메뉴 건너뛰기




Volumn 6, Issue 3, 2011, Pages 388-404

Investigating ADAMTS-mediated aggrecanolysis in mouse cartilage

Author keywords

[No Author keywords available]

Indexed keywords

AGGRECANASE;

EID: 79952405776     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2010.179     Document Type: Article
Times cited : (61)

References (76)
  • 1
    • 0000417267 scopus 로고    scopus 로고
    • (eds. Caterson, B., Archer, C., Benjamin, M. & Ralph, J.) (Harwood Academic Publishers
    • Hascall, V.C., Sandy, J.D. & Handley, C.J. In Biology of the Synovial Joint (eds. Caterson, B., Archer, C., Benjamin, M. & Ralph, J.) (Harwood Academic Publishers, 1999).
    • (1999) Biology of the Synovial Joint
    • Hascall, V.C.1    Sandy, J.D.2    Handley, C.J.3
  • 2
    • 0034253761 scopus 로고    scopus 로고
    • Mechanisms involved in cartilage proteoglycan catabolism
    • DOI 10.1016/S0945-053X(00)00078-0, PII S0945053X00000780
    • Caterson, B., Flannery, C.R., Hughes, C.E. & Little, C.B. Mechanisms involved in cartilage proteoglycan catabolism. Matrix Biol. 19, 333-344 (2000). (Pubitemid 30665657)
    • (2000) Matrix Biology , vol.19 , Issue.4 , pp. 333-344
    • Caterson, B.1    Flannery, C.R.2    Hughes, C.E.3    Little, C.B.4
  • 3
    • 0025968335 scopus 로고
    • Effect of interleukin-1 and insulin-like growth factor-1 on the degradation and turnover of proteoglycan and hyaluronate in pig articular cartilage in explant culture
    • Fosang, AJ., Tyler, J.A. & Hardingham, T.E. Effect of interleukin-1 and insulin-like growth factor-1 on the degradation and turnover of proteoglycan and hyaluronate in pig articular cartilage in explant culture. Matrix 11, 17-24 (1991).
    • (1991) Matrix , vol.11 , pp. 17-24
    • Fosang, A.J.1    Tyler, J.A.2    Hardingham, T.E.3
  • 4
    • 0034693231 scopus 로고    scopus 로고
    • Generation and novel distribution of matrix metalloproteinase-derived aggrecan fragments in porcine cartilage explants
    • Fosang, AJ. et al. Generation and novel distribution of matrix metalloproteinase-derived aggrecan fragments in porcine cartilage explants. J. Biol. Chem. 275, 33027-33037 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 33027-33037
    • Fosang, A.J.1
  • 5
    • 0034840936 scopus 로고    scopus 로고
    • The role of ADAM-TS4 (aggrecanase-1) and ADAM-TS5 (aggrecanase-2) in a model of cartilage degradation
    • DOI 10.1053/joca.2001.0427
    • Tortorella, M.D., Malfait, A., Deccico, C & Arner, E. The role of ADAM-TS4 (aggrecanase-1) and ADAM-TS5 (aggrecanase-2) in a model of cartilage degradation. Osteoarthr. Cartil. 9, 539-552 (2001). (Pubitemid 32842633)
    • (2001) Osteoarthritis and Cartilage , vol.9 , Issue.6 , pp. 539-552
    • Tortorella, M.D.1    Malfait, A.-M.2    Deccico, C.3    Arner, E.4
  • 6
    • 50949112558 scopus 로고    scopus 로고
    • Characterization of an ADAMTS-5-mediated cleavage site in aggrecan in OSM-stimulated bovine cartilage
    • Durigova, M. et al. Characterization of an ADAMTS-5-mediated cleavage site in aggrecan in OSM-stimulated bovine cartilage. Osteoarthr. Cartil. 16, 1245-1252 (2008).
