Biochemical properties and regulation of cathepsin K activity

Biochimie

Volumn 90, Issue 2, 2008, Pages 208-226

  Lecaille, Fabien ^a   Brömme, Dieter ^b   Lalmanach, Gilles ^a  

^a INSERM   (France)

^b UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

Cystatin; Cysteine cathepsin; Cysteine protease; Kininogen; Osteoporosis; Stefin; Substrate specificity

Indexed keywords

CATHEPSIN K; CYSTEINE PROTEINASE; ENZYME PRECURSOR; GLYCOSAMINOGLYCAN; OXIDIZING AGENT;

AMINO ACID SEQUENCE; AMYLOIDOSIS; ARTICLE; ATHEROSCLEROSIS; BONE TURNOVER; CARDIOVASCULAR DISEASE; CATALYSIS; CELL DIFFERENTIATION; CELLULAR DISTRIBUTION; CHEMICAL ANALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME SPECIFICITY; GAUCHER DISEASE; GENOMICS; HUMAN; IN SITU HYBRIDIZATION; NEOPLASM; NONHUMAN; OBESITY; OSTEOARTHRITIS; OSTEOPOROSIS; OXIDATION; PH MEASUREMENT; PNEUMONIA; RHEUMATOID ARTHRITIS; TISSUE DISTRIBUTION;

CATALYSIS; CATHEPSINS; CYSTEINE PROTEINASE INHIBITORS; HUMANS; PROTEIN FOLDING; SUBSTRATE SPECIFICITY;

EID: 38849159247     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2007.08.011     Document Type: Article

References (278)

1. Rawlings N.D., Morton F.R., and Barrett A.J. MEROPS: the peptidase database. Nucleic Acids Res. 34 (2006) D270-D272
2. Yamashita D.S., Smith W.W., Zhao B., Janson C.A., Tomaszek T.A., Bossard M.J., Levy M.A., Oh H.-J., Carr T.J., Thomson S.K., Ijames C.F., McQueney M., D'Alessio K.J., Amegadzie B.Y., Hanning C.R., Abdel-Meguid S., Desjarlais R.L., Gleason J.G., and Veber D.F. Structure and design of potent and selective cathepsin K inhibitors. J. Am. Chem. Soc. 119 (1997) 11351-11352
3. Lecaille F., Kaleta J., and Bromme D. Human and parasitic papain-like cysteine proteases: their role in physiology and pathology and recent developments in inhibitor design. Chem. Rev. 102 (2002) 4459-4488
4. Yasuda Y., Kaleta J., and Bromme D. The role of cathepsins in osteoporosis and arthritis: rationale for the design of new therapeutics. Adv. Drug Deliv. Rev. 57 (2005) 973-993
5. Leung-Toung R., Zhao Y., Li W., Tam T.F., Karimian K., and Spino M. Thiol proteases: inhibitors and potential therapeutic targets. Curr. Med. Chem. 13 (2006) 547-581
6. Turk B. Targeting proteases: successes, failures and future prospects. Nat. Rev. Drug Discov. 5 (2006) 785-799
7. Hernandez A.A., and Roush W.R. Recent advances in the synthesis, design and selection of cysteine protease inhibitors. Curr. Opin. Chem. Biol. 6 (2002) 459-465
8. Deaton D.N., and Tavares F.X. Design of cathepsin K inhibitors for osteoporosis. Curr. Top. Med. Chem. 5 (2005) 1639-1675
9. Willstaetter R., and Bamann E. Ueber die Proteasen der Magenschleimhaut, Hoppe-Seyler's Z. Physiol. Chem. 180 (1929) 127-143
10. Tezuka K., Tezuka Y., Maejima A., Sato T., Nemoto K., Kamioka H., Hakeda Y., and Kumegawa M. Molecular cloning of a possible cysteine proteinase predominantly expressed in osteoclasts. J. Biol. Chem. 269 (1994) 1106-1109
11. Shi G.P., Chapman H.A., Bhairi S.M., DeLeeuw C., Reddy V.Y., and Weiss S.J. Molecular cloning of human cathepsin O, a novel endoproteinase and homologue of rabbit OC2. FEBS Lett. 357 (1995) 129-134
12. Inaoka T., Bilbe G., Ishibashi O., Tezuka K.I., Kumegawa M., and Kokubo T. Molecular cloning of human cDNA for cathepsin K: Novel cysteine proteinase predominantly expressed in bone. Biochem. Biophys. Res. Commun. 206 (1995) 89-96
13. Drake F.H., Dodds R.A., James I.E., Connor J.R., Debouck C., Richardson S., Lee-Rykaczewski E., Coleman L., Rieman D., Barthlow R., Hastings G., Gowen M., and Cathepsin K. B. but not cathepsins L, or S, is abundantly expressed in human osteoclasts. J. Biol. Chem. 271 (1996) 12511-12516
14. Li Y.-P., Alexander M., Wucherpfennig A.L., Yelick P., Chen W., and Shashenko P. Cloning and complete coding sequence of a novel human cathepsin expressed in giant cells of osteoclastomas. J. Bone Mineral. Res. 10 (1995) 1197-1202
15. Bromme D., and Okamoto K. Human cathepsin O2, a novel cysteine protease highly expressed in osteoclastomas and ovary molecular cloning, sequencing and tissue distribution. Biol. Chem. Hoppe Seyler. 376 (1995) 379-384
16. Hadman M., Gabos L., Loo M., Sehgal A., and Bos T.J. Isolation and cloning of JTAP-1: a cathepsin like gene upregulated in response to V-jun induced cell transformation. Oncogene 12 (1996) 135-142
17. Shi G.P., Webb A.C., Foster K.E., Knoll J.H., Lemere C.A., Munger J.S., Chapman H.A., and Human cathepsin S. chromosomal localization, gene structure, and tissue distribution. J. Biol. Chem. 269 (1994) 11530-11536
18. Rood J.A., Van Horn S., Drake F.H., Gowen M., and Debouck C. Genomic organization and chromosome localization of the human cathepsin K gene (CTSK). Genomics 41 (1997) 169-176
19. Chauhan S.S., Popescu N.C., Ray D., Fleischmann R., Gottesman M.M., and Troen B.R. Cloning, genomic organization, and chromosomal localization of human cathepsin L. J. Biol. Chem. 268 (1993) 1039-1045
20. Faisst S., and Meyer S. Compilation of vertebrate-encoded transcription factors. Nucleic Acids Res. 20 (1992) 3-26
21. Gelb B.D., Shi G.-P., Heller M., Weremowicz S., Morton C., Desnick R.J., and Chapman H.A. Structure and chromosomal assignment of the human cathepsin K gene. Genomics 41 (1997) 258-262
22. Motyckova G., Weilbaecher K.N., Horstmann M., Rieman D.J., Fisher D.Z., and Fisher D.E. Linking osteopetrosis and pycnodysostosis: regulation of cathepsin K expression by the microphthalmia transcription factor family, Proc. Natl. Acad. Sci. USA 98 (2001) 5798-5803
23. Chiellini C., Costa M., Novelli S.E., Amri E.Z., Benzi L., Bertacca A., Cohen P., Del Prato S., Friedman J.M., and Maffei M. Identification of cathepsin K as a novel marker of adiposity in white adipose tissue. J. Cell Physiol 195 (2003) 309-321
24. Li Y.P., and Chen W. Characterization of mouse cathepsin K gene, the gene promoter, and the gene expression. J. Bone Miner. Res. 14 (1999) 487-499
25. Maroulakou I.G., Papas T.S., and Green J.E. Differential expression of ets-1 and ets-2 proto-oncogenes during murine embryogenesis. Oncogene 9 (1994) 1551-1565
26. Gum R., Lengyel E., Juarez J., Chen J.H., Sato H., Seiki M., and Boyd D. Stimulation of 92-kDa gelatinase B promoter activity by ras is mitogen-activated protein kinase kinase 1-independent and requires multiple transcription factor binding sites including closely spaced PEA3/ets and AP-1 sequences. J. Biol. Chem. 271 (1996) 10672-10680
27. Zhang D.E., Hetherington C.J., Chen H.M., and Tenen D.G. The macrophage transcription factor PU.1 directs tissue-specific expression of the macrophage colony-stimulating factor receptor. Mol. Cell. Biol. 14 (1994) 373-381
28. Ebisui C., Tsujinaka T., Morimoto T., Kan K., Iijima S., Yano M., Kominami E., Tanaka K., and Monden M. Interleukin-6 induces proteolysis by activating intracellular proteases (cathepsins B and L, proteasome) in C2C12 myotubes, Clin. Sci. (Lond.) 89 (1995) 431-439
29. Ling H., Vamvakas S., Busch G., Dammrich J., Schramm L., Lang F., and Heidland A. Suppressing role of transforming growth factor-beta 1 on cathepsin activity in cultured kidney tubule cells. Am. J. Physiol 269 (1995) F911-F917
