Stable expression and purification of a secreted human recombinant prethrombin-2 and its activation to thrombin

Protein Expression and Purification

Volumn 10, Issue 2, 1997, Pages 214-225

  Russo, Giulia ^a   Gast, Alain ^b   Schlaeger, Ernst Jürgen ^b   Angiolillo, Antonietta ^a   Pietropaolo, Concetta ^a  

^a UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^b Preclinical Research   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; CRICETINAE; MAMMALIA;

EID: 0031193598     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1997.0733     Document Type: Article

References (40)

1. Stubbs M. T., Bode W. A player of many parts: The spotlight falls on thrombin structure. Thromb. Res. 69:1993;1-58.
2. Vu T-K. H., Hung D. T., Wheaton V. I., Coughlin S. R. Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation. Cell. 64:1991;1057-1068.
3. Vu T-K. H., Wheaton V. I., Hung D. T., Charo I., Coughlin S. R. Domains specifying thrombin-receptor interaction. Nature. 353:1991;674-677.
4. 2+. FEBS Lett. 288:1991;123-128.
5. Zhong C., Hayzer D. J., Corson M. A., Runge M. S. Molecular cloning of the rat vascular smooth muscle thrombin receptor: Evidence forin vivo. J. Biol. Chem. 267:1992;16975-16979.
6. Tsiang M., Jain A. K., Dunn K. E., Rojas M. E., Leung L. L. K., Gibbs C. S. Functional mapping of the surface residues of human thrombin. J. Biol. Chem. 270:1995;16854-16863.
7. Gibbs C. S., Coutré S. E., Tsiang M., Li W-X., Jain A. K., Dunn K. E., Law V. S., Mao C. T., Matsumur S. J., Mejza S. J., Paborsky S. L., Leung L. L. K. Conversion of thrombin into an anticoagulant by protein engineering. Nature. 378:1995;413-416.
8. So I. S., Lee S., Kim S. W., Hahm K., Kim J. Purification and activation of recombinant human prethrombin 2 produced inE coli. Korean Biochem. J. 25:1992;60-65.
9. Fenton J. W. II, Fasco M. J., Stackrow A. B., Aronson D. L., Young A. M., Finlayson J. S. Human thrombins. Production, evaluation, and properties of α-thrombin. J. Biol. Chem. 252:1977;3587-3598.
10. Chase T., Shaw E. pp. Biochem. Biophys. Res. Commun. 29:1967;508-514.
11. Fasco M. J., Fenton J. W. II. Specificity of thrombin. I. Esterolytic properties of thrombin, plasmin, trypsin and chymotrypsin with substituted guanidino derivatives ofpp. Arch. Biochem. Biophys. 152:1973;802-812.
12. Carter P., Bedouelle H., Winter G. Improved oligonucleotide site-directed mutagenesis using M13 vectors. Nucleic Acids Res. 13:1985;4431-4443.
13. Costanzo F., Castagnoli L., Dente L., Arcari P., Smith M., Costanzo P., Raugei G., Izzo P., Pietropaolo T. C., Bougueleret L., Cimino F., Salvatore F., Cortese R. Cloning of several cDNA segments coding for human liver proteins. EMBO J. 2:1983;57-61.
14. +In vitro. DNA. 7:1988;651-661.
15. Deen K. C., McDougal J. S., Inacker R., Folena-Wasserman G., Arthos J., Rosenberg J., Maddon P. J., Axel R., Sweet R. W. A soluble form of CD4 (T4) protein inhibits AIDS virus infection. Nature. 331:1988;82-84.
16. Knowles B. B., Howe C. C., Aden D. P. Human hepatocellular carcinoma cell lines secrete the major plasma proteins and hepatitis B surface antigen. Science. 209:1980;497-499.
17. Wigler M., Silverstein S., Lee L., Pellicer A., Cheng T., Axel R. Transfer of purified herpes virus thymidine kinase gene to cultured mouse cells. Cell. 11:1977;223-232.
18. Urlaub G., Kas E., Carothers A. M., Chasin L. Deletion of the diploid dihydrofolate reductase locus from cultured mammalian cells. Cell. 33:1983;405-412.
