Reviewers

Authors

• Elmira Mohammadi ¹
• Hooria Seyedhosseini-Ghaheh ²
• Karim Mahnam ³
• Ali Jahanian-Najafabadi ¹
• Hamid Mir Mohammad Sadeghi ¹

¹ Department of Pharmaceutical Biotechnology, School of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences, Isfahan, Iran

² Young Researchers and Elites Club, Science and Research Branch, Islamic Azad University, Tehran, Iran

³ Department of Biology, Faculty of Science, Shahrekord University, Shahr-e Kord, Iran

Abstract

Thrombolytic drugs activate plasminogen which creates a cleaved form called plasmin, a proteolytic enzyme that breaks the crosslinks between fibrin molecules. The crosslinks create blood clots, so reteplase dissolves blood clots. Tissue plasminogen activator (tPA) is a well-known thrombolytic drug and is fibrin specific. Reteplase is a modified nonglycosylated recombinant form of tPA used to dissolve intracoronary emboli, lysis of acute pulmonary emboli, and handling of myocardial infarction. This protein contains kringle-2 and serine protease domains. The lack of glycosylation means that a prokaryotic system can be used to express reteplase. Therefore, the production of reteplase is more affordable than that of tPA. Different methods have been proposed to improve the production of reteplase. This article reviews the structure and function of reteplase as well as the methods used to produce it.

Keywords

• Bacterial expression
• fibrin specificity
• reteplase
• thrombolytic drug