메뉴 건너뛰기




Volumn 15, Issue , 2008, Pages 11-26

ADAMTS-5: The story so far

Author keywords

ADAMTS 4; ADAMTS 5; Aggrecanase; Aggrecanolysis; Arthritis; Cartilage; Metalloproteinase

Indexed keywords

ADAM PROTEIN; AGGRECANASE; CYTOKINE; DISINTEGRIN; METALLOPROTEINASE; NEUTRALIZING ANTIBODY; PROTEIN ADAMTS 4; PROTEIN ADAMTS 5; SMALL INTERFERING RNA; AGGRECAN; GLYCOSAMINOGLYCAN; PROTEINASE;

EID: 41949131462     PISSN: 14732262     EISSN: None     Source Type: Journal    
DOI: 10.22203/eCM.v015a02     Document Type: Review
Times cited : (103)

References (159)
  • 2
    • 34447509660 scopus 로고    scopus 로고
    • Global analyses of gene expression in early experimental osteoarthritis
    • Appleton CT, Pitelka V, Henry J, Beier F (2007) Global analyses of gene expression in early experimental osteoarthritis. Arthritis Rheum 56: 1854-1868.
    • (2007) Arthritis Rheum , vol.56 , pp. 1854-1868
    • Appleton, C.T.1    Pitelka, V.2    Henry, J.3    Beier, F.4
  • 4
    • 0030910398 scopus 로고    scopus 로고
    • Cleavage of native cartilage aggrecan by neutrophil collagenase (MMP-8) is distinct from endogenous cleavage by aggrecanase
    • Arner EC, Decicco CP, Cherney R, Tortorella MD (1997) Cleavage of native cartilage aggrecan by neutrophil collagenase (MMP-8) is distinct from endogenous cleavage by aggrecanase. J Biol Chem 272: 9294-9299.
    • (1997) J Biol Chem , vol.272 , pp. 9294-9299
    • Arner, E.C.1    Decicco, C.P.2    Cherney, R.3    Tortorella, M.D.4
  • 5
    • 0033525533 scopus 로고    scopus 로고
    • Generation and Characterization of Aggrecanase. A soluble, cartilage- derived aggrecan-degrading activity
    • Arner EC, Pratta MA, Trzaskos JM, Decicco CP, Tortorella MD (1999) Generation and Characterization of Aggrecanase. A soluble, cartilage- derived aggrecan-degrading activity. J Biol Chem 274: 6594-6601.
    • (1999) J Biol Chem , vol.274 , pp. 6594-6601
    • Arner, E.C.1    Pratta, M.A.2    Trzaskos, J.M.3    Decicco, C.P.4    Tortorella, M.D.5
  • 6
    • 0026760277 scopus 로고
    • Hyaluronan-binding region of aggrecan from pig laryngeal cartilage
    • Barry FP, Gaw JU, Young CN, Neame PJ (1992) Hyaluronan-binding region of aggrecan from pig laryngeal cartilage. Biochem J 286: 761-769.
    • (1992) Biochem J , vol.286 , pp. 761-769
    • Barry, F.P.1    Gaw, J.U.2    Young, C.N.3    Neame, P.J.4
  • 7
    • 0028982223 scopus 로고
    • N- and O-linked keratan sulfate on the hyaluronan binding region of aggrecan from mature and immature bovine cartilage
    • Barry FP, Rosenberg LC, Gaw JU, Koob TJ, Neame PJ (1995) N- and O-linked keratan sulfate on the hyaluronan binding region of aggrecan from mature and immature bovine cartilage. J Biol Chem 270: 20516-20524.
    • (1995) J Biol Chem , vol.270 , pp. 20516-20524
    • Barry, F.P.1    Rosenberg, L.C.2    Gaw, J.U.3    Koob, T.J.4    Neame, P.J.5
  • 8
    • 0036822797 scopus 로고    scopus 로고
    • Relative messenger RNA expression profiling of collagenases and aggrecanases in human articular chondrocytes in vivo and in vitro
    • Bau B, Gebhard PM, Haag J, Knorr T, Bartnik E, Aigner T (2002) Relative messenger RNA expression profiling of collagenases and aggrecanases in human articular chondrocytes in vivo and in vitro. Arthritis Rheum 46: 2648-2657.
    • (2002) Arthritis Rheum , vol.46 , pp. 2648-2657
    • Bau, B.1    Gebhard, P.M.2    Haag, J.3    Knorr, T.4    Bartnik, E.5    Aigner, T.6
  • 10
    • 0032533543 scopus 로고    scopus 로고
    • An aggrecan-degrading activity associated with chondrocyte membranes
    • Billington CJ, Clark IM, Cawston TE (1998) An aggrecan-degrading activity associated with chondrocyte membranes. Biochem J 336: 207-212.
    • (1998) Biochem J , vol.336 , pp. 207-212
    • Billington, C.J.1    Clark, I.M.2    Cawston, T.E.3
  • 11
    • 33646481194 scopus 로고    scopus 로고
    • Connective tissue growth factor/CCN2 overexpression in mouse synovial lining results in transient fibrosis and cartilage damage
    • Blaney Davidson EN, Vitters EL, Mooren FM, Oliver N, Berg WB, van der Kraan PM (2006) Connective tissue growth factor/CCN2 overexpression in mouse synovial lining results in transient fibrosis and cartilage damage. Arthritis Rheum 54: 1653-1661.
    • (2006) Arthritis Rheum , vol.54 , pp. 1653-1661
    • Blaney Davidson, E.N.1    Vitters, E.L.2    Mooren, F.M.3    Oliver, N.4    Berg, W.B.5    van der Kraan, P.M.6
  • 13
    • 33846815065 scopus 로고    scopus 로고
    • The role of synovial macrophages and macrophage-produced cytokines in driving aggrecanases, matrix metalloproteinases, and other destructive and inflammatory responses in osteoarthritis
    • Bondeson J, Wainwright SD, Lauder S, Amos N, Hughes CE (2006) The role of synovial macrophages and macrophage-produced cytokines in driving aggrecanases, matrix metalloproteinases, and other destructive and inflammatory responses in osteoarthritis. Arthritis Res Ther 8: R187.
    • (2006) Arthritis Res Ther , vol.8
    • Bondeson, J.1    Wainwright, S.D.2    Lauder, S.3    Amos, N.4    Hughes, C.E.5
  • 14
    • 33847686338 scopus 로고    scopus 로고
    • Adenoviral gene transfer of the endogenous inhibitor IkappaBalpha into human osteoarthritis synovial fibroblasts demonstrates that several matrix metalloproteinases and aggrecanases are nuclear factor-kappaB-dependent
    • Bondeson J, Lauder S, Wainwright S, Amos N, Evans A, Hughes C, Feldmann M, Caterson B (2007) Adenoviral gene transfer of the endogenous inhibitor IkappaBalpha into human osteoarthritis synovial fibroblasts demonstrates that several matrix metalloproteinases and aggrecanases are nuclear factor-kappaB-dependent. J Rheumatol 34: 523-533.
    • (2007) J Rheumatol , vol.34 , pp. 523-533
    • Bondeson, J.1    Lauder, S.2    Wainwright, S.3    Amos, N.4    Evans, A.5    Hughes, C.6    Feldmann, M.7    Caterson, B.8
  • 17
    • 0032127129 scopus 로고    scopus 로고
    • Membrane type 1 matrix metalloproteinase (MT1-MMP) cleaves the recombinant aggrecan substrate rAgg1mut at the 'aggrecanase' and the MMP sites. Characterization of mt1-mmp catabolic activities on the interglobular domain of aggrecan
    • Büttner FH, Hughes CE, Margerie D, Lichte A, Tschesche H, Caterson B, Bartnik E (1998) Membrane type 1 matrix metalloproteinase (MT1-MMP) cleaves the recombinant aggrecan substrate rAgg1mut at the 'aggrecanase' and the MMP sites. Characterization of mt1-mmp catabolic activities on the interglobular domain of aggrecan. Biochem J 333: 159-165.