    • (2008) Osteoarthr. Cartil. , vol.16 , pp. 1245-1252
    • Durigova, M.1
  • 7
    • 0036499471 scopus 로고    scopus 로고
    • The mechanism of aggrecan release from cartilage differs with tissue origin and the agent used to stimulate catabolism
    • DOI 10.1042/0264-6021:3620465
    • Sztrolovics, R., White, RJ., Roughley, PJ. & Mort, J.S. The mechanism of aggrecan release from cartilage differs with tissue origin and the agent used to stimulate catabolism. Biochem. J. 362, 465-472 (2002). (Pubitemid 34214490)
    • (2002) Biochemical Journal , vol.362 , Issue.2 , pp. 465-472
    • Sztrolovics, R.1    White, R.J.2    Roughley, P.J.3    Mort, J.S.4
  • 8
    • 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
    • DOI 10.1042/0264-6021:3580615
    • Sandy, J.D. & Verscharen, C Analysis of aggrecan in human knee cartilage and synovial fuid 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). (Pubitemid 32896949)
    • (2001) Biochemical Journal , vol.358 , Issue.3 , pp. 615-626
    • Sandy, J.D.1    Verscharen, C.2
  • 10
    • 0025776382 scopus 로고
    • Catabolism of aggrecan in cartilage expiants: Identification of a major cleavage site within the interglobular domain
    • Sandy, J.D., Neame, P.J., Boynton, R.E. & Flannery, C.R. Catabolism of aggrecan in cartilage explants. Identifcation of a major cleavage site within the interglobular domain. J. Biol. Chem. 266, 8683-8685 (1991). (Pubitemid 21906567)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.14 , pp. 8683-8685
    • Sandy, J.D.1    Neame, P.J.2    Boynton, R.E.3    Flannery, C.R.4
  • 11
    • 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, C.A. 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 (Part 2): 589-593 (1992).
    • (1992) Biochem. J. , vol.284 , Issue.PART 2 , pp. 589-593
    • Loulakis, P.1    Shrikhande, A.2    Davis, G.3    Maniglia, C.A.4
  • 14
    • 34247891816 scopus 로고    scopus 로고
    • ADAMTS-5 deficiency does not block aggrecanolysis at preferred cleavage sites in the chondroitin sulfate-rich region of aggrecan
    • DOI 10.1074/jbc.M605750200
    • East, CJ., Stanton, H., Golub, S.B., Rogerson, F.M. & Fosang, AJ. ADAMTS-5 defciency does not block aggrecanolysis at preferred cleavage sites in the chondroitin sulphate-rich region of aggrecan. J. Biol. Chem. 282, 8632-8640 (2007). (Pubitemid 47093500)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.12 , pp. 8632-8640
    • East, C.J.1    Stanton, H.2    Golub, S.B.3    Rogerson, F.M.4    Fosang, A.J.5
  • 15
    • 38049115682 scopus 로고    scopus 로고
    • Distinguishing aggrecan loss from aggrecan proteolysis in ADAMTS-4 and ADAMTS-5 single and double defcient mice
    • Ilic, M.Z., East, C.J., Rogerson, F.M., Fosang, AJ. & Handley, C.J. Distinguishing aggrecan loss from aggrecan proteolysis in ADAMTS-4 and ADAMTS-5 single and double defcient mice. J. Biol. Chem. 282, 37420-37428 (2007).
    • (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
  • 19
    • 0019914963 scopus 로고
    • A direct spectrophotometric microassay for sulfated glycosaminoglycans in cartilage cultures
    • Farndale, R.W., Sayers, C.A. & Barrett, A.J. A direct spectrophotometric microassay for sulfated glycosaminoglycans in cartilage cultures. Connect. Tissue Res. 9, 247-248 (1982). (Pubitemid 12009669)
    • (1982) Connective Tissue Research , vol.9 , Issue.4 , pp. 247-248
    • Farndale, R.W.1    Sayers, C.A.2    Barrett, A.J.3
  • 20
    • 0023734876 scopus 로고
    • Increased concentrations of proteoglycan components in the synovial fuids of patients with acute but not chronic joint disease
    • Ratcliffe, A., Doherty, M., Maini, R.N. & Hardingham, T.E. Increased concentrations of proteoglycan components in the synovial fuids of patients with acute but not chronic joint disease. Ann. Rheum. Dis. 47, 826-832 (1988).