19. Russo G., Mertens K., De Magistris L., Lange H., Cortese R., Pietropaolo C. Biologically active recombinant prothrombin and antithrombin III expressed in a human hepatoma/vaccinia system. Biotech. Appl. Biochem. 14:1991;222-233.
20. Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:1987;156-159.
21. Sambrook J., Fritsch E. F., Maniatis T. Molecular Cloning: A Laboratory Manual. 1989;Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
22. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;2922-2928.
23. Schlaeger E-J., Schumpp B. Propagation of mouse myeloma cell line J558L producing human CD4 immunoglobulin G1. J. Immunol. Methods. 146:1992;111-120.
24. Schlaeger E-J., Foggetta M., Vonach J. M., Christensen K. SF-1, a low cost culture medium for the production of recombinant proteins in baculovirus infected insect cells. Biotechnol. Tech. 7:1993;183-188.
25. Wilm M., Mann M. Analytical properties of the nanoelectrospray ion source. Anal. Chem. 68:1996;1-8.
26. Degryse E. Determination of the specific activity of recombinant hirudin. Thromb. Res. 60:1990;433-443.
27. Lottenberg R., Jackson C. M. Solution composition dependent variation in extinction coefficients forp. Biochim. Biophys. Acta. 742:1983;558-564.
28. min enzyme reactions. Science. 116:1952;329-331.
29. Hilpert K., Ackermann J., Banner D. W., Gast A., Gubernator K., Hadváry P., Labler L., Müller K., Schmid G., Tschopp T. B., van de Waterbeemd H. Design and synthesis of potent and highly selective thrombin inhibitors. J. Med. Chem. 37:1994;3889-3901.
30. Plow E. F., Marguerie G. Inhibition of fibrinogen binding to human platelets by the tetrapeptide glycyl-LLL. Proc. Natl. Acad. Sci. USA. 79:1982;3711-3715.
31. Kaczmarek E., Kaminski M., McDonagh J. Fibrinogen-Sepharose interaction with prothrombin, prethrombin 1, prethrombin 2 and thrombin. Biochim. Biophys. Acta. 914:1987;275-282.
32. Liu L-W., Ye J., Johnson A. E., Esmon C. T. Proteolytic formation of either the two prothrombin activation intermediates results in formation of a hirugen-binding site. J. Biol. Chem. 266:1991;23632-23636.
33. Vijayalakshmi J., Padmanabhan K. P., Mann K. G., Tulinski A. The isomorphous structures of prethrombin-2, hirugen-, and PPACK-thrombin: Changes accompanying activation and exosite binding to thrombin. Protein Sci. 3:1994;2254-2271.
34. DiBella E. E., Maurer M. C., Scheraga H. A. Expression and folding of recombinant bovine prethrombin-2 and its activation to thrombin. J. Biol. Chem. 270:1994;163-169.
35. Wu Q., Picard V., Aiach M., Sadler J. E. Activation-induced exposure of the thrombin anion-binding exosite. J. Biol.Chem. 269:1994;3725-3730.
36. Fischer B., Mitterer A., Dorner F., Eibl J. Comparison ofN. J. Thromb. Thrombol. 3:1996;57-62.
37. Wu Q., Sheehan J. P., Tsiang M., Lentz S. R., Birktoft J. J., Sadler J. E. Single amino acid substitutions dissociate fibrinogen-clotting and thrombomodulin-binding activities of human thrombin. Proc. Natl. Acad. Sci. USA. 88:1991;6775-6779.
38. Sheehan J. P., Sadler J. E. Molecular mapping of the heparin binding exosite of thrombin. Proc. Natl. Acad. Sci. USA. 91:1994;5518-5522.
39. Le Bonniec B. F., Guinto E. R., MacGillivray R. T. A., Stone S. R., Esmon C. T. The role of thrombin's Tyr-Pro-Pro-Trp motif in the interaction with fibrinogen, thrombomodulin, protein C, antithrombin III, and the Kunitz inhibitors. J. Biol. Chem. 268:1993;19055-19061.
40. Barbu V., Dautry F. Northern blot normalization with a 28S rRNA oligonucleotide probe. Nucleic Acids Res. 17:1989;7115.