30. Lugering N., Kucharzik T., Gockel H., Sorg C., Stoll R., and Domschke W. Human intestinal epithelial cells down-regulate IL-8 expression in human intestinal microvascular endothelial cells; role of transforming growth factor-beta 1 (TGF-beta1). Clin. Exp. Immunol 114 (1998) 377-384
31. Sukhova G.K., Shi G.P., Simon D.I., Chapman H.A., and Libby P. Expression of the elastolytic cathepsins S and K in human atheroma and regulation of their production in smooth muscle cells. J. Clin. Invest 102 (1998) 576-583
32. Wang Z., Zheng T., Zhu Z., Homer R.J., Riese R.J., Chapman Jr. H.A., Shapiro S.D., and Elias J.A. Interferon gamma induction of pulmonary emphysema in the adult murine lung. J. Exp. Med 192 (2000) 1587-1600
33. Zheng T., Zhu Z., Wang Z., Homer R.J., Ma B., Riese Jr. R.J., Chapman Jr. H.A., Shapiro S.D., and Elias J.A. Inducible targeting of IL-13 to the adult lung causes matrix metalloproteinase- and cathepsin-dependent emphysema. J. Clin. Invest 106 (2000) 1081-1093
34. van den Brule S., Misson P., Buhling F., Lison D., and Huaux F. Overexpression of cathepsin K during silica-induced lung fibrosis and control by TGF-beta. Respir Res. 6 (2005) 84
35. Kamolmatyakul S., Chen W., Yang S., Abe Y., Moroi R., Ashique A.M., and Li Y.P. IL-1alpha stimulates cathepsin K expression in osteoclasts via the tyrosine kinase-NF-kappaB pathway. J. Dent. Res. 83 (2004) 791-796
36. Fujisaki K., Tanabe N., Suzuki N., Kawato T., Takeichi O., Tsuzukibashi O., Makimura M., Ito K., and Maeno M. Receptor activator of NF-kappaB ligand induces the expression of carbonic anhydrase II, cathepsin K, and matrix metalloproteinase-9 in osteoclast precursor RAW264.7 cells. Life Sci. 80 (2007) 1311-1318
37. Corisdeo S., Gyda M., Zaidi M., Moonga B.S., and Troen B.R. New insights into the regulation of cathepsin K gene expression by osteoprotegerin ligand. Biochem. Biophys. Res. Commun 285 (2001) 335-339
38. Hou W.-S., Li W., Keyszer G., Weber E., Levy R., Klein M.J., Gravallese E.M., Goldring S.R., and Bromme D. Comparison of cathepsins K and S expression within the rheumatoid and osteoarthritic synovium. Arthritis Rheum 46 (2002) 663-674
39. Mandelin J., Hukkanen M., Li T.F., Korhonen M., Liljestrom M., Sillat T., Hanemaaijer R., Salo J., Santavirta S., and Konttinen Y.T. Human osteoblasts produce cathepsin K. Bone 38 (2006) 769-777
40. Bossard M.J., Tomaszek T.T., Thompson S.K., Amegadzies B.Y., Hannings C.R., Jones C., Kurdyla J.T., McNulty D.E., Drake F.H., Gowen M., and Levy M.A. Proteolytic activity of human osteoclast cathepsin K. Expression, purification, activation, and substrate identification. J. Biol. Chem. 271 (1996) 12517-12524
41. Brömme D., Okamoto K., Wang B.B., and Biroc S. Human cathepsin O2, a matrix protein-degrading cysteine protease expressed in osteoclasts. Functional expression of human cathepsin O2 in Spodoptera frugiperda and characterization of the enzyme. J. Biol. Chem. 271 (1996) 2126-2132
42. Bromme D., Nallaseth F.S., and Turk B. Production and activation of recombinant papain-like cysteine proteases. Methods 32 (2004) 199-206
43. Turk B., Turk V., and Turk D. Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors. Biol. Chem. Hoppe-Seyler 378 (1997) 141-150
44. McGrath M.E. The lysosomal cysteine proteases. Annu. Rev. Biophys. Biomol. Struct 28 (1999) 181-204
45. Wex T., Levy B., Wex H., and Bromme D. Human cathepsins F and W: A new subgroup of cathepsins. Biochem. Biophys. Res. Commun 259 (1999) 401-407
46. McGrath M.E., Klaus J.L., Barnes M.G., and Bromme D. Crystal structure of human cathepsin K complexed with a potent inhibitor. Nat. Struct. Biol. 4 (1997) 105-109
47. Brömme D., Rinne R., and Kirschke H. Tight-binding inhibition of cathepsin S by cystatins. Biomed. Biochim. Acta 50 (1991) 631-635
48. Lecaille F., Choe Y., Brandt W., Li Z., Craik C.S., and Bromme D. Selective inhibition of the collagenolytic activity of human cathepsin K by altering its S2 subsite specificity. Biochemistry 41 (2002) 8447-8454
49. Storer A.C., and Menard R. In: Barrett A.J. (Ed). Methods in Enzymology vol. 244 (1994), Academic Press, San Diego 486-500
50. Menard R., and Storer A.C. Oxyanion hole interactions in serine and cysteine proteases. Biol. Chem. Hoppe Seyler 373 (1992) 393-400
51. Otto H.H., and Schirmeister T. Cysteine proteases and their inhibitors. Chem. Rev. 97 (1997) 133-171
52. Schechter I., and Berger A. On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun 27 (1967) 157-162
53. Turk B., Turk D., and Turk V. Lysosomal cysteine proteases: more than scavengers. Biochim. Biophys. Acta 1477 (2000) 98-111
54. Alves M.F., Puzer L., Cotrin S.S., Juliano M.A., Juliano L., Bromme D., and Carmona A.K. S3 to S3′ subsite specificity of recombinant human cathepsin K and development of selective internally quenched fluorescent substrates. Biochem. J. 373 (2003) 981-986
55. Choe Y., Leonetti F., Greenbaum D.C., Lecaille F., Bogyo M., Bromme D., Ellman J.A., and Craik C.S. Substrate profiling of cysteine proteases using a combinatorial peptide library identifies functionally unique specificities. J. Biol. Chem. 281 (2006) 12824-12832
56. Nagler D.K., and Menard R. Family C1 cysteine proteases: biological diversity or redundancy?. Biol. Chem. 384 (2003) 837-843
57. Lecaille F., Chowdhury S., Purisima E., Bromme D., and Lalmanach G. The S2 subsites of cathepsins K and L and their contribution to collagen degradation. Protein Sci. 16 (2007) 662-670
58. Lecaille F., Weidauer E., Juliano M.A., Bromme D., and Lalmanach G. Probing cathepsin K activity with a selective substrate spanning its active site. Biochem. J. 375 (2003) 307-312
59. Jaffer F.A., Kim D.E., Quinti L., Tung C.H., Aikawa E., Pande A.N., Kohler R.H., Shi G.P., Libby P., and Weissleder R. Optical visualization of cathepsin K activity in atherosclerosis with a novel, protease-activatable fluorescence sensor. Circulation 115 (2007) 2292-2298
60. Aibe K., Yazawa H., Abe K., Teramura K., Kumegawa M., Kawashima H., and Honda K. Substrate specificity of recombinant osteoclast-specific cathepsin K from rabbits. Biol. Pharm. Bull. 19 (1996) 1026-1031
61. Xia L., Kilb J., Wex H., Lipyansky A., Breuil V., Stein L., Palmer J.T., Dempster D.W., and Brömme D. Localization of rat cathepsin K in osteoclasts and resorption pits: Inhibition of bone resorption cathepsin K-activity by peptidyl vinyl sulfones. Biol. Chem. 380 (1999) 679-687
62. Rieman D.J., McClung H.A., Dodds R.A., Hwang S.M., Holmes M.W., James I.E., Drake F.H., and Gowen M. Biosynthesis and processing of cathepsin K in cultured human osteoclasts. Bone 28 (2001) 282-289
63. Kasper D., Dittmer F., von Figura K., and Pohlmann R. Neither type of mannose 6-phosphate receptor is sufficient for targeting of lysosomal enzymes along intracellular routes. J. Cell Biol. 134 (1996) 615-623
64. Dittmer F., Ulbrich E.J., Hafner A., Schmahl W., Meister T., Pohlmann R., and von Figura K. Alternative mechanisms for trafficking of lysosomal enzymes in mannose 6-phosphate receptor-deficient mice are cell type-specific. J. Cell Sci. 112 (1999) 1591-1597
65. Linke M., Herzog V., and Brix K. Trafficking of lysosomal cathepsin B-green fluorescent protein to the surface of thyroid epithelial cells involves the endosomal/lysosomal compartment. J. Cell Sci. 115 (2002) 4877-4889