    • (1998) Biochem J , vol.333 , pp. 159-165
    • Büttner, F.H.1    Hughes, C.E.2    Margerie, D.3    Lichte, A.4    Tschesche, H.5    Caterson, B.6    Bartnik, E.7
  • 18
    • 0022616440 scopus 로고
    • Human articular cartilage secretes characteristic metal dependent proteinases upon stimulation by mononuclear cell factor
    • Campbell IK, Golds EE, Mort JS, Roughley PJ (1986) Human articular cartilage secretes characteristic metal dependent proteinases upon stimulation by mononuclear cell factor. J Rheumatol 13: 20-27.
    • (1986) J Rheumatol , vol.13 , pp. 20-27
    • Campbell, I.K.1    Golds, E.E.2    Mort, J.S.3    Roughley, P.J.4
  • 19
    • 0034971357 scopus 로고    scopus 로고
    • Matrix metalloproteinases and aggrecanases cleave aggrecan in different zones of normal cartilage but colocalize in the development of osteoarthritic lesions in STR/ort mice
    • Chambers MG, Cox L, Chong L, Suri N, Cover P, Bayliss MT, Mason RM (2001) Matrix metalloproteinases and aggrecanases cleave aggrecan in different zones of normal cartilage but colocalize in the development of osteoarthritic lesions in STR/ort mice. Arthritis Rheum 44: 1455-1465.
    • (2001) Arthritis Rheum , vol.44 , pp. 1455-1465
    • Chambers, M.G.1    Cox, L.2    Chong, L.3    Suri, N.4    Cover, P.5    Bayliss, M.T.6    Mason, R.M.7
  • 20
    • 33745798175 scopus 로고    scopus 로고
    • Short-term gene expression changes in cartilage explants stimulated with interleukin beta plus glucosamine and chondroitin sulfate
    • Chan PS, Caron JP, Orth MW (2006) Short-term gene expression changes in cartilage explants stimulated with interleukin beta plus glucosamine and chondroitin sulfate. J Rheumatol 33: 1329-1340.
    • (2006) J Rheumatol , vol.33 , pp. 1329-1340
    • Chan, P.S.1    Caron, J.P.2    Orth, M.W.3
  • 22
    • 0030033710 scopus 로고    scopus 로고
    • Chondrocyte matrix metalloproteinase-8: Upregulation of neutrophil collagenase by interleukin-1b in human cartilage from knee and ankle joints
    • Chubinskaya S, Huch K, Mikecz K, Cs.-Szabó G, Hasty KA, Kuettner KE, Cole AA (1996) Chondrocyte matrix metalloproteinase-8: Upregulation of neutrophil collagenase by interleukin-1b in human cartilage from knee and ankle joints. Lab Invest 74: 232-240.
    • (1996) Lab Invest , vol.74 , pp. 232-240
    • Chubinskaya, S.1    Huch, K.2    Mikecz, K.3    Cs4    Szabó, G.5    Hasty, K.A.6    Kuettner, K.E.7    Cole, A.A.8
  • 24
    • 33744905343 scopus 로고    scopus 로고
    • Activation by IL-1 of bovine articular chondrocytes in culture within a 3D collagen-based scaffold. An in vitro model to address the effect of compounds with therapeutic potential in osteoarthritis
    • Cortial D, Gouttenoire J, Rousseau CF, Ronziere MC, Piccardi N, Msika P, Herbage D, Mallein-Gerin F, Freyria AM (2006) Activation by IL-1 of bovine articular chondrocytes in culture within a 3D collagen-based scaffold. An in vitro model to address the effect of compounds with therapeutic potential in osteoarthritis. Osteoarthritis Cartilage 14: 631-640.
    • (2006) Osteoarthritis Cartilage , vol.14 , pp. 631-640
    • Cortial, D.1    Gouttenoire, J.2    Rousseau, C.F.3    Ronziere, M.C.4    Piccardi, N.5    Msika, P.6    Herbage, D.7    Mallein-Gerin, F.8    Freyria, A.M.9
  • 25
    • 0033977182 scopus 로고    scopus 로고
    • n-3 fatty acids specifically modulate catabolic factors involved in articular cartilage degradation
    • Curtis CL, Hughes CE, Flannery CR, Little CB, Harwood JL, Caterson B (2000) n-3 fatty acids specifically modulate catabolic factors involved in articular cartilage degradation. J Biol Chem 275: 721-724.
    • (2000) J Biol Chem , vol.275 , pp. 721-724
    • Curtis, C.L.1    Hughes, C.E.2    Flannery, C.R.3    Little, C.B.4    Harwood, J.L.5    Caterson, B.6
  • 26
    • 18644370594 scopus 로고    scopus 로고
    • ADAMTS-9 is synergistically induced by interleukin-1beta and tumor necrosis factor alpha in OUMS-27 chondrosarcoma cells and in human chondrocytes
    • Demircan K, Hirohata S, Nishida K, Hatipoglu OF, Oohashi T, Yonezawa T, Apte SS, Ninomiya Y (2005) ADAMTS-9 is synergistically induced by interleukin-1beta and tumor necrosis factor alpha in OUMS-27 chondrosarcoma cells and in human chondrocytes. Arthritis Rheum 52: 1451-1460.
    • (2005) Arthritis Rheum , vol.52 , pp. 1451-1460
    • Demircan, K.1    Hirohata, S.2    Nishida, K.3    Hatipoglu, O.F.4    Oohashi, T.5    Yonezawa, T.6    Apte, S.S.7    Ninomiya, Y.8
  • 28
    • 38949136134 scopus 로고    scopus 로고
    • Mechanism of proteoglycan aggregate degradation in cartilage stimulated with oncostatin M
    • in press
    • Durigova M, Roughley PJ, Mort JS (2007) Mechanism of proteoglycan aggregate degradation in cartilage stimulated with oncostatin M. Osteoarthritis Cartilage, in press.
    • (2007) Osteoarthritis Cartilage
    • Durigova, M.1    Roughley, P.J.2    Mort, J.S.3
  • 30
    • 34247891816 scopus 로고    scopus 로고
    • ADAMTS-5 deficiency does not block aggrecanolysis at preferred cleavage sites in the chondroitin sulphate-rich region of aggrecan
    • East CJ, Stanton H, Golub SB, Rogerson FM, Fosang AJ (2007b) ADAMTS-5 deficiency does not block aggrecanolysis at preferred cleavage sites in the chondroitin sulphate-rich region of aggrecan. J Biol Chem 282 :8632-8640.
    • (2007) J Biol Chem , vol.282 , pp. 8632-8640
    • East, C.J.1    Stanton, H.2    Golub, S.B.3    Rogerson, F.M.4    Fosang, A.J.5
  • 31
    • 32944469305 scopus 로고    scopus 로고
    • MMPs and ADAMTSs: Functional studies
    • Flannery CR (2006) MMPs and ADAMTSs: functional studies. Front Biosci 11: 544-569.
    • (2006) Front Biosci , vol.11 , pp. 544-569
    • Flannery, C.R.1
  • 34
    • 0029085839 scopus 로고
    • Development of a cleavage site-specific monoclonal antibody for detecting metalloproteinase- derived aggrecan fragments: Detection of fragments in human synovial fluids
    • Fosang AJ, Last K, Gardiner P, Jackson DC, Brown L (1995) Development of a cleavage site-specific monoclonal antibody for detecting metalloproteinase- derived aggrecan fragments: detection of fragments in human synovial fluids. Biochem J 310: 337-343.
    • (1995) Biochem J , vol.310 , pp. 337-343
    • Fosang, A.J.1    Last, K.2    Gardiner, P.3    Jackson, D.C.4    Brown, L.5
  • 35
    • 0029852094 scopus 로고    scopus 로고
    • Aggrecan is degraded by matrix metalloproteinases in human arthritis. Evidence that matrix metalloproteinase and aggrecanase activities can be independent
    • Fosang AJ, Last K, Maciewicz RA (1996) Aggrecan is degraded by matrix metalloproteinases in human arthritis. Evidence that matrix metalloproteinase and aggrecanase activities can be independent. J Clin Invest 98: 2292-2299.
