The role of proteases in pathologies of the synovial joint

International Journal of Biochemistry and Cell Biology

Volumn 40, Issue 6-7, 2008, Pages 1199-1218

  Jones, Gavin C ^a   Riley, Graham P ^a   Buttle, David J ^b  

^a UNIVERSITY OF EAST ANGLIA   (United Kingdom)

^b UNIVERSITY OF SHEFFIELD   (United Kingdom)

Author keywords

Arthritis; Joint; Pathology; Protease; Tendinopathy

Indexed keywords

CATHEPSIN K; DISINTEGRIN; MATRIX METALLOPROTEINASE; PROTEINASE; THROMBOSPONDIN;

ARTHROPATHY; BONE TURNOVER; CARTILAGE CELL; CELL ACTIVATION; EXTRACELLULAR MATRIX; HOMEOSTASIS; HUMAN; HYPERPLASIA; JOINT CAPSULE; PROTEIN DEGRADATION; PROTEIN STRUCTURE; REVIEW; SYNOVIUM; TENDINITIS; UPREGULATION;

HUMANS; JOINTS; MODELS, BIOLOGICAL; PEPTIDE HYDROLASES; SYNOVIAL MEMBRANE;

EID: 43049088767     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2008.01.024     Document Type: Review

References (195)

1. Abbaszade I., Liu R.Q., Yang F., Rosenfeld S.A., Ross O.H., Link J.R., et al. Cloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS family. J. Biol. Chem. 274 (1999) 23443-23450
2. Abeles A.M., and Pillinger M.H. The role of the synovial fibroblast in rheumatoid arthritis: Cartilage destruction and the regulation of matrix metalloproteinases. Bull. NYU. Hosp. Joint Dis. 64 (2006) 20-24
3. Aimes R.T., and Quigley J.P. Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4- and 1/4-length fragments. J. Biol. Chem. 270 (1995) 5872-5876
4. Almeida P.C., Nantes I.L., Chagas J.R., Rizzi C.C., Faljoni-Alario A., Carmona E., et al. Cathepsin B activity regulation. Heparin-like glycosaminogylcans protect human cathepsin B from alkaline pH-induced inactivation. J. Biol. Chem. 276 (2001) 944-951
5. Andersen R.B., and Gormsen J. Fibrinolytic and fibrin stabilizing activity of synovial membranes. Ann. Rheum. Dis. 29 (1970) 287-293
6. Aström M., and Rausing A. Chronic Achilles tendinopathy. A survey of surgical and histopathologic findings. Clin. Orthop. 316 (1995) 151-164
7. Bader D.L., Kempson G.E., Barrett A.J., and Webb W. The effects of leucocyte elastase on the mechanical properties of adult human articular cartilage in tension. Biochim. Biophys. Acta 677 (1981) 103-108
8. Banda N.K., Kraus D., Vondracek A., Huynh L.H., Bendele A., Holers V.M., et al. Mechanisms of effects of complement inhibition in murine collagen-induced arthritis. Arthritis Rheum. 46 (2002) 3065-3075
9. Bank R.A., TeKoppele J.M., Oostingh G., Hazleman B.L., and Riley G.P. Lysylhydroxylation and non-reducible crosslinking of human supraspinatus tendon collagen: Changes with age and in chronic rotator cuff tendinitis. Ann. Rheum. Dis. 58 (1999) 35-41
10. Barilla M.L., and Carsons S.E. Fibronectin fragments and their role in inflammatory arthritis. Semin. Arthritis Rheum. 29 (2000) 252-265
11. Barrett A.J. Classification of peptidases. Methods Enzymol. 244 (1994) 1-15
12. Benito M.J., Veale D.J., FitzGerald O., van Den Berg W.B., and Bresnihan B. Synovial tissue inflammation in early and late osteoarthritis. Ann. Rheum. Dis. 64 (2005) 1263-1267
13. Benjamin M. The structure and function of tendons. In: Hazleman B., Riley G., and Speed C. (Eds). Soft tissue rheumatology (2004), Oxford University Press, New York 9-19
14. Berardi S., Lang A., Kostoulas G., Hörler D., Vilei E.M., and Baici A. Alternative messenger RNA splicing and enzyme forms of cathepsin B in human osteoarthritic cartilage and cultured chondrocytes. Arthritis Rheum. 44 (2001) 1819-1831
15. Berckmans R.J., Nieuwland R., Tak P.P., Böing A.N., Romijn F.P., Kraan M.C., et al. Cell-derived microparticles in synovial fluid from inflamed arthritic joints support coagulation exclusively via a factor VII-dependent mechanism. Arthritis Rheum. 46 (2002) 2857-2866
16. 2-terminal sequences of late-stage digest fragments. Biochemistry 38 (1999) 13928-13936
17. Black R.A., Rauch C.T., Kozlosky C.J., Peschon J.J., Slack J.L., Wolfson M.F., et al. A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells. Nature 385 (1997) 729-733
18. Blom A.B., van Lent P.L., Libregts S., Holthuysen A.E., van der Kraan P.M., van Rooijen N., et al. Crucial role of macrophages in matrix metalloproteinase-mediated cartilage destruction during experimental osteoarthritis: Involvement of matrix metalloproteinase 3. Arthritis Rheum. 56 (2007) 147-157
19. Braat E.A., Jie A.F., Ronday H.K., Beekman B., and Rijken D.C. Urokinase-mediated fibrinolysis in the synovial fluid of rheumatoid arthritis patients may be affected by the inactivation of single chain urokinase type plasminogen activator by thrombin. Ann. Rheum. Dis. 59 (2000) 315-318
20. Bradley K., North J., Saunders D., Schwaeble W., Jeziorska M., Woolley D.E., et al. Synthesis of classical pathway complement components by chondrocytes. Immunology 88 (1996) 648-656
21. Brennan F.M., Maini R.N., and Feldmann M. TNF alpha-A pivotal role in rheumatoid arthritis?. Br. J. Rheumatol. 31 (1992) 293-298
