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Volumn 57, Issue 7, 2005, Pages 973-993

The role of cathepsins in osteoporosis and arthritis: Rationale for the design of new therapeutics

Author keywords

Arthritis; Cathepsin K; Cathepsin S; Cysteine protease inhibitors; Cysteine proteases; Osteoporosis

Indexed keywords

BODY FLUIDS; DRUG PRODUCTS; ENZYMES; IMMUNOLOGY; MUSCULOSKELETAL SYSTEM;

EID: 18944365919     PISSN: 0169409X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.addr.2004.12.013     Document Type: Review
Times cited : (270)

References (171)
  • 1
    • 0035691325 scopus 로고    scopus 로고
    • Osteoporosis: Pathophysiology and non-pharmacological management
    • G.R. Mundy Osteoporosis: pathophysiology and non-pharmacological management Best Pract. Res., Clin. Rheumatol. 15 2001 727 745
    • (2001) Best Pract. Res., Clin. Rheumatol. , vol.15 , pp. 727-745
    • Mundy, G.R.1
  • 3
    • 0029854239 scopus 로고    scopus 로고
    • European and North American experience with HRT for the prevention of osteoporosis
    • E.F. Eriksen, M. Kassem, and B. Langdahl European and North American experience with HRT for the prevention of osteoporosis Bone 19 1996 179S 183S
    • (1996) Bone , vol.19
    • Eriksen, E.F.1    Kassem, M.2    Langdahl, B.3
  • 4
    • 3543020308 scopus 로고    scopus 로고
    • Rheumatoid arthritis: Symptoms, diagnosis, and management
    • L. Martin Rheumatoid arthritis: symptoms, diagnosis, and management Nurs. Times 100 2004 40 44
    • (2004) Nurs. Times , vol.100 , pp. 40-44
    • Martin, L.1
  • 5
    • 84861808622 scopus 로고    scopus 로고
    • Epidemiology and genetics of rheumatoid arthritis
    • A.J. Silman, and J.E. Pearson Epidemiology and genetics of rheumatoid arthritis Arthritis Res. 4 Suppl. 3 2002 S265 S272
    • (2002) Arthritis Res. , vol.4 , Issue.3 SUPPL.
    • Silman, A.J.1    Pearson, J.E.2
  • 6
    • 1042267249 scopus 로고    scopus 로고
    • Osteoarthritis: Is it a disease of cartilage or of bone?
    • D.T. Felson, and T. Neogi Osteoarthritis: is it a disease of cartilage or of bone? Arthritis Rheum. 50 2004 341 344
    • (2004) Arthritis Rheum. , vol.50 , pp. 341-344
    • Felson, D.T.1    Neogi, T.2
  • 8
    • 6044274282 scopus 로고    scopus 로고
    • Coxibs and cardiovascular disease
    • G.A. Fitzgerald Coxibs and cardiovascular disease N. Engl. J. Med. 351 2004 1709 1711
    • (2004) N. Engl. J. Med. , vol.351 , pp. 1709-1711
    • Fitzgerald, G.A.1
  • 9
    • 0142061680 scopus 로고    scopus 로고
    • Dmard use in early rheumatoid arthritis. Lessons from observations in patients with established disease
    • D. Aletaha, and J.S. Smolen Dmard use in early rheumatoid arthritis. Lessons from observations in patients with established disease Clin. Exp. Rheumatol. 21 2003 S169 S173
    • (2003) Clin. Exp. Rheumatol. , vol.21
    • Aletaha, D.1    Smolen, J.S.2
  • 10
    • 0142124931 scopus 로고    scopus 로고
    • Role of biologics in early arthritis
    • P. Emery, and Y. Seto Role of biologics in early arthritis Clin. Exp. Rheumatol. 21 2003 S191 S194
    • (2003) Clin. Exp. Rheumatol. , vol.21
    • Emery, P.1    Seto, Y.2
  • 11
    • 0142029665 scopus 로고    scopus 로고
    • Disease-modifying anti-rheumatic drug therapy and structural damage in early rheumatoid arthritis
    • R.H. Mullan, and B. Bresnihan Disease-modifying anti-rheumatic drug therapy and structural damage in early rheumatoid arthritis Clin. Exp. Rheumatol. 21 2003 S158 S164
    • (2003) Clin. Exp. Rheumatol. , vol.21
    • Mullan, R.H.1    Bresnihan, B.2
  • 13
    • 0029809357 scopus 로고    scopus 로고
    • Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency
    • B.D. Gelb, G.P. Shi, H.A. Chapman, and R.J. Desnick Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency Science 273 1996 1236 1238
    • (1996) Science , vol.273 , pp. 1236-1238
    • Gelb, B.D.1    Shi, G.P.2    Chapman, H.A.3    Desnick, R.J.4
  • 15
    • 0031659890 scopus 로고    scopus 로고
    • Cysteine proteinases and matrix metalloproteinases play distinct roles in the subosteoclastic resorption zone
    • V. Everts, J.M. Delaisse, W. Korper, and W. Beertsen Cysteine proteinases and matrix metalloproteinases play distinct roles in the subosteoclastic resorption zone J. Bone Miner. Res. 13 1998 1420 1430
    • (1998) J. Bone Miner. Res. , vol.13 , pp. 1420-1430
    • Everts, V.1    Delaisse, J.M.2    Korper, W.3    Beertsen, W.4
  • 17
    • 0026507880 scopus 로고
    • Proteoglycans: Many forms and many functions
    • T.E. Hardingham, and A.J. Fosang Proteoglycans: many forms and many functions FASEB J. 6 1992 861 870
    • (1992) FASEB J. , vol.6 , pp. 861-870
    • Hardingham, T.E.1    Fosang, A.J.2
  • 19
    • 0026091412 scopus 로고
    • Joint destruction in arthritis: Metalloproteinases in the spotlight
    • C. Brinckerhoff Joint destruction in arthritis: metalloproteinases in the spotlight Arthritis Rheum. 34 1991 1073 1075
    • (1991) Arthritis Rheum. , vol.34 , pp. 1073-1075
    • Brinckerhoff, C.1
  • 21
    • 0027997899 scopus 로고
    • Using inhibitors of metalloproteinases to treat arthritis. Easier said than done?
