Activation processing of cathepsin H impairs recognition by its propeptide

Biological Chemistry

Volumn 386, Issue 9, 2005, Pages 941-947

  Horn, Martin ^a   Dolečková Marešová, Lucie ^a   Rulíšek, Lubomír ^a   Máša, Martin ^a,b   Vasiljeva, Olga ^c   Turk, Boris ^c   Gan Erdene, Tudeviin ^a,d   Baudyš, Miroslav ^a,e   Mareš, Michael ^a  

^a INSTITUTE OF ORGANIC CHEMISTRY AND BIOCHEMISTRY   (Czech Republic)

^b CHARLES UNIVERSITY   (Czech Republic)

^c JO EF STEFAN INSTITUTE   (Slovenia)

^d EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

^e UNIVERSITY OF UTAH   (United States)

Author keywords

Aminopeptidase; Cysteine peptidase; Inhibition; Maturation; Mini chain

Indexed keywords

CATHEPSIN H; PROTEINASE;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME INHIBITION; HUMAN; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; CATHEPSINS; CIRCULAR DICHROISM; CYSTEINE ENDOPEPTIDASES; ENZYME ACTIVATION; ENZYME PRECURSORS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN STRUCTURE, TERTIARY;

EID: 26844582473     PISSN: 14316730     EISSN: 14316730     Source Type: Journal    
DOI: 10.1515/BC.2005.109     Document Type: Article

References (33)