22. Brinckerhoff C.E., Suzuki K., Mitchell T.I., Oram F., Coon C.I., Palmiter R.D., et al. Rabbit procollagenase synthesized and secreted by a high-yield mammalian expression vector requires stromelysin (matrix metalloproteinase-3) for maximal activation. J. Biol. Chem. 265 (1990) 22262-22269
23. Brix K., Lemansky P., and Herzog V. Evidence for extracellularly acting cathepsins mediating thyroid hormone liberation in thyroid epithelial cells. Endocrinology 137 (1996) 1963-1974
24. Buck M.R., Karustis D.G., Day N.A., Honn K.V., and Sloane B.F. Degradation of extracellular-matrix proteins by human cathepsin B from normal and tumour tissues. Biochem. J. 282 Pt 1 (1992) 273-278
25. 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
26. Buttle D.J., Abrahamson M., Burnett D., Mort J.S., Barrett A.J., Dando P.M., et al. 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 Pt 2 (1991) 325-331
27. Buttle D.J., Handley C.J., Ilic M.Z., Saklatvala J., Murata M., and Barrett A.J. Inhibition of cartilage proteoglycan release by a specific inactivator of cathepsin B and an inhibitor of matrix metalloproteinases. Evidence for two converging pathways of chondrocyte-mediated proteoglycan degradation. Arthritis Rheum. 36 (1993) 1709-1717
28. Cal S., Arguelles J.M., Fernández P.L., and López-Otín C. Identification, characterization, and intracellular processing of ADAM-TS12, a novel human disintegrin with a complex structural organization involving multiple thrombospondin-1 repeats. J. Biol. Chem. 276 (2001) 17932-17940
29. Campbell I.K., Roughley P.J., and Mort J.S. The action of human articular-cartilage metalloproteinase on proteoglycan and link protein. Similarities between products of degradation in situ and in vitro. Biochem. J. 237 (1986) 117-122
30. Cawston T.E. Proteinases and connective tissue breakdown. Mech. Models Rheum. Arthritis (1995) 333-359
31. Cawston T.E., and Wilson A.J. Understanding the role of tissue degrading enzymes and their inhibitors in development and disease. Best Pract. Res. Clin.Rheumatol. 20 (2006) 983-1002
32. Cesarman-Maus G., and Hajjar K.A. Molecular mechanisms of fibrinolysis. Br. J. Haematol. 129 (2005) 307-321
33. Choi S.J., Kurihara N., Oba Y., and Roodman G.D. Osteoclast inhibitory peptide 2 inhibits osteoclast formation via its C-terminal fragment. J. Bone Miner. Res. 16 (2001) 1804-1811
34. Choi S.J., Reddy S.V., Devlin R.D., Menaa C., Chung H., Boyce B.F., et al. Identification of human asparaginyl endopeptidase (legumain) as an inhibitor of osteoclast formation and bone resorption. J. Biol. Chem. 274 (1999) 27747-27753
35. Cirino G., Napoli C., Bucci M., and Cicala C. Inflammation-coagulation network: Are serine protease receptors the knot?. Trends Pharmacol. Sci. 21 (2000) 170-172
36. Corps A.N., Harrall R.L., Curry V.A., Fenwick S.A., Hazleman B.L., and Riley G.P. Ciprofloxacin enhances the stimulation of matrix metalloproteinase 3 expression by interleukin-1beta in human tendon-derived cells. A potential mechanism of fluoroquinolone-induced tendinopathy. Arthritis Rheum. 46 (2002) 3034-3040
37. Dallas S.L., Rosser J.L., Mundy G.R., and Bonewald L.F. Proteolysis of latent transforming growth factor-beta (TGF-beta)-binding protein-1 by osteoclasts. A cellular mechanism for release of TGF-beta from bone matrix. J. Biol. Chem. 277 (2002) 21352-21360
38. Day A.J. The structure and regulation of hyaluronan-binding proteins. Biochem. Soc. Trans. 27 (1999) 115-121
39. Dayer J.M. The pivotal role of interleukin-1 in the clinical manifestations of rheumatoid arthritis. Rheumatology (Oxford) 42 Suppl. 2 (2003) ii3-ii10
40. Dehrmann F.M., Coetzer T.H., Pike R.N., and Dennison C. Mature cathepsin L is substantially active in the ionic milieu of the extracellular medium. Arch. Biochem. Biophys. 324 (1995) 93-98
41. Delaissé J.M., Andersen T.L., Engsig M.T., Henriksen K., Troen T., and Blavier L. Matrix metalloproteinases (MMP) and cathepsin K contribute differently to osteoclastic activities. Microsc. Res. Technol. 61 (2003) 504-513
42. Deleuran B.W., Chu C.Q., Field M., Brennan F.M., Katsikis P., Feldmann M., et al. Localization of interleukin-1 alpha, type 1 interleukin-1 receptor and interleukin-1 receptor antagonist in the synovial membrane and cartilage/pannus junction in rheumatoid arthritis. Br. J. Rheumatol. 31 (1992) 801-809
43. Deryugina E.I., Ratnikov B.I., Postnova T.I., Rozanov D.V., and Strongin A.Y. Processing of integrin alpha(v) subunit by membrane type 1 matrix metalloproteinase stimulates migration of breast carcinoma cells on vitronectin and enhances tyrosine phosphorylation of focal adhesion kinase. J. Biol. Chem. 277 (2002) 9749-9756
44. Di Girolamo N., Indoh I., Jackson N., Wakefield D., McNeil H.P., Yan W., et al. Human mast cell-derived gelatinase B (matrix metalloproteinase-9) is regulated by inflammatory cytokines: Role in cell migration. J. Immunol. 177 (2006) 2638-2650
45. Dickinson S.C., Vankemmelbeke M.N., Buttle D.J., Rosenberg K., Heinegård D., and Hollander A.P. Cleavage of cartilage oligomeric matrix protein (thrombospondin-5) by matrix metalloproteinases and a disintegrin and metalloproteinase with thrombospondin motifs. Matrix Biol. 22 (2003) 267-278
