Substrate specificity of human matriptase-2

Biochimie

Volumn 97, Issue 1, 2014, Pages 121-127

  Wysocka, M ^a   Gruba, N ^a   Miecznikowska, A ^a   Popow Stellmaszyk, J ^a   Gutschow M ^b   Stirnberg, M ^b   Furtmann, N ^b   Bajorath, J ^b   Lesner, A ^a   Rolka, K ^a  

^a UNIVERSITY OF GDA SK   (Poland)

^b UNIVERSITY OF BONN   (Germany)

Author keywords

Combinatorial chemistry; Fluorogenic substrates; Internally quenched substrates; Matriptase 2

Indexed keywords

AMINO ACID; HEMOJUVELIN; IRON; MATRIPTASE; TETRAPEPTIDE;

ARTICLE; COMBINATORIAL CHEMISTRY; CONTROLLED STUDY; EMBRYO; ENZYME ANALYSIS; ENZYME SPECIFICITY; EVALUATION STUDY; HOMEOSTASIS; HUMAN; HUMAN CELL; PEPTIDE LIBRARY; PEPTIDE SYNTHESIS;

COMBINATORIAL CHEMISTRY; FLUOROGENIC SUBSTRATES; INTERNALLY QUENCHED SUBSTRATES; MATRIPTASE-2;

AMINO ACID SEQUENCE; CATALYTIC DOMAIN; HEK293 CELLS; HUMANS; HYDROLYSIS; KINETICS; MEMBRANE PROTEINS; MOLECULAR DOCKING SIMULATION; MOLECULAR SEQUENCE DATA; OLIGOPEPTIDES; PEPTIDE LIBRARY; RECOMBINANT PROTEINS; SERINE ENDOPEPTIDASES; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EID: 84891882902     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2013.10.001     Document Type: Article

References (33)