    • M.P. Vincenti, I.M. Clark, and C.E. Brinckerhoff Using inhibitors of metalloproteinases to treat arthritis. Easier said than done? Arthritis Rheum. 37 1994 1115 1126
    • (1994) Arthritis Rheum. , vol.37 , pp. 1115-1126
    • Vincenti, M.P.1    Clark, I.M.2    Brinckerhoff, C.E.3
  • 22
    • 0031972206 scopus 로고    scopus 로고
    • Matrix metalloproteinases, IL-6, and nitric oxide in rat antigen-induced arthritis
    • K. Mentzel, and R. Brauer Matrix metalloproteinases, IL-6, and nitric oxide in rat antigen-induced arthritis Clin. Exp. Rheumatol. 16 1998 269 276
    • (1998) Clin. Exp. Rheumatol. , vol.16 , pp. 269-276
    • Mentzel, K.1    Brauer, R.2
  • 23
    • 0030868574 scopus 로고    scopus 로고
    • Collagenase-3 (matrix metalloprotease 13) is preferentially localized in the deep layer of human arthritic cartilage in situ: In vitro mimicking effect by transforming growth factor beta
    • F. Moldovan, J.P. Pelletier, J. Hambor, J.M. Cloutier, and J. Martel-Pelletier Collagenase-3 (matrix metalloprotease 13) is preferentially localized in the deep layer of human arthritic cartilage in situ: in vitro mimicking effect by transforming growth factor beta Arthritis Rheum. 40 1997 1653 1661
    • (1997) Arthritis Rheum. , vol.40 , pp. 1653-1661
    • Moldovan, F.1    Pelletier, J.P.2    Hambor, J.3    Cloutier, J.M.4    Martel-Pelletier, J.5
  • 27
    • 0035375717 scopus 로고    scopus 로고
    • Induction of collagenase-2 (matrix metalloproteinase-8) gene expression by interleukin-1beta in human gingival fibroblasts
    • M. Abe, K. Kawamoto, H. Okamoto, and N. Horiuchi Induction of collagenase-2 (matrix metalloproteinase-8) gene expression by interleukin-1beta in human gingival fibroblasts J. Periodontal Res. 36 2001 153 159
    • (2001) J. Periodontal Res. , vol.36 , pp. 153-159
    • Abe, M.1    Kawamoto, K.2    Okamoto, H.3    Horiuchi, N.4
  • 29
    • 0015984017 scopus 로고
    • Cathepsin b1. A lysosomal enzyme that degrades native collagen
    • M.C. Burleigh, A.J. Barrett, and G.S. Lazarus Cathepsin b1. A lysosomal enzyme that degrades native collagen Biochem. J. 137 1974 387 398
    • (1974) Biochem. J. , vol.137 , pp. 387-398
    • Burleigh, M.C.1    Barrett, A.J.2    Lazarus, G.S.3
  • 30
    • 0020080258 scopus 로고
    • Action of rat liver cathepsin l on collagen and other substrates
    • H. Kirschke, A.A. Kembhavi, P. Bohley, and A.J. Barrett Action of rat liver cathepsin l on collagen and other substrates Biochem. J. 201 1982 367 372
    • (1982) Biochem. J. , vol.201 , pp. 367-372
    • Kirschke, H.1    Kembhavi, A.A.2    Bohley, P.3    Barrett, A.J.4
  • 32
    • 0032080113 scopus 로고    scopus 로고
    • Human cathepsin K cleaves native type I and II collagens at the N-terminal end of the triple helix
    • W. Kafienah, D. Bromme, D.J. Buttle, L.J. Croucher, and A.P. Hollander 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
    • (1998) Biochem. J. , vol.331 , pp. 727-732
    • Kafienah, W.1    Bromme, D.2    Buttle, D.J.3    Croucher, L.J.4    Hollander, A.P.5
  • 33
    • 0023802130 scopus 로고
    • Cartilage proteoglycans. Assembly with hyaluronate and link protein as studied by electron microscopy
    • M. Morgelin, M. Paulsson, T.E. Hardingham, D. Heinegard, and J. Engel Cartilage proteoglycans. Assembly with hyaluronate and link protein as studied by electron microscopy Biochem. J. 253 1988 175 185
    • (1988) Biochem. J. , vol.253 , pp. 175-185
    • Morgelin, M.1    Paulsson, M.2    Hardingham, T.E.3    Heinegard, D.4    Engel, J.5
  • 34
    • 1842365544 scopus 로고    scopus 로고
    • Degradation of type ii collagen, but not proteoglycan, correlates with matrix metalloproteinase activity in cartilage explant cultures
    • L.D. Kozaci, D.J. Buttle, and A.P. Hollander Degradation of type ii collagen, but not proteoglycan, correlates with matrix metalloproteinase activity in cartilage explant cultures Arthritis Rheum. 40 1997 164 174
    • (1997) Arthritis Rheum. , vol.40 , pp. 164-174
    • Kozaci, L.D.1    Buttle, D.J.2    Hollander, A.P.3
  • 35
  • 40
    • 0032211766 scopus 로고    scopus 로고
    • Cathepsin b: An alternative protease for the generation of an aggrecan 'metalloproteinase' cleavage neoepitope
    • J.S. Mort, M.C. Magny, and E.R. Lee Cathepsin b: an alternative protease for the generation of an aggrecan 'metalloproteinase' cleavage neoepitope Biochem. J. 335 1998 491 494
    • (1998) Biochem. J. , vol.335 , pp. 491-494
    • Mort, J.S.1    Magny, M.C.2    Lee, E.R.3
  • 41
    • 0025269177 scopus 로고
    • Cartilage proteoglycan aggregate is degraded more extensively by cathepsin L than by cathepsin B