46. Dioszegi M., Cannon P., and Van Wart H.E. Vertebrate collagenases. Methods Enzymol. 248 (1995) 413-431
47. Dodge G.R., and Poole A.R. Immunohistochemical detection and immunochemical analysis of type II collagen degradation in human normal, rheumatoid, and osteoarthritic articular cartilages and in explants of bovine articular cartilage cultured with interleukin 1. J. Clin. Invest. 83 (1989) 647-661
48. Drake F.H., Dodds R.A., James I.E., Connor J.R., Debouck C., Richardson S., et al. Cathepsin K, but not cathepsins B, L, or S, is abundantly expressed in human osteoclasts. J. Biol. Chem. 271 (1996) 12511-12516
49. Eggelmeijer F., Papapoulos S.E., Westedt M.L., Van Paassen H.C., Dijkmans B.A., and Breedveld F.C. Bone metabolism in rheumatoid arthritis; relation to disease activity. Br. J. Rheumatol. 32 (1993) 387-391
50. Elliott D.H. Structure and function of mammalian tendon. Biol. Rev. Camb. Philos. Soc. 40 (1965) 392-421
51. Engsig M.T., Chen Q.J., Vu T.H., Pedersen A.C., Therkidsen B., Lund L.R., et al. Matrix metalloproteinase 9 and vascular endothelial growth factor are essential for osteoclast recruitment into developing long bones. J. Cell Biol. 151 (2000) 879-889
52. Everts V., Delaissé J.M., Korper W., Jansen D.C., Tigchelaar-Gutter W., Saftig P., et al. The bone lining cell: Its role in cleaning Howship's lacunae and initiating bone formation. J. Bone Miner. Res. 17 (2002) 77-90
53. Everts V., Delaissé J.M., Korper W., Niehof A., Vaes G., and Beertsen W. Degradation of collagen in the bone-resorbing compartment underlying the osteoclast involves both cysteine-proteinases and matrix metalloproteinases. J. Cell Physiol. 150 (1992) 221-231
54. Everts V., Korper W., Jansen D.C., Steinfort J., Lammerse I., Heera S., et al. Functional heterogeneity of osteoclasts: Matrix metalloproteinases participate in osteoclastic resorption of calvarial bone but not in resorption of long bone. FASEB J. 13 (1999) 1219-1230
55. Fan T.J., Han L.H., Cong R.S., and Liang J. Caspase family proteases and apoptosis. Acta Biochim. Biophys. Sin. (Shanghai) 37 (2005) 719-727
56. Fell H.B., and Jubb R.W. The effect of synovial tissue on the breakdown of articular cartilage in organ culture. Arthritis Rheum. 20 (1977) 1359-1371
57. Fernandes J.C., Martel-Pelletier J., and Pelletier J.P. The role of cytokines in osteoarthritis pathophysiology. Biorheology 39 (2002) 237-246
58. Ferrell W.R., Lockhart J.C., Kelso E.B., Dunning L., Plevin R., Meek S.E., et al. Essential role for proteinase-activated receptor-2 in arthritis. J. Clin. Invest. 111 (2003) 35-41
59. Flannery C.R., Zeng W., Corcoran C., Collins-Racie L.A., Chockalingam P.S., Hebert T., et al. Autocatalytic cleavage of ADAMTS-4 (aggrecanase-1) reveals multiple glycosaminoglycan-binding sites. J. Biol. Chem. 277 (2002) 42775-42780
60. Freije J.M., Diez-Itza I., Balbin M., Sánchez L.M., Blasco R., Tolivia J., et al. Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas. J. Biol. Chem. 269 (1994) 16766-16773
61. Fuller K., and Chambers T.J. Localisation of mRNA for collagenase in osteocytic, bone surface and chondrocytic cells but not osteoclasts. J. Cell Sci. 108 Pt 6 (1995) 2221-2230
62. Gao G., Plaas A., Thompson V.P., Jin S., Zuo F., and Sandy J.D. ADAMTS4 (aggrecanase-1) activation on the cell surface involves C-terminal cleavage by glycosylphosphatidyl inositol-anchored membrane type 4-matrix metalloproteinase and binding of the activated proteinase to chondroitin sulfate and heparan sulfate on syndecan-1. J. Biol. Chem. 279 (2004) 10042-10051
63. Gao G., Westling J., Thompson V.P., Howell T.D., Gottschall P.E., and Sandy J.D. Activation of the proteolytic activity of ADAMTS4 (aggrecanase-1) by C- terminal truncation. J. Biol. Chem. 277 (2002) 11034-11041
64. Garnero P., Borel O., Byrjalsen I., Ferreras M., Drake F.H., McQueney M.S., et al. The collagenolytic activity of cathepsin K is unique among mammalian proteinases. J. Biol. Chem. 273 (1998) 32347-32352
65. Glasson S.S., Askew R., Sheppard B., Carito B.A., Blanchet T., Ma H.L., et al. Characterization of and osteoarthritis susceptibility in ADAMTS-4-knockout mice. Arthritis Rheum. 50 (2004) 2547-2558
66. Glasson S.S., Askew R., Sheppard B., Carito B., Blanchet T., Ma H.L., et al. Deletion of active ADAMTS5 prevents cartilage degradation in a murine model of osteoarthritis. Nature 434 (2005) 644-648
67. Gruber B.L., Marchese M.J., Suzuki K., Schwartz L.B., Okada Y., Nagase H., et al. Synovial procollagenase activation by human mast cell tryptase dependence upon matrix metalloproteinase 3 activation. J. Clin. Invest. 84 (1989) 1657-1662
68. Gulati P., Guc D., Lemercier C., Lappin D., and Whaley K. Expression of the components and regulatory proteins of the classical pathway of complement in normal and diseased synovium. Rheumatol. Int. 14 (1994) 13-19
69. Hakala M., Risteli L., Manelius J., Nieminen P., and Risteli J. Increased type I collagen degradation correlates with disease severity in rheumatoid arthritis. Ann. Rheum. Dis. 52 (1993) 866-869
