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Volumn 97, Issue 9, 1996, Pages 2011-2019

The new collagenase, collagenase-3, is expressed and synthesized by human chondrocytes but not by synoviocytes: A role in osteoarthritis

Author keywords

arthritis; cartilage; chondrocytes; collagen; cytokines

Indexed keywords

COLLAGEN; COLLAGEN TYPE 2; COLLAGENASE; CYTOKINE; INTERLEUKIN 1BETA; MESSENGER RNA; STRUCTURAL PROTEIN; TUMOR NECROSIS FACTOR ALPHA;

EID: 0029880393     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI118636     Document Type: Article
Times cited : (439)

References (56)
  • 2
    • 0023069839 scopus 로고
    • The collagens: An overview and update
    • Miller, E.J., and S. Gay. 1987. The collagens: an overview and update. Methods Enzymol. 144:3-41.
    • (1987) Methods Enzymol. , vol.144 , pp. 3-41
    • Miller, E.J.1    Gay, S.2
  • 3
    • 0001931432 scopus 로고
    • Type XI or 1α2α3α collagen
    • R. Mayne and R.E. Burgeson, editors. Academic Press Inc., New York
    • Eyre, D., and J.J. Wu. 1987. Type XI or 1α2α3α collagen. In Structure and Functions of Collagen Types. R. Mayne and R.E. Burgeson, editors. Academic Press Inc., New York. 261-281.
    • (1987) Structure and Functions of Collagen Types , pp. 261-281
    • Eyre, D.1    Wu, J.J.2
  • 4
    • 0025034976 scopus 로고
    • Chondrons from articular cartilage (II): Analysis of the glycosaminoglycans in the cellular microenvironment of isolated canine chondrons
    • Poole, C.A., T. Honda, S.J. Skinner, J.R. Schofield, K.F. Hyde, and H. Shinkai. 1990. Chondrons from articular cartilage (II): analysis of the glycosaminoglycans in the cellular microenvironment of isolated canine chondrons. Connect. Tissue Res. 24:319-330.
    • (1990) Connect. Tissue Res. , vol.24 , pp. 319-330
    • Poole, C.A.1    Honda, T.2    Skinner, S.J.3    Schofield, J.R.4    Hyde, K.F.5    Shinkai, H.6
  • 5
    • 0024513679 scopus 로고
    • Cartilage collagens. What is their function, and are they involved in articular disease?
    • Mayne, R. 1989. Cartilage collagens. What is their function, and are they involved in articular disease? Arthritis & Rheum. 32:241-246.
    • (1989) Arthritis & Rheum. , vol.32 , pp. 241-246
    • Mayne, R.1
  • 6
    • 0024343699 scopus 로고
    • Bovine cartilage types VI and IX collagens. Characterization of their forms in vivo
    • Ayad, S., A. Maniott, K. Morgan, and M.E. Grant. 1989. Bovine cartilage types VI and IX collagens. Characterization of their forms in vivo. Biochem. J. 262:753-761.
    • (1989) Biochem. J. , vol.262 , pp. 753-761
    • Ayad, S.1    Maniott, A.2    Morgan, K.3    Grant, M.E.4
  • 7
    • 0001822851 scopus 로고
    • Type IX collagen
    • R. Mayne and R.E. Burgeson, editors. Academic Press Inc., New York
    • Van der Rest, M., and R. Mayne. 1987. Type IX collagen. In Structure and Functions of Collagen Types. R. Mayne and R.E. Burgeson, editors. Academic Press Inc., New York. 195-221.
    • (1987) Structure and Functions of Collagen Types , pp. 195-221
    • Van Der Rest, M.1    Mayne, R.2
  • 8
    • 0002023957 scopus 로고
    • Type X collagen
    • R. Mayne and R.E. Burgeson, editors. Academic Press Inc., New York
    • Schmid, T.M., and T.F. Linsenmayer. 1987. Type X collagen. In Structure and Functions of Collagen Types. R. Mayne and R.E. Burgeson, editors. Academic Press Inc., New York. 223-257.
    • (1987) Structure and Functions of Collagen Types , pp. 223-257
    • Schmid, T.M.1    Linsenmayer, T.F.2
  • 9
    • 0023615844 scopus 로고
    • A growing family of collagens in articular cartilage: Identification of 5 genetically distinct types
    • Eyre, D.R., J.J. Wu, and S. Apone. 1987. A growing family of collagens in articular cartilage: identification of 5 genetically distinct types. J. Rheumatol. 14:25-27.
