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Volumn 247, Issue 2, 1997, Pages 620-624

Incomplete processing of type II procollagen by a rat chondrosarcoma cell line

Author keywords

Chondrocytes; Chondrosarcoma; Collagen amino proteinase; Collagen type II

Indexed keywords

COLLAGEN FIBRIL; COLLAGEN TYPE 2;

EID: 0030743295     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00620.x     Document Type: Article
Times cited : (18)

References (40)
  • 1
    • 0024595164 scopus 로고
    • Quantitative analysis of collagen expression in embryonic chick chondrocytes having different developmental fates
    • Gerstenfeld, L. C., Finer, M. H. & Boedtker. H. (1989) Quantitative analysis of collagen expression in embryonic chick chondrocytes having different developmental fates. J. Biol. Chem. 264, 5112-5120.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5112-5120
    • Gerstenfeld, L.C.1    Finer, M.H.2    Boedtker, H.3
  • 2
    • 0018292207 scopus 로고
    • Conversion of type II procollagen to collagen. Extracellular removal of the amino-terminal and carboxy-terminal extensions without a preferential sequence
    • Uitto, J., Allan, R. E. & Polak, K. L. (1979) Conversion of type II procollagen to collagen. Extracellular removal of the amino-terminal and carboxy-terminal extensions without a preferential sequence, Eur. J. Biochem. 99, 97-103.
    • (1979) Eur. J. Biochem. , vol.99 , pp. 97-103
    • Uitto, J.1    Allan, R.E.2    Polak, K.L.3
  • 3
    • 0028301441 scopus 로고
    • Self-assembly into fibrils of collagen II by enzymic cleavage of recombinant procollagen II. Lag period, critical concentration, and morphology of fibrils differ from collagen I
    • Fertala, A., Sieron, A. L., Hojima, Y., Ganguly, A. & Prockop, D. J. (1994) Self-assembly into fibrils of collagen II by enzymic cleavage of recombinant procollagen II. Lag period, critical concentration, and morphology of fibrils differ from collagen I, J. Biol. Chem. 269, 11584-11589.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11584-11589
    • Fertala, A.1    Sieron, A.L.2    Hojima, Y.3    Ganguly, A.4    Prockop, D.J.5
  • 4
    • 0030593032 scopus 로고    scopus 로고
    • Bone morphogenetic protein-1 : The type I procollagen C-proteinase
    • Kessler, E., Takahara, K., Biniaminov, L., Brusel, M. & Greenspan, D. S. (1996) Bone morphogenetic protein-1 : the type I procollagen C-proteinase. Science 271, 360-362.
    • (1996) Science , vol.271 , pp. 360-362
    • Kessler, E.1    Takahara, K.2    Biniaminov, L.3    Brusel, M.4    Greenspan, D.S.5
  • 5
    • 0029906315 scopus 로고    scopus 로고
    • The C-proteinase that processes procollagens to fibrillar collagens is identical to the protein previously identified as bone morphogenic protein-1
    • Li, S. W., Sieron, A. L., Fertala. A., Hojima, Y., Arnold, W. V. & Prockop. D. J. (1996) The C-proteinase that processes procollagens to fibrillar collagens is identical to the protein previously identified as bone morphogenic protein-1. Proc. Natl Acad. Sci. USA 93, 5127-5130.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 5127-5130
    • Li, S.W.1    Sieron, A.L.2    Fertala, A.3    Hojima, Y.4    Arnold, W.V.5    Prockop, D.J.6
  • 6
    • 0022392606 scopus 로고
    • Type I procollagen carboxyl-terminal proteinase from chick embryo tendons. Purification and characterization
    • Hojima, Y., van der Rest, M. & Prockop, D. J. (1985) Type I procollagen carboxyl-terminal proteinase from chick embryo tendons. Purification and characterization, J. Biol. Chem. 260, 15996-16003.
    • (1985) J. Biol. Chem. , vol.260 , pp. 15996-16003
    • Hojima, Y.1    Van Der Rest, M.2    Prockop, D.J.3
  • 7
    • 0024818507 scopus 로고
    • Type I procollagen C-proteinase from mouse fibroblasts. Purification and demonstration of a 55-kDa enhancer glycoprotein
    • Kessler, E. & Adar, R. (1989) Type I procollagen C-proteinase from mouse fibroblasts. Purification and demonstration of a 55-kDa enhancer glycoprotein, Eur. J. Biochem. 186, 115-121.
    • (1989) Eur. J. Biochem. , vol.186 , pp. 115-121
    • Kessler, E.1    Adar, R.2
  • 8
    • 0024411470 scopus 로고
    • Type I procollagen N-proteinase from chick embryo tendons. Purification of a new 500-kDa form of the enzyme and identification of the catalytically active polypeptides