70. Handley C.J., Mok M.T., Ilic M.Z., Adcocks C., Buttle D.J., and Robinson H.C. Cathepsin D cleaves aggrecan at unique sites within the interglobular domain and chondroitin sulfate attachment regions that are also cleaved when cartilage is maintained at acid pH. Matrix Biol. 20 (2001) 543-553
71. Hardingham T.E., Fosang A.J., and Dudhia J. The structure, function and turnover of aggrecan, the large aggregating proteoglycan from cartilage. Eur. J. Clin. Chem. Clin. Biochem. 32 (1994) 249-257
72. Hashimoto S., Ochs R.L., Komiya S., and Lotz M. Linkage of chondrocyte apoptosis and cartilage degradation in human osteoarthritis. Arthritis Rheum. 41 (1998) 1632-1638
73. Hashimoto S., Takahashi K., Amiel D., Coutts R.D., and Lotz M. Chondrocyte apoptosis and nitric oxide production during experimentally induced osteoarthritis. Arthritis Rheum. 41 (1998) 1266-1274
74. Holliday L.S., Welgus H.G., Fliszar C.J., Veith G.M., Jeffrey J.J., and Gluck S.L. Initiation of osteoclast bone resorption by interstitial collagenase. J. Biol. Chem. 272 (1997) 22053-22058
75. Hou W.S., Brömme D., Zhao Y., Mehler E., Dushey C., Weinstein H., et al. Characterization of novel cathepsin K mutations in the pro and mature polypeptide regions causing pycnodysostosis. J. Clin. Invest. 103 (1999) 731-738
76. Hou W.S., Li Z., Gordon R.E., Chan K., Klein M.J., Levy R., et al. Cathepsin k is a critical protease in synovial fibroblast-mediated collagen degradation. Am. J. Pathol. 159 (2001) 2167-2177
77. Hou W.S., Li W., Keyszer G., Weber E., Levy R., Klein M.J., et al. Comparison of cathepsins K and S expression within the rheumatoid and osteoarthritic synovium. Arthritis Rheum. 46 (2002) 663-674
78. Hulejová H., Baresová V., Klézl Z., Polanská M., Adam M., and Senolt L. Increased level of cytokines and matrix metalloproteinases in osteoarthritic subchondral bone. Cytokine 38 (2007) 151-156
79. Hummel K.M., Petrow P.K., Franz J.K., Muller-Ladner U., Aicher W.K., Gay R.E., et al. 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
80. Ilic M.Z., Vankemmelbeke M.N., Holen I., Buttle D.J., Clem Robinson H., and Handley C.J. Bovine joint capsule and fibroblasts derived from joint capsule express aggrecanase activity. Matrix Biol. 19 (2000) 257-265
81. Irie K., Tsuruga E., Sakakura Y., Muto T., and Yajima T. Immunohistochemical localization of membrane type 1-matrix metalloproteinase (MT1-MMP) in osteoclasts in vivo. Tissue Cell 33 (2001) 478-482
82. Ishikawa H., Ohno O., and Hirohata K. An electron microscopic study of the synovial-bone junction in rheumatoid arthritis. Rheumatol. Int. 4 (1984) 1-8
83. John T., Stahel P.F., Morgan S.J., and Schulze-Tanzil G. Impact of the complement cascade on posttraumatic cartilage inflammation and degradation. Histol. Histopathol. 22 (2007) 781-790
84. Jones G.C., Corps A.N., Pennington C.J., Clark I.M., Edwards D.R., Bradley M.M., et al. Expression profiling of metalloproteinases and tissue inhibitors of metalloproteinases in normal and degenerate human Achilles tendon. Arthritis Rheum. 54 (2006) 832-842
85. Jones G.C., and Riley G.P. ADAMTS proteinases: A multi-domain, multi-functional family with roles in extracellular matrix turnover and arthritis. Arthritis Res. Ther. 7 (2005) 160-169
86. Józsa L., and Kannus P. In: Józsa L., and Kannus P. (Eds). Structure and metabolism of normal tendons (1997), Human tendons. Anatomy, physiology and pathology, Illinois, Champaign 46-95
87. Kajita M., Itoh Y., Chiba T., Mori H., Okada A., Kinoh H., et al. Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration. J. Cell Biol. 153 (2001) 893-904
88. Kamiya T., Kobayashi Y., Kanaoka K., Nakashima T., Kato Y., Mizuno A., et al. Fluorescence microscopic demonstration of cathepsin K activity as the major lysosomal cysteine proteinase in osteoclasts. J. Biochem. (Tokyo) 123 (1998) 752-759
89. Kannus P., and Józsa L. Histopathological changes preceding spontaneous rupture of a tendon. A controlled study of 891 patients. J. Bone Joint Surg. Am. 73 (1991) 1507-1525
90. Kastelic J., Galeski A., and Baer E. The multicomposite structure of tendon. Connect. Tissue Res. 6 (1978) 11-23
91. Kevorkian L., Young D.A., Darrah C., Donell S.T., Shepstone L., Porter S., et al. Expression profiling of metalloproteinases and their inhibitors in cartilage. Arthritis Rheum. 50 (2004) 131-141
92. Kiani C., Chen L., Wu Y.J., Yee A.J., and Yang B.B. Structure and function of aggrecan. Cell Res. 12 (2002) 19-32
93. Kim H.A., and Song Y.W. Apoptotic chondrocyte death in rheumatoid arthritis. Arthritis Rheum. 42 (1999) 1528-1537
94. Kleftogiannis F., Handley C.J., and Campbell M.A. Characterization of extracellular matrix macromolecules from bovine synovial capsule. J. Orthop. Res. 12 (1994) 365-374
95. Knäuper V., López-Otin C., Smith B., Knight G., and Murphy G. Biochemical characterization of human collagenase-3. J. Biol. Chem. 271 (1996) 1544-1550
96. Kobayashi H., Schmitt M., Goretzki L., Chucholowski N., Calvete J., Kramer M., et al. Cathepsin B efficiently activates the soluble and the tumor cell receptor-bound form of the proenzyme urokinase-type plasminogen activator (Pro-uPA). J. Biol. Chem. 266 (1991) 5147-5152