    • Q. Nguyen, J.S. Mort, and P.J. Roughley Cartilage proteoglycan aggregate is degraded more extensively by cathepsin L than by cathepsin B Biochem. J. 266 1990 569 573
    • (1990) Biochem. J. , vol.266 , pp. 569-573
    • Nguyen, Q.1    Mort, J.S.2    Roughley, P.J.3
  • 42
    • 0025821115 scopus 로고
    • Link protein as a monitor in situ of endogenous proteolysis in adult human articular cartilage
    • Q. Nguyen, J. Liu, P.J. Roughley, and J.S. Mort Link protein as a monitor in situ of endogenous proteolysis in adult human articular cartilage Biochem. J. 278 1991 143 147
    • (1991) Biochem. J. , vol.278 , pp. 143-147
    • Nguyen, Q.1    Liu, J.2    Roughley, P.J.3    Mort, J.S.4
  • 43
    • 0038486755 scopus 로고    scopus 로고
    • Cleavage site specificity of cathepsin K toward cartilage proteoglycans and protease complex formation
    • W.S. Hou, Z. Li, F.H. Buttner, E. Bartnik, and D. Bromme Cleavage site specificity of cathepsin K toward cartilage proteoglycans and protease complex formation Biol. Chem. 384 2003 891 897
    • (2003) Biol. Chem. , vol.384 , pp. 891-897
    • Hou, W.S.1    Li, Z.2    Buttner, F.H.3    Bartnik, E.4    Bromme, D.5
  • 44
    • 0036882393 scopus 로고    scopus 로고
    • Human and parasitic papain-like cysteine proteases: Their role in physiology and pathology and recent developments in inhibitor design
    • F. Lecaille, J. Kaleta, and D. Bromme 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
    • (2002) Chem. Rev. , vol.102 , pp. 4459-4488
    • Lecaille, F.1    Kaleta, J.2    Bromme, D.3
  • 47
    • 0035801514 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: Facts and opportunities
    • V. Turk, B. Turk, and D. Turk Lysosomal cysteine proteases: facts and opportunities EMBO J. 20 2001 4629 4633
    • (2001) EMBO J. , vol.20 , pp. 4629-4633
    • Turk, V.1    Turk, B.2    Turk, D.3
  • 48
    • 0033695299 scopus 로고    scopus 로고
    • Proteolysis in MHC class II antigen presentation: Who's in charge?
    • J.A. Villadangos, and H.L. Ploegh Proteolysis in MHC class II antigen presentation: who's in charge? Immunity 12 2000 233 239
    • (2000) Immunity , vol.12 , pp. 233-239
    • Villadangos, J.A.1    Ploegh, H.L.2
  • 49
    • 0037805704 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases regulate antigen presentation
    • K. Honey, and A.Y. Rudensky Lysosomal cysteine proteases regulate antigen presentation Nat. Rev., Immunol. 3 2003 472 482
    • (2003) Nat. Rev., Immunol. , vol.3 , pp. 472-482
    • Honey, K.1    Rudensky, A.Y.2
  • 50
    • 0034041529 scopus 로고    scopus 로고
    • Cathepsin K and the design of inhibitors of cathepsin K
    • D.S. Yamashita, and R.A. Dodds Cathepsin K and the design of inhibitors of cathepsin K Curr. Pharm. Des. 6 2000 1 24
    • (2000) Curr. Pharm. Des. , vol.6 , pp. 1-24
    • Yamashita, D.S.1    Dodds, R.A.2
  • 54
    • 0030028779 scopus 로고    scopus 로고
    • Invariant chain structure and MHC class II function
    • P. Cresswell Invariant chain structure and MHC class II function Cell 84 1996 505 507
    • (1996) Cell , vol.84 , pp. 505-507
    • Cresswell, P.1
  • 55
    • 0029931108 scopus 로고    scopus 로고
    • Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading
    • R.J. Riese, P. Wolf, D. Bromme, L.R. Natkin, J.A. Villadangos, H.L. Ploegh, and H.A. Chapman Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading Immunity 4 1996 357 366
    • (1996) Immunity , vol.4 , pp. 357-366
    • Riese, R.J.1    Wolf, P.2    Bromme, D.3    Natkin, L.R.4    Villadangos, J.A.5    Ploegh, H.L.6    Chapman, H.A.7
  • 61
    • 0026630108 scopus 로고
    • Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease
    • G.P. Shi, J.S. Munger, J.P. Meara, D.H. Rich, and H.A. Chapman Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease J. Biol. Chem. 267 1992 7258 7262
    • (1992) J. Biol. Chem. , vol.267 , pp. 7258-7262
    • Shi, G.P.1    Munger, J.S.2    Meara, J.P.3    Rich, D.H.4    Chapman, H.A.5
  • 62
    • 0034599498 scopus 로고    scopus 로고
    • Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages
    • G.P. Shi, R.A. Bryant, R. Riese, S. Verhelst, C. Driessen, Z. Li, D. Bromme, H.L. Ploegh, and H.A. Chapman Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages J. Exp. Med. 191 2000 1177 1186
    • (2000) J. Exp. Med. , vol.191 , pp. 1177-1186
    • Shi, G.P.1    Bryant, R.A.2    Riese, R.3    Verhelst, S.4    Driessen, C.5    Li, Z.6    Bromme, D.7    Ploegh, H.L.8    Chapman, H.A.9
  • 63
    • 0032832150 scopus 로고    scopus 로고
    • Dendritic cells: The driving force behind autoimmunity in rheumatoid arthritis?
