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      Reteplase: Structure, Function, and Production

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          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.

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          Recombinant protein folding and misfolding in Escherichia coli.

          François Baneyx, Mirna Mujacic (2004)
          The past 20 years have seen enormous progress in the understanding of the mechanisms used by the enteric bacterium Escherichia coli to promote protein folding, support protein translocation and handle protein misfolding. Insights from these studies have been exploited to tackle the problems of inclusion body formation, proteolytic degradation and disulfide bond generation that have long impeded the production of complex heterologous proteins in a properly folded and biologically active form. The application of this information to industrial processes, together with emerging strategies for creating designer folding modulators and performing glycosylation all but guarantee that E. coli will remain an important host for the production of both commodity and high value added proteins.
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            Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase.

            KunLiang Guan, Jack Dixon (1991)
            Several systems have been developed to allow for rapid and efficient purification of recombinant proteins expressed in bacteria. The expression of polypeptides in frame with glutathione S-transferase (GST) allows for purification of the fusion proteins from crude bacterial extracts under nondenaturing conditions by affinity chromatography on glutathione agarose (D. B. Smith and K. S. Johnson, 1988, Gene 67, 31-40). This vector expression system has also incorporated specific protease cleavage sites to facilitate proteolysis of the bacterial fusion proteins. In our hands, the cleavage of these fusion proteins at a thrombin cleavage site proceeded slowly. To facilitate the cleavage of fusion proteins, we have introduced a glycine-rich linker (glycine kinker) containing the sequence P.G.I.S.G.G.G.G.G located immediately following the thrombin cleavage site. This glycine kinker greatly increases the thrombin cleavage efficiency of several fusion proteins. The introduction of the glycine kinker into fusion proteins allows for the cleavage of the fusion proteins while they are attached to the affinity resin resulting in a single step purification of the recombinant protein. More than 2 mg of the highly purified protein was obtained from the equivalent of 100 ml of bacterial culture within a few hours when a protein tyrosine phosphatase was employed as a test protein. The vector, pGEX-KG, has also been modified to facilitate cloning of a variety of cDNAs in all reading frames and has been successfully used to express several eukaryotic proteins.
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              Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase.

              Zariel I. Johnson, Jeffrey Smith (1988)
              Plasmid expression vectors have been constructed that direct the synthesis of foreign polypeptides in Escherichia coli as fusions with the C terminus of Sj26, a 26-kDa glutathione S-transferase (GST; EC 2.5.1.18) encoded by the parasitic helminth Schistosoma japonicum. In the majority of cases, fusion proteins are soluble in aqueous solutions and can be purified from crude bacterial lysates under non-denaturing conditions by affinity chromatography on immobilised glutathione. Using batch wash procedures several fusion proteins can be purified in parallel in under 2 h with yields of up to 15 micrograms protein/ml of culture. The vectors have been engineered so that the GST carrier can be cleaved from fusion proteins by digestion with site-specific proteases such as thrombin or blood coagulation factor Xa, following which, the carrier and any uncleaved fusion protein can be removed by absorption on glutathione-agarose. This system has been used successfully for the expression and purification of more than 30 different eukaryotic polypeptides.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Adv Biomed Res
                Journal ID (iso-abbrev): Adv Biomed Res
                Journal ID (publisher-id): ABR
                Title: Advanced Biomedical Research
                Publisher: Wolters Kluwer - Medknow (India )
                ISSN (Electronic): 2277-9175
                Publication date Collection: 2019
                Publication date (Electronic): 20 March 2019
                Volume: 8
                Electronic Location Identifier: 19
                Affiliations
                [1] From the Department of Pharmaceutical Biotechnology, School of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences, Isfahan, Iran
                [1 ] Young Researchers and Elites Club, Science and Research Branch, Islamic Azad University, Tehran, Iran
                [2 ] Department of Biology, Faculty of Science, Shahrekord University, Shahr-e Kord, Iran
                Author notes
                Address for correspondence: Dr. Hamid Mir Mohammad Sadeghi, Department of Pharmaceutical Biotechnology, School of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences, Isfahan, Iran. E-mail: h_sadeghi@ 123456pharm.mui.ac.ir
                Article
                Publisher ID: ABR-8-19
                DOI: 10.4103/abr.abr_169_18
                PMC ID: 6446582
                PubMed ID: 31016177
                SO-VID: 2ca22959-79bb-4a38-9bf2-06b3539f6689
                Copyright © Copyright: © 2019 Advanced Biomedical Research
                License:

                This is an open access journal, and articles are distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike 4.0 License, which allows others to remix, tweak, and build upon the work non-commercially, as long as appropriate credit is given and the new creations are licensed under the identical terms.

                History
                Date received : August 2018
                Date accepted : February 2019
                Categories
                Subject: Review Article

                ScienceOpen disciplines: Molecular medicine
                Keywords: bacterial expression,fibrin specificity,reteplase,thrombolytic drug
                Data availability:
                ScienceOpen disciplines: Molecular medicine
                Keywords: bacterial expression, fibrin specificity, reteplase, thrombolytic drug

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