Identification of prolyl oligopeptidase as a cyclosporine-sensitive protease by screening of mouse liver extracts

References

Aumüller, T., Jahreis, G., Fischer, G., and Schiene-Fischer, C. (2010). Role of prolyl cis/trans isomers in cyclophilin-assisted Pseudomonas syringae AvrRpt2 protease activation. Biochemistry 49, 1042–1052.10.1021/bi901813eSearch in Google Scholar

Brandt, I., Scharpé, S., and Lambeir, A.M. (2007). Suggested functions for prolyl oligopeptidase: a puzzling paradox. Clin. Chim. Acta 377, 50–61.10.1016/j.cca.2006.09.001Search in Google Scholar

Cheng, Y. and Prusoff, W.H. (1973). Relationship between the inhibition constant (K_I) and the concentration of inhibitor which causes 50 per cent inhibition (IC₅₀) of an enzymatic reaction. Biochem. Pharmacol. 22, 3099–3108.10.1016/0006-2952(73)90196-2Search in Google Scholar

Ciesek, S., Steinmann, E., Wedemeyer, H., Manns, M.P., Neyts, J., Tautz, N., Madan, V., Bartenschlager, R., von Hahn, T., and Pietschmann, T. (2009). Cyclosporine A inhibits hepatitis C virus nonstructural protein 2 trough cyclophilin A. Hepatology 50, 1638–1645.10.1002/hep.23281Search in Google Scholar

Coaker, G., Falick, A., and Staskawicz, B. (2005). Activation of a phytopathogenic bacterial effector protein by a eukaryotic cyclophilin. Science 308, 548–550.10.1126/science.1108633Search in Google Scholar

Fischer, G., Gallay, P., and Hopkins, S. (2010) Cyclophilin inhibitors for the treatment of HCV infections. Curr. Opin. Investig. Drugs 11, 911–918.Search in Google Scholar

García-Horsman, J.A., Männistö, P.T., and Venäläinen, J.I. (2007). On the role of prolyl oligopeptidase in health and disease. Neuropeptides 41, 1–24.10.1016/j.npep.2006.10.004Search in Google Scholar

Gorrao, S.S., Hemerly, J.P., Lima, A.R., Melo, R.L., Szeltner, Z., Polgar, L., Juliano, M.A., and Juliano, L. (2007). Fluorescence resonance energy transfer (FRET) peptides and cycloretro-inverso peptides derived from bradykinin as substrates and inhibitors of prolyl oligopeptidase. Peptides 28, 2146–2154.10.1016/j.peptides.2007.08.018Search in Google Scholar

Kahyaoglu, A., Haghjoo, K., Kraicsovits, F., Jordan, F., and Polgár, L. (1997). Benzyloxycarbonylprolylprolinal, a transition-state analogue for prolyl oligopeptidase, forms a tetrahedral adduct with catalytic serine, not a reactive cysteine. Biochem. J. 322, 839–843.10.1042/bj3220839Search in Google Scholar

Kataoka, M., Shimizu, Y., Kunikiyo, K., Asahara, Y., Yamashita, K., Ninomiya, M., Morisaki, I., Ohsaki, Y., Kido, J.-I., and Nagata, T. (2000). Cyclosporine A decreases the degradation of type I collagen in rat gingival overgrowth. J. Cell. Physiol. 182, 351–358.10.1002/(SICI)1097-4652(200003)182:3<351::AID-JCP5>3.0.CO;2-USearch in Google Scholar

Kaul, A., Stauffer, S., Berger, C., Pertel, T., Schmitt, J., Kallis, S., Zayas, M., Lohmann, V., Luban, J., and Bartenschlager, R. (2009). Essential role of cyclophilin A for hepatitis C virus replication and virus production and possible link to polyprotein cleavage kinetics. PLoS Pathog 5: e1000546.Search in Google Scholar

Klappa, P., Dierks, T., and Zimmermann, R. (1996). Cyclosporine A inhibits the degradation of signal sequences after processing of presecretory proteins by signal peptidase. Eur. J. Biochem. 239, 509–518.10.1111/j.1432-1033.1996.0509u.xSearch in Google Scholar

Lawandi, J., Gerber-Lemaire, S., Juillerat-Jeanneret, L., and Moitessier, N. (2009). Inhibitors of prolyl oligopeptidases for the therapy of human diseases: defining diseases and inhibitors. J. Med. Chem. 53, 3423–3438.10.1021/jm901104gSearch in Google Scholar

Liu, J., Farmer, J.D. Jr., Lane, W.S., Friedman, J., Weissman, I., and Schreiber, S.L. (1991). Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes. Cell 66, 807–815.10.1016/0092-8674(91)90124-HSearch in Google Scholar

López, A., Tarragó, T., and Giralt, E. (2011). Low molecular weight inhibitors of prolyl oligopeptidase: a review of compounds patented from 2003 to 2010. Expert Opin. Ther. Pat. 21, 1023–1044.10.1517/13543776.2011.577416Search in Google Scholar PubMed

Malešević, M., Kühling, J., Erdmann, F., Balsley, M.A., Bukrinsky, M.I., Constant, S.L. and Fischer, G. (2010). A cyclosporine derivative discriminates between extracellular and intracellular cyclophilins. Angew. Chem. Int. Ed. 49, 213–215.10.1002/anie.200904529Search in Google Scholar PubMed PubMed Central