    • (1988) Ann. Rheum. Dis. , vol.47 , pp. 826-832
    • Ratcliffe, A.1    Doherty, M.2    Maini, R.N.3    Hardingham, T.E.4
  • 21
    • 0022552896 scopus 로고
    • Improved quantitation and discrimination of sulphate glycosaminoglycans by use of dimethylmethylene blue
    • DOI 10.1016/0304-4165(86)90306-5
    • Farndale, R.W., Buttle, DJ. & Barrett, A.J. Improved quantitation and discrimination of sulphated glycosaminoglycans by use of dimethylmethylene blue. Biochim. Biophys. Acta 883, 173-177 (1986). (Pubitemid 16027978)
    • (1986) Biochimica et Biophysica Acta - General Subjects , vol.883 , Issue.2 , pp. 173-177
    • Farndale, R.W.1    Buttle, D.J.2    Barrett, A.J.3
  • 22
    • 0025964961 scopus 로고
    • Human cartilage is degraded by rheumatoid arthritis synovial fuid but not by recombinant cytokines in vitro
    • Hollander, A.P., Atkins, R.M., Eastwood, D.M., Dieppe, P.A. & Elson, CJ. Human cartilage is degraded by rheumatoid arthritis synovial fuid but not by recombinant cytokines in vitro. Clin. Exp. Immunol. 83, 52-57 (1991).
    • (1991) Clin. Exp. Immunol. , vol.83 , pp. 52-57
    • Hollander, A.P.1    Atkins, R.M.2    Eastwood, D.M.3    Dieppe, P.A.4    Elson, C.J.5
  • 25
    • 0036775227 scopus 로고    scopus 로고
    • Characterization of human aggrecanase 2 (ADAM-TS5): Substrate specificity studies and comparison with aggrecanase 1 (ADAM-TS4)
    • DOI 10.1016/S0945-053X(02)00069-0, PII S0945053X02000690
    • Tortorella, M.D., Liu, R.Q., Burn, T., Newton, R.C. & Arner, E. Characterization of human aggrecanase 2 (ADAM-TS5): substrate specifcity studies and comparison with aggrecanase 1 (ADAM-TS4). Matrix Biol. 21, 499-511 (2002). (Pubitemid 35248275)
    • (2002) Matrix Biology , vol.21 , Issue.6 , pp. 499-511
    • Tortorella, M.D.1    Liu, R.-Q.2    Burn, T.3    Newton, R.C.4    Arner, E.5
  • 26
    • 0034306104 scopus 로고    scopus 로고
    • The intermediates of aggrecanase-dependent cleavage of aggrecan in rat chondrosarcoma cells treated with interleukin-1
    • Sandy, J.D., Thompson, V., Doege, K. & Verscharen, C The intermediates of aggrecanase-dependent cleavage of aggrecan in rat chondrosarcoma cells treated with interleukin-1. Biochem. J. 351, 1-166 (2000).
    • (2000) Biochem. J. , vol.351 , pp. 1-166
    • Sandy, J.D.1    Thompson, V.2    Doege, K.3    Verscharen, C.4
  • 27
    • 0019134427 scopus 로고
    • Immunological determinants of proteoglycans. Antibodies against the unsaturated oligosaccharide products of chondroitinase ABC-digested cartilage proteoglycans
    • Christner, J.E., Caterson, B. & Baker, J.R. Immunological determinants of proteoglycans. Antibodies against the unsaturated oligosaccharide products of chondroitinase ABC-digested cartilage proteoglycans. J. Biol. Chem. 255, 7102-7105 (1980). (Pubitemid 11232873)
    • (1980) Journal of Biological Chemistry , vol.255 , Issue.15 , pp. 7102-7105
    • Christner, J.E.1    Caterson, B.2    Baker, J.R.3
  • 29
    • 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, J.D., Gamett, D., Thompson, V. & Verscharen, C Chondrocyte-mediated catabolism of aggrecan: aggrecanase-dependent cleavage induced by interleukin-1 or retinoic acid can be inhibited by glucosamine. Biochem. J. 335, 59-66 (1998). (Pubitemid 28477050)
    • (1998) Biochemical Journal , vol.335 , Issue.1 , pp. 59-66
    • Sandy, J.D.1    Gamett, D.2    Thompson, V.3    Verscharen, C.4
  • 30
    • 61549089342 scopus 로고    scopus 로고
    • Western blot quantifcation of aggrecan fragments in human synovial fuid indicates differences in fragment patterns between joint diseases
    • Struglics, A., Larsson, S., Hansson, M. & Lohmander, L.S. Western blot quantifcation of aggrecan fragments in human synovial fuid indicates differences in fragment patterns between joint diseases. Osteoarthr. Cartil. 17, 497-506 (2009).
    • (2009) Osteoarthr. Cartil. , vol.17 , pp. 497-506
    • Struglics, A.1    Larsson, S.2    Hansson, M.3    Lohmander, L.S.4
  • 31
    • 50549161624 scopus 로고
    • A modifed uronic acid carbazole reaction
    • Bitter, T. & Muir, H.M. A modifed uronic acid carbazole reaction. Anal. Biochem. 4, 330-334 (1962).