97. Kobayashi Y., Yamamoto K., Saido T., Kawasaki H., Oppenheim J.J., and Matsushima K. Identification of calcium-activated neutral protease as a processing enzyme of human interleukin 1 alpha. Proc. Natl. Acad. Sci. U.S.A. 87 (1990) 5548-5552
98. Konttinen Y.T., Ceponis A., Meri S., Vuorikoski A., Kortekangas P., Sorsa T., et al. Complement in acute and chronic arthritides: Assessment of C3c, C9, and protectin (CD59) in synovial membrane. Ann. Rheum. Dis. 55 (1996) 888-894
99. Kuno K., Okada Y., Kawashima H., Nakamura H., Miyasaka M., Ohno H., et al. ADAMTS-1 cleaves a cartilage proteoglycan, aggrecan. FEBS Lett. 478 (2000) 241-245
100. Lee D.M., and Weinblatt M.E. Rheumatoid arthritis. Lancet 358 (2001) 903-911
101. Lees M., Taylor D.J., and Woolley D.E. Mast cell proteinases activate precursor forms of collagenase and stromelysin, but not of gelatinases A and B. Eur. J. Biochem. 223 (1994) 171-177
102. Li Z., Hou W.S., and Brömme D. Collagenolytic activity of cathepsin K is specifically modulated by cartilage-resident chondroitin sulfates. Biochemistry 39 (2000) 529-536
103. Little C.B., Meeker C.T., Golub S.B., Lawlor K.E., Farmer P.J., Smith S.M., et al. Blocking aggrecanase cleavage in the aggrecan interglobular domain abrogates cartilage erosion and promotes cartilage repair. J. Clin. Invest. 117 (2007) 1627-1636
104. Liu H., McKenna L.A., and Dean M.F. An N-terminal peptide from link protein can stimulate biosynthesis of collagen by human articular cartilage. Arch. Biochem. Biophys. 378 (2000) 116-122
105. Lohmander L.S., Neame P.J., and Sandy J.D. The structure of aggrecan fragments in human synovial fluid. Evidence that aggrecanase mediates cartilage degradation in inflammatory joint disease, joint injury, and osteoarthritis. Arthritis Rheum. 36 (1993) 1214-1222
106. Lotz M., Hashimoto S., and Kühn K. Mechanisms of chondrocyte apoptosis. Osteoarthr. Cartilage 7 (1999) 389-391
107. Magaro M., Tricerri A., Piane D., Zoli A., Serra F., Altomonte L., et al. Generalized osteoporosis in non-steroid treated rheumatoid arthritis. Rheumatol. Int. 11 (1991) 73-76
108. Malfait A.M., Liu R.Q., Ijiri K., Komiya S., and Tortorella M.D. Inhibition of ADAM-TS4 and ADAM-TS5 prevents aggrecan degradation in osteoarthritic cartilage. J. Biol. Chem. 277 (2002) 22201-22208
109. Mansell J.P., and Bailey A.J. Abnormal cancellous bone collagen metabolism in osteoarthritis. J. Clin. Invest. 101 (1998) 1596-1603
110. Mansell J.P., Tarlton J.F., and Bailey A.J. Biochemical evidence for altered subchondral bone collagen metabolism in osteoarthritis of the hip. Br. J. Rheumatol. 36 (1997) 16-19
111. Mapp P.I., Avery P.S., McWilliams D.F., Bowyer J., Day C., Moores S., et al. Angiogenesis in two animal models of osteoarthritis. Osteoarthr. Cartilage 16 (2008) 61-69
112. Martel-Pelletier J., McCollum R., Fujimoto N., Obata K., Cloutier J.M., and Pelletier J.P. Excess of metalloproteases over tissue inhibitor of metalloprotease may contribute to cartilage degradation in osteoarthritis and rheumatoid arthritis. Lab. Invest. 70 (1994) 807-815
113. Meredith Jr. J.E., Fazeli B., and Schwartz M.A. The extracellular matrix as a cell survival factor. Mol. Biol. Cell 4 (1993) 953-961
114. Millar A.W., Brown P.D., Moore J., Galloway W.A., Cornish A.G., Lenehan T.J., et al. Results of single and repeat dose studies of the oral matrix metalloproteinase inhibitor marimastat in healthy male volunteers. Br. J. Clin. Pharmacol. 45 (1998) 21-26
115. Milner J.M., Elliott S.F., and Cawston T.E. Activation of procollagenases is a key control point in cartilage collagen degradation: Interaction of serine and metalloproteinase pathways. Arthritis Rheum. 44 (2001) 2084-2096
116. Miyazaki K., Umenishi F., Funahashi K., Koshikawa N., Yasumitsu H., and Umeda M. Activation of TIMP-2/progelatinase A complex by stromelysin. Biochem. Biophys. Res. Commun. 185 (1992) 852-859
117. Mizutani H., Schechter N., Lazarus G., Black R.A., and Kupper T.S. Rapid and specific conversion of precursor interleukin 1 beta (IL-1 beta) to an active IL-1 species by human mast cell chymase. J. Exp. Med. 174 (1991) 821-825
118. Mor A., Abramson S.B., and Pillinger M.H. The fibroblast-like synovial cell in rheumatoid arthritis: A key player in inflammation and joint destruction. Clin. Immunol. 115 (2005) 118-128
119. Moreland L.W., Schiff M.H., Baumgartner S.W., Tindall E.A., Fleischmann R.M., Bulpitt K.J., et al. Etanercept therapy in rheumatoid arthritis. A randomized, controlled trial. Ann. Intern. Med. 130 (1999) 478-486
120. Morko J.P., Söderström M., Säämänen 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
121. Mort J.S., Dodge G.R., Roughley P.J., Liu J., Finch S.J., DiPasquale G., et al. Direct evidence for active metalloproteinases mediating matrix degradation in interleukin 1-stimulated human articular cartilage. Matrix 13 (1993) 95-102
