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Volumn 161, Issue 9, 1998, Pages 5000-5007

Oncostatin M up-regulates tissue inhibitor of metalloproteinases-3 gene expression in articular chondrocytes viade novo transcription, protein synthesis, and tyrosine kinase- and mitogen-activated protein kinase- dependent mechanisms

Author keywords

[No Author keywords available]

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; CYTOKINE; GROWTH FACTOR; MITOGEN ACTIVATED PROTEIN KINASE; ONCOSTATIN M; STROMELYSIN; TISSUE INHIBITOR OF METALLOPROTEINASE;

EID: 0001155860     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (39)

References (63)
  • 1
    • 0028833075 scopus 로고
    • Clinical implications of osteoarthritis and ageing
    • Hamerman D. Clinical implications of osteoarthritis and ageing. 1995. Ann. Rheum. Dis. 54:82.
    • (1995) Ann. Rheum. Dis. , vol.54 , pp. 82
    • Hamerman, D.1
  • 2
    • 0029981825 scopus 로고    scopus 로고
    • Cytokines in osteoarthritis: Mediators or markers of joint destruction?
    • Westacott, C. I., and M. Sharif. 1996. Cytokines in osteoarthritis: mediators or markers of joint destruction? Semin. Arthritis Rheum. 25:254.
    • (1996) Semin. Arthritis Rheum. , vol.25 , pp. 254
    • Westacott, C.I.1    Sharif, M.2
  • 3
    • 0028091155 scopus 로고
    • Immunological markers of joint inflammation, skeletal damage and repair: Where are we now?
    • Poole, A. R. 1994. Immunological markers of joint inflammation, skeletal damage and repair: where are we now? Ann. Rheum. Dis. 53:3.
    • (1994) Ann. Rheum. Dis. , vol.53 , pp. 3
    • Poole, A.R.1
  • 4
    • 0029150795 scopus 로고
    • Proteolytic remodeling of extracellular matrix
    • Birkedal-Hansen, H. 1995. Proteolytic remodeling of extracellular matrix. Cur. Opin. Cell Biol. 7:728.
    • (1995) Cur. Opin. Cell Biol. , vol.7 , pp. 728
    • Birkedal-Hansen, H.1
  • 5
    • 0026896029 scopus 로고
    • The matrix-degrading metalloproteinases
    • Matrisian, L. M. 1992. The matrix-degrading metalloproteinases. BioEssays 14: 455.
    • (1992) BioEssays , vol.14 , pp. 455
    • Matrisian, L.M.1
  • 7
    • 0024394212 scopus 로고
    • Tissue inhibitor of metalloproteinase (TIMP-2), a new member of the metalloproteinase inhibitor family
    • Stetler-Stevenson, W. G., H. C. Krutzsch, and L. A. Liotta. 1989. Tissue inhibitor of metalloproteinase (TIMP-2), a new member of the metalloproteinase inhibitor family. J. Biol. Chem. 264:17374.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17374
    • Stetler-Stevenson, W.G.1    Krutzsch, H.C.2    Liotta, L.A.3
  • 8
    • 0028125576 scopus 로고
    • Cloning of the cDNA encoding human tissue inhibitor of metalloproteinases-3 (TIMP-3) and mapping of the TIMP3 gene to chromosome 22
    • Apte, S. S., M. G. Mattei, and B. R. Olsen. 1994. Cloning of the cDNA encoding human tissue inhibitor of metalloproteinases-3 (TIMP-3) and mapping of the TIMP3 gene to chromosome 22. Genomics 19:86.