1. R. Szabo, and T.H. Bugge Type II transmembrane serine proteases in development and disease Int. J. Biochem. Cell. Biol. 40 2008 1297 1316
2. G. Velasco, S. Cal, V. Quesada, L.M. Sánchez, and C. López-Otín Matriptase-2, a membrane bound mosaic serine proteinase predominantly expressed in human liver and showing degrading activity against extracellular matrix proteins J. Biol. Chem. 277 2002 37637 37646
3. K.E. Finberg, M.M. Heeney, D.R. Campagna, Y. Aydinok, H.A. Pearson, K.R. Hartman, M.M. Mayo, S.M. Samuel, J.J. Strouse, K. Markianos, N.C. Andrews, and M.D. Fleming Mutations in TMPRSS6 cause iron-refractory iron deficiency anemia (IRIDA) Nat. Genet. 40 2008 569 571
4. X. Du, E. She, T. Gelbart, J. Truksa, P. Lee, Y. Xia, K. Khovananth, S. Mudd, N. Mann, E.M. Moresco, E. Beutler, and B. Beutler The serine protease TMPRSS6 is required to sense iron deficiency Science 320 2008 1088 1092
5. L. Silvestri, A. Pagani, A. Nai, I. De Domenico, J. Kaplan, and C. Camaschella The serine protease matriptase-2 (TMPRSS6) inhibits hepcidin activation by cleaving membrane hemojuvelin Cell Metab. 8 2008 502 511
6. J.E. Maxson, J. Chen, C.A. Enns, and A.S. Zhang Matriptase-2- and proprotein convertase-cleaved forms of hemojuvelin have different roles in the down-regulation of hepcidin expression J. Biol. Chem. 285 2010 39021 39028
7. M. Stirnberg, E. Maurer, A. Horstmeyer, S. Kolp, S. Frank, T. Bald, K. Arenz, A. Janzer, K. Prager, P. Wunderlich, J. Walter, and M. Gütschow Proteolytic processing of the serine protease matriptase-2: identification of the cleavage sites required for its autocatalytic release from the cell surface Biochem. J. 430 2010 87 95
8. M. Stirnberg, and M. Gütschow Matriptase-2, a regulatory protease of iron homeostasis: possible substrates, cleavage sites and inhibitors Curr. Pharm. Des. 19 2013 1052 1061
9. E. Maurer, M. Gütschow, and M. Stirnberg Hepatocyte growth factor activator inhibitor type 2 (HAI-2) modulates hepcidin expression by inhibiting the cell surface protease matriptase-2 Biochem. J. 450 2013 583 593
10. C.J. Farady, and C.S. Craik Mechanisms of macromolecular protease inhibitors ChemBioChem 11 2010 2341 2346
11. M.T. Sisay, T. Steinmetzer, M. Stirnberg, E. Maurer, M. Hammami, J. Bajorath, and M. Gütschow Identification of the first low-molecular-weight inhibitors of matriptase-2 J. Med. Chem. 53 2010 5523 5535
12. F. Béliveau, A. Désilets, and R. Leduc Probing the substrate specificities of matriptase, matriptase-2, hepsin and DESC1 with internally quenched fluorescent peptides FEBS J. 276 2009 2213 2226
13. K.E. Finberg Striking the target in iron overload disorders J. Clin. Invest. 123 2013 1424 1427
14. L. De Falco, M. Sanchez, L. Silvestri, C. Kannengiesser, M.U. Muckenthaler, A. Iolascon, L. Gouya, C. Camaschella, and C. Beaumont Iron refractory iron deficiency anemia Haematologica 98 2013 845 853
15. M. Wysocka, B. Spichalska, A. Lesner, M. Jaros, K. Brzozowski, A. Łegowska, and K. Rolka Substrate specificity and inhibitory study of human airway trypsin-like protease Bioorg. Med. Chem. 18 2010 5504 5509
16. N.A. Sole, and G. Barany Optimization of solid-phase synthesis of [Ala8]-dynorphin A J. Org. Chem. 57 1992 5399 5403
17. J.L. Harris, B.J. Backes, F. Leonetti, S. Mahrus, J.A. Ellman, and C.S. Craik Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries Proc. Natl. Acad. Sci. U. S. A. 97 2000 7754 7759
18. A. Furka, F. Sebestyn, M. Asgedom, and G. Dibó General method for rapid synthesis of multicomponent peptide mixtures Int. J. Pept. Protein Res. 37 1991 487 493
19. R.A. Houghten, C. Pinilla, S.E. Blondelle, J.R. Appel, C.T. Dooley, and J.H. Cuervo Generation and use of synthetic peptide combinatorial libraries for basic research and drug discovery Nature 354 1991 84 86
20. S. Dosa, M. Stirnberg, V. Lülsdorff, D. Häußler, E. Maurer, and M. Gütschow Active site mapping of trypsin, thrombin and matriptase-2 by sulfamoyl benzamidines Bioorg. Med. Chem. 20 2012 6489 6505
21. T. Chase Jr., and E. Shaw p-Nitrophenyl-p'-guanidinobenzoate HCl: a new active site titrant for trypsin Biochem. Biophys. Res. Commun. 29 1967 508 514
22. M. Wysocka, A. Lesner, N. Gruba, B. Korkmaz, F. Gauthier, M. Kitamatsu, A. Łȩgowska, and K. Rolka Three wavelength substrate system of neutrophil serine proteinases Anal. Chem. 84 2012 7241 7248
23. G.M. Morris, R. Huey, W. Lindstrom, M.F. Sanner, R.K. Belew, D.S. Goodsell, and A.S. Olson AutoDock4 and AutoDockTools4: automated docking with selective receptor flexibility J. Comput. Chem. 16 2009 2785 2791
24. Molecular Operating Environment (MOE), 2012.10, Chemical Computing Group Inc., 1010 Sherbooke St. West, Suite #910, Montreal, QC, Canada H3A 2R7, 2012.
25. E. Maurer, M.T. Sisay, M. Stirnberg, T. Steinmetzer, J. Bajorath, and M. Gütschow Insights into matriptase-2 substrate binding and inhibition mechanisms by analyzing active-site-mutated variants ChemMedChem 7 2012 68 72
26. I. Schechter, and A. Berger On the size of the active site in proteases I. Papain Biochem. Biophys. Res. Commun. 27 1967 157 162
27. M. Meldal, and K. Breddam Anthranilamide and nitrotyrosine as a donor-acceptor pair in internally quenched fluorescent substrates for endopeptidases: multicolumn peptide synthesis of enzyme substrates for subtilisin Carlsberg and pepsin Anal. Biochem. 195 1991 141 147
28. R. Friedrich, P. Fuentes-Prior, E. Ong, G. Coombs, M. Hunter, R. Oehler, D. Pierson, R. Gonzalez, R. Huber, W. Bode, and E.L. Madison Catalytic domain structures of MT-SP1/matriptase, a matrix-degrading transmembrane serine proteinase J. Biol. Chem. 277 2002 2160 2168
29. C. Yuan, L. Chen, E.J. Meehan, N. Daly, D.J. Craik, M. Huang, and J.C. Ngo Structure of catalytic domain of matriptase in complex with sunflower trypsin inhibitor-1 BMC Struct. Biol. 11 2011 30 42
30. N.D. Rawlings, A.J. Barrett, and A. Bateman MEROPS: the database of proteolytic enzymes, their substrates and inhibitors Nucl. Acids Res. 40 2012 D343 D350
31. F. Guillem, S. Lawson, C. Kannengiesser, M. Westerman, C. Beaumont, and B. Grandchamp Two nonsense mutations in the TMPRSS6 gene in a patient with microcytic anemia and iron deficiency Blood 112 2008 2089 2091
32. F. Béliveau, C. Brulé, A. Désilets, B. Zimmerman, S.A. Laporte, C.L. Lavoie, and R. Leduc Essential role of endocytosis of the type II transmembrane serine protease TMPRSS6 in regulating its functionality J. Biol. Chem. 286 2011 29035 29043
33. D. Meynard, V. Vaja, C.C. Sun, E. Corradini, S. Chen, C. López-Otín, L. Grgurevic, C.C. Hong, M. Stirnberg, M. Gütschow, S. Vukicevic, J.L. Babitt, and H.Y. Lin Regulation of TMPRSS6 by BMP6 and iron in human cells and mice Blood 118 2011 747 756