ABSTRACT
In recent years, recombinant human urokinase (rhPro-UK) has been widely used in the treatment of a variety of thromboembolic diseases, with significant efficacy and no obvious adverse reactions. In addition, it has a wide range of applications in many new technology fields. This article focuses on the application of rhPro-UK in the treatment of acute myocardial infarction, cerebrovascular disease, lower extremity deep vein thrombosis, arterial thrombosis and other diseases. rhPro-UK has demonstrated good thrombolytic efficacy and safety in these diseases, especially in patients with acute myocardial infarction, and adjuvant PCI therapy can significantly increase myocardial reperfusion, improve cardiac function, and do not increase the risk of bleeding. For cerebrovascular disease, rhPro-UK can significantly improve the degree of neurological deficit and has a high safety profile. In the treatment of lower extremity deep vein thrombosis, rhPro-UK has shown superior thrombolytic efficacy and safety compared with urokinase. For arterial thrombosis and biological stents, the use of rhPro-UK has also achieved some efficacy, but more research is needed to confirm its efficacy and safety. In addition, ultrasound-mediated drug-loaded thrombolysis systems also have potential applications in rhPro-UK therapy. Future research on rhPro-UK will focus more on the development of new technologies.
ABSTRACT
Objective To predict and analyze the physicochemical properties, structural characteristics, and antigenic epitopes of viral protein (VP) VP1 of Coxsackievirus A10 (CV-A10) by bioinformatics methods. Methods The physicochemical properties and structural characteristics of CV-A10 VP1 were predicted by ProtParam, SOPMA, SWISS-MODEL, PDBsum, and ProSA-web. The antigenic epitopes of CV-A10 VP1 were predicted and analyzed by DNAstar, ABCpred, Bepipred 2.0, ElliPro, DiscoTope-2.0, NetMHCpan-4.1, NetMHCIIpan-4.0, Consurf, VaxiJen v.2.0, AllerTOP v.2.0, ToxinPred2, and IEDB immunogenicity. Results Bioinformatics analysis showed that CV-A10 VP1 was a basic, unstable, and hydrophilic protein, of which the secondary structure mainly consisted of random coil. The analysis revealed that CV-A10 VP1 had multiple potential B and T cell antigenic epitopes as well as a dominant antigenic epitope based on the potential epitope. Conclusion CV-A10 VP1 has multiple potential sites that induce specific humoral and cellular immunity, providing important support for its experimental identification, molecular epidemiological studies, and vaccine development.