    • (1962) Anal. Biochem. , vol.4 , pp. 330-334
    • Bitter, T.1    Muir, H.M.2
  • 32
    • 0027300720 scopus 로고
    • Simultaneous preparation and quantitation of proteoglycans by precipitation with Alcian blue
    • DOI 10.1006/abio.1993.1197
    • Björnsson, S. Simultaneous preparation and quantitation of proteoglycans by precipitation with alcian blue. Anal. Biochem. 210, 282-291 (1993). (Pubitemid 23171019)
    • (1993) Analytical Biochemistry , vol.210 , Issue.2 , pp. 282-291
    • Bjornsson, S.1
  • 33
    • 77956010112 scopus 로고    scopus 로고
    • Development of a novel clinical biomarker assay to detect and quantify aggrecanase-generated aggrecan fragments in human synovial fuid, serum and urine
    • Swearingen, C et al. Development of a novel clinical biomarker assay to detect and quantify aggrecanase-generated aggrecan fragments in human synovial fuid, serum and urine. Osteoarthr. Cartil. 18, 1150-1158 (2010).
    • (2010) Osteoarthr. Cartil. , vol.18 , pp. 1150-1158
    • Swearingen, C.1
  • 34
    • 0028919163 scopus 로고
    • Monoclonal antibodies that specifcally recognise neo-epitope sequences generated by 'aggrecanase' and matrix metalloproteinase cleavage of aggrecan: Application to catabolism in situ and in vitro
    • Hughes, C.E., Caterson, B., Fosang, AJ., Roughley, PJ. & Mort, J.S. Monoclonal antibodies that specifcally 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).
    • (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
  • 35
    • 77956230956 scopus 로고    scopus 로고
    • An immunoaffnity LC/MS/MS Assay for detection of endogenous aggrecan fragments in biological fuids. Use as a biomarker for aggrecanase activity and cartilage degradation
    • Dufeld, D.R. et al. An immunoaffnity LC/MS/MS Assay for detection of endogenous aggrecan fragments in biological fuids. Use as a biomarker for aggrecanase activity and cartilage degradation. Anal. Biochem. 406, 113-123 (2010).
    • (2010) Anal. Biochem. , vol.406 , pp. 113-123
    • Dufeld, D.R.1
  • 36
    • 16244421736 scopus 로고    scopus 로고
    • Transcriptional regulation of chondrocyte maturation: Potential involvement of transcription factors in OA pathogenesis
    • DOI 10.1016/j.mam.2005.01.003, Musculoskeletal System: Kolecular Changes Associated with Aging
    • Drissi, H., Zuscik, M., Rosier, R. & O'Keefe, R. Transcriptional regulation of chondrocyte maturation: potential involvement of transcription factors in OA pathogenesis. Mol. Aspects Med. 26, 169-179 (2005). (Pubitemid 40462025)
    • (2005) Molecular Aspects of Medicine , vol.26 , Issue.3 , pp. 169-179
    • Drissi, H.1    Zuscik, M.2    Rosier, R.3    O'Keefe, R.4
  • 39
    • 69949118870 scopus 로고    scopus 로고
    • Syndecan-4 regulates ADAMTS-5 activation and cartilage breakdown in osteoarthritis
    • Echtermeyer, F. et al. Syndecan-4 regulates ADAMTS-5 activation and cartilage breakdown in osteoarthritis. Nat Med. 15, 1072-1077 (2009).
    • (2009) Nat Med. , vol.15 , pp. 1072-1077
    • Echtermeyer, F.1
  • 40
    • 77953067173 scopus 로고    scopus 로고
    • MicroRNA-140 plays dual roles in both cartilage development and homeostasis
    • Miyaki, S. et al. MicroRNA-140 plays dual roles in both cartilage development and homeostasis. Genes Dev. 24, 1173-1185 (2010).
    • (2010) Genes Dev. , vol.24 , pp. 1173-1185
    • Miyaki, S.1
  • 41
    • 56749175339 scopus 로고    scopus 로고
    • Defning the roles of infammatory and anabolic cytokines in cartilage metabolism
    • Goldring, M.B., Otero, M., Tsuchimochi, K., Ijiri, K. & Li, Y. Defning the roles of infammatory and anabolic cytokines in cartilage metabolism. Ann Rheum Dis. 67 (Suppl 3), iii75-iii82 (2008).