    • A.R. Pettit, and R. Thomas Dendritic cells: the driving force behind autoimmunity in rheumatoid arthritis? Immunol. Cell Biol. 77 1999 420 427
    • (1999) Immunol. Cell Biol. , vol.77 , pp. 420-427
    • Pettit, A.R.1    Thomas, R.2
  • 64
    • 0022970858 scopus 로고
    • Cathepsin S. The cysteine proteinase from bovine lymphoid tissue is distinct from cathepsin l (ec 3.4.22.15)
    • H. Kirschke, I. Schmidt, and B. Wiederanders 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
    • (1986) Biochem. J. , vol.240 , pp. 455-459
    • Kirschke, H.1    Schmidt, I.2    Wiederanders, B.3
  • 66
    • 0029007093 scopus 로고
    • Pericellular mobilization of the tissue-destructive cysteine proteinases, cathepsins B, L, and S, by human monocyte-derived macrophages
    • V.Y. Reddy, Q.Y. Zhang, and S.J. Weiss Pericellular mobilization of the tissue-destructive cysteine proteinases, cathepsins B, L, and S, by human monocyte-derived macrophages Proc. Natl. Acad. Sci. U. S. A. 92 1995 3849 3853
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 3849-3853
    • Reddy, V.Y.1    Zhang, Q.Y.2    Weiss, S.J.3
  • 67
    • 0029091894 scopus 로고
    • Control of matrix synthesis in isolated bovine chondrocytes by extracellular and intracellular pH
    • R.J. Wilkins, and A.C. Hall Control of matrix synthesis in isolated bovine chondrocytes by extracellular and intracellular pH J. Cell. Physiol. 164 1995 474 481
    • (1995) J. Cell. Physiol. , vol.164 , pp. 474-481
    • Wilkins, R.J.1    Hall, A.C.2
  • 70
    • 0030026637 scopus 로고    scopus 로고
    • Human cathepsin O2, a matrix protein-degrading cysteine protease expressed in osteoclasts. Functional expression of human cathepsin O2 in f and characterization of the enzyme
    • D. Brömme, K. Okamoto, B.B. Wang, and S. Biroc Human cathepsin O2, a matrix protein-degrading cysteine protease expressed in osteoclasts. Functional expression of human cathepsin O2 in f and characterization of the enzyme J. Biol. Chem. 271 1996 2126 2132
    • (1996) J. Biol. Chem. , vol.271 , pp. 2126-2132
    • Brömme, D.1    Okamoto, K.2    Wang, B.B.3    Biroc, S.4
  • 73
    • 0029310512 scopus 로고
    • Human cathepsin O2, a novel cysteine protease highly expressed in osteoclastomas and ovary molecular cloning, sequencing and tissue distribution
    • D. Bromme, and K. Okamoto 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
    • (1995) Biol. Chem. Hoppe-Seyler , vol.376 , pp. 379-384
    • Bromme, D.1    Okamoto, K.2
  • 76
    • 0032145836 scopus 로고    scopus 로고
    • Expression of the elastolytic cathepsins s and k in human atheroma and regulation of their production in smooth muscle cells
    • G.K. Sukhova, G. Shi, P.D.I. Simon, H.A. Chapman, and P. Libby 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
    • (1998) J. Clin. Invest. , vol.102 , pp. 576-583
    • Sukhova, G.K.1    Shi, G.2    Simon, P.D.I.3    Chapman, H.A.4    Libby, P.5
  • 78
    • 0023752014 scopus 로고
    • Effects of proteinase inhibitors leupeptin and e-64 on osteoclastic bone resorption
    • V. Everts, W. Beertsen, and R. Schroder Effects of proteinase inhibitors leupeptin and e-64 on osteoclastic bone resorption Calcif. Tissue Int. 43 1988 172 178
    • (1988) Calcif. Tissue Int. , vol.43 , pp. 172-178
    • Everts, V.1    Beertsen, W.2    Schroder, R.3
  • 81
    • 0345465541 scopus 로고
    • E. Rubenstein D.D. Federman Scientific American, Inc. New York
    • S.M. Krane, and L. Simon E. Rubenstein D.D. Federman Scientific American Medicine 1994 Scientific American, Inc. New York 1 26
    • (1994) Scientific American Medicine , pp. 1-26
    • Krane, S.M.1    Simon, L.2
  • 82
    • 0021991222 scopus 로고
    • Phagocytosis of bone collagen by osteoclasts in two cases of pycnodysostosis
    • V. Everts, D.C. Aronson, and W. Beertsen Phagocytosis of bone collagen by osteoclasts in two cases of pycnodysostosis Calcif. Tissue Int. 37 1985 25 31
    • (1985) Calcif. Tissue Int. , vol.37 , pp. 25-31
    • Everts, V.1    Aronson, D.C.2    Beertsen, W.3
  • 83
  • 89
    • 0037047275 scopus 로고    scopus 로고
    • Collagenase activity of cathepsin K depends on complex formation with chondroitin sulfate