    • Hojima, Y., McKenzie, J. A., van der Rest, M. & Prockop. D. J. (1989) Type I procollagen N-proteinase from chick embryo tendons. Purification of a new 500-kDa form of the enzyme and identification of the catalytically active polypeptides. J. Biol. Chem. 264, 11336-11345.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11336-11345
    • Hojima, Y.1    McKenzie, J.A.2    Van Der Rest, M.3    Prockop, D.J.4
  • 9
    • 0027996812 scopus 로고
    • Cleavage of type I procollagen by C- and N-proteinases is more rapid if the substrate is aggregated with dextran sulfate or polyethylene glycol
    • Hojima, Y., Behta, B., Romanic, A. M. & Prockop, D. J. (1994) Cleavage of type I procollagen by C- and N-proteinases is more rapid if the substrate is aggregated with dextran sulfate or polyethylene glycol, Anal. Biochem. 223, 173-180.
    • (1994) Anal. Biochem. , vol.223 , pp. 173-180
    • Hojima, Y.1    Behta, B.2    Romanic, A.M.3    Prockop, D.J.4
  • 10
    • 0029067409 scopus 로고
    • Characterization and partial amino acid sequencing of a 107-kDa procollagen I N-proteinase purified by affinity chromatography on immobilized type XIV collagen
    • Colige, A., Beschin, A., Samyn, B., Goebels, Y., Van Beeumen, J., Nusgens, B. V. & Lapiere, C. M. (1995) Characterization and partial amino acid sequencing of a 107-kDa procollagen I N-proteinase purified by affinity chromatography on immobilized type XIV collagen. J Biol. Chem. 270, 16724-16730.
    • (1995) J Biol. Chem. , vol.270 , pp. 16724-16730
    • Colige, A.1    Beschin, A.2    Samyn, B.3    Goebels, Y.4    Van Beeumen, J.5    Nusgens, B.V.6    Lapiere, C.M.7
  • 11
    • 0016439286 scopus 로고
    • Procollagen peptidase: Its mode of action on the native substrate
    • Goldberg, B., Taubman, M. B. & Radin. A. (1975) Procollagen peptidase: its mode of action on the native substrate. Cell 4, 45-50.
    • (1975) Cell , vol.4 , pp. 45-50
    • Goldberg, B.1    Taubman, M.B.2    Radin, A.3
  • 12
    • 0019482461 scopus 로고
    • Detection of cell-associated aminoterminal procollagen peptidase activity in cultured fibroblasts
    • Layman, D. L. (1981) Detection of cell-associated aminoterminal procollagen peptidase activity in cultured fibroblasts. Proc. Soc. Exp. Biol. Med. 166, 325-329.
    • (1981) Proc. Soc. Exp. Biol. Med. , vol.166 , pp. 325-329
    • Layman, D.L.1
  • 13
    • 0023009265 scopus 로고
    • Defects in the processing of procollagen to collagen are demonstrable in cultured fibroblasts from patients with the Ehlers-Danlos and osteogenesis imperfecta syndromes
    • Minor, R. R., Sippola-Thiele, M., McKeon, J., Berger. J. & Prockop, D. J. (1986) Defects in the processing of procollagen to collagen are demonstrable in cultured fibroblasts from patients with the Ehlers-Danlos and osteogenesis imperfecta syndromes. J. Biol. Chem. 261, 10006-10014.
    • (1986) J. Biol. Chem. , vol.261 , pp. 10006-10014
    • Minor, R.R.1    Sippola-Thiele, M.2    McKeon, J.3    Berger, J.4    Prockop, D.J.5
  • 14
    • 0025308559 scopus 로고
    • Assessment of procollagen processing defects by fibroblasts cultured in the presence of dextran sulphate
    • Bateman, J. F. & Golub. S. B. (1990) Assessment of procollagen processing defects by fibroblasts cultured in the presence of dextran sulphate, Biochem. J. 267, 573-577.
    • (1990) Biochem. J. , vol.267 , pp. 573-577
    • Bateman, J.F.1    Golub, S.B.2
  • 15
    • 0026742497 scopus 로고
    • Human dermatosparaxis: A form of Ehlers-Danlos syndrome that results from failure to remove the N-terminal propeptide of type I procollagen
    • Smith, L. T., Wertelecki, W., Milstone, L. M., Petty, E. M., Seashore, M. R., Braverman, I. M., Jenkins, T. G. & Byers, P. H. (1992) Human dermatosparaxis: a form of Ehlers-Danlos syndrome that results from failure to remove the N-terminal propeptide of type I procollagen, Am. J. Hum. Genet. 51, 235-244.
    • (1992) Am. J. Hum. Genet. , vol.51 , pp. 235-244
    • Smith, L.T.1    Wertelecki, W.2    Milstone, L.M.3    Petty, E.M.4    Seashore, M.R.5    Braverman, I.M.6    Jenkins, T.G.7    Byers, P.H.8
  • 16
    • 0020442640 scopus 로고
    • Metabolism of low molecular mass collagen by chondrocytes obtained from histologically distinct zones of the chick embryo tibiotarsus