    • (1994) Genomics , vol.19 , pp. 86
    • Apte, S.S.1    Mattei, M.G.2    Olsen, B.R.3
  • 9
    • 0029806813 scopus 로고    scopus 로고
    • Molecular cloning and characterization of human tissue inhibitor of metalloproteinase 4
    • Greene, J., M. S. Wang, Y. E. Liu, L. A. Raymond, C. Rosen, and Y. E. Shi. 1996. Molecular cloning and characterization of human tissue inhibitor of metalloproteinase 4. J. Biol. Chem. 271:30375.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30375
    • Greene, J.1    Wang, M.S.2    Liu, Y.E.3    Raymond, L.A.4    Rosen, C.5    Shi, Y.E.6
  • 10
    • 0024712236 scopus 로고
    • Evidence for metalloproteinase and metalloproteinase inhibitor imbalance in human osteoarthritic cartilage
    • Dean D. D., J. Martel-Pelletier, J.-P. Pelletier, D. S. Howell, and J. F. Woessner, Jr. 1989 Evidence for metalloproteinase and metalloproteinase inhibitor imbalance in human osteoarthritic cartilage. J. Clin. Invest. 84:678.
    • (1989) J. Clin. Invest. , vol.84 , pp. 678
    • Dean, D.D.1    Martel-Pelletier, J.2    Pelletier, J.-P.3    Howell, D.S.4    Woessner Jr., J.F.5
  • 11
    • 0028132867 scopus 로고
    • Cell growth-promoting activity of tissue inhibitor of metalloproteinases-2 (TIMP-2)
    • Hayakawa, T., K. Yamashita, E. Ohuchi, and A. Shinagawa. 1994. Cell growth-promoting activity of tissue inhibitor of metalloproteinases-2 (TIMP-2). J. Cell Sci. 107:2373.
    • (1994) J. Cell Sci. , vol.107 , pp. 2373
    • Hayakawa, T.1    Yamashita, K.2    Ohuchi, E.3    Shinagawa, A.4
  • 12
    • 0030605008 scopus 로고    scopus 로고
    • Tyrosine phosphorylation is crucial for growth signaling by tissue inhibitors of metalloproteinases (TIMP-1 and TIMP-2)
    • Yamashita, K., M. Suzuki, H. Iwata, T. Koike, M. Hamaguchi, A. Shinagawa, T. Noguchi, and T. Hayakawa. 1996. Tyrosine phosphorylation is crucial for growth signaling by tissue inhibitors of metalloproteinases (TIMP-1 and TIMP-2). FEBS Lett. 396:103.
    • (1996) FEBS Lett. , vol.396 , pp. 103
    • Yamashita, K.1    Suzuki, M.2    Iwata, H.3    Koike, T.4    Hamaguchi, M.5    Shinagawa, A.6    Noguchi, T.7    Hayakawa, T.8
  • 13
    • 0020664964 scopus 로고
    • Transformation-sensitive protein associated with the cell substratum of chicken embryo fibroblasts
    • Blenis, J., and S. P. Hawkes. 1983. Transformation-sensitive protein associated with the cell substratum of chicken embryo fibroblasts. Proc. Natl. Acad. Sci. USA 80:770.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 770
    • Blenis, J.1    Hawkes, S.P.2
  • 14
    • 0026794057 scopus 로고
    • A new inhibitor of metalloproteinases from chicken: ChIMP-3, a third member of the TIMP family
    • Pavloff, N., P. W. Staskus, N. S. Kishnani, and S. P. Hawkes. 1992. A new inhibitor of metalloproteinases from chicken: ChIMP-3, a third member of the TIMP family. J. Biol. Chem. 267:17321.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17321
    • Pavloff, N.1    Staskus, P.W.2    Kishnani, N.S.3    Hawkes, S.P.4
  • 15
    • 0026465338 scopus 로고
    • Role of the 21-kDa protein TIMP-3 in oncogenic transformation of cultured chicken embryo fibroblasts
    • Yang, T. T., and S. P. Hawkes. 1992. Role of the 21-kDa protein TIMP-3 in oncogenic transformation of cultured chicken embryo fibroblasts. Proc. Natl. Acad. Sci. USA 89:10676.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10676
    • Yang, T.T.1    Hawkes, S.P.2
  • 16
    • 0028355007 scopus 로고
    • Cloning of cDNAs encoding human TIMP-3, a novel member of the tissue inhibitor of metalloproteinase family
    • Silbiger, S. M., V. L. Jacobsen, R. L. Cupples, and R. A. Koski. 1994. Cloning of cDNAs encoding human TIMP-3, a novel member of the tissue inhibitor of metalloproteinase family. Gene 141:293.