    • (2008) Ann Rheum Dis. , vol.67 , Issue.SUPPL. 3
    • Goldring, M.B.1    Otero, M.2    Tsuchimochi, K.3    Ijiri, K.4    Li, Y.5
  • 42
    • 61749093337 scopus 로고    scopus 로고
    • Wnt signaling and osteoarthritis
    • Luyten, F.P., Tylzanowski, P. & Lories, RJ. Wnt signaling and osteoarthritis. Bone 44, 522-527 (2009).
    • (2009) Bone , vol.44 , pp. 522-527
    • Luyten, F.P.1    Tylzanowski, P.2    Lories, R.J.3
  • 43
    • 49149118566 scopus 로고    scopus 로고
    • Wnt signaling in cartilage development and degeneration
    • Chun, J.S., Oh, H., Yang, S. & Park, M. Wnt signaling in cartilage development and degeneration. BMB Rep. 41, 485-494 (2008).
    • (2008) BMB Rep. , vol.41 , pp. 485-494
    • Chun, J.S.1    Oh, H.2    Yang, S.3    Park, M.4
  • 44
    • 56649084972 scopus 로고    scopus 로고
    • Integrative microRNA and proteomic approaches identify novel osteoarthritis genes and their collaborative metabolic and infammatory networks
    • Iliopoulos, D., Malizos, K.N., Oikonomou, P. & Tsezou, A. Integrative microRNA and proteomic approaches identify novel osteoarthritis genes and their collaborative metabolic and infammatory networks. PLoS ONE 3, e3740 (2008).
    • (2008) PLoS ONE , vol.3
    • Iliopoulos, D.1    Malizos, K.N.2    Oikonomou, P.3    Tsezou, A.4
  • 45
    • 69449103973 scopus 로고    scopus 로고
    • MicroRNA-140 is expressed in differentiated human articular chondrocytes and modulates interleukin-1 responses
    • Miyaki, S. et al. MicroRNA-140 is expressed in differentiated human articular chondrocytes and modulates interleukin-1 responses. Arthritis Rheum. 60, 2723-2730 (2009).
    • (2009) Arthritis Rheum. , vol.60 , pp. 2723-2730
    • Miyaki, S.1
  • 46
    • 55349088908 scopus 로고    scopus 로고
    • Exuberant expression of chemokine genes by adult human articular chondrocytes in response to IL-1beta
    • Sandell, LJ. et al. Exuberant expression of chemokine genes by adult human articular chondrocytes in response to IL-1beta. Osteoarthr. Cartil. 16, 1560-1571 (2008).
    • (2008) Osteoarthr. Cartil. , vol.16 , pp. 1560-1571
    • Sandell, L.J.1
  • 47
    • 34447509660 scopus 로고    scopus 로고
    • Global analyses of gene expression in early experimental osteoarthritis
    • DOI 10.1002/art.22711
    • Appleton, C.T., Pitelka, V., Henry, J. & Beier, F. Global analyses of gene expression in early experimental osteoarthritis. Arthritis Rheum. 56, 1854-1868 (2007). (Pubitemid 47110385)
    • (2007) Arthritis and Rheumatism , vol.56 , Issue.6 , pp. 1854-1868
    • Appleton, C.T.G.1    Pitelka, V.2    Henry, J.3    Beier, F.4
  • 48
    • 43949145269 scopus 로고    scopus 로고
    • Identification of the molecular response of articular cartilage to injury, by microarray screening: Wnt-16 expression and signaling after injury and in osteoarthritis
    • DOI 10.1002/art.23444
    • Dell'accio, F., De Bari, C., Eltawil, N.M., Vanhummelen, P. & Pitzalis, C Identifcation of the molecular response of articular cartilage to injury, by microarray screening: Wnt-16 expression and signaling after injury and in osteoarthritis. Arthritis Rheum. 58, 1410-1421 (2008). (Pubitemid 351705930)
    • (2008) Arthritis and Rheumatism , vol.58 , Issue.5 , pp. 1410-1421
    • Dell'Accio, F.1    De Bari, C.2    Eltawil, N.M.3    Vanhummelen, P.4    Pitzalis, C.5
  • 49
    • 41349116135 scopus 로고    scopus 로고
    • The eukaryotic genome as an RNA machine
    • DOI 10.1126/science.1155472
    • Amaral, P.P., Dinger, M.E., Mercer, T.R. & Mattick, J.S. The eukaryotic genome as an RNA machine. Science 319, 1787-1789 (2008). (Pubitemid 351451554)
    • (2008) Science , vol.319 , Issue.5871 , pp. 1787-1789
    • Amaral, P.P.1    Dinger, M.E.2    Mercer, T.R.3    Mattick, J.S.4
  • 50
    • 0029085839 scopus 로고
    • Development of a cleavage site-specifc monoclonal antibody for detecting metalloproteinase-derived aggrecan fragments: Detection of fragments in human synovial fuids
    • Fosang, AJ., Last, K., Gardiner, P., Jackson, D.C. & Brown, L. Development of a cleavage site-specifc monoclonal antibody for detecting metalloproteinase-derived aggrecan fragments: detection of fragments in human synovial fuids. Biochem. J. 310, 337-343 (1995).