66. Nishimura Y., Kawabata T., and Kato K. Identification of latent procathepsins B and L in microsomal lumen: characterization of enzymatic activation and proteolytic processing in vitro. Arch. Biochem. Biophys 261 (1988) 64-71
67. Rowan A.D., Mason P., Mach L., Mort J.S., and Rat procathepsin B. Proteolytic processing to the mature form in vitro. J. Biol. Chem. 267 (1992) 15993-15999
68. Vasiljeva O., Dolinar M., Pungercar J.R., Turk V., and Turk B. Recombinant human procathepsin S is capable of autocatalytic processing at neutral pH in the presence of glycosaminoglycans. FEBS Lett. 579 (2005) 1285-1290
69. Park Y.G., Kim Y.H., Kang S.K., and Kim C.H. cAMP-PKA signaling pathway regulates bone resorption mediated by processing of cathepsin K in cultured mouse osteoclasts. Int. Immunopharmacol 6 (2006) 947-956
70. Hiesberger T., Huttler S., Rohlmann A., Schneider W., Sandhoff K., and Herz J. Cellular uptake of saposin (SAP) precursor and lysosomal delivery by the low density lipoprotein receptor-related protein (LRP). EMBO J 17 (1998) 4617-4625
71. Nielsen R., Courtoy P.J., Jacobsen C., Dom G., Lima W.R., Jadot M., Willnow T.E., Devuyst O., and Christensen E.I. Endocytosis provides a major alternative pathway for lysosomal biogenesis in kidney proximal tubular cells. Proc. Natl. Acad. Sci. USA 104 (2007) 5407-5412
72. Almeida P.C., Nantes I.L., Chagas J.R., Rizzi C.C., Faljoni-Alario A., Carmona E., Juliano L., Nader H.B., and Tersariol I.L. Cathepsin B activity regulation. Heparin-like glycosaminoglycans protect human cathepsin B from alkaline pH-induced inactivation. J. Biol. Chem. 276 (2001) 944-951
73. Chwieralski C.E., Welte T., and Buhling F. Cathepsin-regulated apoptosis. Apoptosis 11 (2006) 143-149
74. Turk B., and Stoka V. Protease signalling in cell death: caspases versus cysteine cathepsins. FEBS Lett. 581 (2007) 2761-2767
75. Lazner F., Gowen M., and Kola I. An animal model for pycnodysostosis: the role of cathepsin K in bone remodelling. Mol. Med. Today 5 (1999) 413-414
76. Punturieri A., Filippov S., Allen E., Caras I., Murray R., Reddy V., and Weiss S.J. Regulation of elastinolytic cysteine proteinase activity in normal and cathepsin K-deficient human macrophages. J Exp. Med 192 (2000) 789-800
77. Blair H.C., Teitelbaum S.L., Ghiselli R., and Gluck S. Osteoclastic bone resorption by a polarized vacuolar proton pump. Science 245 (1989) 855-857
78. Vaananen H.K., Zhao H., Mulari M., and Halleen J.M. The cell biology of osteoclast function. J. Cell Sci. 113 (2000) 377-381
79. Littlewood-Evans A., Kokubo T., Ishibashi O., Inaoka T., Wlodarski B., Gallagher J.A., and Bilbe G. Localization of cathepsin K in human osteoclasts by in situ hybridization and immunohistochemistry. Bone 20 (1997) 81-86
80. Yamaza T., Goto T., Kamiya T., Kobayashi Y., Sakai H., and Tanaka T. Study of immunoelectron microscopic localization of cathepsin K in osteoclasts and other bone cells in the mouse femur. Bone 23 (1998) 499-509
81. Sahara T., Itoh K., Debari K., and Sasaki T. Specific biological functions of vacuolar-type H(+)-ATPase and lysosomal cysteine proteinase, cathepsin K, in osteoclasts. Anat. Rec. A. Discov. Mol. Cell. Evol. Biol. 270 (2003) 152-161
82. Rantakokko J., Aro H.T., Savontaus M., Vuorio E., and Mouse cathepsin K. cDNA cloning and predominant expression of the gene in osteoclasts, and in some hypertrophying chondrocytes during mouse development. FEBS Lett. 393 (1996) 307-313
83. Votta B.J., Levy M.A., Badger A., Bradbeer J., Dodds R.A., James I.E., Thompson S., Bosshard M.J., Carr T., Connor J.R., Tomaszek T.A., Szewczuk L., Drake F.H., Veber D.F., and Gowen M. Peptide aldehyde inhibitors of cathepsin K inhibit bone resorption both in vitro and in vivo. J. Bone Miner. Res. 12 (1997) 1396-1406
84. Kamiya T., Kobayashi Y., Kanaoka K., Nakashima T., Kato Y., Mizuno A., and Sakai H. Fluorescence microscopic demonstration of cathepsin K activity as the major lysosomal cysteine proteinase in osteoclasts. J. Biochem. (Tokyo) 123 (1998) 752-759
85. Hou W.-S., Brömme D., Zhao Y., Mehler E., Dushey C., Weinstein H., Miranda C.S., Fraga C., Greig F., Carey J., Rimoin D.L., Desnick R.J., Gelb B.D., and Cathepsin K. Characterization of novel Mutations in the pro and mature polypeptide regions causing pycnodysostosis. J. Clin. Invest 103 (1999) 731-738
86. Hummel K.M., Petrow P.K., Franz J.K., Muller-Ladner U., Aicher W.K., Gay R.E., Brömme D., and Gay S. Cysteine proteinase cathepsin K mRNA is expressed in synovium of patients with rheumatoid arthritis and is detected at sites of synovial bone destruction. J. Rheumatol 25 (1998) 1887-1894
87. Morko J., Kiviranta R., Joronen K., Saamanen A.M., Vuorio E., and Salminen-Mankonen H. Spontaneous development of synovitis and cartilage degeneration in transgenic mice overexpressing cathepsin K. Arthritis Rheum 52 (2005) 3713-3717
88. Haeckel C., Krueger S., Buehling F., Broemme D., Franke K., Schuetze A., Roese I., and Roessner A. Expression of cathepsin K in the human embryo and fetus. Dev. Dyn 216 (1999) 89-95
89. Buhling F., Fengler A., Brandt W., Welte T., Ansorge S., and Nagler D.K. Review: novel cysteine proteases of the papain family. Adv. Exp. Med. Biol. 477 (2000) 241-254
90. Tepel C., Bromme D., Herzog V., and Brix K. Cathepsin K in thyroid epithelial cells: sequence, localization and possible function in extracellular proteolysis of thyroglobulin. J. Cell Sci. 113 (2000) 4487-4498
91. Perdereau C., Godat E., Maurel M.C., Hazouard E., Diot E., and Lalmanach G. Cysteine cathepsins in human silicotic bronchoalveolar lavage fluids. Biochim. Biophys. Acta 1762 (2006) 351-356
92. Serveau-Avesque C., Martino M.F., Herve-Grepinet V., Hazouard E., Gauthier F., Diot E., and Lalmanach G. Active cathepsins B, H, K, L and S in human inflammatory bronchoalveolar lavage fluids. Biol. Cell 98 (2006) 15-22
93. Ahlberg J., Berkenstam A., Henell F., and Glaumann H. Degradation of short and long lived proteins in isolated rat liver lysosomes. Effects of pH, temperature, and proteolytic inhibitors. J. Biol. Chem. 260 (1985) 5847-5854
94. Kirschke H., Barrett A.J., and Rawlings N.D. Proteinases 1: lysosomal cysteine proteinases. Protein Profile 2 (1995) 1581-1643
95. Chapman H.A., Riese R.J., and Shi G.P. Emerging roles for cysteine proteases in human biology. Annu. Rev. Physiol 59 (1997) 63-88
96. Vasiljeva O., Reinheckel T., Peters C., Turk D., Turk V., and Turk B. Emerging roles of cysteine cathepsins in disease and their potential as drug targets. Curr. Pharm. Des 13 (2007) 385-401
97. Friedrichs B., Tepel C., Reinheckel T., Deussing J., von Figura K., Herzog V., Peters C., Saftig P., and Brix K. Thyroid functions of mouse cathepsins B, K, and L. J. Clin. Invest 111 (2003) 1733-1745
98. Honey K., and Rudensky A.Y. Lysosomal cysteine proteases regulate antigen presentation. Nat. Rev. Immunol 3 (2003) 472-482
99. Saftig P., Wehmeyer O., Hunziker E., Jones S., Boyde A., Rommerskirch W., and von Figura K. Impaired osteoclastic bone resorption leads to osteopetrosis in cathepsin K-deficient mice. Proc. Natl. Acad. Sci. USA 95 (1998) 13453-13458
100. Saftig P., Hunziker E., Everts V., Jones S., Boyde A., Wehmeyer O., Suter A., and von Figura K. Functions of cathepsin K in bone resorption. Lessons from cathepsin K deficient mice. Adv. Exp. Med. Biol. 477 (2000) 293-303
