Inhibitory Mechanisms of Low Concentrations of Oxidized Low-Density Lipoprotein on Platelet Aggrigation

English | 正體中文 | 简体中文 | Items with full text/Total items : 45422/58598 (78%)
Visitors : 2539543 Online Users : 203

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

Home ‧ Login ‧ Upload ‧ Help ‧ About ‧ Administer

TMUIR > College of Medicine > Department of Medicine > Department of Pharmacology > Periodical Article > Item 987654321/8883

Please use this identifier to cite or link to this item: http://libir.tmu.edu.tw/handle/987654321/8883

Title:	Inhibitory Mechanisms of Low Concentrations of Oxidized Low-Density Lipoprotein on Platelet Aggrigation
Authors:	蔡妍菊;蕭哲志;陳增福;周敦穗 Chou DS;Chan CH;Hsiao G;Shen MY;Tsai YJ;Chen TF;Sheu JR
Contributors:	醫學院藥理學系
Date:	2006
Issue Date:	2009-10-07 14:51:10 (UTC+8)
Abstract:	The intracellular mechanisms underlying oxidized low-density lipoprotein (oxLDL)-signaling pathways in platelets are not yet completely understood. Therefore, the aim of this study was to further examine the effects of oxLDL in prevention of platelet aggregation. In this study, oxLDL concentration-dependently (40–120 \upmuUnknown control sequence '\upmu'g/ml) inhibited platelet aggregation in human platelet-rich plasma stimulated by agonists. Moreover, oxLDL (40 and 80 \upmuUnknown control sequence '\upmu'g/ml) markedly decreased the fluorescence intensity of platelet membranes tagged with diphenylhexatriene. Rapid phosphorylation of a protein of Mr 47,000 (P47), a marker of protein kinase C activation, was triggered by PDBu (150 nM). This phosphorylation was markedly inhibited by oxLDL (40 and 80 \upmuUnknown control sequence '\upmu'g/ml) in phosphorus-32-labeled platelets. In addition, oxLDL (40 and 80 \upmuUnknown control sequence '\upmu'g/ml) markedly increased levels of cyclic AMP and cyclic AMP-induced vasodilator-stimulated phosphoprotein (VASP) Ser157 phosphorylation. The thrombin-evoked increase in pHi was inhibited in the presence of oxLDL (40 and 80 \upmuUnknown control sequence '\upmu'g/ml). These results indicate that the antiplatelet activity of oxLDL may involve the following pathways. (1) oxLDL may initially induce conformational changes in platelet membranes, leading to inhibition of the activation of protein kinase C, followed by inhibition of P47 protein phosphorylation, and intracellular Ca2+ mobilization. (2) oxLDL also activated formation of cyclic AMP and cyclic AMP-induced VASP Ser157 phosphorylation, resulting in inhibition of the Na+/H+exchanger; this leads to reduced intracellular Ca2+ mobilization, and ultimately to inhibition of platelet aggregation. This study further provides new insights concerning the effects of low concentrations of oxLDL on platelet aggregation.
Relation:	J Biomed Sci.(13):333-343.
Data Type:	article
Appears in Collections:	[Department of Pharmacology] Periodical Article

Files in This Item:

File	Description	Size	Format
51.pdf		278Kb	Adobe PDF	54	View/Open
摘要.pdf		42Kb	Adobe PDF	72	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...