Purification of the proprotein convertase furin by affinity chromatography based on PC-specific inhibitors

Biological Chemistry

Volumn 392, Issue 11, 2011, Pages 973-981

  Kuester, Miriam ^a   Becker, Gero L ^b   Hardes, Kornelia ^b   Lindberg, Iris ^c   Steinmetzer, Torsten ^b   Than, Manuel E ^a  

^a FRITZ LIPMANN INSTITUTE   (Germany)

^b PHILIPPS UNIVERSITY MARBURG   (Germany)

^c UNIVERSITY OF MARYLAND SCHOOL OF MEDICINE   (United States)

Author keywords

affinity chromatography; furin; proprotein convertase; protease inhibitor; protein purification

Indexed keywords

BIOTIN; ENZYME INHIBITOR; FURIN; SEPHAROSE; STREPTAVIDIN;

AFFINITY CHROMATOGRAPHY; ANIMAL CELL; ARTICLE; CHO CELL; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME BINDING; ENZYME INHIBITION; ENZYME PURIFICATION; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FAMILY;

ANIMALS; CHO CELLS; CHROMATOGRAPHY, AFFINITY; CRICETINAE; FURIN; GENE EXPRESSION; MICE; PROTEASE INHIBITORS;

EUKARYOTA;

EID: 80053620359     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/BC.2011.100     Document Type: Article

References (35)

