메뉴 건너뛰기




Volumn 78, Issue 17, 2006, Pages 1975-1982

The effect of IL-1α on the expression of matrix metalloproteinases, plasminogen activators, and their inhibitors in osteoblastic ROS 17/2.8 cells

Author keywords

Interleukin 1 ; Matrix metalloproteinases; Plasminogen activation system; Tissue inhibitor of matrix metalloproteinases

Indexed keywords

COLLAGENASE 3; GELATINASE A; INTERLEUKIN 1; INTERLEUKIN 1ALPHA; INTERSTITIAL COLLAGENASE; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE 14; MESSENGER RNA; PLASMINOGEN ACTIVATOR; PLASMINOGEN ACTIVATOR INHIBITOR; PLASMINOGEN ACTIVATOR INHIBITOR 1; STROMELYSIN; TISSUE INHIBITOR OF METALLOPROTEINASE; TISSUE INHIBITOR OF METALLOPROTEINASE 1; TISSUE INHIBITOR OF METALLOPROTEINASE 2; TISSUE INHIBITOR OF METALLOPROTEINASE 3; TISSUE PLASMINOGEN ACTIVATOR; UROKINASE;

EID: 33644619595     PISSN: 00243205     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.lfs.2005.08.036     Document Type: Article
Times cited : (26)