    • Z. Li, W.S. Hou, C.R. Escalante-Torres, B.D. Gelb, and D. Bromme Collagenase activity of cathepsin K depends on complex formation with chondroitin sulfate J. Biol. Chem. 277 2002 28669 28676
    • (2002) J. Biol. Chem. , vol.277 , pp. 28669-28676
    • Li, Z.1    Hou, W.S.2    Escalante-Torres, C.R.3    Gelb, B.D.4    Bromme, D.5
  • 90
    • 0034711762 scopus 로고    scopus 로고
    • Collagenolytic activity of cathepsin K is specifically modulated by cartilage-resident chondroitin sulfates
    • Z. Li, W.S. Hou, and D. Bromme Collagenolytic activity of cathepsin K is specifically modulated by cartilage-resident chondroitin sulfates Biochemistry 39 2000 529 536
    • (2000) Biochemistry , vol.39 , pp. 529-536
    • Li, Z.1    Hou, W.S.2    Bromme, D.3
  • 92
    • 0020198689 scopus 로고
    • Current problems in mechanistic studies of serine and cysteine proteinases
    • L. Polgar, and P. Halasz Current problems in mechanistic studies of serine and cysteine proteinases Biochem. J. 207 1982 1 10
    • (1982) Biochem. J. , vol.207 , pp. 1-10
    • Polgar, L.1    Halasz, P.2
  • 94
    • 0027296221 scopus 로고
    • The effects of fluoromethyl ketone inhibitors of cathepsin B on adjuvant-induced arthritis
    • R.E. Esser, L.M. Watts, R.A. Angelo, L.P. Thornburg, J.J. Prior, and J.T. Palmer The effects of fluoromethyl ketone inhibitors of cathepsin B on adjuvant-induced arthritis J. Rheumatol. 20 1993 1176 1183
    • (1993) J. Rheumatol. , vol.20 , pp. 1176-1183
    • Esser, R.E.1    Watts, L.M.2    Angelo, R.A.3    Thornburg, L.P.4    Prior, J.J.5    Palmer, J.T.6
  • 95
    • 2442690116 scopus 로고    scopus 로고
    • Cathepsin K inhibitor-polymer conjugates: Potential drugs for the treatment of osteoporosis and rheumatoid arthritis
    • D. Wang, W. Li, M. Pechar, P. Kopečkova, D. Brömme, and J. Kopeček Cathepsin K inhibitor-polymer conjugates: potential drugs for the treatment of osteoporosis and rheumatoid arthritis Int. J. Pharm. 277 2004 73 79
    • (2004) Int. J. Pharm. , vol.277 , pp. 73-79
    • Wang, D.1    Li, W.2    Pechar, M.3    Kopečkova, P.4    Brömme, D.5    Kopeček, J.6
  • 96
    • 0037118691 scopus 로고    scopus 로고
    • Inhibition of cathepsin K with lysosomotropic macromolecular inhibitors
    • D. Wang, M. Pechar, W. Li, P. Kopečkova, D. Brömme, and J. Kopeček Inhibition of cathepsin K with lysosomotropic macromolecular inhibitors Biochemistry 41 2002 8849 8859
    • (2002) Biochemistry , vol.41 , pp. 8849-8859
    • Wang, D.1    Pechar, M.2    Li, W.3    Kopečkova, P.4    Brömme, D.5    Kopeček, J.6
  • 98
    • 0035986223 scopus 로고    scopus 로고
    • Thiol-dependent cathepsins: Pathophysiological implications and recent advances in inhibitor design
    • D. Bromme, and J. Kaleta Thiol-dependent cathepsins: pathophysiological implications and recent advances in inhibitor design Curr. Pharm. Des. 8 2002 1639 1658
    • (2002) Curr. Pharm. Des. , vol.8 , pp. 1639-1658
    • Bromme, D.1    Kaleta, J.2
  • 100
    • 0034628448 scopus 로고    scopus 로고
    • Protease inhibitors: Current status and future prospects
    • D. Leung, G. Abbenante, and D.P. Fairlie Protease inhibitors: current status and future prospects J. Med. Chem. 43 2000 305 341
    • (2000) J. Med. Chem. , vol.43 , pp. 305-341
    • Leung, D.1    Abbenante, G.2    Fairlie, D.P.3
  • 101
    • 0343433408 scopus 로고    scopus 로고
    • Cysteine proteases and their inhibitors
    • H.H. Otto, and T. Schirmeister Cysteine proteases and their inhibitors Chem. Rev. 97 1997 133 171
    • (1997) Chem. Rev. , vol.97 , pp. 133-171
    • Otto, H.H.1    Schirmeister, T.2
  • 112
    • 4744350185 scopus 로고    scopus 로고
    • Ketoamide-based inhibitors of cysteine protease, cathepsin K: P3 modifications
    • F.X. Tavares, D.N. Deaton, L.R. Miller, and L.L. Wright Ketoamide-based inhibitors of cysteine protease, cathepsin K: P3 modifications J. Med. Chem. 47 2004 5057 5068
    • (2004) J. Med. Chem. , vol.47 , pp. 5057-5068
    • Tavares, F.X.1    Deaton, D.N.2    Miller, L.R.3    Wright, L.L.4
  • 116
    • 18944363962 scopus 로고    scopus 로고
    • Medivir UK Ltd/peptimmune US, EP 1 413 580 A1 (2004).
