Staphylokinase-annexin XI chimera exhibited efficient in vitro thrombolytic activities

Jeng Fong Chiou, Ming Dar Woon, Shin Nan Cheng, Chih Hsueng Hsu, Shiou Chi Cherng, Feng Ken Hsieh, Shou Ming Lin, Chia Yang Shiau

研究成果: 雜誌貢獻文章同行評審

10 引文 斯高帕斯(Scopus)

摘要

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.

原文英語
頁(從 - 到)1122-1129
頁數8
期刊Bioscience, Biotechnology and Biochemistry
71
發行號5
DOIs
出版狀態已發佈 - 2007

ASJC Scopus subject areas

  • 生物技術
  • 分析化學
  • 生物化學
  • 應用微生物與生物技術
  • 分子生物學
  • 有機化學

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