    • (1987) J. Rheumatol. , vol.14 , pp. 25-27
    • Eyre, D.R.1    Wu, J.J.2    Apone, S.3
  • 10
    • 0015937841 scopus 로고
    • The tensile properties of the cartilage of human femoral condyles related to the content of collagen and glycosaminoglycans
    • Kempson, G.E., H. Muir, C. Pollard, and M. Tuke. 1973. The tensile properties of the cartilage of human femoral condyles related to the content of collagen and glycosaminoglycans. Biochim. Biophys. Acta. 297:456-472.
    • (1973) Biochim. Biophys. Acta , vol.297 , pp. 456-472
    • Kempson, G.E.1    Muir, H.2    Pollard, C.3    Tuke, M.4
  • 11
    • 0017160389 scopus 로고
    • The effects of proteolytic enzymes on the mechanical properties of adult human articular cartilage
    • Kempson, G.E., M.A. Tuke, J.T. Dingle, A.J. Barrett, and P.H. Horsfield. 1976. The effects of proteolytic enzymes on the mechanical properties of adult human articular cartilage. Biochim. Biophys. Acta. 428:741-760.
    • (1976) Biochim. Biophys. Acta , vol.428 , pp. 741-760
    • Kempson, G.E.1    Tuke, M.A.2    Dingle, J.T.3    Barrett, A.J.4    Horsfield, P.H.5
  • 12
    • 0024549792 scopus 로고
    • Immunohistochemical detection and immunochemical analysis of type II collagen degradation in human normal, rheumatoid, and osteoarthritic articular cartilages and in explants of bovine articular cartilage cultured with interleukin 1
    • Dodge, G.R., and A.R. Poole. 1989. Immunohistochemical detection and immunochemical analysis of type II collagen degradation in human normal, rheumatoid, and osteoarthritic articular cartilages and in explants of bovine articular cartilage cultured with interleukin 1. J. Clin. Invest. 83:647-661.
    • (1989) J. Clin. Invest. , vol.83 , pp. 647-661
    • Dodge, G.R.1    Poole, A.R.2
  • 15
    • 0025897125 scopus 로고
    • Proteinase-mediated cartilage degradation in osteoarthritis
    • Dean, D.D. 1991. Proteinase-mediated cartilage degradation in osteoarthritis. Semin. Arthritis Rheum. 20:2-11.
    • (1991) Semin. Arthritis Rheum. , vol.20 , pp. 2-11
    • Dean, D.D.1
  • 17
    • 0024853170 scopus 로고
    • Matrix metalloproteinases and tissue inhibitor of metalloproteinases: A review of their role in tumorigenesis and tissue invasion
    • Khokha, R., and D.T. Denhardt. 1989. Matrix metalloproteinases and tissue inhibitor of metalloproteinases: a review of their role in tumorigenesis and tissue invasion. Invasion & Metastasis. 9:391-405.
    • (1989) Invasion & Metastasis , vol.9 , pp. 391-405
    • Khokha, R.1    Denhardt, D.T.2
  • 18
    • 0018068793 scopus 로고
    • The role of polar and hydrophobic interactions for the molecular packing of type I collagen: A three-dimensional evaluation of the amino acid sequence
    • Hofmann, H., P.P. Fietzek, and K. Kuhn. 1978. The role of polar and hydrophobic interactions for the molecular packing of type I collagen: a three-dimensional evaluation of the amino acid sequence. J. Mol. Biol. 125:137-165.
    • (1978) J. Mol. Biol. , vol.125 , pp. 137-165
    • Hofmann, H.1    Fietzek, P.P.2    Kuhn, K.3
  • 20
    • 0018598695 scopus 로고
    • Covalent structure of collagen: Amino acid sequence of alpha 2-CB5 of chick skin collagen containing the animal collagenase cleavage site
    • Dixit, S.N., C.L. Mainardi, J.M. Seyer, and A.H. Kang. 1979. Covalent structure of collagen: amino acid sequence of alpha 2-CB5 of chick skin collagen containing the animal collagenase cleavage site. Biochemistry. 18:5416-5422.
    • (1979) Biochemistry , vol.18 , pp. 5416-5422
    • Dixit, S.N.1    Mainardi, C.L.2    Seyer, J.M.3    Kang, A.H.4
  • 21
    • 0025847582 scopus 로고
    • Matrix metalloproteinases and their inhibitors in connective tissue remodeling
    • Woessner, J. F., Jr. 1991. Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB J. 5:2145-2154.
