Staphylokinase-Annexin XI Chimera Exhibited Efficient in Vitro Thrombolytic activities

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TMUIR > College of Medicine > Department of Medicine > Department of Radiology > Periodical Article > Item 987654321/1199

Please use this identifier to cite or link to this item: http://libir.tmu.edu.tw/handle/987654321/1199

Title:	Staphylokinase-Annexin XI Chimera Exhibited Efficient in Vitro Thrombolytic activities
Authors:	邱仲峰 Chiou JF;Woon MD;Cheng SN;Hsu CH;Cherng SC;Hsieh FK;Lin SM;Shiau CY
Contributors:	醫學系放射線學科
Date:	2007
Issue Date:	2009-08-14 12:59:03 (UTC+8)
Abstract:	Annexins (ANXs) are a family of calcium dependent phospholipid binding proteins. Phospholipids such as phosphatidylserine are rapidly exposed on the surfaces of injured endothelial cells, activated platelets, and apoptotic cells in a large number of disorders. In this study, annexin V and XI (ANXV and ANXXI) were individually fused to the C-terminal of staphylokinase (SAK), a fibrin-selective thrombolytic protein, to form chimeras for evaluation of their in-vitro thrombolytic activities. The two chimeras were found to have plasminogen activation activity of comparable efficiency. When the chimeras were challenged under higher concentrations of plasmin for 1 h, hydrolysis of them into moieties was not seen on SDS-PAGE. In two thrombolytic assays, SAK-ANXXI was found to resolve both platelet rich plasma (PRP) clots and platelet poor plasma (PPP) clots with an efficiency similar to that of SAK. However, SAK-ANXV showed significantly reduced efficiency. With regard to anticoagulation ability, SAK-ANXXI was also found to have a stronger effect on dose-dependent extension of clotting time among the four tested proteins. The unique long N-terminal tail of ANXXI, composed of 202 residues, in contrast to the 16 residues of ANXV, probably served successfully to dispatch two moieties to function properly in a complicated microenvironment. Hence, a new option other than the most committed ANXV for the ANX based chimera without elaboration of linker construction is presented.
Relation:	Bioscience, Biotechnology, and Biochemistry.(71): 602791-602798.
Data Type:	article
Appears in Collections:	[Department of Radiology] Periodical Article

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