101. Konttinen Y.T., Mandelin J., Li T.F., Salo J., Lassus J., Liljestrom M., Hukkanen M., Takagi M., Virtanen I., and Santavirta S. Acidic cysteine endoproteinase cathepsin K in the degeneration of the superficial articular hyaline cartilage in osteoarthritis. Arthritis Rheum 46 (2002) 953-960
102. Troen B.R. The role of cathepsin K in normal bone resorption. Drug News Perspect 17 (2004) 19-28
103. Shingleton W.D., Hodges D.J., Brick P., and Cawston T.E. Collagenase: a key enzyme in collagen turnover. Biochem. Cell. Biol. 74 (1996) 759-775
104. Kafienah W., Bromme D., Buttle D.J., Croucher L.J., and Hollander A.P. Human cathepsin K cleaves native type I and II collagens at the N-terminal end of the triple helix. Biochem. J. 331 (1998) 727-732
105. Goto T., Yamaza T., and Tanaka T. Cathepsins in the osteoclast. J. Electron Microsc. (Tokyo) 52 (2003) 551-558
106. Garnero P., Borel O., Byrjalsen I., Ferreras M., Drake F.H., McQueney M.S., Foged N.T., Delmas P.D., and Delaisse J.M. The collagenolytic activity of cathepsin K is unique among mammalian proteinases. J. Biol. Chem. 273 (1998) 32347-32352
107. French M.F., Mookhtiar K.A., and Van Wart H.E. Limited proteolysis of type I collagen at hyperreactive sites by class I and II Clostridium histolyticum collagenases: complementary digestion patterns. Biochemistry 26 (1987) 681-687
108. Welgus H.G., Jeffrey J.J., and Eisen A.Z. The collagen substrate specificity of human skin fibroblast collagenase. J. Biol. Chem. 256 (1981) 9511-9515
109. Atley L.M., Mort J.S., Lalumiere M., and Eyre D.R. Proteolysis of human bone collagen by cathepsin K: characterization of the cleavage sites generating by cross-linked N-telopeptide neoepitope. Bone 26 (2000) 241-247
110. Sassi M.L., Eriksen H., Risteli L., Niemi S., Mansell J., Gowen M., and Risteli J. Immunochemical characterization of assay for carboxyterminal telopeptide of human type I collagen: loss of antigenicity by treatment with cathepsin K. Bone 26 (2000) 367-373
111. Calvo M.S., Eyre D.R., and Gundberg C.M. Molecular basis and clinical application of biological markers of bone turnover. Endocr. Rev. 17 (1996) 333-368
112. Clemens J.D., Herrick M.V., Singer F.R., and Eyre D.R. Evidence that serum NTx (collagen-type I N-telopeptides) can act as an immunochemical marker of bone resorption. Clin. Chem. 43 (1997) 2058-2063
113. Kirschke H., Kembhavi A.A., Bohley P., and Barrett A.J. Action of rat liver cathepsin L on collagen and other substrates. Biochem. J. 201 (1982) 367-372
114. Burleigh M.C., Barrett A.J., and Lazarus G.S. Cathepsin B1. A lysosomal enzyme that degrades native collagen. Biochem. J. 137 (1974) 387-398
115. Everts V., Beertsen W., and Tigchelaar-Gutter W. The digestion of phagocytosed collagen is inhibited by the proteinase inhibitors leupeptin and E-64. Collagen Relat. Res. 5 (1985) 315-336
116. Inui T., Ishibashi O., Inaoka T., Origane Y., Kumegawa M., Kokubo T., and Yamamura T. Cathepsin K antisense oligodeoxynucleotide inhibits osteoclastic bone resorption. J. Biol. Chem. 272 (1997) 8109-8112
117. Li Z., Hou W.S., and Bromme D. Collagenolytic activity of cathepsin K is specifically modulated by cartilage-resident chondroitin sulfates. Biochemistry 39 (2000) 529-536
118. Li Z., Hou W.S., Escalante-Torres C.R., Gelb B.D., and Bromme D. Collagenase activity of cathepsin K depends on complex formation with chondroitin sulfate. J. Biol. Chem. 277 (2002) 28669-28676
119. Selent J., Kaleta J., Li Z., Lalmanach G., and Bromme D. Selective inhibition of the collagenase activity of cathepsin K. J. Biol. Chem. 282 (2007) 16492-16501
120. Troen B.R. Molecular mechanisms underlying osteoclast formation and activation. Exp. Gerontol 38 (2003) 605-614
121. Troen B.R. The regulation of cathepsin K gene expression. Ann. N.Y. Acad. Sci 1068 (2006) 165-172
122. Kamata I., Yamada M., Uchikawa R., Matsuda S., and Arizono N. Cysteine protease of the nematode Nippostrongylus brasiliensis preferentially evokes an IgE/IgG1 antibody response in rats. Clin. Exp. Immunol 102 (1995) 71-77
123. Matsumoto M., Kogawa M., Wada S., Takayanagi H., Tsujimoto M., Katayama S., Hisatake K., and Nogi Y. Essential role of p38 mitogen-activated protein kinase in cathepsin K gene expression during osteoclastogenesis through association of NFATc1 and PU.1. J. Biol. Chem. 279 (2004) 45969-45979
124. Sharma S.M., Bronisz A., Hu R., Patel K., Mansky K.C., Sif S., and Ostrowski M.C. MITF and PU.1 recruit p38 MAPK and NFATc1 to target genes during osteoclast differentiation. J. Biol. Chem. 282 (2007) 15921-15929
125. Novinec M., Grass R.N., Stark W.J., Turk V., Baici A., and Lenarcic B. Interaction between human cathepsins K, L, and S and elastins: mechanism of elastinolysis and inhibition by macromolecular inhibitors. J. Biol. Chem. 282 (2007) 7893-7902
126. Yasuda Y., Li Z., Greenbaum D., Bogyo M., Weber E., and Bromme D. Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages. J. Biol. Chem. 279 (2004) 36761-36770
127. Runger T.M., Quintanilla-Dieck M.J., and Bhawan J. Role of cathepsin K in the turnover of the dermal extracellular matrix during scar formation. J. Invest. Dermatol 127 (2007) 293-297
128. Ohba T., Ohba Y., and Moriyama K. Synthesis of mRNAs for cathepsins L and K during development of the rat mandibular condylar cartilage. Cell. Tissue Res. 302 (2000) 343-352
129. Buhling F., Peitz U., Kruger S., Kuster D., Vieth M., Gebert I., Roessner A., Weber E., Malfertheiner P., and Wex T. Cathepsins K, L, B, X and W are differentially expressed in normal and chronically inflamed gastric mucosa. Biol. Chem. 385 (2004) 439-445
130. Buhling F., Waldburg N., Kruger S., Rocken C., Wiesner O., Weber E., and Welte T. Expression of cathepsins B, H, K, L, and S during human fetal lung development. Dev. Dyn 225 (2002) 14-21
131. Lange A.W., and Yutzey K.E. NFATc1 expression in the developing heart valves is responsive to the RANKL pathway and is required for endocardial expression of cathepsin K. Dev. Biol. 292 (2006) 407-417
132. Platt M.O., Ankeny R.F., Shi G.P., Weiss D., Vega J.D., Taylor W.R., and Jo H. Expression of cathepsin K is regulated by shear stress in cultured endothelial cells and is increased in endothelium in human atherosclerosis. Am. J. Physiol. Heart Circ. Physiol 292 (2007) H1479-H1486
133. Anway M.D., Wright W.W., Zirkin B.R., Korah N., Mort J.S., and Hermo L. Expression and localization of cathepsin k in adult rat sertoli cells. Biol. Reprod 70 (2004) 562-569
134. Wright W.W., Smith L., Kerr C., and Charron M. Mice that express enzymatically inactive cathepsin L exhibit abnormal spermatogenesis. Biol. Reprod 68 (2003) 680-687
135. Toomes C., James J., Wood A.J., Wu C.L., McCormick D., Lench N., Hewitt C., Moynihan L., Roberts E., Woods C.G., Markham A., Wong M., Widmer R., Ghaffar K.A., Pemberton M., Hussein I.R., Temtamy S.A., Read D.R.A.P., Sloan P., Dixon M.J., and Thakker N.S. Loss-of-function mutations in the cathepsin C gene result in periodontal disease and palmoplantar keratosis. Nat. Genet. 23 (1999) 421-424
136. Gelb B.D., Shi G.P., Chapman H.A., and Desnick R.J. Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency. Science 273 (1996) 1236-1238