    • (1991) FASEB J. , vol.5 , pp. 2145-2154
    • Woessner Jr., J.F.1
  • 22
    • 0025230509 scopus 로고
    • Metalloproteinases and their inhibitors in matrix remodeling
    • Matrisian, L.M. 1990. Metalloproteinases and their inhibitors in matrix remodeling. Trends Genet. 6:121-125.
    • (1990) Trends Genet. , vol.6 , pp. 121-125
    • Matrisian, L.M.1
  • 23
    • 0024603047 scopus 로고
    • Purification of the neutral proteoglycan-degrading metalloproteinase from human articular cartilage tissue and its identification as stromelysin matrix metalloproteinase-3
    • Gunja-Smith, Z., H. Nagase, and J.F. Woessner, Jr. 1989. Purification of the neutral proteoglycan-degrading metalloproteinase from human articular cartilage tissue and its identification as stromelysin matrix metalloproteinase-3. Biochem. J. 258:115-119.
    • (1989) Biochem. J. , vol.258 , pp. 115-119
    • Gunja-Smith, Z.1    Nagase, H.2    Woessner Jr., J.F.3
  • 24
    • 0028947020 scopus 로고
    • Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4- and 1/4-length fragments
    • Aimes, R.T., and J.P. Quigley. 1995. Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4- and 1/4-length fragments. J. Biol. Chem. 270:5872-5876.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5872-5876
    • Aimes, R.T.1    Quigley, J.P.2
  • 25
    • 0025949206 scopus 로고
    • Sites of stromelysin cleavage in collagen types II, IX, X, and XI of cartilage
    • Wu, J.J., M.W. Lark, L.E. Chun, and D.R. Eyre. 1991. Sites of stromelysin cleavage in collagen types II, IX, X, and XI of cartilage. J. Biol. Chem. 266: 5625-5628.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5625-5628
    • Wu, J.J.1    Lark, M.W.2    Chun, L.E.3    Eyre, D.R.4
  • 26
    • 0028322352 scopus 로고
    • Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas
    • Freije, J.M., I. Diez-Itza, M. Balbin, L.M. Sanchez, R. Blasco, J. Tolivia, and C. Lopez-Otin. 1994. Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas. J. Biol. Chem. 269:16766-16773.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16766-16773
    • Freije, J.M.1    Diez-Itza, I.2    Balbin, M.3    Sanchez, L.M.4    Blasco, R.5    Tolivia, J.6    Lopez-Otin, C.7
  • 27
    • 0029001324 scopus 로고
    • The human collagenase-3 (CLG-3) gene is located on chromosome 11q22.3 clustered to other members of the matrix metalloproteinase gene family
    • Pendas, A.M., T. Matilla, X. Estivill, and C. Lopez-Otin. 1995. The human collagenase-3 (CLG-3) gene is located on chromosome 11q22.3 clustered to other members of the matrix metalloproteinase gene family. Genomics. 26: 615-618.
    • (1995) Genomics , vol.26 , pp. 615-618
    • Pendas, A.M.1    Matilla, T.2    Estivill, X.3    Lopez-Otin, C.4
  • 29
    • 0028247201 scopus 로고
    • Excess of metalloproteases over tissue inhibitor of metalloprotease may contribute to cartilage degradation in osteoarthritis and rheumatoid arthritis
    • Martel-Pelletier, J., R. McCollum, N. Fujimoto, K. Obata, J.M. Cloutier, and J.P. Pelletier. 1994. Excess of metalloproteases over tissue inhibitor of metalloprotease may contribute to cartilage degradation in osteoarthritis and rheumatoid arthritis. Lab. Invest. 70:807-815.
    • (1994) Lab. Invest. , vol.70 , pp. 807-815
    • Martel-Pelletier, J.1    McCollum, R.2    Fujimoto, N.3    Obata, K.4    Cloutier, J.M.5    Pelletier, J.P.6
  • 30
    • 0029085898 scopus 로고
    • Human synovial fibroblasts coexpress interleukin-1 receptor type I and type II mRNA: The increased level of the interleukin-1 receptor in osteoarthritic cells is related to an increased level of the type 1 receptor
    • Sadouk, M., J.P. Pelletier, G. Tardif, K. Kiansa, J.M. Cloutier, and J. Martel-Pelletier. 1995. Human synovial fibroblasts coexpress interleukin-1 receptor type I and type II mRNA: the increased level of the interleukin-1 receptor in osteoarthritic cells is related to an increased level of the type 1 receptor. Lab. Invest. 73:347-355.