122. Movin T., Gad A., Reinholt F.P., and Rolf C. Tendon pathology in long-standing achillodynia. Biopsy findings in 40 patients. Acta Orthop. Scand. 68 (1997) 170-175
123. Mudgett J.S., Hutchinson N.I., Chartrain N.A., Forsyth A.J., McDonnell J., Singer I.I., et al. Susceptibility of stromelysin 1-deficient mice to collagen-induced arthritis and cartilage destruction. Arthritis Rheum. 41 (1998) 110-121
124. Murphy G., Cockett M.I., Stephens P.E., Smith B.J., and Docherty A.J. Stromelysin is an activator of procollagenase. A study with natural and recombinant enzymes. Biochem. J. 248 (1987) 265-268
125. Murphy G., Ward R., Gavrilovic J., and Atkinson S. Physiological mechanisms for metalloproteinase activation. Matrix Suppl. 1 (1992) 224-230
126. Myers S.L., Brandt K.D., Ehlich J.W., Braunstein E.M., Shelbourne K.D., Heck D.A., et al. Synovial inflammation in patients with early osteoarthritis of the knee. J. Rheumatol. 17 (1990) 1662-1669
127. Nagase H., and Woessner Jr. J.F. Matrix metalloproteinases. J. Biol. Chem. 274 (1999) 21491-21494
128. Nakagawa T.Y., Brissette W.H., Lira P.D., Griffiths R.J., Petrushova N., Stock J., et al. Impaired invariant chain degradation and antigen presentation and diminished collagen-induced arthritis in cathepsin S null mice. Immunity 10 (1999) 207-217
129. Nakagawa K., Sakiyama H., Tsuchida T., Yamaguchi K., Toyoguchi T., Masuda R., et al. Complement C1s activation in degenerating articular cartilage of rheumatoid arthritis patients: Immunohistochemical studies with an active form specific antibody. Ann. Rheum. Dis. 58 (1999) 175-181
130. Nguyen Q., Mort J.S., and Roughley P.J. Cartilage proteoglycan aggregate is degraded more extensively by cathepsin L than by cathepsin B. Biochem. J. 266 (1990) 569-573
131. Nguyen Q., Murphy G., Hughes C.E., Mort J.S., and Roughley P.J. Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein. Biochem. J. 295 Pt 2 (1993) 595-598
132. Nguyen Q., Murphy G., Roughley P.J., and Mort J.S. Degradation of proteoglycan aggregate by a cartilage metalloproteinase. Evidence for the involvement of stromelysin in the generation of link protein heterogeneity in situ. Biochem. J. 259 (1989) 61-67
133. Nigrovic P.A., and Lee D.M. Synovial mast cells: Role in acute and chronic arthritis. Immunol. Rev. 217 (2007) 19-37
134. Ohta S., Harigai M., Tanaka M., Kawaguchi Y., Sugiura T., Takagi K., et al. Tumor necrosis factor-alpha (TNF-alpha) converting enzyme contributes to production of TNF-alpha in synovial tissues from patients with rheumatoid arthritis. J. Rheumatol. 28 (2001) 1756-1763
135. Ohuchi E., Imai K., Fujii Y., Sato H., Seiki M., and Okada Y. Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules. J. Biol. Chem. 272 (1997) 2446-2451
136. Oleesky D.A., Daniels R.H., Williams B.D., Amos N., and Morgan B.P. Terminal complement complexes and C1/C1 inhibitor complexes in rheumatoid arthritis and other arthritic conditions. Clin. Exp. Immunol. 84 (1991) 250-255
137. Onuma H., Masuko-Hongo K., Yuan G., Sakata M., Nakamura H., Kato T., et al. Expression of the anaphylatoxin receptor C5aR (CD88) by human articular chondrocytes. Rheumatol. Int. 22 (2002) 52-55
138. Parikka V., Lehenkari P., Sassi M.L., Halleen J., Risteli J., Härkönen P., et al. Estrogen reduces the depth of resorption pits by disturbing the organic bone matrix degradation activity of mature osteoclasts. Endocrinology 142 (2001) 5371-5378
139. Pettipher E.R., Higgs G.A., and Henderson B. Interleukin 1 induces leukocyte infiltration and cartilage proteoglycan degradation in the synovial joint. Proc. Natl. Acad. Sci. U.S.A. 83 (1986) 8749-8753
140. Poole A.R., Alini M., and Hollander A.P. Cellular biology of cartilage degradation. In: Henderson B., Edwards J.C.W., and Pettipher E.R. (Eds). Mechanisms and models in rheumatoid arthritis (1995), Academic Press Ltd., London 163-204
141. Pratta M.A., Yao W., Decicco C., Tortorella M.D., Liu R.Q., Copeland R.A., et al. Aggrecan protects cartilage collagen from proteolytic cleavage. J. Biol. Chem. 278 (2003) 45539-45545
142. Rawlings N.D., and Barrett A.J. MEROPS: The peptidase database. Nucleic Acids Res. 27 (1999) 325-331
143. Rawlings N.D., Tolle D.P., and Barrett A.J. MEROPS: The peptidase database. Nucleic Acids Res. 32 (2004) D160-D164
144. Redlich K., Hayer S., Ricci R., David J.P., Tohidast-Akrad M., Kollias G., et al. Osteoclasts are essential for TNF-alpha-mediated joint destruction. J. Clin. Invest. 110 (2002) 1419-1427
145. Riese R.J., Wolf P.R., Brömme D., Natkin L.R., Villadangos J.A., Ploegh H.L., et al. Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading. Immunity 4 (1996) 357-366
146. Riley G. Tendon and ligament biochemistry and pathology. In: Hazleman B., Riley G., and Speed C. (Eds). Soft tisssue rheumatology (2004), Oxford University Press, New York 20-53
147. Riley G.P. Gene expression and matrix turnover in overused and damaged tendons. Scand. J. Med. Sci. Sports 15 (2005) 241-251
148. Riley G.P., Curry V., DeGroot J., van El B., Verzijl N., Hazleman B.L., et al. Matrix metalloproteinase activities and their relationship with collagen remodelling in tendon pathology. Matrix Biol. 21 (2002) 185-195