    • M. Quibell, S. Taylor, Medivir UK Ltd/peptimmune US, EP 1 413 580 A1 (2004).
    • Quibell, M.1    Taylor, S.2
  • 119
    • 2142645950 scopus 로고    scopus 로고
    • An update on bisphosphonates
    • S.B. Cohen An update on bisphosphonates Curr. Rheumatol. Rep. 6 2004 59 65
    • (2004) Curr. Rheumatol. Rep. , vol.6 , pp. 59-65
    • Cohen, S.B.1
  • 121
    • 0033385251 scopus 로고    scopus 로고
    • The impact of estrogen replacement therapy and raloxifene on osteoporosis, cardiovascular disease, and gynecologic cancers
    • E.M. Umland, C. Rinaldi, S.M. Parks, and E.G. Boyce The impact of estrogen replacement therapy and raloxifene on osteoporosis, cardiovascular disease, and gynecologic cancers Ann. Pharmacother. 33 1999 1315 1328
    • (1999) Ann. Pharmacother. , vol.33 , pp. 1315-1328
    • Umland, E.M.1    Rinaldi, C.2    Parks, S.M.3    Boyce, E.G.4
  • 122
    • 0031803314 scopus 로고    scopus 로고
    • The roles of calcium and vitamin d in the prevention of osteoporosis
    • I.R. Reid The roles of calcium and vitamin d in the prevention of osteoporosis Endocrinol. Metab. Clin. N. Am. 27 1998 389 398
    • (1998) Endocrinol. Metab. Clin. N. Am. , vol.27 , pp. 389-398
    • Reid, I.R.1
  • 123
    • 0036679570 scopus 로고    scopus 로고
    • Meta-analyses of therapies for postmenopausal osteoporosis: VI. Meta-analysis of calcitonin for the treatment of postmenopausal osteoporosis
    • A. Cranney, P. Tugwell, N. Zytaruk, V. Robinson, B. Weaver, B. Shea, G. Wells, J. Adachi, L. Waldegger, and G. Guyatt Meta-analyses of therapies for postmenopausal osteoporosis: VI. Meta-analysis of calcitonin for the treatment of postmenopausal osteoporosis Endocr. Rev. 23 2002 540 551
    • (2002) Endocr. Rev. , vol.23 , pp. 540-551
    • Cranney, A.1    Tugwell, P.2    Zytaruk, N.3    Robinson, V.4    Weaver, B.5    Shea, B.6    Wells, G.7    Adachi, J.8    Waldegger, L.9    Guyatt, G.10
  • 125
    • 0035985787 scopus 로고    scopus 로고
    • Molecular action of methotrexate in inflammatory diseases
    • E.S. Chan, and B.N. Cronstein Molecular action of methotrexate in inflammatory diseases Arthritis Res. 4 2002 266 273
    • (2002) Arthritis Res. , vol.4 , pp. 266-273
    • Chan, E.S.1    Cronstein, B.N.2
  • 126
    • 0025021611 scopus 로고
    • The effect of gold sodium thiomalate and auranofin on lipopolysaccharide-induced interleukin-1 production by blood monocytes in vitro: Variation in healthy subjects and patients with arthritis
    • V.A. Danis, A.J. Kulesz, D.S. Nelson, and P.M. Brooks The effect of gold sodium thiomalate and auranofin on lipopolysaccharide-induced interleukin-1 production by blood monocytes in vitro: variation in healthy subjects and patients with arthritis Clin. Exp. Immunol. 79 1990 335 340
    • (1990) Clin. Exp. Immunol. , vol.79 , pp. 335-340
    • Danis, V.A.1    Kulesz, A.J.2    Nelson, D.S.3    Brooks, P.M.4
  • 127
    • 0037333440 scopus 로고    scopus 로고
    • Down-regulation of the nonspecific and antigen-specific T cell cytokine response in ankylosing spondylitis during treatment with infliximab
    • J. Zou, M. Rudwaleit, J. Brandt, A. Thiel, J. Braun, and J. Sieper Down-regulation of the nonspecific and antigen-specific T cell cytokine response in ankylosing spondylitis during treatment with infliximab Arthritis Rheum. 48 2003 780 790
    • (2003) Arthritis Rheum. , vol.48 , pp. 780-790
    • Zou, J.1    Rudwaleit, M.2    Brandt, J.3    Thiel, A.4    Braun, J.5    Sieper, J.6
  • 128
    • 0033383526 scopus 로고    scopus 로고
    • Leflunomide: A review of its use in active rheumatoid arthritis
    • A. Prakash, and B. Jarvis Leflunomide: a review of its use in active rheumatoid arthritis Drugs 58 1999 1137 1164
    • (1999) Drugs , vol.58 , pp. 1137-1164
    • Prakash, A.1    Jarvis, B.2
  • 129
    • 0033764113 scopus 로고    scopus 로고
    • Leflunomide: Mode of action in the treatment of rheumatoid arthritis
    • F.C. Breedveld, and J.M. Dayer Leflunomide: mode of action in the treatment of rheumatoid arthritis Ann. Rheum. Dis. 59 2000 841 849