References (44)
  • 1
    • 15244338619 scopus 로고    scopus 로고
    • Collagenases in cancer
    • R. Ala-aho, and V.M. Kahari Collagenases in cancer Biochimie 87 2005 273 286
    • (2005) Biochimie , vol.87 , pp. 273-286
    • Ala-Aho, R.1    Kahari, V.M.2
  • 2
    • 0642377387 scopus 로고    scopus 로고
    • The interleukin-1 system: An attractive and viable therapeutic target in neurodegenerative disease
    • S.M. Allan, and E. Pinteaux The interleukin-1 system: an attractive and viable therapeutic target in neurodegenerative disease Current Drug Targets. CNS and Neurological Disorders 2 2003 293 302
    • (2003) Current Drug Targets. CNS and Neurological Disorders , vol.2 , pp. 293-302
    • Allan, S.M.1    Pinteaux, E.2
  • 3
    • 0026237106 scopus 로고
    • Immunoreactivity for interleukin-1β and tumor necrosis factor-α and ultrastructural features of monocytes/macrophages in periapical granulomas
    • L. Artese, A. Piattelli, M. Quaranta, A. Colasante, and P. Musani Immunoreactivity for interleukin-1β and tumor necrosis factor-α and ultrastructural features of monocytes/macrophages in periapical granulomas Journal of Endodontics 17 1991 483 487
    • (1991) Journal of Endodontics , vol.17 , pp. 483-487
    • Artese, L.1    Piattelli, A.2    Quaranta, M.3    Colasante, A.4    Musani, P.5
  • 4
    • 0031039965 scopus 로고    scopus 로고
    • Membrane-type-2 matrix metalloproteinase can initiate the processing of progelatinase a and is regulated by the tissue inhibitors of metalloproteinases
    • G.S. Butler, H. Will, S.J. Atkinson, and G. Murphy Membrane-type-2 matrix metalloproteinase can initiate the processing of progelatinase A and is regulated by the tissue inhibitors of metalloproteinases European Journal of Biochemistry 244 1997 653 657
    • (1997) European Journal of Biochemistry , vol.244 , pp. 653-657
    • Butler, G.S.1    Will, H.2    Atkinson, S.J.3    Murphy, G.4
  • 5
    • 0022259759 scopus 로고
    • Mammalian collagenase predisposes bone surfaces to osteoclastic resorption
    • T.J. Chambers, J.A. Darby, and K. Fuller Mammalian collagenase predisposes bone surfaces to osteoclastic resorption Cell and Tissue Research 241 1985 671 675
    • (1985) Cell and Tissue Research , vol.241 , pp. 671-675
    • Chambers, T.J.1    Darby, J.A.2    Fuller, K.3
  • 7
    • 0032522576 scopus 로고    scopus 로고
    • Induction of matrix metalloproteinase activation cascades based on membrane-type 1 matrix metalloproteinase: Associated activation of gelatinase A, gelatinase B and collagenase 3
    • S. Cowell, V. Knauper, M.L. Stewart, M.P. D'Ortho, H. Stanton, R.M. Hembry, C. Lopez-Otin, J.J. Reynolds, and G. Murphy Induction of matrix metalloproteinase activation cascades based on membrane-type 1 matrix metalloproteinase: associated activation of gelatinase A, gelatinase B and collagenase 3 Biochemical Journal 331 1998 453 458
    • (1998) Biochemical Journal , vol.331 , pp. 453-458
    • Cowell, S.1    Knauper, V.2    Stewart, M.L.3    D'Ortho, M.P.4    Stanton, H.5    Hembry, R.M.6    Lopez-Otin, C.7    Reynolds, J.J.8    Murphy, G.9
  • 9
    • 2542436756 scopus 로고    scopus 로고
    • Matrix metalloproteinases and their endogenous inhibitors in neuronal physiology of the adult brain
    • J. Dzwonek, M. Rylski, and L. Kaczmarek Matrix metalloproteinases and their endogenous inhibitors in neuronal physiology of the adult brain FEBS Letters 567 2004 129 135
    • (2004) FEBS Letters , vol.567 , pp. 129-135
    • Dzwonek, J.1    Rylski, M.2    Kaczmarek, L.3
  • 10
    • 0017644625 scopus 로고
    • Further studies on the activation of procollagenase, the latent precursor of bone collagenase. Effects of lysosomal cathepsin B, plasmin and kallikrein, and spontaneous activation
    • Y. Eeckhout, and G. Vaes Further studies on the activation of procollagenase, the latent precursor of bone collagenase. Effects of lysosomal cathepsin B, plasmin and kallikrein, and spontaneous activation Biochemical Journal 166 1977 21 31
    • (1977) Biochemical Journal , vol.166 , pp. 21-31
    • Eeckhout, Y.1    Vaes, G.2
  • 11
    • 0025518517 scopus 로고
    • Temporal sequence of interleukin 1α-mediated stimulation and inhibition of bone formation by isolated fetal rat calvaria cells in vitro
    • L.G. Ellies, and J.E. Aubin Temporal sequence of interleukin 1α-mediated stimulation and inhibition of bone formation by isolated fetal rat calvaria cells in vitro Cytokine 2 1990 430 437
