메뉴 건너뛰기




Volumn 16, Issue 7, 2008, Pages 749-755

Identification of opticin, a member of the small leucine-rich repeat proteoglycan family, in human articular tissues: a novel target for MMP-13 in osteoarthritis

Author keywords

MMP 13; Opticin; Osteoarthritis; SLRP

Indexed keywords

COLLAGENASE 3; GLYCOPROTEIN; GUANIDINE; MESSENGER RNA; OPTICIN; PROTEOGLYCAN; SMALL LEUCINE RICH REPEAT PROTEOGLYCAN;

EID: 45449087754     PISSN: 10634584     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.joca.2007.11.007     Document Type: Article
Times cited : (41)

References (43)
  • 1
    • 0031968825 scopus 로고    scopus 로고
    • Estimates of the prevalence of arthritis and selected musculoskeletal disorders in the United States
    • Lawrence R.C., Helmick C.G., Arnett F.C., Deyo R.A., Felson D.T., Giannini E.H., et al. Estimates of the prevalence of arthritis and selected musculoskeletal disorders in the United States. Arthritis Rheum 41 (1998) 778-799
    • (1998) Arthritis Rheum , vol.41 , pp. 778-799
    • Lawrence, R.C.1    Helmick, C.G.2    Arnett, F.C.3    Deyo, R.A.4    Felson, D.T.5    Giannini, E.H.6
  • 2
    • 0001926190 scopus 로고    scopus 로고
    • Pathogenesis of structural changes in the osteoarthritic joint
    • Brandt K.D., Doherty M., and Lohmander S.L. (Eds), Oxford University Press Inc., New York
    • Heinegard D., Bayliss M., and Lorenzo P. Pathogenesis of structural changes in the osteoarthritic joint. In: Brandt K.D., Doherty M., and Lohmander S.L. (Eds). Osteoarthritis. 2nd edn. (2003), Oxford University Press Inc., New York 73-92
    • (2003) Osteoarthritis. 2nd edn. , pp. 73-92
    • Heinegard, D.1    Bayliss, M.2    Lorenzo, P.3
  • 4
    • 33747781400 scopus 로고    scopus 로고
    • Structural correlations in the family of small leucine-rich repeat proteins and proteoglycans
    • McEwan P.A., Scott P.G., Bishop P.N., and Bella J. Structural correlations in the family of small leucine-rich repeat proteins and proteoglycans. J Struct Biol 155 (2006) 294-305
    • (2006) J Struct Biol , vol.155 , pp. 294-305
    • McEwan, P.A.1    Scott, P.G.2    Bishop, P.N.3    Bella, J.4
  • 5
    • 0033516558 scopus 로고    scopus 로고
    • The biology of the small leucine-rich proteoglycans. Functional network of interactive proteins
    • Iozzo R.V. The biology of the small leucine-rich proteoglycans. Functional network of interactive proteins. J Biol Chem 274 (1999) 18843-18846
    • (1999) J Biol Chem , vol.274 , pp. 18843-18846
    • Iozzo, R.V.1
  • 6
    • 0031044872 scopus 로고    scopus 로고
    • Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility
    • Danielson K.G., Baribault H., Holmes D.F., Graham H., Kadler K.E., and Iozzo R.V. Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility. J Cell Biol 136 (1997) 729-743
    • (1997) J Cell Biol , vol.136 , pp. 729-743
    • Danielson, K.G.1    Baribault, H.2    Holmes, D.F.3    Graham, H.4    Kadler, K.E.5    Iozzo, R.V.6
  • 7
    • 0032101311 scopus 로고    scopus 로고
    • Lumican regulates collagen fibril assembly: skin fragility and corneal opacity in the absence of lumican
    • Chakravarti S., Magnuson T., Lass J.H., Jepsen K.J., LaMantia C., and Carroll H. Lumican regulates collagen fibril assembly: skin fragility and corneal opacity in the absence of lumican. J Cell Biol 141 (1998) 1277-1286
    • (1998) J Cell Biol , vol.141 , pp. 1277-1286
    • Chakravarti, S.1    Magnuson, T.2    Lass, J.H.3    Jepsen, K.J.4    LaMantia, C.5    Carroll, H.6
  • 8
    • 0040436000 scopus 로고    scopus 로고
    • Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon
    • Svensson L., Aszodi A., Reinholt F.P., Fassler R., Heinegard D., and Oldberg A. Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon. J Biol Chem 274 (1999) 9636-9647
    • (1999) J Biol Chem , vol.274 , pp. 9636-9647
    • Svensson, L.1    Aszodi, A.2    Reinholt, F.P.3    Fassler, R.4    Heinegard, D.5    Oldberg, A.6
  • 9
    • 0034695439 scopus 로고    scopus 로고
    • Identification in vitreous and molecular cloning of opticin, a novel member of the family of leucine-rich repeat proteins of the extracellular matrix
    • Reardon A.J., Le Goff M., Briggs M.D., McLeod D., Sheehan J.K., Thornton D.J., et al. Identification in vitreous and molecular cloning of opticin, a novel member of the family of leucine-rich repeat proteins of the extracellular matrix. J Biol Chem 275 (2000) 2123-2129
    • (2000) J Biol Chem , vol.275 , pp. 2123-2129
    • Reardon, A.J.1    Le Goff, M.2    Briggs, M.D.3    McLeod, D.4    Sheehan, J.K.5    Thornton, D.J.6
  • 10
    • 0036330632 scopus 로고    scopus 로고
    • The role of the posterior ciliary body in the biosynthesis of vitreous humour
    • Bishop P.N., Takanosu M., Le Goff M., and Mayne R. The role of the posterior ciliary body in the biosynthesis of vitreous humour. Eye 16 (2002) 454-460
    • (2002) Eye , vol.16 , pp. 454-460
    • Bishop, P.N.1    Takanosu, M.2    Le Goff, M.3    Mayne, R.4
  • 11
    • 1942453405 scopus 로고    scopus 로고
    • Immunolocalisation of opticin in the human eye
    • Ramesh S., Bonshek R.E., and Bishop P.N. Immunolocalisation of opticin in the human eye. Br J Ophthalmol 88 (2004) 697-702
    • (2004) Br J Ophthalmol , vol.88 , pp. 697-702
    • Ramesh, S.1    Bonshek, R.E.2    Bishop, P.N.3
  • 13
    • 1642293197 scopus 로고    scopus 로고
    • The expression pattern of opticin during chicken embryogenesis
    • Frolova E.I., Fokina V.M., and Beebe D.C. The expression pattern of opticin during chicken embryogenesis. Gene Expr Patterns 4 (2004) 335-338
    • (2004) Gene Expr Patterns , vol.4 , pp. 335-338
    • Frolova, E.I.1    Fokina, V.M.2    Beebe, D.C.3
  • 14
    • 0037045417 scopus 로고    scopus 로고
    • Cloning and characterization of opticin cDNA: evaluation as a candidate for canine oculo-skeletal dysplasia
    • Pellegrini B., Acland G.M., and Ray J. Cloning and characterization of opticin cDNA: evaluation as a candidate for canine oculo-skeletal dysplasia. Gene 282 (2002) 121-131
    • (2002) Gene , vol.282 , pp. 121-131
    • Pellegrini, B.1    Acland, G.M.2    Ray, J.3
  • 15
    • 0242496519 scopus 로고    scopus 로고
    • Characterization of opticin and evidence of stable dimerization in solution
    • Le Goff M.M., Hindson V.J., Jowitt T.A., Scott P.G., and Bishop P.N. Characterization of opticin and evidence of stable dimerization in solution. J Biol Chem 278 (2003) 45280-45287
    • (2003) J Biol Chem , vol.278 , pp. 45280-45287
    • Le Goff, M.M.1    Hindson, V.J.2    Jowitt, T.A.3    Scott, P.G.4    Bishop, P.N.5
  • 16
    • 0034003134 scopus 로고    scopus 로고
    • Structural macromolecules and supramolecular organisation of the vitreous gel
    • Bishop P.N. Structural macromolecules and supramolecular organisation of the vitreous gel. Prog Retin Eye Res 19 (2000) 323-344
    • (2000) Prog Retin Eye Res , vol.19 , pp. 323-344
    • Bishop, P.N.1
  • 22
    • 4444355703 scopus 로고    scopus 로고
    • Ten years in the life of an enzyme: the story of the human MMP-13 (collagenase-3)
    • Tardif G., Reboul P., Pelletier J.P., and Martel-Pelletier J. Ten years in the life of an enzyme: the story of the human MMP-13 (collagenase-3). Mod Rheumatol 14 (2004) 197-204