137. Everts V., Hou W.S., Rialland X., Tigchelaar W., Saftig P., Bromme D., Gelb B.D., and Beertsen W. Cathepsin K deficiency in pycnodysostosis results in accumulation of non-digested phagocytosed collagen in fibroblasts. Calcif. Tissue Int 73 (2003) 380-386
138. Donnarumma M., Regis S., Tappino B., Rosano C., Assereto S., Corsolini F., Di Rocco M., and Filocamo M. Molecular analysis and characterization of nine novel CTSK mutations in twelve patients affected by pycnodysostosis. Hum. Mutat 28 (2007) 524
139. Schilling A.F., Mulhausen C., Lehmann W., Santer R., Schinke T., Rueger J.M., and Amling M. High bone mineral density in pycnodysostotic patients with a novel mutation in the propeptide of cathepsin K. Osteoporos. Int 18 (2007) 659-669
140. Gowen M., Lazner F., Dodds R., Kapadia R., Feild J., Tavaria M., Bertoncello I., Drake F., Zavarselk S., Tellis I., Hertzog P., Debouck C., and Kola I. Cathepsin K knockout mice develop osteopetrosis due to a deficit in matrix degradation but not demineralization. J. Bone Miner. Res. 14 (1999) 1654-1663
141. Selinger C.I., Day C.J., and Morrison N.A. Optimized transfection of diced siRNA into mature primary human osteoclasts: inhibition of cathepsin K mediated bone resorption by siRNA. J. Cell Biochem 96 (2005) 996-1002
142. Meier C., Meinhardt U., Greenfield J.R., De Winter J., Nguyen T.V., Dunstan C.R., and Seibel M.J. Serum cathepsin K concentrations reflect osteoclastic activity in women with postmenopausal osteoporosis and patients with Paget's disease. Clin. Lab 52 (2006) 1-10
143. Kiviranta R., Morko J., Uusitalo H., Aro H.T., Vuorio E., and Rantakokko J. Accelerated turnover of metaphyseal trabecular bone in mice overexpressing cathepsin K. J. Bone Miner. Res. 16 (2001) 1444-1452
144. Stroup G.B., Lark M.W., Veber D.F., Bhattacharyya A., Blake S., Dare L.C., Erhard K.F., Hoffman S.J., James I.E., Marquis R.W., Ru Y., Vasko-Moser J.A., Smith B.R., Tomaszek T., and Gowen M. Potent and selective inhibition of human cathepsin K leads to inhibition of bone resorption in vivo in a nonhuman primate. J. Bone Miner. Res. 16 (2001) 1739-1746
145. Garnero P., Ferreras M., Karsdal M.A., Nicamhlaoibh R., Risteli J., Borel O., Qvist P., Delmas P.D., Foged N.T., and Delaisse J.M. The type I collagen fragments ICTP and CTX reveal distinct enzymatic pathways of bone collagen degradation. J. Bone Miner. Res. 18 (2003) 859-867
146. Stoka V., Turk B., and Turk V. Lysosomal cysteine proteases: structural features and their role in apoptosis. IUBMB Life 57 (2005) 347-353
147. Vancompernolle K., Van Herreweghe F., Pynaert G., Van de Craen M., De Vos K., Totty N., Sterling A., Fiers W., Vandenabeele P., and Grooten J. Atractyloside-induced release of cathepsin B, a protease with caspase-processing activity. FEBS Lett. 438 (1998) 150-158
148. Guicciardi M.E., Deussing J., Miyoshi H., Bronk S.F., Svingen P.A., Peters C., Kaufmann S.H., and Gores G.J. Cathepsin B contributes to TNF-alpha-mediated hepatocyte apoptosis by promoting mitochondrial release of cytochrome c. J. Clin. Invest 106 (2000) 1127-1137
149. Stoka V., Turk B., Schendel S.L., Kim T.H., Cirman T., Snipas S.J., Ellerby L.M., Bredesen D., Freeze H., Abrahamson M., Bromme D., Krajewski S., Reed J.C., Yin X.M., Turk V., and Salvesen G.S. Lysosomal protease pathways to apoptosis. Cleavage of bid, not pro-caspases, is the most likely route. J. Biol. Chem. 276 (2001) 3149-3157
150. Lalmanach G., Diot E., Godat E., Lecaille F., and Herve-Grepinet V. Cysteine cathepsins and caspases in silicosis. Biol. Chem. 387 (2006) 863-870
151. Chen W., Yang S., Abe Y., Li M., Wang Y., Shao J., Li E., and Li Y.P. Novel pycnodysostosis mouse model uncovers cathepsin K function as a potential regulator of osteoclast apoptosis and senescence. Hum. Mol. Genet. 16 (2007) 410-423
152. Kempson G.E., Muir H., Pollard C., and Tuke M. The tensile properties of the cartilage of human femoral condyles related to the content of collagen and glycosaminoglycans. Biochim. Biophys. Acta 297 (1973) 456-472
153. Kempson G.E. The effects of proteoglycan and collagen degradation on the mechanical properties of adult human articular cartilage. In: Burleigh P.M.C., and Poole A.R. (Eds). Dynamics of Connective Tissue Macromolecules (1975), Elsevier, New York 277-305
154. Dodds R.A., Connor J.R., Drake F.H., and Gowen M. Expression of cathepsin K messenger RNA in giant cells and their precursors in human osteoarthritic synovial tissues. Arthritis Rheum 42 (1999) 1588-1593
155. Pelletier J.P., Boileau C., Brunet J., Boily M., Lajeunesse D., Reboul P., Laufer S., and Martel-Pelletier J. The inhibition of subchondral bone resorption in the early phase of experimental dog osteoarthritis by licofelone is associated with a reduction in the synthesis of MMP-13 and cathepsin K. Bone 34 (2004) 527-538
156. Ma J., Tanaka K.F., Yamada G., and Ikenaka K. Induced expression of cathepsins and cystatin C in a murine model of demyelination. Neurochem. Res. 32 (2007) 311-320
157. Morko J.P., Soderstrom M., Saamanen A.M., Salminen H.J., and Vuorio E.I. Up regulation of cathepsin K expression in articular chondrocytes in a transgenic mouse model for osteoarthritis. Ann. Rheum. Dis 63 (2004) 649-655
158. Yamaza T., Tsuji Y., Goto T., Kido M.A., Nishijima K., Moroi R., Akamine A., and Tanaka T. Comparison in localization between cystatin C and cathepsin K in osteoclasts and other cells in mouse tibia epiphysis by immunolight and immunoelectron microscopy. Bone 29 (2001) 42-53
159. Lenarcic B., Krasovec M., Ritonja A., Olafsson I., and Turk V. Inactivation of human cystatin C and kininogen by human cathepsin D. FEBS Lett. 280 (1991) 211-215
160. Li Z., Yasuda Y., Li W., Bogyo M., Katz N., Gordon R.E., Fields G.B., and Bromme D. Regulation of collagenase activities of human cathepsins by glycosaminoglycans. J. Biol. Chem. 279 (2004) 5470-5479
161. Skoumal M., Haberhauer G., Kolarz G., Hawa G., Woloszczuk W., and Klingler A. Serum cathepsin K levels of patients with longstanding rheumatoid arthritis: correlation with radiological destruction. Arthritis Res. Ther 7 (2005) R65-R70
162. Shi G.P., Sukhova G.K., Grubb A., Ducharme A., Rhode L.H., Lee R.T., Ridker P.M., Libby P., and Chapman H.A. Cystatin C deficiency in human atherosclerosis and aortic aneurysms. J. Clin. Invest 104 (1999) 1191-1197
163. Pentikainen M.O., Oorni K., Ala-Korpela M., and Kovanen P.T. Modified LDL-trigger of atherosclerosis and inflammation in the arterial intima. J. Intern. Med 247 (2000) 359-370
164. Lutgens E., Lutgens S.P., Faber B.C., Heeneman S., Gijbels M.M., de Winther M.P., Frederik P., van der Made I., Daugherty A., Sijbers A.M., Fisher A., Long C.J., Saftig P., Black D., Daemen M.J., and Cleutjens K.B. Disruption of the cathepsin K gene reduces atherosclerosis progression and induces plaque fibrosis but accelerates macrophage foam cell formation. Circulation 113 (2006) 98-107
165. Linke M., Gordon R.E., Brillard M., Lecaille F., Lalmanach G., and Bromme D. Degradation of apolipoprotein B-100 by lysosomal cysteine cathepsins. Biol. Chem. 387 (2006) 1295-1303
166. Platt M.O., Ankeny R.F., and Jo H. Laminar shear stress inhibits cathepsin L activity in endothelial cells. Arterioscler. Thromb. Vasc. Biol. 26 (2006) 1784-1790
167. S.P. Lutgens, K.B. Cleutjens, M.J. Daemen, S. Heeneman, Cathepsin cysteine proteases in cardiovascular disease, FASEB J. in press.