    • (1994) Gene , vol.141 , pp. 293
    • Silbiger, S.M.1    Jacobsen, V.L.2    Cupples, R.L.3    Koski, R.A.4
  • 17
    • 0028355246 scopus 로고
    • Structure and expression in breast tumors of human TIMP-3, a new member of the metalloproteinase inhibitor family
    • Uría, J. A., A. A. Ferrando, G. Velasco, J. M. P. Freije, and C. López-Otín. 1994. Structure and expression in breast tumors of human TIMP-3, a new member of the metalloproteinase inhibitor family. Cancer Res. 54:2091.
    • (1994) Cancer Res. , vol.54 , pp. 2091
    • Uría, J.A.1    Ferrando, A.A.2    Velasco, G.3    Freije, J.M.P.4    López-Otín, C.5
  • 18
    • 0028244447 scopus 로고
    • Tissue inhibitor of metalloproteinases-3 (TIMP-3) is an extracellular matrix-associated protein with a distinctive pattern of expression in mouse cells and tissues
    • Leco, K. J., R. Khokha, N. Pavloff, S. P. Hawkes, and D. R. Edwards. 1994. Tissue inhibitor of metalloproteinases-3 (TIMP-3) is an extracellular matrix-associated protein with a distinctive pattern of expression in mouse cells and tissues. J. Biol. Chem. 269:9352.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9352
    • Leco, K.J.1    Khokha, R.2    Pavloff, N.3    Hawkes, S.P.4    Edwards, D.R.5
  • 20
    • 0031013169 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinases-3 is a component of Bruch's membrane of the eye
    • Fariss, R. N., S. S. Apte, B. R. Olsen, K. Iwata, and A. H. Milam. 1997. Tissue inhibitor of metalloproteinases-3 is a component of Bruch's membrane of the eye. Am. J. Pathol. 150:323.
    • (1997) Am. J. Pathol. , vol.150 , pp. 323
    • Fariss, R.N.1    Apte, S.S.2    Olsen, B.R.3    Iwata, K.4    Milam, A.H.5
  • 21
    • 0028097367 scopus 로고
    • Mutations in the tissue inhibitor of metalloproteinases-3 (TIMP-3) in patients with Sorsby's fundus dystrophy
    • Weber, B. H. F., G. Vogt, R. C. Pruett, H. Stöhr, and U. Felbor. 1994. Mutations in the tissue inhibitor of metalloproteinases-3 (TIMP-3) in patients with Sorsby's fundus dystrophy. Nat. Gen. 8:352.
    • (1994) Nat. Gen. , vol.8 , pp. 352
    • Weber, B.H.F.1    Vogt, G.2    Pruett, R.C.3    Stöhr, H.4    Felbor, U.5
  • 23
    • 0029810478 scopus 로고    scopus 로고
    • Suppression of in vivo tumor growth and induction of suspension cell death by tissue inhibitor of metalloproteinases (TIMP)-3
    • Bian, J. H., Y. Wang, M. R. Smith, H. Kim, C. Jacobs, J. Jackman, H. F. Kung, N. H. Colburn, and Y. Sun. 1996. Suppression of in vivo tumor growth and induction of suspension cell death by tissue inhibitor of metalloproteinases (TIMP)-3. Carcinogenesis 17:1805.
    • (1996) Carcinogenesis , vol.17 , pp. 1805
    • Bian, J.H.1    Wang, Y.2    Smith, M.R.3    Kim, H.4    Jacobs, C.5    Jackman, J.6    Kung, H.F.7    Colburn, N.H.8    Sun, Y.9
  • 24
    • 0030323007 scopus 로고    scopus 로고
    • A review of tissue inhibitor of metalloproteinases-3 (TIMP-3) and experimental analysis of its effect on primary tumor growth
    • Anande-Apte, B., L. Bao, R. Smith, K. Iwata, B. R. Olsen, B. Zetter, and S. S. Apte. 1996. A review of tissue inhibitor of metalloproteinases-3 (TIMP-3) and experimental analysis of its effect on primary tumor growth. Biochem. Cell Biol. 74:853.