    • (1996) J Clin Invest , vol.98 , pp. 2292-2299
    • Fosang, A.J.1    Last, K.2    Maciewicz, R.A.3
  • 36
    • 4444291440 scopus 로고    scopus 로고
    • Keratan sulphate in the aggrecan interglobular domain has a microstructure that is distinct from keratan sulphate elsewhere on aggrecan
    • San Francisco
    • Fosang AJ, Last K, Plaas AH, Poon CJ (2004) Keratan sulphate in the aggrecan interglobular domain has a microstructure that is distinct from keratan sulphate elsewhere on aggrecan. Trans Orthop Res Soc, San Francisco, 232.
    • (2004) Trans Orthop Res Soc , pp. 232
    • Fosang, A.J.1    Last, K.2    Plaas, A.H.3    Poon, C.J.4
  • 37
    • 0037192814 scopus 로고    scopus 로고
    • Activation of the Proteolytic Activity of ADAMTS4 (Aggrecanase-1) by C-terminal Truncation
    • Gao G, Westling J, Thompson VP, Howell TD, Gottschall PE, Sandy JD (2002) Activation of the Proteolytic Activity of ADAMTS4 (Aggrecanase-1) by C-terminal Truncation. J Biol Chem 277: 11034-11041.
    • (2002) J Biol Chem , vol.277 , pp. 11034-11041
    • Gao, G.1    Westling, J.2    Thompson, V.P.3    Howell, T.D.4    Gottschall, P.E.5    Sandy, J.D.6
  • 38
    • 1642354112 scopus 로고    scopus 로고
    • 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
    • Gao G, Plaas A, Thompson VP, Jin S, Zuo F, Sandy JD (2004) 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: 10042-10051.
    • (2004) J Biol Chem , vol.279 , pp. 10042-10051
    • Gao, G.1    Plaas, A.2    Thompson, V.P.3    Jin, S.4    Zuo, F.5    Sandy, J.D.6
  • 39
    • 0345735683 scopus 로고    scopus 로고
    • TIMP-3 inhibits aggrecanase-mediated glycosaminoglycan release from cartilage explants stimulated by catabolic factors
    • Gendron C, Kashiwagi M, Hughes C, Caterson B, Nagase H (2003) TIMP-3 inhibits aggrecanase-mediated glycosaminoglycan release from cartilage explants stimulated by catabolic factors. FEBS Lett 555: 431-436.
    • (2003) FEBS Lett , vol.555 , pp. 431-436
    • Gendron, C.1    Kashiwagi, M.2    Hughes, C.3    Caterson, B.4    Nagase, H.5
  • 44
    • 0038019916 scopus 로고    scopus 로고
    • Structural aspects of the metzincin clan of metalloendopeptidases
    • Gomis-Ruth F (2003) Structural aspects of the metzincin clan of metalloendopeptidases. Mol Biotechnol 24: 157-202.
    • (2003) Mol Biotechnol , vol.24 , pp. 157-202
    • Gomis-Ruth, F.1
  • 46
    • 0035853456 scopus 로고    scopus 로고
    • Inhibition of ADAMTS4 (aggrecanase-1) by tissue inhibitors of metalloproteinases (TIMP-1, 2, 3 and 4)
    • Hashimoto G, Aoki T, Nakamura H, Tanzawa K, Okada Y (2001) Inhibition of ADAMTS4 (aggrecanase-1) by tissue inhibitors of metalloproteinases (TIMP-1, 2, 3 and 4). FEBS Lett 494: 192-195.
    • (2001) FEBS Lett , vol.494 , pp. 192-195
    • Hashimoto, G.1    Aoki, T.2    Nakamura, H.3    Tanzawa, K.4    Okada, Y.5
  • 47
    • 3543004686 scopus 로고    scopus 로고
    • ADAMTS4 (aggrecanase-1) interaction with the C-terminal domain of fibronectin inhibits proteolysis of aggrecan
    • Hashimoto G, Shimoda M, Okada Y (2004) ADAMTS4 (aggrecanase-1) interaction with the C-terminal domain of fibronectin inhibits proteolysis of aggrecan. J Biol Chem 279: 32483-32491.
    • (2004) J Biol Chem , vol.279 , pp. 32483-32491
    • Hashimoto, G.1    Shimoda, M.2    Okada, Y.3
  • 48
    • 0031572290 scopus 로고    scopus 로고
    • Complete coding sequence of bovine aggrecan: Comparative structural analysis
    • Hering TM, Kollar J, Huynh TD (1997) Complete coding sequence of bovine aggrecan: comparative structural analysis. Arch Biochem Biophys 345: 259-270.
    • (1997) Arch Biochem Biophys , vol.345 , pp. 259-270
    • Hering, T.M.1    Kollar, J.2    Huynh, T.D.3
  • 49
    • 0027941838 scopus 로고
    • Families of zinc metalloproteases
    • Hooper NM (1994) Families of zinc metalloproteases. FEBS Lett 354: 1-6.
    • (1994) FEBS Lett , vol.354 , pp. 1-6
    • Hooper, N.M.1
  • 50
    • 0028919163 scopus 로고
    • Monoclonal antibodies that specifically recognise neo-epitope sequences generated by "aggrecanase" and matrix metalloproteinase cleavage of aggrecan: Application to catabolism in situ and in vitro
    • Hughes CE, Caterson B, Fosang AJ, Roughley PJ, Mort JS (1995) Monoclonal antibodies that specifically recognise neo-epitope sequences generated by "aggrecanase" and matrix metalloproteinase cleavage of aggrecan: application to catabolism in situ and in vitro. Biochem J 305: 799-804.
    • (1995) Biochem J , vol.305 , pp. 799-804
    • Hughes, C.E.1    Caterson, B.2    Fosang, A.J.3    Roughley, P.J.4    Mort, J.S.5
  • 51
    • 27444448206 scopus 로고    scopus 로고
    • Oncostatin M in combination with tumour necrosis factor {alpha} induces a chondrocyte membrane associated aggrecanase that is distinct from ADAMTS aggrecanase-1 or -2
    • Hui W, Barksby HE, Young DA, Cawston TE, McKie N, Rowan AD (2005) Oncostatin M in combination with tumour necrosis factor {alpha} induces a chondrocyte membrane associated aggrecanase that is distinct from ADAMTS aggrecanase-1 or -2. Ann Rheum Dis 64: 1624-1632.
    • (2005) Ann Rheum Dis , vol.64 , pp. 1624-1632
    • Hui, W.1    Barksby, H.E.2    Young, D.A.3    Cawston, T.E.4    McKie, N.5    Rowan, A.D.6
  • 52
    • 0033520318 scopus 로고    scopus 로고
    • ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases. General features and genomic distribution of the ADAM-TS family
    • Hurskainen TL, Hirohata S, Seldin MF, Apte SS (1999) ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases. General features and genomic distribution of the ADAM-TS family. J Biol Chem 274: 25555-25563.
    • (1999) J Biol Chem , vol.274 , pp. 25555-25563
    • Hurskainen, T.L.1    Hirohata, S.2    Seldin, M.F.3    Apte, S.S.4
  • 54
    • 38049115682 scopus 로고    scopus 로고
    • Distinguishing aggrecan loss from aggrecan proteolysis in ADAMTS-4 and ADAMTS-5 single and double deficient mice
    • Ilic MZ, East CJ, Rogerson FM, Fosang AJ, Handley CJ (2007) Distinguishing aggrecan loss from aggrecan proteolysis in ADAMTS-4 and ADAMTS-5 single and double deficient mice. J Biol Chem 282: 37420-37428.
    • (2007) J Biol Chem , vol.282 , pp. 37420-37428
    • Ilic, M.Z.1    East, C.J.2    Rogerson, F.M.3    Fosang, A.J.4    Handley, C.J.5
  • 56
    • 0242655673 scopus 로고    scopus 로고
    • Collagenase 3 is a target of Cbfa1, a transcription factor of the runt gene family involved in bone formation
    • Jimenez MJ, Balbin M, Lopez JM, Alvarez J, Komori T, Lopez-Otin C (1999) Collagenase 3 is a target of Cbfa1, a transcription factor of the runt gene family involved in bone formation. Mol Cell Biol 19: 4431-4442.