168. Buhling F., Rocken C., Brasch F., Hartig R., Yasuda Y., Saftig P., Bromme D., and Welte T. Pivotal role of cathepsin K in lung fibrosis. Am. J. Pathol 164 (2004) 2203-2216
169. Bhoola K.D., Figueroa C.D., and Worthy K. Bioregulation of kinins: kallikreins, kininogens, and kininases. Pharmacol. Rev. 44 (1992) 1-80
170. Kozik A., Moore R.B., Potempa J., Imamura T., Rapala-Kozik M., and Travis J. A novel mechanism for bradykinin production at inflammatory sites. Diverse effects of a mixture of neutrophil elastase and mast cell tryptase versus tissue and plasma kallikreins on native and oxidized kininogens. J. Biol. Chem. 273 (1998) 33224-33229
171. Desmazes C., Gauthier F., and Lalmanach G. Cathepsin L, but not cathepsin B, is a potential kininogenase. Biol. Chem. 382 (2001) 811-815
172. Desmazes C., Galineau L., Gauthier F., Bromme D., and Lalmanach G. Kininogen-derived peptides for investigating the putative vasoactive properties of human cathepsins K and L. Eur. J. Biochem 270 (2003) 171-178
173. Puzer L., Vercesi J., Alves M.F., Barros N.M., Araujo M.S., Aparecida Juliano M., Reis M.L., Juliano L., and Carmona A.K. A possible alternative mechanism of kinin generation in vivo by cathepsin L. Biol. Chem. 386 (2005) 699-704
174. Godat E., Lecaille F., Desmazes C., Duchene S., Weidauer E., Saftig P., Bromme D., Vandier C., Lalmanach G., and Cathepsin K. a cysteine protease with unique kinin-degrading properties. Biochem. J. 383 (2004) 501-506
175. Lecaille F., Vandier C., Godat E., Herve-Grepinet V., Bromme D., and Lalmanach G. Modulation of hypotensive effects of kinins by cathepsin K. Arch. Biochem. Biophys 459 (2007) 129-136
176. Jedeszko C., and Sloane B.F. Cysteine cathepsins in human cancer. Biol. Chem. 385 (2004) 1017-1027
177. Mohamed M.M., and Sloane B.F. Cysteine cathepsins: multifunctional enzymes in cancer. Nat. Rev. Cancer 6 (2006) 764-775
178. Joyce J.A., Baruch A., Chehade K., Meyer-Morse N., Giraudo E., Tsai F.Y., Greenbaum D.C., Hager J.H., Bogyo M., and Hanahan D. Cathepsin cysteine proteases are effectors of invasive growth and angiogenesis during multistage tumorigenesis. Cancer Cell. 5 (2004) 443-453
179. Littlewood-Evans A.J., Bilbe G., Bowler W.B., Farley D., Wlodarski B., Kokubo T., Inaoka T., Sloane J., Evans D.B., and Gallagher J.A. The osteoclast-associated protease cathepsin K is expressed in human breast carcinoma. Cancer Res. 57 (1997) 5386-5390
180. Gaumann A., Hansen T., Kohler H.H., Kommoss F., Mann W., Maurer J., Kirkpatrick C.J., and Kriegsmann J. The expression of cathepsins in osteoclast-like giant cells of an anaplastic thyroid carcinoma with tracheal perforation. Pathol. Res. Pract 197 (2001) 257-262
181. Brubaker K.D., Vessella R.L., True L.D., Thomas R., and Corey E. Cathepsin K mRNA and protein expression in prostate cancer progression. J. Bone Miner. Res. 18 (2003) 222-230
182. Rapa I., Volante M., Cappia S., Rosas R., Scagliotti G.V., and Papotti M. Cathepsin K is selectively expressed in the stroma of lung adenocarcinoma but not in bronchioloalveolar carcinoma. A useful marker of invasive growth. Am. J. Pathol 125 (2006) 847-854
183. Lindeman J.H., Hanemaaijer R., Mulder A., Dijkstra P.D., Szuhai K., Bromme D., Verheijen J.H., and Hogendoorn P.C. Cathepsin K is the principal protease in giant cell tumor of bone. Am. J. Pathol 165 (2004) 593-600
184. Hansen T., Unger R.E., Gaumann A., Hundorf I., Maurer J., Kirkpatrick C.J., and Kriegsmann J. Expression of matrix-degrading cysteine proteinase cathepsin K in cholesteatoma. Mod. Pathol 14 (2001) 1226-1231
185. Rocken C., Stix B., Bromme D., Ansorge S., Roessner A., and Buhling F. A putative role for cathepsin K in degradation of AA and AL amyloidosis. Am. J. Pathol 158 (2001) 1029-1238
186. Bohne S., Sletten K., Menard R., Buhling F., Vockler S., Wrenger E., Roessner A., and Rocken C. Cleavage of AL amyloid proteins and AL amyloid deposits by cathepsins B, K, and L. J. Pathol 203 (2004) 528-537
187. Rocken C., Fandrich M., Stix B., Tannert A., Hortschansky P., Reinheckel T., Saftig P., Kahne T., Menard R., Ancsin J.B., and Buhling F. Cathepsin protease activity modulates amyloid load in extracerebral amyloidosis. J. Pathol 210 (2006) 478-487
188. Moran M.T., Schofield J.P., Hayman A.R., Shi G.P., Young E., and Cox T.M. Pathologic gene expression in Gaucher disease: up-regulation of cysteine proteinases including osteoclastic cathepsin K. Blood 96 (2000) 1969-1978
189. Sukhova G.K., Zhang Y., Pan J.H., Wada Y., Yamamoto T., Naito M., Kodama T., Tsimikas S., Witztum J.L., Lu M.L., Sakara Y., Chin M.T., Libby P., and Shi G.P. Deficiency of cathepsin S reduces atherosclerosis in LDL receptor-deficient mice. J. Clin. Invest 111 (2003) 897-906
190. Taleb S., Lacasa D., Bastard J.P., Poitou C., Cancello R., Pelloux V., Viguerie N., Benis A., Zucker J.D., Bouillot J.L., Coussieu C., Basdevant A., Langin D., Clement K., and Cathepsin S. a novel biomarker of adiposity: relevance to atherogenesis. FASEB J 19 (2005) 1540-1542
191. Taleb S., and Clement K. Emerging role of cathepsin S in obesity and its associated diseases. Clin. Chem. Lab. Med 45 (2007) 328-332
192. Kirschke H., Schmidt I., Wiederanders B., and Cathepsin S. The cysteine proteinase from bovine lymphoid tissue is distinct from cathepsin L (EC 3.4.22.15). Biochem. J. 240 (1986) 455-459
193. Kirschke H., Wiederanders B., Bromme D., and Rinne A. Cathepsin S from bovine spleen. Purification, distribution, intracellular localization and action on proteins. Biochem. J. 264 (1989) 467-473
194. Turk B., Dolenc I., Lenarcic B., Krizaj I., Turk V., Bieth J.G., and Bjork I. Acidic pH as a physiological regulator of human cathepsin L activity. Eur. J. Biochem 259 (1999) 926-932
195. Brömme D. Cysteine proteases as therapeutic targets. Drug News Perspect 12 (1999) 73-82
196. Cygler M., and Mort J.S. Proregion structure of members of the papain superfamily. Mode of inhibition of enzymatic activity. Biochimie 79 (1997) 645-652
197. Groves M.R., Coulombe R., Jenkins J., and Cygler M. Structural basis for specificity of papain-like cysteine protease proregions toward their cognate enzymes. Proteins 32 (1998) 504-514
198. Wiederanders B. Structure-function relationships in class CA1 cysteine peptidase propeptides. Acta Biochim. Pol 50 (2003) 691-713
199. LaLonde J.M., Zhao B., Janson C.A., D'Alessio K.J., McQueney M.S., Orsini M.J., Debouck C.M., and WW S. The crystal structure of human procathepsin K. Biochemistry 38 (1999) 862-869
200. Sivaraman J., Lalumiere M., Menard R., and Cygler M. Crystal structure of wild-type human procathepsin K. Protein Sci. 8 (1999) 283-290
201. Billington C.J., Mason P., Magny M.C., and Mort J.S. The slow-binding inhibition of cathepsin K by its propeptide. Biochem. Biophys. Res. Commun 276 (2000) 924-929
202. Guay J., Falgueyret J.P., Ducret A., Percival M.D., and Mancini J.A. Potency and selectivity of inhibition of cathepsin K, L and S by their respective propeptides. Eur. J. Biochem 267 (2000) 6311-6318
203. Chowdhury S.F., Sivaraman J., Wang J., Devanathan G., Lachance P., Qi H., Menard R., Lefebvre J., Konishi Y., Cygler M., Sulea T., and Purisima E.O. Design of noncovalent inhibitors of human cathepsin L. From the 96-residue proregion to optimized tripeptides. J. Med. Chem. 45 (2002) 5321-5329
204. Tersariol I.L., Pimenta D.C., Chagas J.R., and Almeida P.C. Proteinase activity regulation by glycosaminoglycans. Braz. J. Med. Biol. Res. 35 (2002) 135-144
205. Smith A.J., Singhrao S.K., Newman G.R., Waddington R.J., and Embery G. A biochemical and immuno-electron microscopical analysis of chondroitin sulphate-rich proteoglycans in human alveolar bone. Histochem. J. 29 (1997) 1-9
206. Li R., Chen X., Gong B., Selzer P.M., Li Z., Davidson E., Kurzban G., Miller R.E., Nuzum E.O., McKerrow J.H., Fletterick R.J., Gillmor S.A., Craik C.S., Kuntz I.D., Cohen F.E., and Kenyon G.L. Structure-based design of parasitic protease inhibitors. Bioorg. Med. Chem. 4 (1996) 1421-1427