    • (1995) Lab. Invest. , vol.73 , pp. 347-355
    • Sadouk, M.1    Pelletier, J.P.2    Tardif, G.3    Kiansa, K.4    Cloutier, J.M.5    Martel-Pelletier, J.6
  • 32
    • 0015716692 scopus 로고
    • A rapid, sensitive, and specific method for the determination of protein in dilute solution
    • Schaffner, W., and C. Weissmann. 1973. A rapid, sensitive, and specific method for the determination of protein in dilute solution. Anal. Biochem. 56: 502-514.
    • (1973) Anal. Biochem. , vol.56 , pp. 502-514
    • Schaffner, W.1    Weissmann, C.2
  • 33
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 34
    • 0019888405 scopus 로고
    • Human skin fibroblast collagenase. Assessment of activation energy and deuterium isotope effect with collagenous substrates
    • Welgus, H.G., J.J. Jeffrey, and A.Z. Eisen. 1981. Human skin fibroblast collagenase. Assessment of activation energy and deuterium isotope effect with collagenous substrates. J. Biol. Chem. 256:9516-9521.
    • (1981) J. Biol. Chem. , vol.256 , pp. 9516-9521
    • Welgus, H.G.1    Jeffrey, J.J.2    Eisen, A.Z.3
  • 35
    • 0021052777 scopus 로고
    • The collagen substrate specificity of rat uterus collagenase
    • Welgus, H.G., D.K. Kobayashi, and J.J. Jeffrey. 1983. The collagen substrate specificity of rat uterus collagenase. J. Biol. Chem. 258:14162-14165.
    • (1983) J. Biol. Chem. , vol.258 , pp. 14162-14165
    • Welgus, H.G.1    Kobayashi, D.K.2    Jeffrey, J.J.3
  • 36
    • 0023492506 scopus 로고
    • Cloning of a complementary DNA for rabbit pro-activator. A metalloproteinase that activates synovial cell collagenase, shares homology with stromelysin and transin, and is coordinately regulated with collagenase
    • Fini, M.E., M.J. Karmilowicz, P.L. Ruby, A.M. Beeman, K.A. Borges, and C.E. Brinckerhoff. 1987. Cloning of a complementary DNA for rabbit pro-activator. A metalloproteinase that activates synovial cell collagenase, shares homology with stromelysin and transin, and is coordinately regulated with collagenase. Arthritis & Rheum. 30:1255-1264.
    • (1987) Arthritis & Rheum. , vol.30 , pp. 1255-1264
    • Fini, M.E.1    Karmilowicz, M.J.2    Ruby, P.L.3    Beeman, A.M.4    Borges, K.A.5    Brinckerhoff, C.E.6
  • 38
    • 0021717618 scopus 로고
    • Cytokines and other mediators in rheumatoid arthritis
    • Dayer, J.M., and S. Demczuk. 1984. Cytokines and other mediators in rheumatoid arthritis. Springer Semin. Immunopathol. 7:387-413.
    • (1984) Springer Semin. Immunopathol. , vol.7 , pp. 387-413
    • Dayer, J.M.1    Demczuk, S.2
  • 39
    • 0024473876 scopus 로고
    • Immunolocalization of matrix metalloproteinase 3 (stromelysin) in rheumatoid synovioblasts (B cells): Correlation with rheumatoid arthritis
    • Okada, Y., N. Takeuchi, K. Tomita, I. Nakanishi, and H. Nagase. 1989. Immunolocalization of matrix metalloproteinase 3 (stromelysin) in rheumatoid synovioblasts (B cells): correlation with rheumatoid arthritis. Ann. Rheum. Dis. 48:645-653.
    • (1989) Ann. Rheum. Dis. , vol.48 , pp. 645-653
    • Okada, Y.1    Takeuchi, N.2    Tomita, K.3    Nakanishi, I.4    Nagase, H.5
  • 41
    • 0024330327 scopus 로고
    • SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages
    • Wilhelm, S.M., I.E. Collier, B.L. Marmer, A.Z. Eisen, G.A. Grant, and G.I. Goldberg. 1989. SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages. J. Biol. Chem. 264:17213-17221.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17213-17221
    • Wilhelm, S.M.1    Collier, I.E.2    Marmer, B.L.3    Eisen, A.Z.4    Grant, G.A.5    Goldberg, G.I.6
  • 42
    • 0025616093 scopus 로고
    • Matrix metalloproteinase 2 from human rheumatoid synovial fibroblasts. Purification and activation of the precursor and enzymic properties
    • Okada, Y., T. Morodomi, J.J. Enghild, K. Suzuki, A. Yasui, I. Nakanishi, G. Salvesen, and H. Nagase. 1990. Matrix metalloproteinase 2 from human rheumatoid synovial fibroblasts. Purification and activation of the precursor and enzymic properties. Eur. J. Biochem. 194:721-730.