    • (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
  • 51
    • 0033527662 scopus 로고    scopus 로고
    • Recombinant human aggrecan G1-G2 exhibits native binding properties and substrate specifcity for matrix metalloproteinases and aggrecanase
    • Mercuri, F.A. et al. Recombinant human aggrecan G1-G2 exhibits native binding properties and substrate specifcity for matrix metalloproteinases and aggrecanase. J. Biol. Chem. 274, 32387-32395 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 32387-32395
    • Mercuri, F.A.1
  • 52
    • 77950347524 scopus 로고    scopus 로고
    • Neoepitope antibodies against MMP-cleaved and aggrecanase-cleaved aggrecan
    • Fosang, AJ. et al. Neoepitope antibodies against MMP-cleaved and aggrecanase-cleaved aggrecan. Methods Mol. Biol. 622, 312-347 (2010).
    • (2010) Methods Mol. Biol. , vol.622 , pp. 312-347
    • Fosang, A.J.1
  • 53
    • 0028968899 scopus 로고
    • Quantifcation of a matrix metalloproteinase-generated aggrecan G1 fragment using monospecifc anti-peptide serum
    • Lark, M.W. et al. Quantifcation of a matrix metalloproteinase-generated aggrecan G1 fragment using monospecifc anti-peptide serum. Biochem. J. 307, 245-252 (1995).
    • (1995) Biochem. J. , vol.307 , pp. 245-252
    • Lark, M.W.1
  • 55
    • 0028871942 scopus 로고
    • Use of an antibody against the matrix metalloproteinase-generated aggrecan neoepitope FVDIPEN-COOH to assess the effects of stromelysin in a rabbit model of cartilage degradation
    • Bayne, E.K. et al. Use of an antibody against the matrix metalloproteinase-generated aggrecan neoepitope FVDIPEN-COOH to assess the effects of stromelysin in a rabbit model of cartilage degradation. Arthritis Rheum. 38, 1400-1409 (1995).
    • (1995) Arthritis Rheum. , vol.38 , pp. 1400-1409
    • Bayne, E.K.1
  • 57
    • 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
    • DOI 10.1002/1529-0131(200106)44:6<1455::AID-ART241>3.0.CO;2-J
    • Chambers, M.G. et al. 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). (Pubitemid 32537547)
    • (2001) Arthritis and Rheumatism , vol.44 , Issue.6 , 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
  • 58
    • 0031688163 scopus 로고    scopus 로고
    • 342 bond, as an indicator of the location of the metalloproteinases active in the lysis of the rat growth plate
    • DOI 10.1002/(SICI)1097-0185(199809)252:1<117::AID-AR10>3.0.CO;2-R
    • Lee, E.R. et al. 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). (Pubitemid 28397565)
    • (1998) Anatomical Record , vol.252 , Issue.1 , 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
  • 61
    • 4344601054 scopus 로고    scopus 로고
    • 720, a site which is readily cleaved by m-calpain
    • DOI 10.1042/BJ20040113
    • Oshita, H. et al. Mature bovine articular cartilage contains abundant aggrecan that is C-terminally truncated at Ala719-Ala720, a site which is readily cleaved by m-calpain. Biochem. J. 382, 253-259 (2004). (Pubitemid 39141589)
    • (2004) Biochemical Journal , vol.382 , Issue.1 , 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
  • 62
    • 77956673890 scopus 로고    scopus 로고
    • Calpain is involved in C-terminal truncation of human aggrecan
    • Struglics, A. & Hansson, M. Calpain is involved in C-terminal truncation of human aggrecan. Biochem. J. 430, 531-538 (2010).