    • (2004) Mod Rheumatol , vol.14 , pp. 197-204
    • Tardif, G.1    Reboul, P.2    Pelletier, J.P.3    Martel-Pelletier, J.4
  • 23
    • 0030958072 scopus 로고    scopus 로고
    • Degradation of decorin by matrix metalloproteinases: identification of the cleavage sites, kinetic analyses and transforming growth factor-beta1 release
    • Imai K., Hiramatsu A., Fukushima D., Pierschbacher M.D., and Okada Y. Degradation of decorin by matrix metalloproteinases: identification of the cleavage sites, kinetic analyses and transforming growth factor-beta1 release. Biochem J 322 (1997) 809-814
    • (1997) Biochem J , vol.322 , pp. 809-814
    • Imai, K.1    Hiramatsu, A.2    Fukushima, D.3    Pierschbacher, M.D.4    Okada, Y.5
  • 24
    • 1342346601 scopus 로고    scopus 로고
    • Cleavage of fibromodulin in cartilage explants involves removal of the N-terminal tyrosine sulfate-rich region by proteolysis at a site that is sensitive to matrix metalloproteinase-13
    • Heathfield T.F., Onnerfjord P., Dahlberg L., and Heinegard D. Cleavage of fibromodulin in cartilage explants involves removal of the N-terminal tyrosine sulfate-rich region by proteolysis at a site that is sensitive to matrix metalloproteinase-13. J Biol Chem 279 (2004) 6286-6295
    • (2004) J Biol Chem , vol.279 , pp. 6286-6295
    • Heathfield, T.F.1    Onnerfjord, P.2    Dahlberg, L.3    Heinegard, D.4
  • 25
    • 4944233738 scopus 로고    scopus 로고
    • Cleavage of lumican by membrane-type matrix metalloproteinase-1 abrogates this proteoglycan-mediated suppression of tumor cell colony formation in soft agar
    • Li Y., Aoki T., Mori Y., Ahmad M., Miyamori H., Takino T., et al. Cleavage of lumican by membrane-type matrix metalloproteinase-1 abrogates this proteoglycan-mediated suppression of tumor cell colony formation in soft agar. Cancer Res 64 (2004) 7058-7064
    • (2004) Cancer Res , vol.64 , pp. 7058-7064
    • Li, Y.1    Aoki, T.2    Mori, Y.3    Ahmad, M.4    Miyamori, H.5    Takino, T.6
  • 26
    • 70350516243 scopus 로고    scopus 로고
    • Degradation of small leucine-rich repeat proteoglycans by matrix metalloprotease-13: identification of a new biglycan cleavage site
    • Monfort J., Tardif G., Reboul P., Mineau F., Roughley P., Pelletier J.P., et al. Degradation of small leucine-rich repeat proteoglycans by matrix metalloprotease-13: identification of a new biglycan cleavage site. Arthritis Res Ther 8 (2006) R26
    • (2006) Arthritis Res Ther , vol.8
    • Monfort, J.1    Tardif, G.2    Reboul, P.3    Mineau, F.4    Roughley, P.5    Pelletier, J.P.6
  • 27
    • 0022465236 scopus 로고
    • Development of criteria for the classification and reporting of osteoarthritis. Classification of osteoarthritis of the knee
    • Altman R.D., Asch E., Bloch D.A., Bole G., Borenstein D., Brandt K.D., et al. Development of criteria for the classification and reporting of osteoarthritis. Classification of osteoarthritis of the knee. Arthritis Rheum 29 (1986) 1039-1049
    • (1986) Arthritis Rheum , vol.29 , pp. 1039-1049
    • Altman, R.D.1    Asch, E.2    Bloch, D.A.3    Bole, G.4    Borenstein, D.5    Brandt, K.D.6
  • 28
    • 0022345224 scopus 로고
    • Identification of a hyaluronic acid-binding protein that interferes with the preparation of high-buoyant-density proteoglycan aggregates from adult human articular cartilage
    • Roughley P.J., White R.J., and Poole A.R. Identification of a hyaluronic acid-binding protein that interferes with the preparation of high-buoyant-density proteoglycan aggregates from adult human articular cartilage. Biochem J 231 (1985) 129-138
    • (1985) Biochem J , vol.231 , pp. 129-138