    • (1999) Mol Cell Biol , vol.19 , pp. 4431-4442
    • Jimenez, M.J.1    Balbin, M.2    Lopez, J.M.3    Alvarez, J.4    Komori, T.5    Lopez-Otin, C.6
  • 57
    • 21644449866 scopus 로고    scopus 로고
    • ADAMTS proteinases: A multi-domain, multi-functional family with roles in extracellular matrix turnover and arthritis
    • Jones GC, Riley GP (2005) ADAMTS proteinases: a multi-domain, multi-functional family with roles in extracellular matrix turnover and arthritis. Arthritis Res Ther 7:160-169.
    • (2005) Arthritis Res Ther , vol.7 , pp. 160-169
    • Jones, G.C.1    Riley, G.P.2
  • 58
    • 0032170247 scopus 로고    scopus 로고
    • Cultured human ankle and knee cartilage differ in susceptibility to damage mediated by fibronectin fragments
    • Kang Y, Koepp H, Cole AA, Kuettner KE, Homandberg GA (1998) Cultured human ankle and knee cartilage differ in susceptibility to damage mediated by fibronectin fragments. J Orthop Res 16: 551-556.
    • (1998) J Orthop Res , vol.16 , pp. 551-556
    • Kang, Y.1    Koepp, H.2    Cole, A.A.3    Kuettner, K.E.4    Homandberg, G.A.5
  • 59
    • 0035918309 scopus 로고    scopus 로고
    • TIMP-3 Is a Potent Inhibitor of Aggrecanase 1 (ADAMTS4) and Aggrecanase 2 (ADAM-TS5)
    • Kashiwagi M, Tortorella M, Nagase H, Brew K (2001) TIMP-3 Is a Potent Inhibitor of Aggrecanase 1 (ADAMTS4) and Aggrecanase 2 (ADAM-TS5). J Biol Chem 276: 12501-12504.
    • (2001) J Biol Chem , vol.276 , pp. 12501-12504
    • Kashiwagi, M.1    Tortorella, M.2    Nagase, H.3    Brew, K.4
  • 61
    • 0034029067 scopus 로고    scopus 로고
    • The new kids on the block: ADAMTSs, potentially multifunctional metalloproteinases of the ADAM family
    • Kaushal GP, Shah SV (2000) The new kids on the block: ADAMTSs, potentially multifunctional metalloproteinases of the ADAM family. J Clin Invest 105: 1335-1337.
    • (2000) J Clin Invest , vol.105 , pp. 1335-1337
    • Kaushal, G.P.1    Shah, S.V.2
  • 64
    • 0036222734 scopus 로고    scopus 로고
    • The modulation of matrix metalloproteinase and ADAM gene expression in human chondrocytes by interleukin-1 and oncostatin M: A time-course study using real-time quantitative reverse transcription-polymerase chain reaction
    • Koshy PJ, Lundy CJ, Rowan AD, Porter S, Edwards DR, Hogan A, Clark IM, Cawston TE (2002) The modulation of matrix metalloproteinase and ADAM gene expression in human chondrocytes by interleukin-1 and oncostatin M: A time-course study using real-time quantitative reverse transcription-polymerase chain reaction. Arthritis Rheum 46: 961-967.
    • (2002) Arthritis Rheum , vol.46 , pp. 961-967
    • Koshy, P.J.1    Lundy, C.J.2    Rowan, A.D.3    Porter, S.4    Edwards, D.R.5    Hogan, A.6    Clark, I.M.7    Cawston, T.E.8
  • 65
    • 0032577568 scopus 로고    scopus 로고
    • ADAMTS-1 protein anchors at the extracellular matrix through the thrombospondin type I motifs and its spacing region
    • Kuno K, Matsushima K (1998) ADAMTS-1 protein anchors at the extracellular matrix through the thrombospondin type I motifs and its spacing region. J Biol Chem 273:13912-13917.
    • (1998) J Biol Chem , vol.273 , pp. 13912-13917
    • Kuno, K.1    Matsushima, K.2
  • 70
  • 71
    • 0031688163 scopus 로고    scopus 로고
    • Immunolocalization of the cleavage of the aggrecan core protein at the Asn341-Phe342 bond, as an indicator of the location of the metalloproteinases active in the lysis of the rat growth plate
    • Lee ER, Lamplugh L, Leblond CP, Mordier S, Magny MC, Mort JS (1998) Immunolocalization of the cleavage of the aggrecan core protein at the Asn341-Phe342 bond, as an indicator of the location of the metalloproteinases active in the lysis of the rat growth plate. Anat Rec 252: 117-132.
    • (1998) Anat Rec , vol.252 , pp. 117-132
    • Lee, E.R.1    Lamplugh, L.2    Leblond, C.P.3    Mordier, S.4    Magny, M.C.5    Mort, J.S.6
  • 72
    • 0027373233 scopus 로고
    • cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia
    • Li H, Schwartz NB, Vertel BM (1993) cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia. J Biol Chem 268: 23504-23511.
    • (1993) J Biol Chem , vol.268 , pp. 23504-23511
    • Li, H.1    Schwartz, N.B.2    Vertel, B.M.3
  • 75
    • 34249897267 scopus 로고    scopus 로고
    • Blocking aggrecanase cleavage in the aggrecan interglobular domain abrogates cartilage erosion and promotes cartilage repair
    • Little CB, Meeker CT, Golub SB, Lawlor KE, Farmer PJ, Smith SM, Fosang AJ (2007) Blocking aggrecanase cleavage in the aggrecan interglobular domain abrogates cartilage erosion and promotes cartilage repair. J Clin Invest 117: 1627-1636.
    • (2007) J Clin Invest , vol.117 , pp. 1627-1636
    • Little, C.B.1    Meeker, C.T.2    Golub, S.B.3    Lawlor, K.E.4    Farmer, P.J.5    Smith, S.M.6    Fosang, A.J.7
  • 76
    • 0027445981 scopus 로고
    • The structure of aggrecan fragments in human synovial fluid. Evidence that aggrecanase mediates cartilage degradation in inflammatory joint disease, joint injury, and osteoarthritis
    • Lohmander LS, Neame PJ, Sandy JD (1993) 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: 1214-1222.
    • (1993) Arthritis Rheum , vol.36 , pp. 1214-1222
    • Lohmander, L.S.1    Neame, P.J.2    Sandy, J.D.3
  • 77
    • 0026771893 scopus 로고
    • N-terminal sequence of proteoglycan fragments isolated from medium of interleukin-1-treated articular-cartilage cultures. Putative site(s) of enzymic cleavage
    • Loulakis P, Shrikhande A, Davis G, Maniglia CA (1992) N-terminal sequence of proteoglycan fragments isolated from medium of interleukin-1-treated articular-cartilage cultures. Putative site(s) of enzymic cleavage. Biochem J 284: 589-593.
    • (1992) Biochem J , vol.284 , pp. 589-593
    • Loulakis, P.1    Shrikhande, A.2    Davis, G.3    Maniglia, C.A.4
  • 78
    • 38449102464 scopus 로고    scopus 로고
    • G1-G2 aggrecan product that can be generated by M-calpain on truncation at Ala709-Ala710 is present abundantly in human articular cartilage
    • Maehara H, Suzuki K, Sasaki T, Oshita H, Wada E, Inoue T, Shimizu K (2007) G1-G2 aggrecan product that can be generated by M-calpain on truncation at Ala709-Ala710 is present abundantly in human articular cartilage. J Biochem (Tokyo) 141: 469-477.
    • (2007) J Biochem (Tokyo) , vol.141 , pp. 469-477
    • Maehara, H.1    Suzuki, K.2    Sasaki, T.3    Oshita, H.4    Wada, E.5    Inoue, T.6    Shimizu, K.7
  • 79
    • 0344875565 scopus 로고    scopus 로고
    • Cleavage of the ADAMTS13 propeptide is not required for protease activity
    • Majerus EM, Zheng X, Tuley EA, Sadler JE (2003) Cleavage of the ADAMTS13 propeptide is not required for protease activity. J Biol Chem 278: 46643-46648.