1. Angliker, H. (1995). Synthesis of tight binding inhibitors and their action on the proprotein-processing enzyme furin. J. Med. Chem. 38, 4014-4018.
2. Basak, A. (2005). Inhibitors of proprotein convertases. J. Mol. Med. 83, 844-855. (Pubitemid 41598685)
3. Bassi, D.E., Fu, J., Lopez de Cicco, R., and Klein-Szanto, A.J. (2005). Proprotein convertases: "master switches" in the regulation of tumor growth and progression. Mol. Carcinog. 44, 151-161. (Pubitemid 41552748)
4. Becker, G.L., Hardes, K., and Steinmetzer, T. (2011). New substrate analogue furin inhibitors derived from 4-amidinobenzylamide. Bioorg. Med. Chem. Lett. 21, 4695-4697.
5. Becker, G.L., Sielaff, F., Than, M.E., Lindberg, I., Routhier, S., Day, R., Lu, Y., Garten, W., and Steinmetzer, T. (2010). Potent inhibitors of furin and furin-like proprotein convertases containing decarboxylated P1 arginine mimetics. J. Med. Chem. 53, 1067-1075.
6. Bodvard, K., Mohlin, J., and Knecht, W. (2007). Recombinant expression, purification, and kinetic and inhibitor characterisation of human site-1-protease. Protein Expr. Purif. 51, 308-319. (Pubitemid 44830118)
7. Bontemps, Y., Scamuffa, N., Calvo, F., and Khatib, A.M. (2007). Potential opportunity in the development of new therapeutic agents based on endogenous and exogenous inhibitors of the proprotein convertases. Med. Res. Rev. 27, 631-648. (Pubitemid 47282447)
8. Cameron, A., Appel, J., Houghten, R.A., and Lindberg, I. (2000). Polyarginines are potent furin inhibitors. J. Biol. Chem. 275, 36741-36749. (Pubitemid 32002081)
9. Creemers, J.W., Siezen, R.J., Roebroek, A.J., Ayoubi, T.A., Huylebroeck, D., and Van de Ven, W.J. (1993). Modulation of furin-mediated proprotein processing activity by site-directed mutagenesis. J. Biol. Chem. 268, 21826-21834. (Pubitemid 23320684)
10. Feliciangeli, S.F., Thomas, L., Scott, G.K., Subbian, E., Hung, C.H., Molloy, S.S., Jean, F., Shinde, U., and Thomas, G. (2006). Identification of a pH sensor in the furin propeptide that regulates enzyme activation. J. Biol. Chem. 281, 16108-16116. (Pubitemid 43848506)
11. Fugere, M. and Day, R. (2005). Cutting back on pro-protein conver-tases: the latest approaches to pharmacological inhibition. Trends Pharmacol. Sci. 26, 294-301. (Pubitemid 40733522)
12. Hallenberger, S., Bosch, V., Angliker, H., Shaw, E., Klenk, H.D., and Garten, W. (1992). Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160. Nature 360, 358-361. (Pubitemid 23000676)
13. Hatsuzawa, K., Murakami, K., and Nakayama, K. (1992). Molecular and enzymatic properties of furin, a Kex2-like endoprotease involved in precursor cleavage at Arg-X-Lys/Arg-Arg sites. J. Biochem. (Tokyo) 111, 296-301.
14. Henrich, S., Cameron, A., Bourenkov, G.P., Kiefersauer, R., Huber, R., Lindberg, I., Bode, W., and Than, M.E. (2003). The crystal structure of the proprotein processing proteinase furin explains its stringent specificity. Nat. Struct. Biol. 10, 520-526. (Pubitemid 36792902)
15. Henrich, S., Lindberg, I., Bode, W., and Than, M.E. (2005). Proprotein convertase models based on the crystal structures of furin and kexin: explanation of their specificity. J. Mol. Biol. 345, 211-227. (Pubitemid 39574845)
16. Holyoak, T., Wilson, M.A., Fenn, T.D., Kettner, C.A., Petsko, G.A., Fuller, R.S., and Ringe, D. (2003). 2.4 A resolution crystal structure of the prototypical hormone-processing protease Kex2 in complex with an Ala-Lys-Arg boronic acid inhibitor. Biochemistry 42, 6709-6718. (Pubitemid 36666111)
17. Hoshino, A., Kowalska, D., Jean, F., Lazure, C., and Lindberg, I. (2011). Modulation of PC1/3 activity by self-interaction and substrate binding. Endocrinology 152, 1402-1411.
18. Jiao, G.S., Cregar, L., Wang, J., Millis, S.Z., Tang, C., O'Malley, S., Johnson, A.T., Sareth, S., Larson, J., and Thomas, G. (2006). Synthetic small molecule furin inhibitors derived from 2,5-dideoxystreptamine. Proc. Natl. Acad. Sci. USA 103, 19707-19712. (Pubitemid 46037496)
19. Kacprzak, M.M., Peinado, J.R., Than, M.E., Appel, J., Henrich, S., Lipkind, G., Houghten, R.A., Bode, W., and Lindberg, I. (2004). Inhibition of furin by polyarginine-containing peptides: nano-molar inhibition by nona-D-arginine. J. Biol. Chem. 279, 36788-36794. (Pubitemid 39129027)
20. Komiyama, T. (2005). Interaction of EGLIN C variants with the extended subsites of the precursor processing proteases. Protein Pept. Lett. 12, 415-420. (Pubitemid 40912663)
21. Komiyama, T., Coppola, J.M., Larsen, M.J., van Dort, M.E., Ross, B.D., Day, R., Rehemtulla, A., and Fuller, R.S. (2009). Inhibition of furin/proprotein convertase-catalyzed surface and intracellular processing by small molecules. J. Biol. Chem. 284, 15729-15738.
22. Nakayama, K. (1997). Furin: a mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins. Biochem. J. 327, 625-635. (Pubitemid 27487665)
23. Rockwell, N.C. and Thorner, J.W. (2004). The kindest cuts of all: crystal structures of Kex2 and furin reveal secrets of precursor processing. Trends Biochem. Sci. 29, 80-87. (Pubitemid 38186578)
24. Scamuffa, N., Calvo, F., Chretien, M., Seidah, N.G., and Khatib, A.M. (2006). Proprotein convertases: lessons from knockouts. FASEB J. 20, 1954-1963. (Pubitemid 44953895)
25. Seidah, N.G. and Chretien, M. (1997). Eukaryotic protein processing: endoproteolysis of precursor proteins. Curr. Opin. Biotech-nol. 8, 602-607. (Pubitemid 27455338)
26. Seidah, N.G. and Prat, A. (2002). Precursor convertases in the secretory pathway, cytosol and extracellular milieu. Essays Biochem. 38, 79-94. (Pubitemid 36589196)
27. Seidah, N.G. and Prat, A. (2007). The proprotein convertases are potential targets in the treatment of dyslipidemia. J. Mol. Med. 85, 685-696. (Pubitemid 47063524)
28. Seidah, N.G., Mayer, G., Zaid, A., Rousselet, E., Nassoury, N., Poirier, S., Essalmani, R., and Prat, A. (2008). The activation and physiological functions of the proprotein convertases. Int. J. Biochem. Cell Biol. 40, 1111-1125.
29. Sielaff, F., Than, M.E., Bevec, D., Lindberg, I., and Steinmetzer, T. (2011). New furin inhibitors based on weakly basic amidino-hydrazones. Bioorg. Med. Chem. Lett. 21, 836-840.
30. Steiner, D.F. (1998). The proprotein convertases. Curr. Opin. Chem. Biol. 2, 31-39. (Pubitemid 128419196)
31. 2q ions stabilizing its N-terminus and the unique S1 specificity pocket. Acta Crystallogr. D Biol. Crystallogr. 61, 505-512. (Pubitemid 44336721)
32. Thomas, G. (2002). Furin at the cutting edge: from protein traffic to embryogenesis and disease. Nat. Rev. Mol. Cell Biol. 3, 753-766.
33. Urh, M., Simpson, D., and Zhao, K. (2009). Affinity chromatog-raphy: general methods. Methods Enzymol. 463, 417-438.
34. von Eggelkraut-Gottanka, R. and Beck-Sickinger, A.G. (2004). Biosynthesis of peptide hormones derived from precursor sequences. Curr. Med. Chem. 11, 2651-2665. (Pubitemid 39255554)
35. Weber, P.C., Ohlendorf, D.H., Wendoloski, J.J., and Salemme, F.R. (1989). Structural origins of high-affinity biotin binding to strep-tavidin. Science 243, 85-88. (Pubitemid 19027930)