| Chiou JF |
------>authors3_c= ------>paper_class1=1 ------>Impact_Factor=1.101 ------>paper_class3=2 ------>paper_class2=1 ------>vol=71 ------>confirm_bywho=wingchan ------>insert_bywho=solomanc ------>Jurnal_Rank=30.1 ------>authors4_c= ------>comm_author= ------>patent_EDate=None ------>authors5_c= ------>publish_day=25 ------>paper_class2Letter=None ------>page2=602798 ------>medlineContent= ------>unit=E0119 ------>insert_date=20070507 ------>iam=1 ------>update_date=None ------>author=??? ------>change_event=4 ------>ISSN= ------>authors_c= ------>score=500 ------>journal_name=Bioscience, Biotechnology, and Biochemistry ------>paper_name=Staphylokinase-Annexin XI Chimera Exhibited Efficient in Vitro Thrombolytic activities ------>confirm_date=20070507 ------>tch_id=089030 ------>pmid=17485856 ------>page1=602791 ------>fullAbstract=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. ------>tmu_sno=None ------>sno=15594 ------>authors2=Woon MD ------>authors3=Cheng SN ------>authors4=Hsu CH ------>authors5=Cherng SC ------>authors6=Hsieh FK, Lin SM, Shiau CY ------>authors6_c= ------>authors=Chiou JF ------>delete_flag=0 ------>SCI_JNo=None ------>authors2_c= ------>publish_area=0 ------>updateTitle=Staphylokinase-annexin XI chimera exhibited efficient in vitro thrombolytic activities. ------>language=2 ------>check_flag=None ------>submit_date=None ------>country=None ------>no= ------>patent_SDate=None ------>update_bywho=None ------>publish_year=2007 ------>submit_flag=None ------>publish_month=1 |