    • Roughley, P.J.1    White, R.J.2    Poole, A.R.3
  • 29
    • 0029880393 scopus 로고    scopus 로고
    • The new collagenase, collagenase-3, is expressed and synthesized by human chondrocytes but not by synoviocytes: a role in osteoarthritis
    • Reboul P., Pelletier J.P., Tardif G., Cloutier J.M., and Martel-Pelletier J. The new collagenase, collagenase-3, is expressed and synthesized by human chondrocytes but not by synoviocytes: a role in osteoarthritis. J Clin Invest 97 (1996) 2011-2019
    • (1996) J Clin Invest , vol.97 , pp. 2011-2019
    • Reboul, P.1    Pelletier, J.P.2    Tardif, G.3    Cloutier, J.M.4    Martel-Pelletier, J.5
  • 30
    • 32844456504 scopus 로고    scopus 로고
    • Modulation of insulin-like growth factor 1 levels in human osteoarthritic subchondral bone osteoblasts
    • Massicotte F., Fernandes J.C., Martel-Pelletier J., Pelletier J.P., and Lajeunesse D. Modulation of insulin-like growth factor 1 levels in human osteoarthritic subchondral bone osteoblasts. Bone 38 (2006) 333-341
    • (2006) Bone , vol.38 , pp. 333-341
    • Massicotte, F.1    Fernandes, J.C.2    Martel-Pelletier, J.3    Pelletier, J.P.4    Lajeunesse, D.5
  • 31
    • 0031945874 scopus 로고    scopus 로고
    • Effects of tenidap on canine experimental osteoarthritis II: study of the expression of collagenase-1 and IL1β by in situ hybridization
    • Fernandes J.C., Martel-Pelletier J., Jovanovic D., Tardif G., Di Battista J.A., Lascau-Coman V., et al. Effects of tenidap on canine experimental osteoarthritis II: study of the expression of collagenase-1 and IL1β by in situ hybridization. J Rheumatol 25 (1998) 951-958
    • (1998) J Rheumatol , vol.25 , pp. 951-958
    • Fernandes, J.C.1    Martel-Pelletier, J.2    Jovanovic, D.3    Tardif, G.4    Di Battista, J.A.5    Lascau-Coman, V.6
  • 32
    • 0019914963 scopus 로고
    • A direct spectrophotometric microassay for sulfated glycosaminoglycans in cartilage cultures
    • Farndale R.W., Sayers C.A., and Barrett A.J. A direct spectrophotometric microassay for sulfated glycosaminoglycans in cartilage cultures. Connect Tissue Res 9 (1982) 247-248
    • (1982) Connect Tissue Res , vol.9 , pp. 247-248
    • Farndale, R.W.1    Sayers, C.A.2    Barrett, A.J.3
  • 33
    • 4043100538 scopus 로고    scopus 로고
    • Differential gene expression and regulation of the bone morphogenetic protein antagonists follistatin and gremlin in normal and osteoarthritic human chondrocytes and synovial fibroblasts
    • Tardif G., Hum D., Pelletier J.P., Boileau C., Ranger P., and Martel-Pelletier J. Differential gene expression and regulation of the bone morphogenetic protein antagonists follistatin and gremlin in normal and osteoarthritic human chondrocytes and synovial fibroblasts. Arthritis Rheum 50 (2004) 2521-2530
    • (2004) Arthritis Rheum , vol.50 , pp. 2521-2530
    • Tardif, G.1    Hum, D.2    Pelletier, J.P.3    Boileau, C.4    Ranger, P.5    Martel-Pelletier, J.6
  • 35
    • 0030024311 scopus 로고    scopus 로고
    • Degradation of cartilage aggrecan by collagenase-3 (MMP-13)
    • Fosang A.J., Last K., Knauper V., Murphy G., and Neame P.J. Degradation of cartilage aggrecan by collagenase-3 (MMP-13). FEBS Lett 380 (1996) 17-20
    • (1996) FEBS Lett , vol.380 , pp. 17-20
    • Fosang, A.J.1    Last, K.2    Knauper, V.3    Murphy, G.4    Neame, P.J.5
  • 36
    • 0034613174 scopus 로고    scopus 로고
    • Substrate specificity of human collagenase 3 assessed using a phage-displayed peptide library
    • Deng S.J., Bickett D.M., Mitchell J.L., Lambert M.H., Blackburn R.K., Carter III H.L., et al. Substrate specificity of human collagenase 3 assessed using a phage-displayed peptide library. J Biol Chem 275 (2000) 31422-31427