    • (1996) Biochem. Cell Biol. , vol.74 , pp. 853
    • Anande-Apte, B.1    Bao, L.2    Smith, R.3    Iwata, K.4    Olsen, B.R.5    Zetter, B.6    Apte, S.S.7
  • 25
    • 0029019867 scopus 로고
    • The gene structure of tissue inhibitor of metalloproteinases (TIMP)-3 and its inhibitory activities define the distinct TIMP gene family
    • Apte, S. S., B. R. Olsen, and G. Murphy. 1995. The gene structure of tissue inhibitor of metalloproteinases (TIMP)-3 and its inhibitory activities define the distinct TIMP gene family. J. Biol. Chem. 270:14313.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14313
    • Apte, S.S.1    Olsen, B.R.2    Murphy, G.3
  • 26
    • 0030016342 scopus 로고    scopus 로고
    • The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation-regulation by TIMP-2 and TIMP-3
    • Will, H., S. J. Atkinson, G. S. Butler, B. Smith, and G. Murphy. 1996. The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation-regulation by TIMP-2 and TIMP-3. J. Biol. Chem. 271:17119.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17119
    • Will, H.1    Atkinson, S.J.2    Butler, G.S.3    Smith, B.4    Murphy, G.5
  • 27
    • 0027932836 scopus 로고
    • Gene encoding a novel murine tissue inhibitor of metalloproteinases (TIMP), TIMP-3. is expressed in developing mouse epithelia, cartilage, and muscle, and is located on mouse chromosome 10
    • Apte, S. S., K. Hayashi, M. F. Seldin, M. G. Mattei, M. Hayashi, and B. R. Olsen. 1994. Gene encoding a novel murine tissue inhibitor of metalloproteinases (TIMP), TIMP-3. is expressed in developing mouse epithelia, cartilage, and muscle, and is located on mouse chromosome 10. Dev. Dyn. 200:177.
    • (1994) Dev. Dyn. , vol.200 , pp. 177
    • Apte, S.S.1    Hayashi, K.2    Seldin, M.F.3    Mattei, M.G.4    Hayashi, M.5    Olsen, B.R.6
  • 28
    • 0031008068 scopus 로고    scopus 로고
    • Matrix metalloproteinases regulate morphogenesis, migration and remodeling of epithelium, tongue skeletal muscle and cartilage in the mandibular arch
    • Chin, J. R., and Z. Werb. 1997. Matrix metalloproteinases regulate morphogenesis, migration and remodeling of epithelium, tongue skeletal muscle and cartilage in the mandibular arch. Development 124:1519.
    • (1997) Development , vol.124 , pp. 1519
    • Chin, J.R.1    Werb, Z.2
  • 29
    • 0030470870 scopus 로고    scopus 로고
    • Regulation of tissue inhibitor of metalloproteinases-3 gene expression by transforming growth factor β and dexamethasone in bovine and human articular chondrocytes
    • Su, S., F. Dehnade, and M. Zafarullah. 1996. Regulation of tissue inhibitor of metalloproteinases-3 gene expression by transforming growth factor β and dexamethasone in bovine and human articular chondrocytes. DNA Cell Biol. 15:1039.
    • (1996) DNA Cell Biol. , vol.15 , pp. 1039
    • Su, S.1    Dehnade, F.2    Zafarullah, M.3
  • 33
    • 0030906014 scopus 로고    scopus 로고
    • Detection of oncostatin M in synovial fluid from patients with rheumatoid arthritis
    • Hui, W., M. Bell, and G. Carroll. 1997. Detection of oncostatin M in synovial fluid from patients with rheumatoid arthritis. Ann. Rheum. Dis. 56:184.