    • (2010) Biochem. J. , vol.430 , pp. 531-538
    • Struglics, A.1    Hansson, M.2
  • 63
    • 70350448424 scopus 로고    scopus 로고
    • Identifcation of a novel HtrA1-susceptible cleavage site in human aggrecan: Evidence for the involvement of HtrA1 in aggrecan proteolysis in vivo
    • Chamberland, A. et al. Identifcation of a novel HtrA1-susceptible cleavage site in human aggrecan: evidence for the involvement of HtrA1 in aggrecan proteolysis in vivo. J. Biol. Chem. 284, 27352-27359 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 27352-27359
    • Chamberland, A.1
  • 64
    • 77955438432 scopus 로고    scopus 로고
    • Inhibition of bone resorption blunts osteoarthritis in mice with high bone remodelling
    • Kadri, A. et al. Inhibition of bone resorption blunts osteoarthritis in mice with high bone remodelling. Ann. Rheum. Dis. 69, 1533-1538 (2010).
    • (2010) Ann. Rheum. Dis. , vol.69 , pp. 1533-1538
    • Kadri, A.1
  • 65
    • 78249235622 scopus 로고    scopus 로고
    • Cytokine-induced increases in ADAMTS-4 mRNA expression do not lead to increased aggrecanase activity in ADAMTS-5-defcient mice
    • Rogerson, F.M., Chung, Y.M., Deutscher, M.E., Last, K. & Fosang, AJ. Cytokine-induced increases in ADAMTS-4 mRNA expression do not lead to increased aggrecanase activity in ADAMTS-5-defcient mice. Arthritis Rheum. 62, 3365-3373 (2010).
    • (2010) Arthritis Rheum. , vol.62 , pp. 3365-3373
    • Rogerson, F.M.1    Chung, Y.M.2    Deutscher, M.E.3    Last, K.4    Fosang, A.J.5
  • 66
    • 72149123653 scopus 로고    scopus 로고
    • Reporting laboratory experiments
    • Ranstam, J. Reporting laboratory experiments. Osteoarthr. Cartil. 18, 3-4 (2010).
    • (2010) Osteoarthr. Cartil. , vol.18 , pp. 3-4
    • Ranstam, J.1
  • 67
    • 0032076280 scopus 로고    scopus 로고
    • Cytokine-induced cartilage proteoglycan degradation is mediated by aggrecanase
    • DOI 10.1053/joca.1998.0114
    • Arner, E.C., Hughes, C.E., Decicco, C.P., Caterson, B. & Tortorella, M.D. Cytokine-induced cartilage proteoglycan degradation is mediated by aggrecanase. Osteoarthr. Cartil. 6, 214-228 (1998). (Pubitemid 28255112)
    • (1998) Osteoarthritis and Cartilage , vol.6 , Issue.3 , pp. 214-228
    • Arner, E.C.1    Hughes, C.E.2    Decicco, C.P.3    Caterson, B.4    Tortorella, M.D.5
  • 68
    • 0345735683 scopus 로고    scopus 로고
    • TIMP-3 inhibits aggrecanase-mediated glycosaminoglycan release from cartilage explants stimulated by catabolic factors
    • DOI 10.1016/S0014-5793(03)01295-X
    • Gendron, C., Kashiwagi, M., Hughes, C., Caterson, B. & Nagase, H. TIMP-3 inhibits aggrecanase-mediated glycosaminoglycan release from cartilage explants stimulated by catabolic factors. FEBS Lett 555, 431-436 (2003). (Pubitemid 37532588)
    • (2003) FEBS Letters , vol.555 , Issue.3 , pp. 431-436
    • Gendron, C.1    Kashiwagi, M.2    Hughes, C.3    Caterson, B.4    Nagase, H.5
  • 69
    • 0033571592 scopus 로고    scopus 로고
    • Aggrecanase versus matrix metalloproteinases in the catabolism of the interglobular domain of aggrecan in vitro
    • Little, C.B. et al. Aggrecanase versus matrix metalloproteinases in the catabolism of the interglobular domain of aggrecan in vitro. Biochem. J. 344, 62-68 (1999).