149. Riley G.P., Harrall R.L., Constant C.R., Chard M.D., Cawston T.E., and Hazleman B.L. Tendon degeneration and chronic shoulder pain: Changes in the collagen composition of the human rotator cuff tendons in rotator cuff tendinitis. Ann. Rheum. Dis. 53 (1994) 359-366
150. Rodriguez-Manzaneque J.C., Milchanowski A.B., Dufour E.K., Leduc R., and Iruela-Arispe M.L. Characterization of METH-1/ADAMTS1 processing reveals two distinct active forms. J. Biol. Chem. 275 (2000) 33471-33479
151. Ronday H.K., Smits H.H., Van Muijen G.N., Pruszczynski M.S., Dolhain R.J., Van Langelaan E.J., et al. Difference in expression of the plasminogen activation system in synovial tissue of patients with rheumatoid arthritis and osteoarthritis. Br. J. Rheumatol. 35 (1996) 416-423
152. Roughley P.J., Poole A.R., and Mort J.S. The heterogeneity of link proteins isolated from human articular cartilage proteoglycan aggregates. J. Biol. Chem. 257 (1982) 11908-11914
153. Saarinen J., Kalkkinen N., Welgus H.G., and Kovanen P.T. Activation of human interstitial procollagenase through direct cleavage of the Leu83-Thr84 bond by mast cell chymase. J. Biol. Chem. 269 (1994) 18134-18140
154. Saffarian S., Collier I.E., Marmer B.L., Elson E.L., and Goldberg G. Interstitial collagenase is a Brownian ratchet driven by proteolysis of collagen. Science 306 (2004) 108-111
155. Saklatvala J., Pilsworth L.M., Sarsfield S.J., Gavrilovic J., and Heath J.K. Pig catabolin is a form of interleukin 1. Cartilage and bone resorb, fibroblasts make prostaglandin and collagenase, and thymocyte proliferation is augmented in response to one protein. Biochem. J. 224 (1984) 461-466
156. Sánchez-Pernaute O., Largo R., Calvo E., Alvarez-Soria M.A., Egido J., and Herrero-Beaumont G. A fibrin based model for rheumatoid synovitis. Ann. Rheum. Dis. 62 (2003) 1135-1138
157. Sandy J.D., Flannery C.R., Neame P.J., and Lohmander L.S. The structure of aggrecan fragments in human synovial fluid. Evidence for the involvement in osteoarthritis of a novel proteinase which cleaves the Glu 373-Ala 374 bond of the interglobular domain. J. Clin. Invest. 89 (1992) 1512-1516
158. Sandy J.D., Neame P.J., Boynton R.E., and Flannery C.R. Catabolism of aggrecan in cartilage explants. Identification of a major cleavage site within the interglobular domain. J. Biol. Chem. 266 (1991) 8683-8685
159. Sandy J.D., and Verscharen C. Analysis of aggrecan in human knee cartilage and synovial fluid indicates that aggrecanase (ADAMTS) activity is responsible for the catabolic turnover and loss of whole aggrecan whereas other protease activity is required for C-terminal processing in vivo. Biochem. J. 358 (2001) 615-626
160. Sandy J.D., Westling J., Kenagy R.D., Iruela-Arispe M.L., Verscharen C., Rodriguez-Mazaneque J.C., et al. Versican V1 proteolysis in human aorta in vivo occurs at the Glu441-Ala442 bond, a site that is cleaved by recombinant ADAMTS-1 and ADAMTS-4. J. Biol. Chem. 276 (2001) 13372-13378
161. Sato T., Foged N.T., and Delaissé J.M. The migration of purified osteoclasts through collagen is inhibited by matrix metalloproteinase inhibitors. J. Bone Miner. Res. 13 (1998) 59-66
162. Seibel M.J., Duncan A., and Robins S.P. Urinary hydroxy-pyridinium crosslinks provide indices of cartilage and bone involvement in arthritic diseases. J. Rheumatol. 16 (1989) 964-970
163. Shi G.P., Villadangos J.A., Dranoff G., Small C., Gu L., Haley K.J., et al. Cathepsin S required for normal MHC class II peptide loading and germinal center development. Immunity 10 (1999) 197-206
164. Shin H., Kitajima I., Nakajima T., Shao Q., Tokioka T., Takasaki I., et al. Thrombin receptor mediated signals induce expressions of interleukin 6 and granulocyte colony stimulating factor via NF-kappa B activation in synovial fibroblasts. Ann. Rheum. Dis. 58 (1999) 55-60
165. Sjoberg A., Onnerfjord P., Mörgelin M., Heinegård D., and Blom A.M. The extracellular matrix and inflammation: Fibromodulin activates the classical pathway of complement by directly binding C1q. J. Biol. Chem. 280 (2005) 32301-32308
166. Smeets T.J., Barg E.C., Kraan M.C., Smith M.D., Breedveld F.C., and Tak P.P. Analysis of the cell infiltrate and expression of proinflammatory cytokines and matrix metalloproteinases in arthroscopic synovial biopsies: Comparison with synovial samples from patients with end stage, destructive rheumatoid arthritis. Ann. Rheum. Dis. 62 (2003) 635-638
167. Southan C. A genomic perspective on human proteases. FEBS Lett. 498 (2001) 214-218
168. Stanton H., Rogerson F.M., East C.J., Golub S.B., Lawlor K.E., Meeker C.T., et al. ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro. Nature 434 (2005) 648-652
169. Starkey P.M., Barrett A.J., and Burleigh M.C. The degradation of articular collagen by neutrophil proteinases. Biochim. Biophys. Acta 483 (1977) 386-397
170. Tchetverikov I., Ronday H.K., van El B., Kiers G.H., Verzijl N., TeKoppele J.M., et al. MMP profile in paired serum and synovial fluid samples of patients with rheumatoid arthritis. Ann. Rheum. Dis. 63 (2004) 881-883