    • (2000) Ann. Rheum. Dis. , vol.59 , pp. 841-849
    • Breedveld, F.C.1    Dayer, J.M.2
  • 130
    • 3142705798 scopus 로고    scopus 로고
    • Molecular mechanisms of neuroprotective action of immunosuppressants- facts and hypotheses
    • B. Kaminska, K. Gaweda-Walerych, and M. Zawadzka Molecular mechanisms of neuroprotective action of immunosuppressants-facts and hypotheses J. Cell. Mol. Med. 8 2004 45 58
    • (2004) J. Cell. Mol. Med. , vol.8 , pp. 45-58
    • Kaminska, B.1    Gaweda-Walerych, K.2    Zawadzka, M.3
  • 132
    • 0023765043 scopus 로고
    • Suppression of human fibroblast proliferation by d-penicillamine and copper sulfate in vitro
    • T. Matsubara, and K. Hirohata Suppression of human fibroblast proliferation by d-penicillamine and copper sulfate in vitro Arthritis Rheum. 31 1988 964 972
    • (1988) Arthritis Rheum. , vol.31 , pp. 964-972
    • Matsubara, T.1    Hirohata, K.2
  • 133
    • 0027502211 scopus 로고
    • Mechanism of action of immunosuppressive agents
    • B.M. Frey Mechanism of action of immunosuppressive agents Ther. Umsch. 50 1993 71 76
    • (1993) Ther. Umsch. , vol.50 , pp. 71-76
    • Frey, B.M.1
  • 134
    • 0027434905 scopus 로고
    • Mechanism of action of hydroxychloroquine as an antirheumatic drug
    • R.I. Fox Mechanism of action of hydroxychloroquine as an antirheumatic drug Semin. Arthritis Rheum. 23 1993 82 91
    • (1993) Semin. Arthritis Rheum. , vol.23 , pp. 82-91
    • Fox, R.I.1
  • 135
    • 0142165030 scopus 로고    scopus 로고
    • The mechanism of action of aspirin
    • J.R. Vane, and R.M. Botting The mechanism of action of aspirin Thromb. Res. 110 2003 255 258
    • (2003) Thromb. Res. , vol.110 , pp. 255-258
    • Vane, J.R.1    Botting, R.M.2
  • 136
    • 0032737734 scopus 로고    scopus 로고
    • Specific cyclooxygenase 2 inhibitors: A new choice of nonsteroidal anti-inflammatory drug therapy
    • M. Osiri, and L.W. Moreland Specific cyclooxygenase 2 inhibitors: a new choice of nonsteroidal anti-inflammatory drug therapy Arthritis Care Res. 12 1999 351 362
    • (1999) Arthritis Care Res. , vol.12 , pp. 351-362
    • Osiri, M.1    Moreland, L.W.2
  • 137
    • 0036845148 scopus 로고    scopus 로고
    • Et tu, acetaminophen?
    • S.B. Abramson Et tu, acetaminophen? Arthritis Rheum. 46 2002 2831 2835
    • (2002) Arthritis Rheum. , vol.46 , pp. 2831-2835
    • Abramson, S.B.1
  • 140
    • 0032561376 scopus 로고    scopus 로고
    • Synthesis of peptide aldehyde derivatives as selective inhibitors of human cathepsin L and their inhibitory effect on bone resorption
    • T. Yasuma, S. Oi, N. Choh, T. Nomura, N. Furuyama, A. Nishimura, Y. Fujisawa, and T. Sohda Synthesis of peptide aldehyde derivatives as selective inhibitors of human cathepsin L and their inhibitory effect on bone resorption J. Med. Chem. 41 1998 4301 4308
    • (1998) J. Med. Chem. , vol.41 , pp. 4301-4308
    • Yasuma, T.1    Oi, S.2    Choh, N.3    Nomura, T.4    Furuyama, N.5    Nishimura, A.6    Fujisawa, Y.7    Sohda, T.8
  • 145
    • 18944396957 scopus 로고    scopus 로고
    • Novartis, Wo 01/58886 (2001).
    • Novartis, Wo 01/58886 (2001).
  • 146
    • 18944368469 scopus 로고    scopus 로고
    • BoehringerIngelheim, WO 02/20485 (2002).
    • BoehringerIngelheim, WO 02/20485 (2002).
  • 147
    • 18944372945 scopus 로고    scopus 로고
    • BoehringerIngelheim, WO 01/09110 (2001).
    • BoehringerIngelheim, WO 01/09110 (2001).
  • 148
    • 18944373695 scopus 로고    scopus 로고
    • BoehringerIngelheim, WO 01/19816 (2001).
    • BoehringerIngelheim, WO 01/19816 (2001).
  • 151
    • 18944362284 scopus 로고    scopus 로고
    • 6-substituted amino-4-oxa-1-azabicyclo 3,2,0 heptan-t-one derivatives as cysteine protease inhibitors, US 5,905,076 (1999).
    • R. Singh, N.E. Zhou, D. Guo, A. Cameron, J. Kaleta, E. Purisima, R. Menard, R.G. Micetich, 6-substituted amino-4-oxa-1-azabicyclo 3,2,0 heptan-t-one derivatives as cysteine protease inhibitors, US 5,905,076 (1999).