    • (1997) Ann. Rheum. Dis. , vol.56 , pp. 184
    • Hui, W.1    Bell, M.2    Carroll, G.3
  • 34
    • 0030903094 scopus 로고    scopus 로고
    • The synovial expression and serum levels of interleukin-6, interleukin-11, leukemia inhibitory factor, and oncostatin M in rheumatoid arthritis
    • Okamoto, H., M. Yamamura, Y. Monta, S. Harada, H. Makino, and Z. Ota. 1997. The synovial expression and serum levels of interleukin-6, interleukin-11, leukemia inhibitory factor, and oncostatin M in rheumatoid arthritis. Arthritis Rheum. 40:1096.
    • (1997) Arthritis Rheum. , vol.40 , pp. 1096
    • Okamoto, H.1    Yamamura, M.2    Monta, Y.3    Harada, S.4    Makino, H.5    Ota, Z.6
  • 35
    • 0027195980 scopus 로고
    • Selective regulation of metalloproteinase inhibitor (TIMP-1) by oncostatin M in fibroblasts in culture
    • Richards, C. D., M. Shoyab, T. J. Brown, and J. Gauldie. 1993. Selective regulation of metalloproteinase inhibitor (TIMP-1) by oncostatin M in fibroblasts in culture. J. Immunol. 150:5596.
    • (1993) J. Immunol. , vol.150 , pp. 5596
    • Richards, C.D.1    Shoyab, M.2    Brown, T.J.3    Gauldie, J.4
  • 36
    • 0030175403 scopus 로고    scopus 로고
    • Oncostatin M (OSM) stimulates resorption and inhibits synthesis of proteoglycan in porcine articular cartilage explants
    • Hui, W., M. Bell, and G. Carroll. 1996. Oncostatin M (OSM) stimulates resorption and inhibits synthesis of proteoglycan in porcine articular cartilage explants. Cytokine 8:495.
    • (1996) Cytokine , vol.8 , pp. 495
    • Hui, W.1    Bell, M.2    Carroll, G.3
  • 37
    • 0028871313 scopus 로고
    • Interleukin-1 and oncostatin M in combination promote the release of collagen fragments from bovine nasal cartilage in culture
    • Cawston, T. E., A. J. Ellis, G. Humm, E. Lean, D. Ward, and V. Curry. 1995. Interleukin-1 and oncostatin M in combination promote the release of collagen fragments from bovine nasal cartilage in culture. Biochem. Biophys. Res. Commun. 215:377.
    • (1995) Biochem. Biophys. Res. Commun. , vol.215 , pp. 377
    • Cawston, T.E.1    Ellis, A.J.2    Humm, G.3    Lean, E.4    Ward, D.5    Curry, V.6
  • 38
    • 0029960961 scopus 로고    scopus 로고
    • Stimulation of TIMP-1 production by oncostatin M in human articular cartilage
    • Nemoto, O., H. Yamada, M. Mukaida, and M. Shimmei. 1996. Stimulation of TIMP-1 production by oncostatin M in human articular cartilage. Arthritis Rheum. 39:560.
    • (1996) Arthritis Rheum. , vol.39 , pp. 560
    • Nemoto, O.1    Yamada, H.2    Mukaida, M.3    Shimmei, M.4
  • 39
    • 0029849180 scopus 로고    scopus 로고
    • Oncostatin M differentially regulates tissue inhibitors of metalloproteinases TIMP-1 and TIMP-3 gene expression in human synovial lining cells
    • Gastios, P., H. D. Haubeck, E. Van de Leur, W. Frisch, S. S. Apte, H. Greiling, P. C. Heinrich, and L. Graeve. 1996. Oncostatin M differentially regulates tissue inhibitors of metalloproteinases TIMP-1 and TIMP-3 gene expression in human synovial lining cells. Ear. J. Biochem. 241:56.
    • (1996) Ear. J. Biochem. , vol.241 , pp. 56
    • Gastios, P.1    Haubeck, H.D.2    Van De Leur, E.3    Frisch, W.4    Apte, S.S.5    Greiling, H.6    Heinrich, P.C.7    Graeve, L.8
  • 40
    • 0029583775 scopus 로고
    • The chondrocyte, architect of cartilage: Biomechanics, structure, function and molecular biology of cartilage matrix macromolecules
    • Muir, H. 1995 The chondrocyte, architect of cartilage: biomechanics, structure, function and molecular biology of cartilage matrix macromolecules. BioEssays 17:1039.