    • (1990) Cytokine , vol.2 , pp. 430-437
    • Ellies, L.G.1    Aubin, J.E.2
  • 13
    • 23944469951 scopus 로고    scopus 로고
    • Localization of matrix metalloproteinases (MMPs) their tissue inhibitors, and vascular endothelial growth factor (VEGF) in growth plates of children and adolescents indicates a role for MMPs in human postnatal growth and skeletal maturation
    • G. Haeusler, I. Walter, M. Helmreich, and M. Egerbacher Localization of matrix metalloproteinases (MMPs) their tissue inhibitors, and vascular endothelial growth factor (VEGF) in growth plates of children and adolescents indicates a role for MMPs in human postnatal growth and skeletal maturation Calcified Tissue International 76 2005 326 335
    • (2005) Calcified Tissue International , vol.76 , pp. 326-335
    • Haeusler, G.1    Walter, I.2    Helmreich, M.3    Egerbacher, M.4
  • 14
    • 0015900838 scopus 로고
    • Prostaglandin production and bone resorption by dental cysts
    • M. Harris, M.V. Jenkins, A. Bennett, and M.R. Wills Prostaglandin production and bone resorption by dental cysts Nature 245 1973 213 215
    • (1973) Nature , vol.245 , pp. 213-215
    • Harris, M.1    Jenkins, M.V.2    Bennett, A.3    Wills, M.R.4
  • 15
    • 0036217851 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinases-4 (TIMP-4) gene expression is in creased in human osteoarthritic femoral head cartilage
    • W. Huang, W.Q. Li, F. Dehnade, and M. Zafarullah Tissue inhibitor of metalloproteinases-4 (TIMP-4) gene expression is in creased in human osteoarthritic femoral head cartilage Journal of Cellular Biochemistry 85 2002 295 303
    • (2002) Journal of Cellular Biochemistry , vol.85 , pp. 295-303
    • Huang, W.1    Li, W.Q.2    Dehnade, F.3    Zafarullah, M.4
  • 16
    • 0038512014 scopus 로고    scopus 로고
    • Characterization of the 5′-flanking region of the rat AJ18 gene
    • A.H. Jheon, N. Suzuki, T. Nishiyama, S. Cheifetz, Y. Sodek, and B. Ganss Characterization of the 5′-flanking region of the rat AJ18 gene Gene 310 2003 203 213
    • (2003) Gene , vol.310 , pp. 203-213
    • Jheon, A.H.1    Suzuki, N.2    Nishiyama, T.3    Cheifetz, S.4    Sodek, Y.5    Ganss, B.6
  • 17
    • 0034956272 scopus 로고    scopus 로고
    • The role of matrix metalloproteinases in tumor angiogenesis and tumor metastasis
    • A. John, and G. Tuszynski The role of matrix metalloproteinases in tumor angiogenesis and tumor metastasis Pathology Oncology Research 7 2001 14 23
    • (2001) Pathology Oncology Research , vol.7 , pp. 14-23
    • John, A.1    Tuszynski, G.2
  • 18
    • 0031738172 scopus 로고    scopus 로고
    • Regulation of matrix metalloproteinases (MMP-2, -3, -9, and -13) by interleukin-1 and interleukin-6 in mouse calvaria: Association of MMP induction with bone resorption
    • K. Kusano, C. Miyaura, M. Inada, T. Tamura, A. Ito, H. Nagase, K. Kamoi, and T. Suda Regulation of matrix metalloproteinases (MMP-2, -3, -9, and -13) by interleukin-1 and interleukin-6 in mouse calvaria: association of MMP induction with bone resorption Endocrinology 139 1998 1338 1345
    • (1998) Endocrinology , vol.139 , pp. 1338-1345
    • Kusano, K.1    Miyaura, C.2    Inada, M.3    Tamura, T.4    Ito, A.5    Nagase, H.6    Kamoi, K.7    Suda, T.8
  • 22
    • 0022005644 scopus 로고
    • Glucocorticoid regulation of alkaline phosphatase in the osteoblastic osteosarcoma cell line ROS17/2.8
    • R.J. Majeska, B.C. Nair, and G.A. Rodan Glucocorticoid regulation of alkaline phosphatase in the osteoblastic osteosarcoma cell line ROS17/2.8 Endocrinology 116 1985 170 179
    • (1985) Endocrinology , vol.116 , pp. 170-179
    • Majeska, R.J.1    Nair, B.C.2    Rodan, G.A.3
  • 23
    • 25144480967 scopus 로고    scopus 로고
    • FMS*Calciumfluor specifically increases mRNA levels and induces signaling via MAPK 42, 44 and not FAK in differentiating rat osteoblasts
    • P. Manduca, S. Marchisio, S. Astigiano, S. Zanotti, F. Galmozzi, C. Palermo, and D. Palmieri FMS*Calciumfluor specifically increases mRNA levels and induces signaling via MAPK 42, 44 and not FAK in differentiating rat osteoblasts Cell Biology International 29 2005 629 637
    • (2005) Cell Biology International , vol.29 , pp. 629-637
    • Manduca, P.1    Marchisio, S.2    Astigiano, S.3    Zanotti, S.4    Galmozzi, F.5    Palermo, C.6    Palmieri, D.7
  • 26
    • 0030977009 scopus 로고    scopus 로고
    • Control of type IV collagenase activity by components of the urokinase-plasmin system: A regulatory mechanism with cell-bound reactants