1. Baudys, M., Meloun, B., Gan-Erdene, T., Fusek, M., Mares, M., Kostka, V., Pohl, J., and Blake, C.C. (1991). S-S bridges of cathepsin B and H from bovine spleen: a basis for cathepsin B model building and possible functional implications for discrimination between exo- and endopeptidase activities among cathepsins B, H and L. Biomed. Biochim. Acta 50, 569-577.
2. Carmona, E., Dufour, E., Plouffe, C., Takebe, S., Mason, P., Mort, J.S., and Menard, R. (1996). Potency and selectivity of the cathepsin L propeptide as an inhibitor of cysteine proteases. Biochemistry 35, 8149-8157.
3. Chagas, J.R., Ferrer-Di Martino, M., Gauthier, F., and Lalmanach, G. (1996). Inhibition of cathepsin B by its propeptide: use of overlapping peptides to identify a critical segment. FEBS Lett. 392, 233-236.
4. Chen, Y., Plouffe, C., Menard, R., and Storer, A.C. (1996). Delineating functionally important regions and residues in the cathepsin B propeptide for inhibitory activity. FEBS Lett. 393, 24-26.
5. Cirman, T., Oresic, K., Droga-Mazovec, G., Turk, V., Reed, J.C., Myers, R.M., Salvesen, G.S., and Turk, B. (2004) Selective disruption of lysosomes in HeLa cells triggers apoptosis, mediated by cleavage of Bid by multiple papain-like lysosomal cathepsins. J. Biol. Chem. 279, 3578-3587.
6. Cygler, M., Sivaraman, J., Grochulski, P., Coulombe, R., Storer, A.C., and Mort, J.S. (1996). Structure of rat procathepsin B: model for inhibition of cysteine protease activity by the proregion. Structure 4, 405-416.
7. del Re, E.C., Shuja, S., Cai, J., and Murnane, M.J. (2000). Alterations in cathepsin H activity and protein patterns in human colorectal carcinomas. Br. J. Cancer 82, 1317-1326.
8. Delaria, K., Fiorentino, L., Wallace, L., Tamburini, P., Brownell, E., and Muller, D. (1994). Inhibition of cathepsin L-like cysteine proteases by cytotoxic T-lymphocyte antigen-2β. J. Biol. Chem. 269, 25172-25177.
9. Dixon, M. (1953). The determination of enzyme inhibitor constants. Biochem. J. 55, 170-171.
10. Dodt, J. and Reichwein, J. (2003). Human cathepsin H: deletion of the mini-chain switches substrate specificity from aminopeptidase to endopeptidase. Biol. Chem. 384, 1327-1332.
11. Fox, T., de Miguel, E., Mort, J.S., and Storer, A.C. (1992). Potent slow-binding inhibition of cathepsin B by its propeptide. Biochemistry 31, 12571-12576.
12. Groves, M.R., Coulombe, R., Jenkins, J., and Cygler, M. (1998). Structural basis for specificity of papain-like cysteine protease proregions toward their cognate enzymes. Proteins 32, 504-514.
13. Guay, J., Falgueyret, J.P., Ducret, A., Percival, M.D., and Mancini J.A. (2000). Potency and selectivity of inhibition of cathepsin K, L and S by their respective propeptides. Eur. J. Biochem. 267, 6311-6318.
14. Guex, N. and Peitsch, M.C. (1997). SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18, 2714-2723.
15. Guncar, G., Podobnik, M., Pungercar, J., Strukelj, B., Turk, V., and Turk, D. (1998). Crystal structure of porcine cathepsin H determined at 2.1 Å resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function. Structure 6, 51-61.
16. Jenko, S., Dolenc, I., Guncar, G., Dobersek, A, Podobnik, M., and Turk, D. (2003). Crystal structure of stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo- and exopeptidases. J. Mol. Biol. 326, 875-885.
17. Karrer, K.M., Peiffer, S.L., and DiTomas, M.E. (1993). Two distinct gene subfamilies within the family of cysteine protease genes. Proc. Natl. Acad. Sci. USA 90, 3063-3067.
18. Koga, H., Mori, N., Yamada, H., Nishimura, Y., Tokuda, K., Kato, K., and Imoto, T. (1992). Endo- and aminopeptidase activities of rat cathepsin H. Chem. Pharm. Bull. (Tokyo) 40, 965-970.
19. Kos, J., Stabuc, B., Schweiger, A., Krasovec, M., Cimerman, N., Kopitar-Jerala, N., and Vrhovec, I. (1997). Cathepsins B, H, and L and their inhibitors stefin A and cystatin C in sera of melanoma patients. Clin. Cancer Res. 3, 1815-1822.
20. Kurata, M., Yamamoto, Y., Watabe, S., Makino, Y., Ogawa, K., and Takahashi, S.Y. (2001). Bombyx cysteine proteinase inhibitor (BCPI) homologous to propeptide regions of cysteine proteinases is a strong, selective inhibitor of cathepsin L-like cysteine proteinases. J. Biochem. (Tokyo) 130, 857-863.
21. Lalmanach, G., Lecaille, F., Chagas, J.R., Authie, E., Scharfstein, J., Juliano, M.A., and Gauthier, F. (1998). Inhibition of trypanosomal cysteine proteinases by their propeptides. J. Biol. Chem. 273, 25112-25116.
22. Lazo, N.D. and Downing, D.T. (1997). Circular dichroism of model peptides emulating the amphipathic α-helical regions of intermediate filaments. Biochemistry 36, 2559-2565.
23. Mach, L., Mort, J.S., and Glossl, J. (1994). Noncovalent complexes between the lysosomal proteinase cathepsin B and its propeptide account for stable, extracellular, high molecular mass forms of the enzyme. J. Biol. Chem. 269, 13036-13040.
24. Ponder, J.W. and Case, D.A. (2003). Force fields for protein simulations. Adv. Prot. Chem. 66, 27-85.
25. Ritonja, A., Popovic, T., Kotnik, M., Machleidt, W., and Turk, V. (1988). Amino acid sequences of the human kidney cathepsins H and L. FEBS Lett. 228, 341-545.
26. Rothe, M., Zichner, A., Auerswald, E.A., and Dodt, J. (1994). Structure/function implications for the aminopeptidase specificity of aleurain. Eur. J. Biochem. 224, 559-565.
27. Takahashi, T., Dehdarani, A.H., and Tang, J. (1988). Porcine spleen cathepsin H hydrolyzes oligopeptides solely by aminopeptidase activity. J. Biol. Chem. 263, 10952-10957.
28. Tao, K., Stearns, N.A., Dong, J., Wu, Q.L., and Sahagian, G.G. (1994). The proregion of cathepsin L is required for proper folding, stability, and ER exit. Arch. Biochem. Biophys. 311, 19-27.
29. Ueno, T., Linder, S., Na, C.L., Rice, W.R., Johansson, J., and Weaver, T.E. (2004). Processing of pulmonary surfactant protein B by napsin and cathepsin H. J. Biol. Chem. 279, 16178-16184.
30. Vasiljeva, O., Dolinar, M., Turk, V., and Turk, B. (2003). Recombinant human cathepsin H lacking the mini chain is an endopeptidase. Biochemistry 42, 13522-13528.
31. Vernet, T., Berti, P.J., de Montigny, C., Musil, R., Tessier, D.C., Menard, R., Magny, M.C., Storer, A.C., and Thomas, D.Y. (1995). Processing of the papain precursor. The ionization state of a conserved amino acid motif within the Pro region participates in the regulation of intramolecular processing. J. Biol. Chem. 270, 10838-10846.
32. Waghray, A., Keppler, D., Sloane, B.F., Schuger, L., and Chen, Y.Q. (2002). Analysis of a truncated form of cathepsin H in human prostate tumor cells. J. Biol. Chem. 277, 11533-11538.
33. Wiederanders, B., Kaulmann, G., and Schilling, K. (2003). Functions of propeptide parts in cysteine proteases. Curr. Protein Pept. Sci. 4, 309-326.