    • (1995) BioEssays , vol.17 , pp. 1039
    • Muir, H.1
  • 41
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P., and N. Sacchi. 1987. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162: 156.
    • (1987) Anal. Biochem. , vol.162 , pp. 156
    • Chomczynski, P.1    Sacchi, N.2
  • 42
    • 0027287364 scopus 로고
    • Elevated metalloproteinase and tissue inhibitor of metalloproteinase mRNA in human osteoarthritic synovia
    • Zafarullah, M., J.-P. Pelletier, J. M. Cloutier, and J. Martel-Pelletier. 1993. Elevated metalloproteinase and tissue inhibitor of metalloproteinase mRNA in human osteoarthritic synovia. J. Rheumatol. 20:693.
    • (1993) J. Rheumatol. , vol.20 , pp. 693
    • Zafarullah, M.1    Pelletier, J.-P.2    Cloutier, J.M.3    Martel-Pelletier, J.4
  • 44
    • 2442724379 scopus 로고
    • Transforming growth factor β modulates the expression of collagenase and metalloproteinase inhibitor
    • Edwards, D. R., G. Murphy, J. J. Reynolds, S. E. Whitham, A. J. P. Docherty, P. Angel, and J. K. Heath. 1987. Transforming growth factor β modulates the expression of collagenase and metalloproteinase inhibitor. EMBO J. 6:1899.
    • (1987) EMBO J. , vol.6 , pp. 1899
    • Edwards, D.R.1    Murphy, G.2    Reynolds, J.J.3    Whitham, S.E.4    Docherty, A.J.P.5    Angel, P.6    Heath, J.K.7
  • 46
    • 0025734094 scopus 로고
    • Interleukin-6 induces the synthesis of tissue inhibitor of metalloproteinases-1/erythroid potentiating activity (TTMP-1/EPA)
    • Lotz, M., and P.-A. Gueme. 1991. Interleukin-6 induces the synthesis of tissue inhibitor of metalloproteinases-1/erythroid potentiating activity (TTMP-1/EPA). J. Biol. Chem. 266:2017.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2017
    • Lotz, M.1    Gueme, P.-A.2
  • 47
    • 0027527343 scopus 로고
    • Interleukin-11, an inducible cytokine in human articular chondrocytes and synoviocytes, stimulates the production of the tissue inhibitor of metalloproteinases
    • Maier, R., V. Ganu, and M. Lotz. 1993. Interleukin-11, an inducible cytokine in human articular chondrocytes and synoviocytes, stimulates the production of the tissue inhibitor of metalloproteinases. J. Biol. Chem. 268:21527.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21527
    • Maier, R.1    Ganu, V.2    Lotz, M.3
  • 48
    • 0031456588 scopus 로고    scopus 로고
    • Oncostatin M stimulates monocyte chemoattractant protein-1 and interleukin-1-induced matrix metalloproteinase-1 production by human synovial fibroblasts
    • Langdon, C., J. Leith, F. Smith, and C. D. Richards. 1997. Oncostatin M stimulates monocyte chemoattractant protein-1 and interleukin-1-induced matrix metalloproteinase-1 production by human synovial fibroblasts. Arthritis Rheum. 40: 2139.
    • (1997) Arthritis Rheum. , vol.40 , pp. 2139
    • Langdon, C.1    Leith, J.2    Smith, F.3    Richards, C.D.4
  • 49
    • 0025014781 scopus 로고
    • IL-6 production by human articular chondrocytes: Modulation of its synthesis by cytokines, growth factors, and hormones in vitro
    • Gueme, P.-A., D. A. Carson, and M. Lotz. 1990. IL-6 production by human articular chondrocytes: modulation of its synthesis by cytokines, growth factors, and hormones in vitro. J. Immunol. 144:499.