    • (2003) J Biol Chem , vol.278 , pp. 46643-46648
    • Majerus, E.M.1    Zheng, X.2    Tuley, E.A.3    Sadler, J.E.4
  • 80
    • 36048985974 scopus 로고    scopus 로고
    • Double-knockout of ADAMTS-4 and ADAMTS-5 in mice results in physiologically normal animals and prevents the progression of osteoarthritis
    • Majumdar MK, Askew R, Schelling S, Stedman N, Blanchet T, Hopkins B, Morris EA, Glasson SS (2007) Double-knockout of ADAMTS-4 and ADAMTS-5 in mice results in physiologically normal animals and prevents the progression of osteoarthritis. Arthritis Rheum 56: 3670-3674.
    • (2007) Arthritis Rheum , vol.56 , pp. 3670-3674
    • Majumdar, M.K.1    Askew, R.2    Schelling, S.3    Stedman, N.4    Blanchet, T.5    Hopkins, B.6    Morris, E.A.7    Glasson, S.S.8
  • 82
    • 0037151084 scopus 로고    scopus 로고
    • Inhibition of ADAM-TS4 and ADAM-TS5 Prevents Aggrecan Degradation in Osteoarthritic Cartilage
    • Malfait A-M, Liu R-Q, Ijiri K, Komiya S, Tortorella MD (2002) Inhibition of ADAM-TS4 and ADAM-TS5 Prevents Aggrecan Degradation in Osteoarthritic Cartilage. J Biol Chem 277: 22201-22208.
    • (2002) J Biol Chem , vol.277 , pp. 22201-22208
    • Malfait, A.-M.1    Liu, R.-Q.2    Ijiri, K.3    Komiya, S.4    Tortorella, M.D.5
  • 83
    • 0033527662 scopus 로고    scopus 로고
    • Recombinant human aggrecan G1-G2 exhibits native binding properties and substrate specificity for matrix metalloproteinases and aggrecanase
    • Mercuri FA, Doege KJ, Arner EC, Pratta MA, Last K, Fosang AJ (1999) Recombinant human aggrecan G1-G2 exhibits native binding properties and substrate specificity for matrix metalloproteinases and aggrecanase. J Biol Chem 274: 32387-32395.
    • (1999) J Biol Chem , vol.274 , pp. 32387-32395
    • Mercuri, F.A.1    Doege, K.J.2    Arner, E.C.3    Pratta, M.A.4    Last, K.5    Fosang, A.J.6
  • 84
    • 0032211766 scopus 로고    scopus 로고
    • Cathepsin B: An alternative protease for the generation of an aggrecan 'metalloproteinase' cleavage neoepitope
    • Mort JS, Magny MC, Lee ER (1998) Cathepsin B: an alternative protease for the generation of an aggrecan 'metalloproteinase' cleavage neoepitope. Biochem J 335: 491-494.
    • (1998) Biochem J , vol.335 , pp. 491-494
    • Mort, J.S.1    Magny, M.C.2    Lee, E.R.3
  • 85
    • 1542390443 scopus 로고    scopus 로고
    • Use of anti-neoepitope antibodies for the analysis of degradative events in cartilage and the molecular basis for neoepitope specificity
    • Mort JS, Flannery CR, Makkerh J, Krupa JC, Lee ER (2003) Use of anti-neoepitope antibodies for the analysis of degradative events in cartilage and the molecular basis for neoepitope specificity. Biochem Soc Symp 70: 107-114.
    • (2003) Biochem Soc Symp , vol.70 , pp. 107-114
    • Mort, J.S.1    Flannery, C.R.2    Makkerh, J.3    Krupa, J.C.4    Lee, E.R.5
  • 87
    • 0033784028 scopus 로고    scopus 로고
    • Calcium pentosan polysulfate inhibits the catabolism of aggrecan in articular cartilage explant cultures
    • Munteanu SE, Ilic MZ, Handley CJ (2000) Calcium pentosan polysulfate inhibits the catabolism of aggrecan in articular cartilage explant cultures. Arthritis Rheum 43: 2211-2218.
    • (2000) Arthritis Rheum , vol.43 , pp. 2211-2218
    • Munteanu, S.E.1    Ilic, M.Z.2    Handley, C.J.3
  • 88
    • 0036701822 scopus 로고    scopus 로고
    • Highly sulfated glycosaminoglycans inhibit aggrecanase degradation of aggrecan by bovine articular cartilage explant cultures
    • Munteanu SE, Ilic MZ, Handley CJ (2002) Highly sulfated glycosaminoglycans inhibit aggrecanase degradation of aggrecan by bovine articular cartilage explant cultures. Matrix Biol 21: 429-440.
    • (2002) Matrix Biol , vol.21 , pp. 429-440
    • Munteanu, S.E.1    Ilic, M.Z.2    Handley, C.J.3
  • 89
    • 0038639763 scopus 로고    scopus 로고
    • Aggrecanases and cartilage matrix degradation
    • Nagase H, Kashiwagi M (2003) Aggrecanases and cartilage matrix degradation. Arthritis Res Ther 5: 94-103.
    • (2003) Arthritis Res Ther , vol.5 , pp. 94-103
    • Nagase, H.1    Kashiwagi, M.2
  • 90
    • 0035837658 scopus 로고    scopus 로고
    • Paradoxical effects of trichostatin A: Inhibition of NF-Y-associated histone acetyltransferase activity, phosphorylation of hGCN5 and downregulation of cyclin A and B1 mRNA
    • Nair AR, Boersma LJ, Schiltz L, Chaudhry MA, Muschel RJ (2001) Paradoxical effects of trichostatin A: inhibition of NF-Y-associated histone acetyltransferase activity, phosphorylation of hGCN5 and downregulation of cyclin A and B1 mRNA. Cancer Lett 166: 55-64.
    • (2001) Cancer Lett , vol.166 , pp. 55-64
    • Nair, A.R.1    Boersma, L.J.2    Schiltz, L.3    Chaudhry, M.A.4    Muschel, R.J.5
  • 91
    • 4344601054 scopus 로고    scopus 로고
    • Mature bovine articular cartilage contains abundant aggrecan that is C-terminally truncated at Ala719-Ala720, a site which is readily cleaved by mcalpain
    • Oshita H, Sandy JD, Suzuki K, Akaike A, Bai Y, Sasaki T, Shimizu K (2004) Mature bovine articular cartilage contains abundant aggrecan that is C-terminally truncated at Ala719-Ala720, a site which is readily cleaved by mcalpain. Biochem J 382: 253-259.
    • (2004) Biochem J , vol.382 , pp. 253-259
    • Oshita, H.1    Sandy, J.D.2    Suzuki, K.3    Akaike, A.4    Bai, Y.5    Sasaki, T.6    Shimizu, K.7
  • 92
    • 0036741135 scopus 로고    scopus 로고
    • Molecular determinants of metalloproteinase substrate specificity: Matrix metalloproteinase substrate binding domains, modules, and exosites
    • Overall CM (2002) Molecular determinants of metalloproteinase substrate specificity: matrix metalloproteinase substrate binding domains, modules, and exosites. Mol Biotechnol 22: 51-86.
    • (2002) Mol Biotechnol , vol.22 , pp. 51-86
    • Overall, C.M.1
  • 93
    • 25644459306 scopus 로고    scopus 로고
    • Collagen and Aggrecan Degradation Is Blocked in Interleukin-1-Treated Cartilage Explants by an Inhibitor of I{kappa}B Kinase through Suppression of Metalloproteinase Expression
    • Pattoli MA, Macmaster JF, Gregor KR, Burke JR (2005) Collagen and Aggrecan Degradation Is Blocked in Interleukin-1-Treated Cartilage Explants by an Inhibitor of I{kappa}B Kinase through Suppression of Metalloproteinase Expression. J Pharmacol Exp Ther 315: 382-388.
    • (2005) J Pharmacol Exp Ther , vol.315 , pp. 382-388
    • Pattoli, M.A.1    Macmaster, J.F.2    Gregor, K.R.3    Burke, J.R.4
  • 94
    • 14944371238 scopus 로고    scopus 로고
    • Analysis of ADAMTS4 and MT4-MMP indicates that both are involved in aggrecanolysis in interleukin-1-treated bovine cartilage
    • Patwari P, Gao G, Lee JH, Grodzinsky AJ, Sandy JD (2005) Analysis of ADAMTS4 and MT4-MMP indicates that both are involved in aggrecanolysis in interleukin-1-treated bovine cartilage. Osteoarthritis Cartilage 13: 269-277.
