Adobe PDF	115	View/Open
摘要.pdf		40Kb	Adobe PDF	66	View/Open

著作權聲明 Copyright Notice

本平台之數位內容為臺北醫學大學所收錄之機構典藏，包含體系內各式學術著作及學術產出。秉持開放取用的精神，提供使用者進行資料檢索、下載與取用，惟仍請適度、合理地於合法範圍內使用本平台之內容，以尊重著作權人之權益。商業上之利用，請先取得著作權人之授權。
The digital content on this platform is part of the Taipei Medical University Institutional Repository, featuring various academic works and outputs from the institution. It offers free access to academic research and public education for non-commercial use. Please use the content appropriately and within legal boundaries to respect copyright owners' rights. For commercial use, please obtain prior authorization from the copyright owner.
瀏覽或使用本平台，視同使用者已完全接受並瞭解聲明中所有規範、中華民國相關法規、一切國際網路規定及使用慣例，並不得為任何不法目的使用TMUIR。
By utilising the platform, users are deemed to have fully accepted and understood all the regulations set out in the statement, relevant laws of the Republic of China, all international internet regulations, and usage conventions. Furthermore, users must not use TMUIR for any illegal purposes.
本平台盡力防止侵害著作權人之權益。若發現本平台之數位內容有侵害著作權人權益情事者，煩請權利人通知本平台維護人員([email protected])，將立即採取移除該數位著作等補救措施。
TMUIR is made to protect the interests of copyright owners. If you believe that any material on the website infringes copyright, please contact our staff([email protected]). We will remove the work from the repository.

Loading...