    • (1990) J. Immunol. , vol.144 , pp. 499
    • Gueme, P.-A.1    Carson, D.A.2    Lotz, M.3
  • 50
    • 0026660176 scopus 로고
    • Leukemia inhibitory factor is expressed in cartilage and synovium and can contribute to the pathogenesis of arthritis
    • Lotz M., T. Moats, and P. M. Villiger. 1992. Leukemia inhibitory factor is expressed in cartilage and synovium and can contribute to the pathogenesis of arthritis. J. Clin. Invest. 90:888.
    • (1992) J. Clin. Invest. , vol.90 , pp. 888
    • Lotz, M.1    Moats, T.2    Villiger, P.M.3
  • 51
    • 0028026939 scopus 로고
    • Responsiveness of articular cartilage from normal and inflamed mouse knee joints to various growth factors
    • Verschure, P. J., L. A. Joosten, P. M. van der Kraan, and W. B. Van den Berg. 1994. Responsiveness of articular cartilage from normal and inflamed mouse knee joints to various growth factors. Ann. Rheum. Dis. 53:455.
    • (1994) Ann. Rheum. Dis. , vol.53 , pp. 455
    • Verschure, P.J.1    Joosten, L.A.2    Van Der Kraan, P.M.3    Van Den Berg, W.B.4
  • 52
    • 0030498390 scopus 로고    scopus 로고
    • Cytokines involving gp130 in signal transduction suppressed growth of a mouse hybridoma cell line and enhanced its antibody production
    • Terada, S., E. Suzuki, H. Ueda, and F. Makishima. 1996. Cytokines involving gp130 in signal transduction suppressed growth of a mouse hybridoma cell line and enhanced its antibody production. Cytokine 8:889.
    • (1996) Cytokine , vol.8 , pp. 889
    • Terada, S.1    Suzuki, E.2    Ueda, H.3    Makishima, F.4
  • 53
    • 0025188132 scopus 로고
    • Transcriptional interference between c-Jun and the glucocorticoid receptor: Mutual inhibition of DNA binding due to direct protein-protein interaction
    • Yang-Yen, H.-F., J.-C. Chambard, Y.-L. Sun, T. Smeal, T. J. Schmidt, J. Drouin, and M. Karin. 1990. Transcriptional interference between c-Jun and the glucocorticoid receptor: mutual inhibition of DNA binding due to direct protein-protein interaction. Cell 62:1205.
    • (1990) Cell , vol.62 , pp. 1205
    • Yang-Yen, H.-F.1    Chambard, J.-C.2    Sun, Y.-L.3    Smeal, T.4    Schmidt, T.J.5    Drouin, J.6    Karin, M.7
  • 54
    • 0031105350 scopus 로고    scopus 로고
    • Glucocorticoids inhibit oncostatin M-induced phospholipase A2 gene expression in human hepatoma cells
    • Haselmann, J., and M. Goppelt-Struebe. 1997. Glucocorticoids inhibit oncostatin M-induced phospholipase A2 gene expression in human hepatoma cells. Cytokine 9:199.
    • (1997) Cytokine , vol.9 , pp. 199
    • Haselmann, J.1    Goppelt-Struebe, M.2
  • 55
    • 0031159942 scopus 로고    scopus 로고
    • Enhancement of gp130-mediated tyrosine phosphorylation of STAT3 and its DNA-binding activity in dexamethasone-treated AIDS-associated Kaposi's sarcoma cells: Selective synergy between dexamethasone and gp130-related growth factors in Kaposi's sarcoma cell proliferation
    • Murakami-Mori, K., S. Mori, T. Taga, T. Kishimoto, and S. Nakamura. 1997. Enhancement of gp130-mediated tyrosine phosphorylation of STAT3 and its DNA-binding activity in dexamethasone-treated AIDS-associated Kaposi's sarcoma cells: selective synergy between dexamethasone and gp130-related growth factors in Kaposi's sarcoma cell proliferation. J. Immunol. 158:5518.