    • (2005) Osteoarthritis Cartilage , vol.13 , pp. 269-277
    • Patwari, P.1    Gao, G.2    Lee, J.H.3    Grodzinsky, A.J.4    Sandy, J.D.5
  • 96
    • 0024409824 scopus 로고
    • Immunoglobulin fold and tandem repeat structures in proteoglycan N-terminal domains and link protein
    • Perkins SJ, Nealis AS, Dudhia J, Hardingham TE (1989) Immunoglobulin fold and tandem repeat structures in proteoglycan N-terminal domains and link protein. J Mol Biol 206: 737-754.
    • (1989) J Mol Biol , vol.206 , pp. 737-754
    • Perkins, S.J.1    Nealis, A.S.2    Dudhia, J.3    Hardingham, T.E.4
  • 97
    • 34249999133 scopus 로고    scopus 로고
    • Aggrecanolysis in human osteoarthritis: Confocal localization and biochemical characterization of ADAMTS5-hyaluronan complexes in articular cartilages
    • Plaas A, Osborn B, Yoshihara Y, Bai Y, Bloom T, Nelson F, Mikecz K, Sandy JD (2007) Aggrecanolysis in human osteoarthritis: confocal localization and biochemical characterization of ADAMTS5-hyaluronan complexes in articular cartilages. Osteoarthritis Cartilage 15: 719-734.
    • (2007) Osteoarthritis Cartilage , vol.15 , pp. 719-734
    • Plaas, A.1    Osborn, B.2    Yoshihara, Y.3    Bai, Y.4    Bloom, T.5    Nelson, F.6    Mikecz, K.7    Sandy, J.D.8
  • 98
    • 0015643003 scopus 로고
    • Experimentally induced osteoarthritis in the dog
    • Pond MJ, Nuki G (1973) Experimentally induced osteoarthritis in the dog. Ann Rheum Dis 32: 387-388.
    • (1973) Ann Rheum Dis , vol.32 , pp. 387-388
    • Pond, M.J.1    Nuki, G.2
  • 99
    • 21244433240 scopus 로고    scopus 로고
    • N-linked keratan sulfate in the aggrecan interglobular domain potentiates aggrecanase activity
    • Poon CJ, Plaas AH, Keene DR, McQuillan DJ, Last K, Fosang AJ (2005) N-linked keratan sulfate in the aggrecan interglobular domain potentiates aggrecanase activity. J Biol Chem 280: 23615-23621.
    • (2005) J Biol Chem , vol.280 , pp. 23615-23621
    • Poon, C.J.1    Plaas, A.H.2    Keene, D.R.3    McQuillan, D.J.4    Last, K.5    Fosang, A.J.6
  • 101
    • 34848871992 scopus 로고    scopus 로고
    • Low molecular weight isoforms of the aggrecanases are responsible for the cytokine-induced proteolysis of aggrecan in a porcine chondrocyte culture system
    • Powell AJ, Little CB, Hughes CE (2007) Low molecular weight isoforms of the aggrecanases are responsible for the cytokine-induced proteolysis of aggrecan in a porcine chondrocyte culture system. Arthritis Rheum 56: 3010-3019.
    • (2007) Arthritis Rheum , vol.56 , pp. 3010-3019
    • Powell, A.J.1    Little, C.B.2    Hughes, C.E.3
  • 102
    • 0037231877 scopus 로고    scopus 로고
    • Induction of aggrecanase 1 (ADAM-TS4) by interleukin-1 occurs through activation of constitutively produced protein
    • Pratta MA, Scherle PA, Yang G, Liu RQ, Newton RC (2003a) Induction of aggrecanase 1 (ADAM-TS4) by interleukin-1 occurs through activation of constitutively produced protein. Arthritis Rheum 48: 119-133.
    • (2003) Arthritis Rheum , vol.48 , pp. 119-133
    • Pratta, M.A.1    Scherle, P.A.2    Yang, G.3    Liu, R.Q.4    Newton, R.C.5
  • 103
    • 0034671485 scopus 로고    scopus 로고
    • Agerelated changes in aggrecan glycosylation affect cleavage by aggrecanase
    • Pratta MA, Tortorella MD, Arner EC (2000) Agerelated changes in aggrecan glycosylation affect cleavage by aggrecanase. J Biol Chem 275: 39096-39102.
    • (2000) J Biol Chem , vol.275 , pp. 39096-39102
    • Pratta, M.A.1    Tortorella, M.D.2    Arner, E.C.3
  • 105
    • 0022515653 scopus 로고
    • Articular cartilage cultured with interleukin 1. Increased release of link protein, hyaluronate-binding region and other proteoglycan fragments
    • Ratcliffe A, Tyler JA, Hardingham TE (1986) Articular cartilage cultured with interleukin 1. Increased release of link protein, hyaluronate-binding region and other proteoglycan fragments. Biochem J 238: 571-580.
    • (1986) Biochem J , vol.238 , pp. 571-580
    • Ratcliffe, A.1    Tyler, J.A.2    Hardingham, T.E.3
  • 106
    • 26844518429 scopus 로고    scopus 로고
    • Association between the abnormal expression of matrix-degrading enzymes by human osteoarthritic chondrocytes and demethylation of specific CpG sites in the promoter regions
    • Roach HI, Yamada N, Cheung KS, Tilley S, Clarke NM, Oreffo RO, Kokubun S, Bronner F (2005) Association between the abnormal expression of matrix-degrading enzymes by human osteoarthritic chondrocytes and demethylation of specific CpG sites in the promoter regions. Arthritis Rheum 52: 3110-3124.
    • (2005) Arthritis Rheum , vol.52 , pp. 3110-3124
    • Roach, H.I.1    Yamada, N.2    Cheung, K.S.3    Tilley, S.4    Clarke, N.M.5    Oreffo, R.O.6    Kokubun, S.7    Bronner, F.8
  • 109
    • 27244438584 scopus 로고    scopus 로고
    • Lack of CpG island methylator phenotype defines a clinical subtype of T-cell acute lymphoblastic leukemia associated with good prognosis
    • Roman-Gomez J, Jimenez-Velasco A, Agirre X, Prosper F, Heiniger A, Torres A (2005) Lack of CpG island methylator phenotype defines a clinical subtype of T-cell acute lymphoblastic leukemia associated with good prognosis. J Clin Oncol 23: 7043-7049.
    • (2005) J Clin Oncol , vol.23 , pp. 7043-7049
    • Roman-Gomez, J.1    Jimenez-Velasco, A.2    Agirre, X.3    Prosper, F.4    Heiniger, A.5    Torres, A.6
  • 110
    • 0023058313 scopus 로고
    • Arg-Gly-Asp: A versatile cell recognition signal
    • Ruoslahti E, Pierschbacher MD (1986) Arg-Gly-Asp: a versatile cell recognition signal. Cell 44: 517-518.
    • (1986) Cell , vol.44 , pp. 517-518
    • Ruoslahti, E.1    Pierschbacher, M.D.2
  • 111
    • 33947175117 scopus 로고    scopus 로고
    • Increased collagen and aggrecan degradation with age in the joints of Timp3(-/-) mice
    • Sahebjam S, Khokha R, Mort JS (2007) Increased collagen and aggrecan degradation with age in the joints of Timp3(-/-) mice. Arthritis Rheum 56: 905-909.
    • (2007) Arthritis Rheum , vol.56 , pp. 905-909
    • Sahebjam, S.1    Khokha, R.2    Mort, J.S.3
  • 112
    • 0025776382 scopus 로고
    • Catabolism of aggrecan in cartilage explants. Identification of a major cleavage site within the interglobular domain
    • Sandy JD, Neame PJ, Boynton RE, Flannery CR (1991) Catabolism of aggrecan in cartilage explants. Identification of a major cleavage site within the interglobular domain. J Biol Chem 266: 8683-8685.