    • (1999) Biochem. J. , vol.344 , pp. 62-68
    • Little, C.B.1
  • 70
    • 67349182842 scopus 로고    scopus 로고
    • Removal of O-linked and N-linked oligosaccharides is required for optimum detection of NITEGE neoepitope on ADAMTS4-digested fetal aggrecans: Implications for specifc N-linked glycan-dependent aggrecanolysis at Glu373-Ala 374
    • Frank, J.E., Thompson, V.P., Brown, M.P. & Sandy, J.D. Removal of O-linked and N-linked oligosaccharides is required for optimum detection of NITEGE neoepitope on ADAMTS4-digested fetal aggrecans: implications for specifc N-linked glycan-dependent aggrecanolysis at Glu373-Ala374. Osteoarthr. Cartil. 17, 777-781 (2009).
    • (2009) Osteoarthr. Cartil. , vol.17 , pp. 777-781
    • Frank, J.E.1    Thompson, V.P.2    Brown, M.P.3    Sandy, J.D.4
  • 71
    • 0028982223 scopus 로고
    • N-and O-linked keratan sulfate on the hyaluronan binding region of aggrecan from mature and immature bovine cartilage
    • Barry, F.P., Rosenberg, L.C., Gaw, J.U., Koob, TJ. & Neame, PJ. 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).
    • (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
  • 72
    • 30544448357 scopus 로고    scopus 로고
    • Human osteoarthritis synovial fluid and joint cartilage contain both aggrecanase- and matrix metalloproteinase-generated aggrecan fragments
    • DOI 10.1016/j.joca.2005.07.018, PII S1063458405002025
    • Struglics, A. et al. Human osteoarthritis synovial fuid and joint cartilage contain both aggrecanase-and matrix metalloproteinase-generated aggrecan fragments. Osteoarthr. Cartil. 14, 101-113 (2006). (Pubitemid 43079306)
    • (2006) Osteoarthritis and Cartilage , vol.14 , Issue.2 , pp. 101-113
    • Struglics, A.1    Larsson, S.2    Pratta, M.A.3    Kumar, S.4    Lark, M.W.5    Lohmander, L.S.6
  • 73
    • 0028815147 scopus 로고
    • Cell-mediated catabolism of aggrecan. Evidence that cleavage at the 'aggrecanase' site (Glu373-Ala374) is a primary event in proteolysis of the interglobular domain
    • Lark, M.W. et al Cell-mediated catabolism of aggrecan. Evidence that cleavage at the 'aggrecanase' site (Glu373-Ala374) is a primary event in proteolysis of the interglobular domain. J. Biol. Chem. 270, 2550-2556 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 2550-2556
    • Lark, M.W.1
  • 74
    • 0030931594 scopus 로고    scopus 로고
    • Aggrecan degradation in human intervertebral disc and articular cartilage
    • Sztrolovics, R., Alini, M., Roughley, PJ. & Mort, J.S. Aggrecan degradation in human intervertebral disc and articular cartilage. Biochem. J. 326, 235-241 (1997). (Pubitemid 27386941)
    • (1997) Biochemical Journal , vol.326 , Issue.1 , pp. 235-241
    • Sztrolovics, R.1    Alini, M.2    Roughley, P.J.3    Mort, J.S.4
  • 75
    • 0034854048 scopus 로고    scopus 로고
    • Distribution of aggrecanase (ADAMts 4/5) cleavage products in normal and osteoarthritic human articular cartilage: The influence of age, topography and zone of tissue
    • DOI 10.1053/joca.2001.0425
    • Bayliss, M.T., Hutton, S., Hayward, J. & Maciewicz, R.A. Distribution of aggrecanase (ADAMts 4/5) cleavage products in normal and osteoarthritic human articular cartilage: the infuence of age, topography and zone of tissue. Osteoarthr. Cartil. 9, 553-560 (2001). (Pubitemid 32842634)
    • (2001) Osteoarthritis and Cartilage , vol.9 , Issue.6 , pp. 553-560
    • Bayliss, M.T.1    Hutton, S.2    Hayward, J.3    Maciewicz, R.A.4
  • 76
    • 33746513929 scopus 로고    scopus 로고
    • Estimation of the identity of proteolytic aggrecan fragments using PAGE migration and Western immunoblot
    • DOI 10.1016/j.joca.2006.02.016, PII S106345840600046X
    • Struglics, A., Larsson, S. & Lohmander, L.S. Estimation of the identity of proteolytic aggrecan fragments using PAGE migration and Western immunoblot. Osteoarthr. Cartil. 14, 898-905 (2006). (Pubitemid 44138667)
    • (2006) Osteoarthritis and Cartilage , vol.14 , Issue.9 , pp. 898-905
    • Struglics, A.1    Larsson, S.2    Lohmander, L.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.