    • (1997) J. Immunol. , vol.158 , pp. 5518
    • Murakami-Mori, K.1    Mori, S.2    Taga, T.3    Kishimoto, T.4    Nakamura, S.5
  • 56
    • 0027633575 scopus 로고
    • Induction of Egr-1 by oncostalin M precedes up-regulation of low density lipoprotein receptors in HepG2 cells
    • Liu, J., M. Shoyab, and R. I. Grove. 1993. Induction of Egr-1 by oncostalin M precedes up-regulation of low density lipoprotein receptors in HepG2 cells. Cell Growth Differ. 4:611.
    • (1993) Cell Growth Differ. , vol.4 , pp. 611
    • Liu, J.1    Shoyab, M.2    Grove, R.I.3
  • 57
    • 0028359835 scopus 로고
    • JAK protein tyrosine kinases: Their role in cytokine signaling
    • Ziemiecki, A., A. G. Harper, and A. F. Wilks. 1994. JAK protein tyrosine kinases: their role in cytokine signaling. Trends Cell Biol. 4:207.
    • (1994) Trends Cell Biol. , vol.4 , pp. 207
    • Ziemiecki, A.1    Harper, A.G.2    Wilks, A.F.3
  • 58
    • 0030046753 scopus 로고    scopus 로고
    • STATs: Signal transducers and activators of transcription
    • Ihle, J. N. 1996. STATs: signal transducers and activators of transcription. Cell 84:331.
    • (1996) Cell , vol.84 , pp. 331
    • Ihle, J.N.1
  • 60
    • 0030330489 scopus 로고    scopus 로고
    • Signal transduction and TGF-β superfamily receptors
    • Kolodziejczyk, S. M., and B. K. Hall. 1996. Signal transduction and TGF-β superfamily receptors. Biochem. Cell Biol. 74:299.
    • (1996) Biochem. Cell Biol. , vol.74 , pp. 299
    • Kolodziejczyk, S.M.1    Hall, B.K.2
  • 61
    • 0027297260 scopus 로고
    • Oncostatin-M stimulates tyrosine protein phosphorylation in parallel with the activation of p42 MAPK/ERK-2 in Kaposi's cells: Evidence that this pathway is important in Kaposi cell growth
    • Amaral, M. C., S. Miles, G. Kumar, and A. E. Nel. 1993. Oncostatin-M stimulates tyrosine protein phosphorylation in parallel with the activation of p42 MAPK/ERK-2 in Kaposi's cells: evidence that this pathway is important in Kaposi cell growth. J. Clin. Invest. 92:848.
    • (1993) J. Clin. Invest. , vol.92 , pp. 848
    • Amaral, M.C.1    Miles, S.2    Kumar, G.3    Nel, A.E.4
  • 62
    • 0029624350 scopus 로고
    • Identification of the interleukin-6/oncostatin M response element in the rat tissue inhibitor of metalloproteinases-1 (TIMP-1) promoter
    • Bugno, M., L. Graeve, P. Gatsios, A. Koj, P. C. Heinrich, J. Travis, and T. Kordula. 1995. Identification of the interleukin-6/oncostatin M response element in the rat tissue inhibitor of metalloproteinases-1 (TIMP-1) promoter. Nucleic Acids Res. 23:5041.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 5041
    • Bugno, M.1    Graeve, L.2    Gatsios, P.3    Koj, A.4    Heinrich, P.C.5    Travis, J.6    Kordula, T.7
  • 63
    • 0031022889 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase and JAK-STAT signaling pathways are required for an oncostatin M-responsive element-mediated activation of matrix metalloproteinase 1 gene expression
    • Korzus, E., H. Nagase, R. Rydell, and J. Travis. 1996. The mitogen-activated protein kinase and JAK-STAT signaling pathways are required for an oncostatin M-responsive element-mediated activation of matrix metalloproteinase 1 gene expression. J. Biol. Chem. 272:1188.
    • (1996) J. Biol. Chem. , vol.272 , pp. 1188
    • Korzus, E.1    Nagase, H.2    Rydell, R.3    Travis, J.4


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