Differential action of proteases from Trimeresurus malabaricus, Naja naja and Daboia russellii venoms on hemostasis
Differential action of proteases from Trimeresurus malabaricus, Naja naja and Daboia russellii venoms on hemostasis
复制标题
DOI：
10.1016/j.cbpc.2006.03.001
复制
发表时间：
2006-07-01
影响因子：
3.9
通讯作者：
Vishwanath, B. S.
中科院分区：
文献类型：
--
作者：
Gowda, C. D. Raghavendra;Nataraju, A.;Vishwanath, B. S.
毒液蛋白酶的行动和止血的作用进行了比较，在竹叶青蛇，Daboia russellii和眼镜蛇从西高止山脉，印度南部地区的毒液。这些毒液表现出不同量的蛋白水解活性，也不同地影响止血。马拉巴利刺鳅蛇毒的酪蛋白水解活性分别是白刺鳅的16倍和24倍。naja和D. russellii毒液。在合成底物驯服的情况下，在马拉巴河鲀毒液中观察到最高活性。N.即使在较高浓度下，眼镜蛇毒液也不水解驯服。蛋白水解活性的这些变化也影响凝血过程。T malabaricus和D.罗素氏毒液具有强烈的促凝血作用，并将再钙化时间分别从148秒减少到14秒和12秒。与此相似，马拉巴里T. malabaricus和D.拉塞尔氏毒液使凝血酶原时间从12.5秒降低到6.0秒。另一方面，N.眼镜蛇毒具有抗凝作用，钙化时间为600 s，凝血酶原时间为42 s。尽管对止血有不同的作用，但所有毒液都能水解纤维蛋白原。马拉巴毒蜥毒液水解A α和B β亚基。而D. russellii和N.眼镜蛇毒液仅水解A α。这些毒液都不水解纤维蛋白原的γ亚基。用特异性蛋白酶抑制剂进行的抑制研究表明，N。眼镜蛇和马拉巴河鲀毒液仅含有金属蛋白酶。D.罗素氏毒含有丝氨酸和金属蛋白酶。只有马拉巴河恙虫毒表现出凝血酶样活性，并在58秒内与纯化的纤维蛋白原诱导纤维蛋白凝块形成。尽管D. russellii毒具有促凝血活性，但不具有凝血酶样活性，可能作用于其他凝血因子。(c)2006爱思唯尔公司All rights reserved.
The action of venom proteases and their role in hemostasis has been compared in the venoms of Trimeresurus malabaricus, Daboia russellii and Naja naja from the Southern region of Western Ghats, India. These venoms exhibit varying amounts of proteolytic activity and also influence hemostasis differently. Casein hydrolyzing activity of T malabaricus venoms was 16 and 24 fold higher than those of N. naja and D. russellii venoms, respectively. With the synthetic substrate TAME, the highest activity was observed in T malabaricus venom. N. naja venom did not hydrolyze TAME even at higher concentrations. These variations in proteolytic activity also influenced the coagulation process. T malabaricus and D. russellii venoms are strongly procoagulant and reduce the re-calcification time from 148 to 14 and 12 s, respectively. Similarly, both T malabaricus and D. russellii venoms reduce the prothrombin time from 12.5 to 6.0 s. On the other hand, N. naja venom is anticoagulant and prolongs re-calcification time to 600 s and prothrombin time to 42 s. In spite of varied effects on hemostasis, all the venoms hydrolyze fibrinogen. T malabaricus venom hydrolyses both A alpha and B beta subunits. While D. russellii and N. naja venoms hydrolyse only A alpha. None of these venoms hydrolyze the gamma subunit of fibrinogen. Inhibition studies with specific protease inhibitors revealed that both N. naja and T malabaricus venoms contain only metalloproteases. D. russellii venom contained both serine and metalloproteases. Only, T malabaricus venom exhibited thrombin-like activity and induces fibrin clot formation with purified fibrinogen within 58 s. Even though D. russellii venom exhibits procoagulant activity, it did not show thrombin-like activity and may act on other coagulation factors. (c) 2006 Elsevier Inc. All rights reserved.