    • Singh, R.1    Zhou, N.E.2    Guo, D.3    Cameron, A.4    Kaleta, J.5    Purisima, E.6    Menard, R.7    Micetich, R.G.8
  • 152
  • 158
    • 0037082140 scopus 로고    scopus 로고
    • Structure-based design of specific cathepsin inhibitors and their application to protection of bone metastases of cancer cells
    • N. Katunuma, H. Tsuge, M. Nukatsuka, T. Asao, and M. Fukushima Structure-based design of specific cathepsin inhibitors and their application to protection of bone metastases of cancer cells Arch. Biochem. Biophys. 397 2002 305 311
    • (2002) Arch. Biochem. Biophys. , vol.397 , pp. 305-311
    • Katunuma, N.1    Tsuge, H.2    Nukatsuka, M.3    Asao, T.4    Fukushima, M.5
  • 159
    • 0029099619 scopus 로고
    • Vinyl sulfones as mechanism-based cysteine protease inhibitors
    • J.T. Palmer, D. Rasnick, J.L. Klaus, and D. Brömme Vinyl sulfones as mechanism-based cysteine protease inhibitors J. Med. Chem. 38 1995 3193 3196
    • (1995) J. Med. Chem. , vol.38 , pp. 3193-3196
    • Palmer, J.T.1    Rasnick, D.2    Klaus, J.L.3    Brömme, D.4
  • 160
    • 0029911570 scopus 로고    scopus 로고
    • Peptidyl vinyl sulphones: A new class of potent and selective cysteine protease inhibitors: S2p2 specificity of human cathepsin O2 in comparison with cathepsins S and L
    • D. Brömme, J.L. Klaus, K. Okamoto, D. Rasnick, and J.T. Palmer Peptidyl vinyl sulphones: a new class of potent and selective cysteine protease inhibitors: S2p2 specificity of human cathepsin O2 in comparison with cathepsins S and L Biochem. J. 315 1996 85 89
    • (1996) Biochem. J. , vol.315 , pp. 85-89
    • Brömme, D.1    Klaus, J.L.2    Okamoto, K.3    Rasnick, D.4    Palmer, J.T.5
  • 161
    • 0033058811 scopus 로고    scopus 로고
    • Cysteine protease inhibitors as chemotherapy for parasitic infections
    • J.H. McKerrow, J.C. Engel, and C.R. Caffrey Cysteine protease inhibitors as chemotherapy for parasitic infections Bioorg. Med. Chem. 7 1999 639 644
    • (1999) Bioorg. Med. Chem. , vol.7 , pp. 639-644
    • McKerrow, J.H.1    Engel, J.C.2    Caffrey, C.R.3
  • 163
    • 0028673436 scopus 로고
    • N,o-diacyl hydroxamates as selective and irreversible inhibitors of cysteine proteinases
    • D. Bromme, and H.U. Demuth N,o-diacyl hydroxamates as selective and irreversible inhibitors of cysteine proteinases Methods Enzymol. 244 1994 671 685
    • (1994) Methods Enzymol. , vol.244 , pp. 671-685
    • Bromme, D.1    Demuth, H.U.2
  • 164
    • 0037203970 scopus 로고    scopus 로고
    • Identification of potent and selective mechanism-based inhibitors of the cysteine protease cruzain using solid-phase parallel synthesis
    • L. Huang, A. Lee, and J.A. Ellman Identification of potent and selective mechanism-based inhibitors of the cysteine protease cruzain using solid-phase parallel synthesis J. Med. Chem. 45 2002 676 684
    • (2002) J. Med. Chem. , vol.45 , pp. 676-684
    • Huang, L.1    Lee, A.2    Ellman, J.A.3
  • 165
    • 0028672775 scopus 로고
    • Peptidyl diazomethanes as inhibitors of cysteine and serine proteinases
    • E. Shaw Peptidyl diazomethanes as inhibitors of cysteine and serine proteinases Methods Enzymol. 244 1994 649 656
    • (1994) Methods Enzymol. , vol.244 , pp. 649-656
    • Shaw, E.1
  • 166
    • 0028672696 scopus 로고
    • A.J. Barrett Academic Press New York
    • A. Krantz A.J. Barrett Methods Enzymol. vol. 244 1994 Academic Press New York 656 671
    • (1994) Methods Enzymol. , vol.244 , pp. 656-671
    • Krantz, A.1
  • 168
    • 0035906534 scopus 로고    scopus 로고
    • A selective cysteine protease inhibitor is non-toxic and cerebroprotective in rats undergoing transient middle cerebral artery ischemia
    • D.M. Seyfried, R. Veyna, Y. Han, K. Li, N. Tang, R.L. Betts, S. Weinsheimer, M. Chopp, and J. Anagli A selective cysteine protease inhibitor is non-toxic and cerebroprotective in rats undergoing transient middle cerebral artery ischemia Brain Res. 901 2001 94 101
    • (2001) Brain Res. , vol.901 , pp. 94-101
    • Seyfried, D.M.1    Veyna, R.2    Han, Y.3    Li, K.4    Tang, N.5    Betts, R.L.6    Weinsheimer, S.7    Chopp, M.8    Anagli, J.9
  • 169
    • 3142653664 scopus 로고    scopus 로고
    • Part ii. Synthesis and evaluation of 3-substituted-4-oxa-1-azabicyclo[3. 2.0]heptan-7-ones as cysteine protease inhibitors
    • N.E. Zhou, A.V. Reddy, J. Kaleta, R.G. Micetich, and R. Singh Part ii. Synthesis and evaluation of 3-substituted-4-oxa-1-azabicyclo[3.2.0]heptan-7-ones as cysteine protease inhibitors Arkivoc VI 2001 116 121
    • (2001) Arkivoc , vol.6 , pp. 116-121
    • Zhou, N.E.1    Reddy, A.V.2    Kaleta, J.3    Micetich, R.G.4    Singh, R.5
  • 171
    • 18944388211 scopus 로고    scopus 로고
    • Osteonecrosis of the maxilla in a patient with a history of bisphosphonate therapy
    • M.D. Melo, and G. Obeid Osteonecrosis of the maxilla in a patient with a history of bisphosphonate therapy J. Can. Dent. Assoc. 71 2005 111 113
    • (2005) J. Can. Dent. Assoc. , vol.71 , pp. 111-113
    • Melo, M.D.1    Obeid, G.2


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