    • R. Mazzieri, L. Masiero, L. Zanetta, S. Monea, M. Onisto, S. Garbisa, and P. Mignatti Control of type IV collagenase activity by components of the urokinase-plasmin system: a regulatory mechanism with cell-bound reactants EMBO Journal 16 1997 2319 2332
    • (1997) EMBO Journal , vol.16 , pp. 2319-2332
    • Mazzieri, R.1    Masiero, L.2    Zanetta, L.3    Monea, S.4    Onisto, M.5    Garbisa, S.6    Mignatti, P.7
  • 27
    • 0026902313 scopus 로고
    • Anti-proliferative and cytotoxic activity of surface-associated material from periodontopathogenic bacteria
    • S. Meghji, M. Wilson, B. Henderson, and D. Kinnane Anti-proliferative and cytotoxic activity of surface-associated material from periodontopathogenic bacteria Archives of Oral Biology 37 1992 637 644
    • (1992) Archives of Oral Biology , vol.37 , pp. 637-644
    • Meghji, S.1    Wilson, M.2    Henderson, B.3    Kinnane, D.4
  • 28
    • 4444304939 scopus 로고    scopus 로고
    • Regulation of matrix biology by matrix metalloproteinases
    • J.D. Mott, and Z. Werb Regulation of matrix biology by matrix metalloproteinases Current Opinion in Cell Biology 16 2004 558 564
    • (2004) Current Opinion in Cell Biology , vol.16 , pp. 558-564
    • Mott, J.D.1    Werb, Z.2
  • 30
    • 16844362873 scopus 로고    scopus 로고
    • Transcriptional and posttranscriptional regulation of the plasminogen activator system
    • Y. Nagamine, R.L. Medcalf, and P. Munoz-Canoves Transcriptional and posttranscriptional regulation of the plasminogen activator system Thrombosis and Haemostasis 93 2005 661 675
    • (2005) Thrombosis and Haemostasis , vol.93 , pp. 661-675
    • Nagamine, Y.1    Medcalf, R.L.2    Munoz-Canoves, P.3
  • 33
    • 0030669224 scopus 로고    scopus 로고
    • Kinetic analysis of the binding of human matrix metalloproteinase-2 and -9 to tissue inhibitor of metalloproteinase (TIMP)-1 and TIMP-2
    • M.W. Olson, D.C. Gervasi, S. Mobashery, and R. Fridman Kinetic analysis of the binding of human matrix metalloproteinase-2 and -9 to tissue inhibitor of metalloproteinase (TIMP)-1 and TIMP-2 Journal of Biological Chemistry 272 1997 29975 29983
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 29975-29983
    • Olson, M.W.1    Gervasi, D.C.2    Mobashery, S.3    Fridman, R.4
  • 34
    • 0035721955 scopus 로고    scopus 로고
    • Role of the matrix metalloproteinase and plasminogen activator-plasmin systems in angiogenesis
    • M.S. Pepper Role of the matrix metalloproteinase and plasminogen activator-plasmin systems in angiogenesis Arteriosclerosis, Thrombosis, and Vascular Biology 21 2001 1104 1117
    • (2001) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.21 , pp. 1104-1117
    • Pepper, M.S.1
  • 38
    • 0002460180 scopus 로고
    • Non-collagenous bone proteins and their role in substrate-induced bioactivity
    • J.E. Davies University of Toronto Press Toronto
    • J. Sodek, Q. Zhang, H.A. Goldberg, C. Domenicucci, S. Kasugai, and J.L. Wrana Non-collagenous bone proteins and their role in substrate-induced bioactivity J.E. Davies The Bone-Biomaterial Interface 1991 University of Toronto Press Toronto 97 110
    • (1991) The Bone-Biomaterial Interface , pp. 97-110
    • Sodek, J.1    Zhang, Q.2    Goldberg, H.A.3    Domenicucci, C.4    Kasugai, S.5    Wrana, J.L.6
  • 39
    • 2442454904 scopus 로고    scopus 로고
    • Functional roles of the tissue inhibitor of metalloproteinase 3 (TIMP-3) during ascorbate-induced differentiation of osteoblastic MC3T3-E1 cells
    • N. Suzuki, Y. Nezaki, E. Kuno, I. Sugiyama, A. Mizutani, and N. Tsukagoshi Functional roles of the tissue inhibitor of metalloproteinase 3 (TIMP-3) during ascorbate-induced differentiation of osteoblastic MC3T3-E1 cells Bioscience, Biotechnology, and Biochemistry 67 2003 1737 1743
    • (2003) Bioscience, Biotechnology, and Biochemistry , vol.67 , pp. 1737-1743
    • Suzuki, N.1    Nezaki, Y.2    Kuno, E.3    Sugiyama, I.4    Mizutani, A.5    Tsukagoshi, N.6
  • 42
    • 0024838488 scopus 로고
    • Alkaline phosphatase cDNA transfected cells promote calcium and phosphate deposition
    • K. Yoon, E. Golub, and G.A. Rodan Alkaline phosphatase cDNA transfected cells promote calcium and phosphate deposition Connective Tissue Research 22 1989 17 25
    • (1989) Connective Tissue Research , vol.22 , pp. 17-25
    • Yoon, K.1    Golub, E.2    Rodan, G.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.