    • (1990) Eur. J. Biochem. , vol.194 , pp. 721-730
    • Okada, Y.1    Morodomi, T.2    Enghild, J.J.3    Suzuki, K.4    Yasui, A.5    Nakanishi, I.6    Salvesen, G.7    Nagase, H.8
  • 43
    • 0025074287 scopus 로고
    • Induction and stimulation of 92-kDa gelatinase/type IV collagenase production in osteosarcoma and fibrosarcoma cell lines by tumor necrosis factor alpha
    • Okada, Y., H. Tsuchiya, H. Shimizu, K. Tomita, I. Nakanishi, H. Sato, M. Seiki, K. Yamashita, and T. Hayakawa. 1990. Induction and stimulation of 92-kDa gelatinase/type IV collagenase production in osteosarcoma and fibrosarcoma cell lines by tumor necrosis factor alpha. Biochem. Biophys. Res. Commun. 171:610-617.
    • (1990) Biochem. Biophys. Res. Commun. , vol.171 , pp. 610-617
    • Okada, Y.1    Tsuchiya, H.2    Shimizu, H.3    Tomita, K.4    Nakanishi, I.5    Sato, H.6    Seiki, M.7    Yamashita, K.8    Hayakawa, T.9
  • 44
    • 0025728412 scopus 로고
    • Isolation and characterization of a 70-kDa metalloprotease (gelatinase) that is elevated in Rous sarcoma virus-transformed chicken embryo fibroblasts
    • Chen, J.M., R.T. Aimes, G.R. Ward, G.L. Youngleib, and J.P. Quigley. 1991. Isolation and characterization of a 70-kDa metalloprotease (gelatinase) that is elevated in Rous sarcoma virus-transformed chicken embryo fibroblasts. J. Biol. Chem. 266:5113-5121.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5113-5121
    • Chen, J.M.1    Aimes, R.T.2    Ward, G.R.3    Youngleib, G.L.4    Quigley, J.P.5
  • 45
    • 0029009223 scopus 로고
    • Constitutive production of 92-kDa gelatinase B can be suppressed by alterations in cell shape
    • MacDougall, J.R., and R.S. Kerbel. 1995. Constitutive production of 92-kDa gelatinase B can be suppressed by alterations in cell shape. Exp. Cell Res. 218:508-515.
    • (1995) Exp. Cell Res. , vol.218 , pp. 508-515
    • MacDougall, J.R.1    Kerbel, R.S.2
  • 46
    • 0026708439 scopus 로고
    • Preferential mRNA expression of prostromelysin relative to procollagenase and in situ localization in human articular cartilage
    • Nguyen, Q., J.S. Mort, and P.J. Roughley. 1992. Preferential mRNA expression of prostromelysin relative to procollagenase and in situ localization in human articular cartilage. J. Clin. Invest. 89:1189-1197.
    • (1992) J. Clin. Invest. , vol.89 , pp. 1189-1197
    • Nguyen, Q.1    Mort, J.S.2    Roughley, P.J.3
  • 47
    • 0027493767 scopus 로고
    • Differential in vivo expression of collagenase messenger RNA in synovium and cartilage: Quantitative comparison with stromelysin messenger RNA levels in human rheumatoid arthritis and osteoarthritis patients and in two animal models of acute inflammatory arthritis
    • Wolfe, G.C., K.L. MacNaul, F.F. Buechel, J. McDonnell, L.A. Hoerrner, M.W. Lark, V.L. Moore, and N.I. Hutchinson. 1993. Differential in vivo expression of collagenase messenger RNA in synovium and cartilage: quantitative comparison with stromelysin messenger RNA levels in human rheumatoid arthritis and osteoarthritis patients and in two animal models of acute inflammatory arthritis. Arthritis & Rheum. 36:1540-1547.