    • (1991) J Biol Chem , vol.266 , pp. 8683-8685
    • Sandy, J.D.1    Neame, P.J.2    Boynton, R.E.3    Flannery, C.R.4
  • 113
    • 0026682509 scopus 로고
    • 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
    • Sandy JD, Flannery CR, Neame PJ, Lohmander LS (1992) 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: 1512-1516.
    • (1992) J Clin Invest , vol.89 , pp. 1512-1516
    • Sandy, J.D.1    Flannery, C.R.2    Neame, P.J.3    Lohmander, L.S.4
  • 114
    • 0032189902 scopus 로고    scopus 로고
    • Chondrocyte-mediated catabolism of aggrecan: Aggrecanase-dependent cleavage induced by interleukin-1 or retinoic acid can be inhibited by glucosamine
    • Sandy JD, Gamett D, Thompson V, Verscharen C (1998) Chondrocyte-mediated catabolism of aggrecan: aggrecanase-dependent cleavage induced by interleukin-1 or retinoic acid can be inhibited by glucosamine. BiochemJ 335: 59-66.
    • (1998) BiochemJ , vol.335 , pp. 59-66
    • Sandy, J.D.1    Gamett, D.2    Thompson, V.3    Verscharen, C.4
  • 115
    • 0034306104 scopus 로고    scopus 로고
    • The intermediates of aggrecanase-dependent cleavage of aggrecan in rat chondrosarcoma cells treated with interleukin-1
    • Sandy JD, Thompson V, Doege K, Verscharen C (2000) The intermediates of aggrecanase-dependent cleavage of aggrecan in rat chondrosarcoma cells treated with interleukin-1. Biochem J 351: 1-166.
    • (2000) Biochem J , vol.351 , pp. 1-166
    • Sandy, J.D.1    Thompson, V.2    Doege, K.3    Verscharen, C.4
  • 116
    • 0035884605 scopus 로고    scopus 로고
    • 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
    • Sandy JD, Verscharen C (2001) 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: 615-626.
    • (2001) Biochem J , vol.358 , pp. 615-626
    • Sandy, J.D.1    Verscharen, C.2
  • 118
    • 4143129884 scopus 로고    scopus 로고
    • ADAMTS7B, the full-length product of the ADAMTS7 gene, is a chondroitin sulfate proteoglycan containing a mucin domain
    • Somerville RP, Longpré JM, Apel ED, Lewis RM, Wang LW, Sanes JR, Leduc R, Apte SS (2004) ADAMTS7B, the full-length product of the ADAMTS7 gene, is a chondroitin sulfate proteoglycan containing a mucin domain. J Biol Chem 279: 35159-35175.
    • (2004) J Biol Chem , vol.279 , pp. 35159-35175
    • Somerville, R.P.1    Longpré, J.M.2    Apel, E.D.3    Lewis, R.M.4    Wang, L.W.5    Sanes, J.R.6    Leduc, R.7    Apte, S.S.8
  • 123
    • 33746513929 scopus 로고    scopus 로고
    • Estimation of the identity of proteolytic aggrecan fragments using PAGE migration and Western immunoblot
    • Struglics A, Larsson S, Lohmander LS (2006a) Estimation of the identity of proteolytic aggrecan fragments using PAGE migration and Western immunoblot. Osteoarthritis Cartilage 14: 898-905.
    • (2006) Osteoarthritis Cartilage , vol.14 , pp. 898-905
    • Struglics, A.1    Larsson, S.2    Lohmander, L.S.3
  • 124
    • 30544448357 scopus 로고    scopus 로고
    • Human osteoarthritis synovial fluid and joint cartilage contain both aggrecanase- and matrix metalloproteinase-generated aggrecan fragments
    • Struglics A, Larsson S, Pratta MA, Kumar S, Lark MW, Lohmander LS (2006b) Human osteoarthritis synovial fluid and joint cartilage contain both aggrecanase- and matrix metalloproteinase-generated aggrecan fragments. Osteoarthritis Cartilage 14: 101-113.
    • (2006) Osteoarthritis Cartilage , vol.14 , pp. 101-113
    • Struglics, A.1    Larsson, S.2    Pratta, M.A.3    Kumar, S.4    Lark, M.W.5    Lohmander, L.S.6
  • 126
    • 46849083862 scopus 로고    scopus 로고
    • Analysis of aggrecan degradation in human intervertebral disc utilizing neoepitope-specific antibodies
    • Sztrolovics R, Alini M, Mort JS, Roughley PJ (1997a) Analysis of aggrecan degradation in human intervertebral disc utilizing neoepitope-specific antibodies. Trans Orthop Res Soc 22: 147.
    • (1997) Trans Orthop Res Soc , vol.22 , pp. 147
    • Sztrolovics, R.1    Alini, M.2    Mort, J.S.3    Roughley, P.J.4
  • 127
    • 0030931594 scopus 로고    scopus 로고
    • Aggrecan degradation in human intervertebral disc and articular cartilage
    • Sztrolovics R, Alini M, Roughley PJ, Mort JS (1997b) Aggrecan degradation in human intervertebral disc and articular cartilage. Biochem J 326: 235-241.
    • (1997) Biochem J , vol.326 , pp. 235-241
    • Sztrolovics, R.1    Alini, M.2    Roughley, P.J.3    Mort, J.S.4
  • 128
    • 0036499472 scopus 로고    scopus 로고
    • Hyaluronate degradation as an alternative mechanism for proteoglycan release from cartilage during interleukin-1[beta]-stimulated catabolism
    • Sztrolovics R, Recklies AD, Roughley PJ, Mort JS (2002) Hyaluronate degradation as an alternative mechanism for proteoglycan release from cartilage during interleukin-1[beta]-stimulated catabolism. Biochem J 362: 473-479.
    • (2002) Biochem J , vol.362 , pp. 473-479
    • Sztrolovics, R.1    Recklies, A.D.2    Roughley, P.J.3    Mort, J.S.4
  • 130
    • 0035129903 scopus 로고    scopus 로고
    • ADAMTS: A novel family of extracellular matrix proteases
    • Tang BL (2001) ADAMTS: a novel family of extracellular matrix proteases. Int J Biochem Cell Biol 33: 33-44.
    • (2001) Int J Biochem Cell Biol , vol.33 , pp. 33-44
    • Tang, B.L.1
  • 132
    • 35148831210 scopus 로고    scopus 로고
    • Characterization of the human ADAMTS-5 (aggrecanase-2) gene promoter
    • Thirunavukkarasu K, Pei Y, Wei T (2007) Characterization of the human ADAMTS-5 (aggrecanase-2) gene promoter. Mol Biol Rep 34: 225-231.
    • (2007) Mol Biol Rep , vol.34 , pp. 225-231
    • Thirunavukkarasu, K.1    Pei, Y.2    Wei, T.3
  • 133
    • 84961014924 scopus 로고
    • Reversible collapse of rabbit ears after intravenous papain, and prevention of recovery by cortisone
    • Thomas L (1956) Reversible collapse of rabbit ears after intravenous papain, and prevention of recovery by cortisone. J Exp Med 104:245-261.
    • (1956) J Exp Med , vol.104 , pp. 245-261
    • Thomas, L.1
  • 135
    • 0034682773 scopus 로고    scopus 로고
    • The thrombospondin motif of aggrecanase-1 (ADAMTS-4) is critical for aggrecan substrate recognition and cleavage
    • Tortorella M, Pratta M, Liu RQ, Abbaszade I, Ross H, Burn T, Arner E (2000a) The thrombospondin motif of aggrecanase-1 (ADAMTS-4) is critical for aggrecan substrate recognition and cleavage. J Biol Chem 275: 25791-25797.
    • (2000) J Biol Chem , vol.275 , pp. 25791-25797
    • Tortorella, M.1    Pratta, M.2    Liu, R.Q.3    Abbaszade, I.4    Ross, H.5    Burn, T.6    Arner, E.7
  • 137
    • 0034840936 scopus 로고    scopus 로고
    • The role of ADAM-TS4 (aggrecanase-1) and ADAM-TS5 (aggrecanase-2) in a model of cartilage degradation
    • Tortorella MD, Malfait A, Deccico C, Arner E (2001) The role of ADAM-TS4 (aggrecanase-1) and ADAM-TS5 (aggrecanase-2) in a model of cartilage degradation. Osteoarthritis Cartilage 9: 539-552.