171. Tester A.M., Ilic M.Z., Robinson H.C., and Handley C.J. Metabolic processing of newly synthesized link protein in bovine articular cartilage explant cultures. Matrix Biol. 18 (1999) 65-74
172. Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
173. Thornberry N.A., Bull H.G., Calaycay J.R., Chapman K.T., Howard A.D., Kostura M.J., et al. A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes. Nature 356 (1992) 768-774
174. Tortorella M.D., Burn T.C., Pratta M.A., Abbaszade I., Hollis J.M., Liu R., et al. Purification and cloning of aggrecanase-1: A member of the ADAMTS family of proteins. Science 284 (1999) 1664-1666
175. Tuoheti Y., Itoi E., Pradhan R.L., Wakabayashi I., Takahashi S., Minagawa H., et al. Apoptosis in the supraspinatus tendon with stage II subacromial impingement. J. Shoulder Elbow Surg. 14 (2005) 535-541
176. van Meurs J.B., van Lent P.L., Holthuysen A.E., Lambrou D., Bayne E.K., Singer I.I., et al. Active matrix metalloproteinases are present in cartilage during immune complex-mediated arthritis: A pivotal role for stromelysin-1 in cartilage destruction. J. Immunol. 163 (1999) 5633-5639
177. van Meurs J.B., van Lent P.L., Holthuysen A.E., Singer I.I., Bayne E.K., and van Den Berg W.B. Kinetics of aggrecanase- and metalloproteinase-induced neoepitopes in various stages of cartilage destruction in murine arthritis. Arthritis Rheum. 42 (1999) 1128-1139
178. van Meurs J.B., van Lent P.L., Stoop R., Holthuysen A.E., Singer I.I., Bayne E.K., et al. Cleavage of aggrecan at the Asn341-Phe342 site coincides with the initiation of collagen damage in murine antigen-induced arthritis: A pivotal role for stromelysin 1 in matrix metalloproteinase activity. Arthritis Rheum. 42 (1999) 2074-2084
179. van Meurs J.B., van Lent P.L., van de Loo A.A., Holthuysen A.E., Bayne E.K., Singer I.I., et al. Increased vulnerability of postarthritic cartilage to a second arthritic insult: Accelerated MMP activity in a flare up of arthritis. Annal. Rheum. Dis. 58 (1999) 350-356
180. Vankemmelbeke M.N., Holen I., Wilson A.G., Ilic M.Z., Handley C.J., Kelner G.S., et al. Expression and activity of ADAMTS-5 in synovium. Eur. J. Biochem. 268 (2001) 1259-1268
181. Vankemmelbeke M.N., Ilic M.Z., Handley C.J., Knight C.G., and Buttle D.J. Coincubation of bovine synovial or capsular tissue with cartilage generates a soluble "Aggrecanase" activity. Biochem. Biophys. Res. Commun. 255 (1999) 686-691
182. Vankemmelbeke M.N., Jones G.C., Fowles C., Ilic M.Z., Handley C.J., Day A.J., et al. Selective inhibition of ADAMTS-1, -4 and -5 by catechin gallate esters. Eur. J. Biochem. 270 (2003) 2394-2403
183. Villadangos J.A., Bryant R.A., Deussing J., Driessen C., Lennon-Dumenil A.M., Riese R.J., et al. Proteases involved in MHC class II antigen presentation. Immunol. Rev. 172 (1999) 109-120
184. Walport M.J. Complement. First of two parts. N. Engl. J. Med. 344 (2001) 1058-1066
185. Walsh D.A., Bonnet C.S., Turner E.L., Wilson D., Situ M., and McWilliams D.F. Angiogenesis in the synovium and at the osteochondral junction in osteoarthritis. Osteoarthr. Cartilage 15 (2007) 743-751
186. Wang P., Tortorella M., England K., Malfait A.M., Thomas G., Arner E.C., et al. Proprotein convertase furin interacts with and cleaves pro-ADAMTS4 (aggrecanase-1) in the trans-Golgi network. J. Biol. Chem. 279 (2004) 15434-15440
187. Westling J., Gottschall P.E., Thompson V.P., Cockburn A., Perides G., Zimmermann D.R., et al. ADAMTS4 (aggrecanase-1) cleaves human brain versican V2 at Glu405-Gln406 to generate glial hyaluronate binding protein. Biochem. J. 377 (2004) 787-795
188. Williams III R.J., Attia E., Wickiewicz T.L., and Hannafin J.A. The effect of ciprofloxacin on tendon, paratenon, and capsular fibroblast metabolism. Am. J. Sports Med. 28 (2000) 364-369
189. Woolley D.E. Cellular mechanisms of cartilage destruction. In: Henderson B., Edwards J.C.W., and Pettipher E.R. (Eds). Mechanisms and models in rheumatoid arthritis (1995), Academic Press Ltd., London 115-132
190. Yamaguchi K., Sakiyama H., Matsumoto M., Moriya H., and Sakiyama S. Degradation of type I and II collagen by human activated C1-s. FEBS Lett. 268 (1990) 206-208
191. Yasuda T. Cartilage destruction by matrix degradation products. Mod. Rheumatol. 16 (2006) 197-205
192. Yasuda Y., Kaleta J., and Brömme D. The role of cathepsins in osteoporosis and arthritis: Rationale for the design of new therapeutics. Adv. Drug Deliv. Rev. 57 (2005) 973-993
193. Yuan J., Murrell G.A., Wei A.Q., and Wang M.X. Apoptosis in rotator cuff tendonopathy. J. Orthop. Res. 20 (2002) 1372-1379
194. Zhao W., Byrne M.H., Boyce B.F., and Krane S.M. Bone resorption induced by parathyroid hormone is strikingly diminished in collagenase-resistant mutant mice. J. Clin. Invest. 103 (1999) 517-524
195. Zhao W., Oskeritzian C.A., Pozez A.L., and Schwartz L.B. Cytokine production by skin-derived mast cells: Endogenous proteases are responsible for degradation of cytokines. J. Immunol. 175 (2005) 2635-2642