    • (2000) J Biol Chem , vol.275 , pp. 31422-31427
    • Deng, S.J.1    Bickett, D.M.2    Mitchell, J.L.3    Lambert, M.H.4    Blackburn, R.K.5    Carter III, H.L.6
  • 37
    • 0031042368 scopus 로고    scopus 로고
    • Collagenase-3 (MMP-13) is expressed by hypertrophic chondrocytes, periosteal cells, and osteoblasts during human fetal bone development
    • Johansson N., Saarialho-Kere U., Airola K., Herva R., Nissinen L., Westermarck J., et al. Collagenase-3 (MMP-13) is expressed by hypertrophic chondrocytes, periosteal cells, and osteoblasts during human fetal bone development. Dev Dyn 208 (1997) 387-397
    • (1997) Dev Dyn , vol.208 , pp. 387-397
    • Johansson, N.1    Saarialho-Kere, U.2    Airola, K.3    Herva, R.4    Nissinen, L.5    Westermarck, J.6
  • 38
    • 0039167208 scopus 로고    scopus 로고
    • Collagenase-3 (MMP-13) is expressed during human fetal ossification and re-expressed in postnatal bone remodeling and in rheumatoid arthritis
    • Stahle-Backdahl M., Sandstedt B., Bruce K., Lindahl A., Jimenez M.G., Vega J.A., et al. Collagenase-3 (MMP-13) is expressed during human fetal ossification and re-expressed in postnatal bone remodeling and in rheumatoid arthritis. Lab Invest 76 (1997) 717-728
    • (1997) Lab Invest , vol.76 , pp. 717-728
    • Stahle-Backdahl, M.1    Sandstedt, B.2    Bruce, K.3    Lindahl, A.4    Jimenez, M.G.5    Vega, J.A.6
  • 39
    • 0031928795 scopus 로고    scopus 로고
    • Collagenase-1 and collagenase-3 synthesis in early experimental osteoarthritic canine cartilage: an immunohistochemical study
    • Fernandes J.C., Martel-Pelletier J., Lascau-Coman V., Moldovan F., Jovanovic D., Raynauld J.P., et al. Collagenase-1 and collagenase-3 synthesis in early experimental osteoarthritic canine cartilage: an immunohistochemical study. J Rheumatol 25 (1998) 1585-1594
    • (1998) J Rheumatol , vol.25 , pp. 1585-1594
    • Fernandes, J.C.1    Martel-Pelletier, J.2    Lascau-Coman, V.3    Moldovan, F.4    Jovanovic, D.5    Raynauld, J.P.6
  • 40
    • 0030868574 scopus 로고    scopus 로고
    • Collagenase-3 (matrix metalloprotease 13) is preferentially localized in the deep layer of human arthritic cartilage in situ: in vitro mimicking effect by transforming growth factor beta
    • Moldovan F., Pelletier J.P., Hambor J., Cloutier J.M., and Martel-Pelletier J. Collagenase-3 (matrix metalloprotease 13) is preferentially localized in the deep layer of human arthritic cartilage in situ: in vitro mimicking effect by transforming growth factor beta. Arthritis Rheum 40 (1997) 1653-1661
    • (1997) Arthritis Rheum , vol.40 , pp. 1653-1661
    • Moldovan, F.1    Pelletier, J.P.2    Hambor, J.3    Cloutier, J.M.4    Martel-Pelletier, J.5
  • 41
    • 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 P.M., Haag J., Knorr T., Bartnik E., and Aigner T. Relative messenger RNA expression profiling of collagenases and aggrecanases in human articular chondrocytes in vivo and in vitro. Arthritis Rheum 46 (2002) 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
  • 42
    • 0038753846 scopus 로고    scopus 로고
    • Gene expression in chondrocytes assessed with use of microarrays
    • Aigner T., Zien A., Hanisch D., and Zimmer R. Gene expression in chondrocytes assessed with use of microarrays. J Bone Joint Surg Am 85-A Suppl 2 (2003) 117-123
    • (2003) J Bone Joint Surg Am , vol.85 -A , Issue.SUPPL. 2 , pp. 117-123
    • Aigner, T.1    Zien, A.2    Hanisch, D.3    Zimmer, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.