207. Owen C.A. Proteinases and oxidants as targets in the treatment of chronic obstructive pulmonary disease. Proc. Am. Thorac. Soc. 2 (2005) 373-385
208. Henrotin Y.E., Bruckner P., and Pujol J.P. The role of reactive oxygen species in homeostasis and degradation of cartilage. Osteoarthritis Cartilage 11 (2003) 747-755
209. Ameye L.G., and Young M.F. Animal models of osteoarthritis: lessons learned while seeking the "Holy Grail". Curr. Opin. Rheumatol 18 (2006) 537-547
210. Rahman I., Yang S.R., and Biswas S.K. Current concepts of redox signaling in the lungs. Antioxid. Redox. Signal 8 (2006) 681-689
211. Mathy-Hartert M., Martin G., Devel P., Deby-Dupont G., Pujol J.P., Reginster J.Y., and Henrotin Y. Reactive oxygen species downregulate the expression of pro-inflammatory genes by human chondrocytes. Inflamm. Res. 52 (2003) 111-118
212. Percival M.D., Ouellet M., Campagnolo C., Claveau D., and Li C. Inhibition of cathepsin K by nitric oxide donors: evidence for the formation of mixed disulfides and a sulfenic acid. Biochemistry 38 (1999) 13574-13583
213. Bode W., and Huber R. Structural basis of the endoproteinase-protein inhibitor interaction. Biochim. Biophys. Acta 1477 (2000) 241-252
214. Dubin G. Proteinaceous cysteine protease inhibitors. Cell. Mol. Life Sci. 62 (2005) 653-669
215. Bode W., Engh R., Musil D., Thiele U., Huber R., Karshikov A., Brzin J., Kos J., and Turk V. The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases. EMBO J 7 (1988) 2593-2599
216. Stubbs M.T., Laber B., Bode W., Huber R., Jerala R., Lenarcic B., and Turk V. The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction. EMBO J 9 (1990) 1939-1947
217. Jenko S., Dolenc I., Guncar G., Dobersek A., Podobnik M., and Turk D. 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 (2003) 875-885
218. Rawlings N.D., and Barrett A.J. Evolution of proteins of the cystatin superfamily. J. Mol. Evol. 30 (1990) 60-71
219. Turk V., and Bode W. The cystatins: protein inhibitors of cysteine proteinases. FEBS Lett. 285 (1991) 213-219
220. Bode W., Engh R., Musil D., Laber B., Stubbs M., Huber R., and Turk V. Mechanism of interaction of cysteine proteinases and their protein inhibitors as compared to the serine proteinase-inhibitor interaction. Biol. Chem. Hoppe-Seyler 371 (1990) 111-118
221. Henskens Y.M., Veerman E.C., and Nieuw Amerongen A.V. Cystatins in health and disease. Biol Chem Hoppe Seyler 377 (1996) 71-86
222. Zajc I., Sever N., Bervar A., and Lah T.T. Expression of cysteine peptidase cathepsin L and its inhibitors stefins A and B in relation to tumorigenicity of breast cancer cell lines. Cancer Lett. 187 (2002) 185-190
223. Pennacchio L.A., Bouley D.M., Higgins K.M., Scott M.P., Noebels J.L., and Myers R.M. Progressive ataxia, myoclonic epilepsy and cerebellar apoptosis in cystatin B-deficient mice. Nat. Genet. 20 (1998) 251-258
224. Laitala-Leinonen T., Rinne R., Saukko P., Vaananen H.K., and Rinne A. Cystatin B as an intracellular modulator of bone resorption. Matrix Biol. 25 (2006) 149-157
225. Abrahamson M., Barrett A.J., Salvesen G., and Grubb A. Isolation of six cysteine proteinase inhibitors from human urine. Their physicochemical and enzyme kinetic properties and concentrations in biological fluids. J. Biol. Chem. 261 (1986) 11282-11289
226. Abrahamson M., Alvarez-Fernandez M., and Nathanson C.M. Cystatins. Biochem. Soc. Symp (2003) 179-199
227. Zhang J., Shridhar R., Dai Q., Song J., Barlow S.C., Yin L., Sloane B.F., Miller F.R., Meschonat C., Li B.D., Abreo F., and Keppler D. Cystatin m: a novel candidate tumor suppressor gene for breast cancer. Cancer Res. 64 (2004) 6957-6964
228. Abrahamson M. Cystatins. Methods Enzymol 244 (1994) 685-700
229. Cheng T., Hitomi K., van Vlijmen-Willems I.M., de Jongh G.J., Yamamoto K., Nishi K., Watts C., Reinheckel T., Schalkwijk J., and Zeeuwen P.L. Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the legumain-binding site. A novel clue for the role of cystatin M/E in epidermal cornification. J. Biol. Chem. 281 (2006) 15893-15899
230. Barrett A.J., Davies M.E., and Grubb A. The place of human gamma-trace (cystatin C) amongst the cysteine proteinase inhibitors. Biochem. Biophys. Res. Commun 120 (1984) 631-636
231. Altiok O., Yasumatsu R., Bingol-Karakoc G., Riese R.J., Stahlman M.T., Dwyer W., Pierce R.A., Bromme D., Weber E., and Cataltepe S. Imbalance between cysteine proteases and inhibitors in a baboon model of bronchopulmonary dysplasia. Am. J. Respir. Crit. Care Med 173 (2006) 318-326
232. Liu J., Sukhova G.K., Sun J.S., Xu W.H., Libby P., and Shi G.P. Lysosomal cysteine proteases in atherosclerosis. Arterioscler. Thromb. Vasc. Biol. 24 (2004) 1359-1366
233. Muller-Esterl W. Novel functions of the kininogens. Semin. Thromb. Hemost 13 (1987) 115-126
234. DeLa Cadena R.A., and Colman R.W. Structure and functions of human kininogens. Trends Pharmacol. Sci. 12 (1991) 272-275
235. Grubb A., Abrahamson M., Olafsson I., Trojnar J., Kasprzykowska R., Kasprzykowski F., and Grzonka Z. Synthesis of cysteine proteinase inhibitors structurally based on the proteinase interacting N-terminal region of human cystatin C. Biol. Chem. Hoppe Seyler 371 (1990) 137-144
236. Hall A., Abrahamson M., Grubb A., Trojnar J., Kania P., Kasprzykowska R., and Kasprzykowski F. Cystatin C based peptidyl diazomethanes as cysteine proteinase inhibitors: influence of the peptidyl chain length. J. Enzyme Inhib 6 (1992) 113-123
237. Lalmanach G., Mayer R., Serveau C., Scharfstein J., and Gauthier F. Biotin-labelled peptidyl diazomethane inhibitors derived from the substrate-like sequence of cystatin: targeting of the active site of cruzipain, the major cysteine proteinase of Trypanosoma cruzi. Biochem. J. 318 (1996) 395-399
238. Chagas J.R., Authie E., Serveau C., Lalmanach G., Juliano L., and Gauthier F. A comparison of the enzymatic properties of the major cysteine proteinases from Trypanosoma congolense and Trypanosoma cruzi. Mol. Biochem. Parasitol 88 (1997) 85-94
239. Florent I., Lecaille F., Montagne J.J., Gauthier F., Schrevel J., and Lalmanach G. Labelling of four distinct trophozoite falcipains of Plasmodium falciparum by a cystatin-derived probe. Biol. Chem. 386 (2005) 401-406
240. Wieczerzak E., Drabik P., Lankiewicz L., Oldziej S., Grzonka Z., Abrahamson M., Grubb A., and Bromme D. Azapeptides structurally based upon inhibitory sites of cystatins as potent and selective inhibitors of cysteine proteases. J. Med. Chem. 45 (2002) 4202-4211
241. Wieczerzak E., Jankowska E., Rodziewicz-Motowidlo S., Gieldon A., Lagiewka J., Grzonka Z., Abrahamson M., Grubb A., and Bromme D. Novel azapeptide inhibitors of cathepsins B and K. Structural background to increased specificity for cathepsin B. J. Pept. Res. 66 (2005) 1-11
242. Lenarcic B., and Bevec T. Thyropins-new structurally related proteinase inhibitors. Biol. Chem. 379 (1998) 105-111
243. Guncar G., Pungercic G., Klemencic I., Turk V., and Turk D. Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S. EMBO J 18 (1999) 793-803
244. Meh P., Pavsic M., Turk V., Baici A., and Lenarcic B. Dual concentration-dependent activity of thyroglobulin type-1 domain of testican: specific inhibitor and substrate of cathepsin L. Biol. Chem. 386 (2005) 75-83
245. Gettins P.G. Serpin structure, mechanism, and function. Chem. Rev. 102 (2002) 4751-4804
246. Silverman G.A., Bird P.I., Carrell R.W., Church F.C., Coughlin P.B., Gettins P.G., Irving J.A., Lomas D.A., Luke C.J., Moyer R.W., Pemberton P.A., Remold-O'Donnell E., Salvesen G.S., Travis J., and Whisstock J.C. The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature. J. Biol. Chem. 276 (2001) 33293-33296
247. Schick C., Pemberton P.A., Shi G.P., Kamachi Y., Cataltepe S., Bartuski A.J., Gornstein E.R., Bromme D., Chapman H.A., and Silverman G.A. Cross-class inhibition of the cysteine proteinases cathepsins K, L, and S by the serpin squamous cell carcinoma antigen 1: a kinetic analysis. Biochemistry 37 (1998) 5258-5266