    • (1993) Arthritis & Rheum. , vol.36 , pp. 1540-1547
    • Wolfe, G.C.1    MacNaul, K.L.2    Buechel, F.F.3    McDonnell, J.4    Hoerrner, L.A.5    Lark, M.W.6    Moore, V.L.7    Hutchinson, N.I.8
  • 48
    • 0028342981 scopus 로고
    • Analysis of the role of the COOH-terminal domain in the activation, proteolytic activity, and tissue inhihitor of metalloproteinase interactions of gelatinase B
    • Leco, K.J., R. Khokha, N. Pavloff, S.P. Hawkes, and D.R. Edwards. 1994. Analysis of the role of the COOH-terminal domain in the activation, proteolytic activity, and tissue inhihitor of metalloproteinase interactions of gelatinase B. J. Biol. Chem. 269:14967-14973.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14967-14973
    • Leco, K.J.1    Khokha, R.2    Pavloff, N.3    Hawkes, S.P.4    Edwards, D.R.5
  • 49
    • 0029065271 scopus 로고
    • Characterization of rat uterine matrilysin and its cDNA. Relationship to human pump-1 and activation of procollagenases
    • Abramson, S.R., G.E. Conner, H. Nagase, I. Neuhaus, and J.F. Woessner, Jr. 1995. Characterization of rat uterine matrilysin and its cDNA. Relationship to human pump-1 and activation of procollagenases. J. Biol. Chem. 270: 16016-16022.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16016-16022
    • Abramson, S.R.1    Conner, G.E.2    Nagase, H.3    Neuhaus, I.4    Woessner Jr., J.F.5
  • 50
    • 0025614357 scopus 로고
    • Rat collagenase. Cloning, amino acid sequence comparison, and parathyroid hormone regulation in osteoblastic cells
    • Quinn, C.O., D.K. Scott, C.E. Brinckerhoff, L.M. Matrisian, JJ. Jeffrey, and N.C. Partridge. 1990. Rat collagenase. Cloning, amino acid sequence comparison, and parathyroid hormone regulation in osteoblastic cells. J. Biol. Chem. 265:22342-22347.
    • (1990) J. Biol. Chem. , vol.265 , pp. 22342-22347
    • Quinn, C.O.1    Scott, D.K.2    Brinckerhoff, C.E.3    Matrisian, L.M.4    Jeffrey, J.J.5    Partridge, N.C.6
  • 51
    • 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. 269:9352-9360.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9352-9360
    • Leco, K.J.1    Khokha, R.2    Pavloff, N.3    Hawkes, S.P.4    Edwards, D.R.5
  • 52
    • 0026162393 scopus 로고
    • Animal cell shape changes and gene expression
    • Ben-Ze'ev, A. 1991. Animal cell shape changes and gene expression. BioEssays. 13:207-212.
    • (1991) BioEssays , vol.13 , pp. 207-212
    • Ben-Ze'ev, A.1
  • 53
    • 0023746647 scopus 로고
    • Influence of cytochalasin D-induced changes in cell shape on proteoglycan synthesis by cultured articular chondrocytes
    • Newman, P., and F.M. Watt. 1988. Influence of cytochalasin D-induced changes in cell shape on proteoglycan synthesis by cultured articular chondrocytes. Exp. Cell Res. 178:199-210.
    • (1988) Exp. Cell Res. , vol.178 , pp. 199-210
    • Newman, P.1    Watt, F.M.2
  • 54
    • 0025819501 scopus 로고
    • Function follows form, generation of intracellular signals by cell deformation
    • Watson, P.A. 1991. Function follows form, generation of intracellular signals by cell deformation. FASEB J. 5:2013-2019.
    • (1991) FASEB J. , vol.5 , pp. 2013-2019
    • Watson, P.A.1
  • 56
    • 0025996837 scopus 로고
    • Study of O-glycan sialylation in C6 cultured glioma cells: Evidence for post-translational regulation of a beta-galactoside alpha 2.3 sialyltransferase activity by N-glycosylation
    • Broquet, P., P. George, J. Geoffroy, P. Reboul, and P. Louisot. 1991. Study of O-glycan sialylation in C6 cultured glioma cells: evidence for post-translational regulation of a beta-galactoside alpha 2.3 sialyltransferase activity by N-glycosylation. Biochem. Biophys. Res. Commun. 178:1437-1443.
    • (1991) Biochem. Biophys. Res. Commun. , vol.178 , pp. 1437-1443
    • Broquet, P.1    George, P.2    Geoffroy, J.3    Reboul, P.4    Louisot, P.5


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