血小板
蝰蛇科
毒液
蛇毒
金属蛋白酶
基质金属蛋白酶
糖蛋白
化学
生物化学
PMSF公司
流式细胞术
糖蛋白Ib
分子生物学
药理学
血小板膜糖蛋白
免疫学
生物
酶
作者
Yüng-Zu Tseng,Chia‐Jung Lee,Ting Huang
出处
期刊:Thrombosis and Haemostasis
[Georg Thieme Verlag KG]
日期:2004-01-01
卷期号:91 (02): 315-324
被引量:21
摘要
The biologically active components from Viperidae venoms specifically affect cell-matrix interactions, and have been utilized for developing anti-adhesive therapy as anti-thrombotic and anti-angiogenic agents. Utilizing platelet aggregometry coupled with flow cytometry, we found that a metalloproteinase isolated from Trimeresurus flavoviridis, termed triflamp, inhibited heterotypic adhesion between platelets and neutrophils in whole blood samples. Triflamp is a monomeric glycoprotein with a molecular weight of approximately 28 kDa. Triflamp has a N-terminal amino acid sequence homologous to other venom metalloproteinases isolated from T. flavoviridis. The enzymatic activity of triflamp was inhibited by EDTA and phenanthroline but not by PMSF. Moreover, triflamp is a pure alpha-fibrinogenase. Studies aimed at determining the nature of triflamp in affecting platelets or neutrophils revealed a selective inhibitory activity to glycoprotein (GP) Ibalpha-dependent platelet aggregation and PSGL-1-dependent neutrophil homotypic aggregation, indicating that its effects are rather specific. As judged by Western blotting, GPIbalpha on platelets and PSGL-1 on neutrophils are the substrates of triflamp. In conclusion, we suggest the novel role of venom metalloproteinase from Viperidae affecting the blood cell-cell interactions, thus offering a potential approach for further exploration of anti-inflammatory agents.
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