    • (2001) Osteoarthritis Cartilage , vol.9 , pp. 539-552
    • Tortorella, M.D.1    Malfait, A.2    Deccico, C.3    Arner, E.4
  • 138
    • 0036775227 scopus 로고    scopus 로고
    • Characterization of human aggrecanase 2 (ADAMTS5): Substrate specificity studies and comparison with aggrecanase 1 (ADAM-TS4)
    • Tortorella MD, Liu RQ, Burn T, Newton RC, Arner E (2002) Characterization of human aggrecanase 2 (ADAMTS5): substrate specificity studies and comparison with aggrecanase 1 (ADAM-TS4). Matrix Biol 21: 499-511.
    • (2002) Matrix Biol , vol.21 , pp. 499-511
    • Tortorella, M.D.1    Liu, R.Q.2    Burn, T.3    Newton, R.C.4    Arner, E.5
  • 140
    • 0031947366 scopus 로고    scopus 로고
    • van Meurs JB, van Lent PL, Singer II, Bayne EK, van de Loo FA, Van Den Berg WB (1998) Interleukin-1 receptor antagonist prevents expression of the metalloproteinase-generated neoepitope VDIPEN in antigen-induced arthritis. Arthritis Rheum 41: 647-656.
    • van Meurs JB, van Lent PL, Singer II, Bayne EK, van de Loo FA, Van Den Berg WB (1998) Interleukin-1 receptor antagonist prevents expression of the metalloproteinase-generated neoepitope VDIPEN in antigen-induced arthritis. Arthritis Rheum 41: 647-656.
  • 141
    • 17044461667 scopus 로고    scopus 로고
    • 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
    • van Meurs J, van Lent P, Stoop R, Holthuysen A, Singer I, Bayne E, Mudgett J, Poole R, Billinghurst C, van der Kraan P, Buma P, van den Berg W (1999a) 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: 2074-2084.
    • (1999) Arthritis Rheum , vol.42 , pp. 2074-2084
    • van Meurs, J.1    van Lent, P.2    Stoop, R.3    Holthuysen, A.4    Singer, I.5    Bayne, E.6    Mudgett, J.7    Poole, R.8    Billinghurst, C.9    van der Kraan, P.10    Buma, P.11    van den Berg, W.12
  • 142
    • 46849086877 scopus 로고    scopus 로고
    • van Meurs JB, van Lent PL, Holthuysen AE, Singer II, Bayne EK, Van Den Berg WB (1999b) Kinetics of aggrecanase- and metalloproteinase-induced neoepitopes in various stages of cartilage destruction in murine arthritis. Arthritis Rheum 42: 1128-1139.
    • van Meurs JB, van Lent PL, Holthuysen AE, Singer II, Bayne EK, Van Den Berg WB (1999b) Kinetics of aggrecanase- and metalloproteinase-induced neoepitopes in various stages of cartilage destruction in murine arthritis.
  • 143
    • 0033032249 scopus 로고    scopus 로고
    • van Meurs JB, van Lent PL, van de Loo AA, Holthuysen AE, Bayne EK, Singer II, Van Den Berg WB (1999c) Increased vulnerability of postarthritic cartilage to a second arthritic insult: accelerated MMP activity in a flare up of arthritis. Ann Rheum Dis 58:3 50-356.
    • van Meurs JB, van Lent PL, van de Loo AA, Holthuysen AE, Bayne EK, Singer II, Van Den Berg WB (1999c) Increased vulnerability of postarthritic cartilage to a second arthritic insult: accelerated MMP activity in a flare up of arthritis. Ann Rheum Dis 58:3 50-356.
  • 146
    • 33745187332 scopus 로고    scopus 로고
    • An alternative spliced transcript of ADAMTS4 is present in human synovium from OA patients
    • Wainwright SD, Bondeson J, Hughes CE (2006) An alternative spliced transcript of ADAMTS4 is present in human synovium from OA patients. Matrix Biol 25: 317-320.
    • (2006) Matrix Biol , vol.25 , pp. 317-320
    • Wainwright, S.D.1    Bondeson, J.2    Hughes, C.E.3
  • 147
    • 2442595171 scopus 로고    scopus 로고
    • Proprotein convertase furin interacts with and cleaves pro-ADAMTS4 (Aggrecanase-1) in the trans-Golgi network
    • Wang P, Tortorella M, England K, Malfait AM, Thomas G, Arner EC, Pei D (2004a) Proprotein convertase furin interacts with and cleaves pro-ADAMTS4 (Aggrecanase-1) in the trans-Golgi network. J Biol Chem 279: 15434-15440.
    • (2004) J Biol Chem , vol.279 , pp. 15434-15440
    • Wang, P.1    Tortorella, M.2    England, K.3    Malfait, A.M.4    Thomas, G.5    Arner, E.C.6    Pei, D.7
  • 149
    • 34547125794 scopus 로고    scopus 로고
    • TIMP-3 inhibition of ADAMTS-4 (Aggrecanase-1) is modulated by interactions between aggrecan and the C-terminal domain of ADAMTS-4
    • Wayne GJ, Deng SJ, Amour A, Borman S, Matico R, Carter HL, Murphy G (2007) TIMP-3 inhibition of ADAMTS-4 (Aggrecanase-1) is modulated by interactions between aggrecan and the C-terminal domain of ADAMTS-4. J Biol Chem 282:20991-20998.
    • (2007) J Biol Chem , vol.282 , pp. 20991-20998
    • Wayne, G.J.1    Deng, S.J.2    Amour, A.3    Borman, S.4    Matico, R.5    Carter, H.L.6    Murphy, G.7
  • 152
    • 0028097742 scopus 로고
    • Identification of a common hyaluronan binding motif in the hyaluronan binding proteins RHAMM, CD44 and link protein
    • Yang B, Yang BL, Savani RC, Turley EA (1994) Identification of a common hyaluronan binding motif in the hyaluronan binding proteins RHAMM, CD44 and link protein. EMBO J 13: 286-296.
    • (1994) EMBO J , vol.13 , pp. 286-296
    • Yang, B.1    Yang, B.L.2    Savani, R.C.3    Turley, E.A.4
  • 156
    • 0034613296 scopus 로고    scopus 로고
    • TIMP-3 binds to sulfated glycosaminoglycans of the extracellular matrix
    • Yu WH, Yu Ss, Meng Q, Brew K, Woessner JF, Jr. (2000) TIMP-3 binds to sulfated glycosaminoglycans of the extracellular matrix. J Biol Chem 275: 31226-31232.
    • (2000) J Biol Chem , vol.275 , pp. 31226-31232
    • Yu, W.H.1    Yu, S.2    Meng, Q.3    Brew, K.4    Woessner Jr., J.F.5
  • 157
    • 33644883338 scopus 로고    scopus 로고
    • Glycosaminoglycan-binding properties and aggrecanase activities of truncated ADAMTSs: Comparative analyses with ADAMTS-5, -9, -16 and -18
    • Zeng W, Corcoran C, Collins-Racie LA, LaVallie ER, Morris EA, Flannery CR (2006) Glycosaminoglycan-binding properties and aggrecanase activities of truncated ADAMTSs: comparative analyses with ADAMTS-5, -9, -16 and -18. Biochim Biophys Acta 1760: 517-524.
    • (2006) Biochim Biophys Acta , vol.1760 , pp. 517-524
    • Zeng, W.1    Corcoran, C.2    Collins-Racie, L.A.3    LaVallie, E.R.4    Morris, E.A.5    Flannery, C.R.6
  • 158
    • 43749117128 scopus 로고    scopus 로고
    • Functional differences of the catalytic and noncatalytic domains in human ADAMTS-4 and ADAMTS-5 in aggrecanolytic activity
    • in press
    • Fushimi K, Troeberg L, Nakamura H, Lim NH, Nagase H (2008) Functional differences of the catalytic and noncatalytic domains in human ADAMTS-4 and ADAMTS-5 in aggrecanolytic activity. J Biol Chem, in press.
    • (2008) J Biol Chem
    • Fushimi, K.1    Troeberg, L.2    Nakamura, H.3    Lim, N.H.4    Nagase, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.