248. Irving J.A., Shushanov S.S., Pike R.N., Popova E.Y., Bromme D., Coetzer T.H., Bottomley S.P., Boulynko I.A., Grigoryev S.A., and Whisstock J.C. Inhibitory activity of a heterochromatin-associated serpin (MENT) against papain-like cysteine proteinases affects chromatin structure and blocks cell proliferation. J. Biol. Chem. 277 (2002) 13192-13201
249. Jayakumar A., Kang Y., Frederick M.J., Pak S.C., Henderson Y., Holton P.R., Mitsudo K., Silverman G.A., AK E.L.-N., Bromme D., and Clayman G.L. Inhibition of the cysteine proteinases cathepsins K and L by the serpin headpin (serpinB13): a kinetic analysis. Arch. Biochem. Biophys 409 (2003) 367-374
250. Masumoto K., Sakata Y., Arima K., Nakao I., and Izuhara K. Inhibitory mechanism of a cross-class serpin, the squamous cell carcinoma antigen 1. J. Biol. Chem. 278 (2003) 45296-45304
251. Spring P., Nakashima T., Frederick M., Henderson Y., and Clayman G. Identification and cDNA cloning of headpin, a novel differentially expressed serpin that maps to chromosome 18q. Biochem. Biophys. Res. Commun 264 (1999) 299-304
252. Nakashima T., Pak S.C., Silverman G.A., Spring P.M., Frederick M.J., and Clayman G.L. Genomic cloning, mapping, structure and promoter analysis of HEADPIN, a serpin which is down-regulated in head and neck cancer cells. Biochim. Biophys. Acta 1492 (2000) 441-446
253. van Leuven F. Human alpha 2 macroglobulin. Mol. Cell. Biochem 58 (1984) 121-128
254. Mason R.W. Interaction of lysosomal cysteine proteinases with alpha 2-macroglobulin: conclusive evidence for the endopeptidase activities of cathepsins B and H. Arch. Biochem. Biophys 273 (1989) 367-374
255. Buttle D.J., Abrahamson M., Burnett D., Mort J.S., Barrett A.J., Dando P.M., and Hill S.L. Human sputum cathepsin B degrades proteoglycan, is inhibited by alpha 2-macroglobulin and is modulated by neutrophil elastase cleavage of cathepsin B precursor and cystatin C. Biochem. J. 276 (1991) 325-331
256. Nicholls A., Sharp K.A., and Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11 (1991) 281-296
257. Zhao B., Janson C.A., Amegadzie B.Y., D'Alessio K., Griffin C., Kurdyla J., McQueney M., Qiu X., Smith W.W., and Abdel-Meguid S.S. Crystal structure of human osteoclast cathepsin K complex with E-64. Nat. Struct. Biol. 4 (1997) 109-111
258. Thompson S.K., Halbert S.M., Bossard M.J., Tomaszek T.A., Levy M.A., Zhao B., Smith W.W., Abdel-Meguid S.S., Janson C.A., D'Alessio K.J., McQueney M.S., Amegadzie B.Y., Hanning C.R., DesJarlais R.L., Briand J., Sarkar S.K., Huddleston M.J., Ijames C.F., Carr S.A., Garnes K.T., Shu A., Heys J.R., Bradbeer J., Zembryski D., and Lee-Rykaczewski L. Design of potent and selective human cathepsin K inhibitors that span the active site. Proc. Natl. Acad. Sci. USA 94 (1997) 14249-14254
259. Desjarlais R.L., Yamashita D.S., Oh H.J., Uzinskas I.N., Erhard K.F., Allen A.C., Haltiwanger R.C., Zhao B.G., Smith W.W., Abdel-Meguid S.S., Dalessio K., Janson C.A., Mcqueney M.S., Tomaszek T.A., Levy M.A., and Veber D.F. Use of X-ray co-crystal structures and molecular modeling to design potent and selective non-peptide inhibitors of cathepsin K. J. Am. Chem. Soc. 120 (1998) 9114-9115
260. Mbawa Z.R., Gumm I.D., Shaw E., and Lonsdale-Eccles J.D. Characterisation of a cysteine protease from bloodstream forms of Trypanosoma congolense. Eur. J. Biochem 204 (1992) 371-379
261. Marquis R.W., Ru Y., Zeng J., Trout R.E., LoCastro S.M., Gribble A.D., Witherington J., Fenwick A.E., Garnier B., Tomaszek T., Tew D., Hemling M.E., Quinn C.J., Smith W.W., Zhao B., McQueney M.S., Janson C.A., D'Alessio K., and Veber D.F. Cyclic ketone inhibitors of the cysteine protease cathepsin K. J. Med. Chem. 44 (2001) 725-736
262. Catalano J.G., Deaton D.N., Long S.T., McFadyen R.B., Miller L.R., Payne J.A., Wells-Knecht K.J., and Wright L.L. Design of small molecule ketoamide-based inhibitors of cathepsin K. Bioorg. Med. Chem. Lett. 14 (2004) 719-722
263. Boros E.E., Deaton D.N., Hassell A.M., McFadyen R.B., Miller A.B., Miller L.R., Paulick M.G., Shewchuk L.M., Thompson J.B., Willard Jr. D.H., and Wright L.L. Exploration of the P2-P3 SAR of aldehyde cathepsin K inhibitors. Bioorg. Med. Chem. Lett. 14 (2004) 3425-3429
264. Barrett D.G., Catalano J.G., Deaton D.N., Hassell A.M., Long S.T., Miller A.B., Miller L.R., Shewchuk L.M., Wells-Knecht K.J., Willard Jr. D.H., and Wright L.L. Potent and selective P2-P3 ketoamide inhibitors of cathepsin K with good pharmacokinetic properties via favorable P1′, P1, and/or P3 substitutions. Bioorg Med Chem Lett. 14 (2004) 4897-4902
265. Altmann E., Cowan-Jacob S.W., and Missbach M. Novel purine nitrile derived inhibitors of the cysteine protease cathepsin K. J. Med. Chem. 47 (2004) 5833-5836
266. Barrett D.G., Deaton D.N., Hassell A.M., McFadyen R.B., Miller A.B., Miller L.R., Payne J.A., Shewchuk L.M., Willard Jr. D.H., and Wright L.L. Acyclic cyanamide-based inhibitors of cathepsin K. Bioorg. Med. Chem. Lett. 15 (2005) 3039-3043
267. Barrett D.G., Boncek V.M., Catalano J.G., Deaton D.N., Hassell A.M., Jurgensen C.H., Long S.T., McFadyen R.B., Miller A.B., Miller L.R., Payne J.A., Ray J.A., Samano V., Shewchuk L.M., Tavares F.X., Wells-Knecht K.J., Willard Jr. D.H., Wright L.L., and Zhou H.Q. P2-P3 conformationally constrained ketoamide-based inhibitors of cathepsin K. Bioorg. Med. Chem. Lett. 15 (2005) 3540-3546
268. Adkison K.K., Barrett D.G., Deaton D.N., Gampe R.T., Hassell A.M., Long S.T., McFadyen R.B., Miller A.B., Miller L.R., Payne J.A., Shewchuk L.M., Wells-Knecht K.J., Willard Jr. D.H., and Wright L.L. Semicarbazone-based inhibitors of cathepsin K, are they prodrugs for aldehyde inhibitors?. Bioorg. Med. Chem. Lett. 16 (2006) 978-983
269. Barrett D.G., Catalano J.G., Deaton D.N., Hassell A.M., Long S.T., Miller A.B., Miller L.R., Ray J.A., Samano V., Shewchuk L.M., Wells-Knecht K.J., Willard Jr. D.H., and Wright L.L. Novel, potent P2-P3 pyrrolidine derivatives of ketoamide-based cathepsin K inhibitors. Bioorg. Med. Chem. Lett. 16 (2006) 1735-1739
270. Li C.S., Deschenes D., Desmarais S., Falgueyret J.P., Gauthier J.Y., Kimmel D.B., Leger S., Masse F., McGrath M.E., McKay D.J., Percival M.D., Riendeau D., Rodan S.B., Therien M., Truong V.L., Wesolowski G., Zamboni R., and Black W.C. Identification of a potent and selective non-basic cathepsin K inhibitor. Bioorg. Med. Chem. Lett. 16 (2006) 1985-1989
271. Ferreras M., Felbor U., Lenhard T., Olsen B.R., and Delaisse J. Generation and degradation of human endostatin proteins by various proteinases. FEBS Lett. 486 (2000) 247-251
272. Hou W.S., Li Z., Buttner F.H., Bartnik E., and Bromme D. Cleavage site specificity of cathepsin K toward cartilage proteoglycans and protease complex formation. Biol. Chem. 384 (2003) 891-897
273. Gosalia D.N., Salisbury C.M., Ellman J.A., and Diamond S.L. High throughput substrate specificity profiling of serine and cysteine proteases using solution-phase fluorogenic peptide microarrays. Mol. Cell. Proteomics 4 (2005) 626-636
274. Segel I.H. Enzyme Kinetics. 3rd edition (1975), John Wiley and Sons, Toronto
275. Brage M., Abrahamson M., Lindstrom V., Grubb A., and Lerner U.H. Different cysteine proteinases involved in bone resorption and osteoclast formation. Calcif. Tissue Int 76 (2005) 439-447
276. Lenarcic B., Krizaj I., Zunec P., and Turk V. Differences in specificity for the interactions of stefins A, B and D with cysteine proteinases. FEBS Lett. 395 (1996) 113-118
277. Abrahamson M., Mason R.W., Hansson H., Buttle D.J., Grubb A., and Ohlsson K. Human cystatin C. role of the N-terminal segment in the inhibition of human cysteine proteinases and in its inactivation by leucocyte elastase. Biochem. J. 273 (1991) 621-626
278. Salvesen G., Parkes C., Abrahamson M., Grubb A., and Barrett A.J. Human low-Mr kininogen contains three copies of a cystatin sequence that are divergent in structure and in inhibitory activity for cysteine proteinases. Biochem. J. 234 (1986) 429-434