Lee, Y.M. |
------>authors3_c= ------>paper_class1=1 ------>Impact_Factor=2.477 ------>paper_class3=2 ------>paper_class2=1 ------>vol=537 ------>confirm_bywho=chlin ------>insert_bywho=sheujr ------>Jurnal_Rank=32.6 ------>authors4_c= ------>comm_author=1 ------>patent_EDate=None ------>authors5_c= ------>publish_day=1 ------>paper_class2Letter=None ------>page2=58 ------>medlineContent= ------>unit=E0200 ------>insert_date=20061225 ------>iam=5 ------>update_date=None ------>author=??? ------>change_event=4 ------>ISSN= ------>authors_c= ------>score=500 ------>journal_name=Eur. J. Pharmacol. ------>paper_name=Inhibitory mechanisms of activated matrix metalloproteinase-9 on platelet activation. ------>confirm_date=20061226 ------>tch_id=082005 ------>pmid=16624282 ------>page1=52 ------>fullAbstract=The intracellular mechanisms underlying the signaling pathways of activated matrix metalloproteinase-9 (MMP-9) in platelets are not yet completely understood. Therefore, the aim of this study was to further examine the effects of activated MMP-9 in preventing platelet aggregation. In this study, activated MMP-9 time-dependently (3-60 min) inhibited platelet aggregation in washed human platelet suspensions stimulated by agonists. However, activated MMP-9 had no significant effect on the binding of FITC-triflavin to the platelet glycoprotein IIb/IIIa complex. Triflavin is a specific antagonist of the glycoprotein IIb/IIIa complex purified from snake venom. Moreover, activated MMP-9 (21 and 90 ng/ml) markedly decreased the fluorescence intensity of platelet membranes tagged with diphenylhexatriene. The thrombin-evoked increase in pHi was inhibited in the presence of activated MMP-9 (21 and 90 ng/ml). In addition, activated MMP-9 (21 and 90 ng/ml) markedly reduced the electron spin resonance (ESR) signal intensity of hydroxyl radicals in collagen (1 mug/ml)-activated platelets. These results indicate that the antiplatelet activity of activated MMP-9 may involve the following pathways: (1) activated MMP-9 may initially induce conformational changes in platelet membranes and hydroxyl radical formation, leading to inhibition of platelet aggregation; and (2) activated MMP-9 also inhibits the Na(+)/H(+) exchanger, leading to reduced intracellular Ca(2+) mobilization, and ultimately to inhibition of platelet aggregation. This study further provides new insights concerning the effects of activated MMP-9 on platelet aggregation. ------>tmu_sno=None ------>sno=14506 ------>authors2=Lee, J.J. ------>authors3=Shen, M.Y. ------>authors4=Hsiao, G. ------>authors5=Sheu, J.R. ------>authors6= ------>authors6_c= ------>authors=Lee, Y.M. ------>delete_flag=0 ------>SCI_JNo=None ------>authors2_c= ------>publish_area=0 ------>updateTitle=Inhibitory mechanisms of activated matrix metalloproteinase-9 on platelet activation. ------>language=2 ------>check_flag=None ------>submit_date=None ------>country=None ------>no= ------>patent_SDate=None ------>update_bywho=None ------>publish_year=2006 ------>submit_flag=None ------>publish_month=1 |