Olivo, R.A., Nascimento, N.G., Teixeira, C.F., and Silveira, P.F. (2008). Methotrexate and cyclosporine treatments modify the activities of dipeptidyl peptidase IV and prolyl oligopeptidase in murine macrophages. Clin. Dev. Immunol. 2008, 794050.10.1155/2008/794050Search in Google Scholar PubMed PubMed Central

O’Reilly, P.J., Hardison, M.T., Jackson, P.L., Xu, X., Snelgrove, R.J., Gaggar, A., Galin, F.S., and Blalock, J.E. (2009). Neutrophils contain prolyl endopeptidase and generate the chemotactic peptide, PGP, from collagen. J. Neuroimmunol. 217, 51–54.10.1016/j.jneuroim.2009.09.020Search in Google Scholar PubMed PubMed Central

Pallet, N., Rabant, M., Xu-Dubois, Y.C., Lecorre, D., Mucchielli, M.H., Imbeaud, S., Agier, N., Hertig, A., Thervet, E., Legendre, C., et al. (2008). Response of human renal tubular cells to cyclosporine and sirolimus: a toxicogenomic study. Toxicol. Appl. Pharmacol. 229, 184–96.10.1016/j.taap.2008.01.019Search in Google Scholar PubMed

Polgár, L. (1991). pH-dependent mechanism in the catalysis of prolyl endopeptidase from pig muscle. Eur. J. Biochem. 197, 441–447.10.1111/j.1432-1033.1991.tb15930.xSearch in Google Scholar PubMed

Polgár, L. (1992). Unusual secondary specificity of prolyl oligopeptidase and the different reactivities of its two forms toward charged substrates. Biochemistry 31, 7729–773510.1021/bi00148a038Search in Google Scholar PubMed

Prell, E., Kahlert, V., Rücknagel, K.P., Malešević, M., and Fischer, G. (2013). Fine tuning the inhibition profile of cyclosporine A by derivatization of the MeBmt residue. ChemBioChem 14, 63–65.10.1002/cbic.201200621Search in Google Scholar PubMed

Schumann, M., Jahreis, G., Kahlert, V., Lücke, C., and Fischer, G. (2011). Oligopeptide cyclophilin inhibitors: a reassessment. Eur. J. Med. Chem. 46, 5556–5561.10.1016/j.ejmech.2011.09.019Search in Google Scholar

Shevchenko, A., Wilm, M., Vorm, O., and Mann, M. (1996). Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68, 850–858.10.1021/ac950914hSearch in Google Scholar

Szeltner, Z., Renner, V., and Polgár, L. (2000). Substrate- and pH-dependent contribution of oxyanion binding site to the catalysis of prolyl oligopeptidase, a paradigm of the serine oligopeptidase familiy. Protein Sci. 9, 353–360.10.1110/ps.9.2.353Search in Google Scholar

Travis, J. and Pannell, R. (1973). Selective removal of albumin from plasma by affinity chromatography. Clin. Chim. Acta 49, 49–52.10.1016/0009-8981(73)90341-0Search in Google Scholar

Twentyman, P.R., Wright, K.A., and Wallace, H.M. (1992). Effects of cyclosporin-A and a non-immunosuppressive analogue, O-acetyl cyclosporin A, upon the growth of parent and multidrug resistant human lung cancer cells in vitro. Br. J. Cancer 65, 335–340.10.1038/bjc.1992.68Search in Google Scholar

von Ruecker, A.A., Rao, G., and Bidlingmaier, F. (1988). Cyclosporine A inhibits proteolytic cleavage and degradation of membrane-bound protein kinase C in hepatocytes after stimulation by phorbol ester. Biochem. Biophys. Res. Commun. 151, 997–1003.10.1016/S0006-291X(88)80464-9Search in Google Scholar

Wenger, R.M. (1985). Synthesis of cyclosporine and analogues: structural requirements for immunosuppressive activity. Angew. Chem. Int. Ed. 24, 77–85.10.1002/anie.198500773Search in Google Scholar

West, G.M., Tucker, C.L., Xu, T., Park, S.K., Han, X., Yates, J.R., and Fitzgerald, M.C. (2010). Quantitative proteomics approach for identifying protein-drug interactions in complex mixtures using protein stability measurements. Proc. Natl. Acad. Sci. USA 107, 9078–9082.10.1073/pnas.1000148107Search in Google Scholar

Wilmes, A., Limonciel, A., Aschauer, L., Moenks, K., Bielow, C., Leonard, M.O., Hamon, J., Carpi, D., Ruzek, S., Handler, A., et al. (2013). Application of integrated transcriptomic, proteomic and metabolomic profiling for the delineation of mechanisms of drug induced cell stress. J. Proteomics, 79, 180–194.10.1016/j.jprot.2012.11.022Search in Google Scholar

Yonetani, T. and Theorell, H. (1964). Studies on liver alcohol dehydrogenase complexes III. Multiple inhibition kinetics in the presence of two competitive inhibitors. Arch. Biochem. Biophys. 106, 243–251.10.1016/0003-9861(64)90184-5Search in Google Scholar

Yoshimoto, T., Simmons, W.H., Kita, T., and Tsuru, D. (1981). Post-proline cleaving enzyme from lamb brain. J. Biochem. 90, 325–334.10.1093/oxfordjournals.jbchem.a133477Search in Google Scholar PubMed