1. Introduction and pharmacological action
Batroxobin is a protease derived from the venom of pit viper, which has the function of breaking down fibrin and promoting blood circulation and is often used in antithrombotic and thrombolytic therapy. In addition, Batroxobin has also been used to treat thrombotic diseases such as cerebral embolism and coronary heart disease and has achieved good efficacy and safety evaluation.
Batroxase is a non-toxic enzyme hemostatic agent extracted from the venom of pit viper Agkistrodon brasiliensis. It has a thrombokinase-like effect. The drug promotes platelet aggregation at the site of bleeding (the site of vascular damage) and releases a series of clotting factors, including platelet factor 3(PF3), which promotes the degradation of fibrinogen to fibrin I monomer, and then cross-linked polymerization into insoluble fibrin. Its thrombokinase-like effect is caused by the release of PF3, which is similar to the activation of thrombin by PF3 in the blood. When thrombin is activated, it can accelerate the production of thrombin, thus promoting the coagulation process in the local area of the damaged blood vessel. The drug does not promote platelet aggregation in intact blood vessels, nor does it activate the intravascular fibrin stabilization factor (factor ⅹIII). Therefore, the complex formed by the fibrin I monomer promoted by the drug is easily degraded in vivo without causing disseminated intravascular coagulation (DIC).
2. Clinical and medical applications
2.1 Antithrombotic therapy
Atroxobin can break down fibrin in blood clots and promote blood circulation, thereby preventing and treating thrombotic diseases, such as myocardial infarction, cerebral embolism, deep vein thrombosis, etc.
2.2 Thrombolytic therapy
When Batroxobin is injected into the body, it promotes the dissolution of fibrin in the clot, allowing the clot to dissolve and flow out of the body.
The mechanism of action of Batroxobin is mainly to break down fibrin in blood clots and promote blood circulation. The advantages are obvious therapeutic effect and high thrombolytic rate; Does not affect other enzymes in the fibrinolytic system. There are also some disadvantages: it may cause side effects such as bleeding and thrombocytopenia; There may be problems such as drug resistance and pain at the injection site.
Batroxobin is usually administered intravenously or subcutaneously. Specifically, it can break down fibrin in the blood and promote blood circulation, thereby preventing and treating thrombotic diseases such as myocardial infarction, cerebral embolism, deep vein thrombosis, etc. It should be noted that Batroxobin is not a thrombolytic drug, but a protease that acts as a thrombolytic and antithrombotic agent by promoting fibrinolysis. Its main mechanism of action is to cut the aggregation point of fibrin, so that fibrin plays a role in the formation, stability, and degradation of various links of the function of the dysfunction, to promote the dissolution of thrombosis. In addition, Batroxobin can also promote the generation of new blood vessels, improve microcirculation, reduce blood viscosity, etc., to achieve the treatment and prevention of thrombotic diseases. It should be noted that Batroxobin has the effect of cutting fibrin, so it is necessary to pay attention to control the dose and monitor biochemical indicators when using it to avoid serious side effects such as bleeding.
3. Research and development progress
Batroxobin is not currently approved for medical use by the FDA. At present, Batroxobin is still undergoing clinical trials and research worldwide to develop more uses and mechanisms in the medical field, and to explore the optimization of its safety and efficacy. In addition, there are also some related new antithrombotic therapy drugs in research and development, such as Coenzyme Q10, Ticagrelor, etc., they can help prevent or treat thrombotic diseases to varying degrees, but they are still in the clinical trial stage.
References
- K. Stocker, G.H. Barlow. The coagulant enzyme from Bothrops atrox venom (batroxobin), Methods in Enzymology, Academic Press, Volume 45, 1976, 214-223.
- N. Itoh, N. Tanaka, S. Mihashi, I. Yamashina. Molecular cloning and sequence analysis of cDNA for batroxobin, a thrombin-like snake venom enzyme. Journal of Biological Chemistry. Volume 262, Issue 7, 1987, 3132-3135.
- W. You, W. Choi, Y. Koh, et al. Functional characterization of recombinant batroxobin, a snake venom thrombin-like enzyme, expressed from Pichia pastoris. FEBS Letters, Volume 571, Issues 1–3,2004, 67-73.