    • Schmid, T. M. & Conrad, H. E. (1982) Metabolism of low molecular mass collagen by chondrocytes obtained from histologically distinct zones of the chick embryo tibiotarsus, J. Biol. Chem. 257, 12451-12457.
    • (1982) J. Biol. Chem. , vol.257 , pp. 12451-12457
    • Schmid, T.M.1    Conrad, H.E.2
  • 17
    • 0018098234 scopus 로고
    • Pro-Gln: The procollagen peptidase cleavage site in the α1(I) chain of dermatosparaetic calf skin procollagen
    • Horlein, D., Fietzek, P. P. & Kuhn, K. (1978) Pro-Gln: the procollagen peptidase cleavage site in the α1(I) chain of dermatosparaetic calf skin procollagen. FEBS Lett. 89, 279-282.
    • (1978) FEBS Lett. , vol.89 , pp. 279-282
    • Horlein, D.1    Fietzek, P.P.2    Kuhn, K.3
  • 18
    • 0021718453 scopus 로고
    • Isolation and characterization of a cDNA clone for the N-terminal portion of the proα1(II) chain of cartilage collagen
    • Kohno, K., Martin, G. R. & Yamada, Y. (1984) Isolation and characterization of a cDNA clone for the N-terminal portion of the proα1(II) chain of cartilage collagen. J. Biol. Chem. 259, 13668-13673.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13668-13673
    • Kohno, K.1    Martin, G.R.2    Yamada, Y.3
  • 19
    • 0021918647 scopus 로고
    • Structure of the promoter of the rat type II procollagen gene
    • Kohno, K., Sullivan, M. & Yamada, Y. (1985) Structure of the promoter of the rat type II procollagen gene. J. Biol. Chem. 260, 4441-4447.
    • (1985) J. Biol. Chem. , vol.260 , pp. 4441-4447
    • Kohno, K.1    Sullivan, M.2    Yamada, Y.3
  • 20
    • 0025127912 scopus 로고
    • Structural and functional characterization of a splicing mutation in the proα2(I) collagen gene of an Ehlers-Danlos type VII patient
    • Weil, D., D'Alessio, M., Ramirez, F. & Eyre, D. R. (1990) Structural and functional characterization of a splicing mutation in the proα2(I) collagen gene of an Ehlers-Danlos type VII patient, J. Biol. Chem. 265, 16007-16011.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16007-16011
    • Weil, D.1    D'Alessio, M.2    Ramirez, F.3    Eyre, D.R.4
  • 21
    • 8544259186 scopus 로고
    • Swarm rat chondrosareoma cell line synthesizes cartilage collagens in monolayer culture
    • Fernandes, R. J., King, K. B., Kimura, J. H. & Schmid, T. M. (1993) Swarm rat chondrosareoma cell line synthesizes cartilage collagens in monolayer culture. Orthop. Trans. 17, 831.
    • (1993) Orthop. Trans. , vol.17 , pp. 831
    • Fernandes, R.J.1    King, K.B.2    Kimura, J.H.3    Schmid, T.M.4
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0016203040 scopus 로고
    • A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels
    • Bonner, W. M. & Laskey, R. A. (1974) A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels, Eur. J. Biochem. 46, 83-88.
    • (1974) Eur. J. Biochem. , vol.46 , pp. 83-88
    • Bonner, W.M.1    Laskey, R.A.2
  • 26
  • 27
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P. & Sacchi, N. (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 28
    • 0027169767 scopus 로고
    • A reagent for the single-step simultaneous isolation of RNA. DNA and proteins from cell and tissue samples
    • Chomczynski, P. (1993) A reagent for the single-step simultaneous isolation of RNA. DNA and proteins from cell and tissue samples, Biotechniques 15, 532-537.
    • (1993) Biotechniques , vol.15 , pp. 532-537
    • Chomczynski, P.1
  • 30
    • 0025949448 scopus 로고
    • Mouse type II collagen gene. Complete nucleotide sequence, exon structure, and alternative splicing
    • Metsaranta, M., Toman, D., de Crombrugghe, B. & Vuorio, E. (1991) Mouse type II collagen gene. Complete nucleotide sequence, exon structure, and alternative splicing. J. Biol. Chem. 266, 16862-16869.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16862-16869
    • Metsaranta, M.1    Toman, D.2    De Crombrugghe, B.3    Vuorio, E.4
  • 32
    • 0017711226 scopus 로고
    • Biosynthesis of type II collagen. Removal of amino-and carboxy-terminal extensions from procollagen synthesized by chick embryo cartilage cells
    • Uitto, J. (1977) Biosynthesis of type II collagen. Removal of amino-and carboxy-terminal extensions from procollagen synthesized by chick embryo cartilage cells, Biochemistry 16, 3421-3429.
    • (1977) Biochemistry , vol.16 , pp. 3421-3429
    • Uitto, J.1
  • 34
    • 0015219009 scopus 로고
    • Collagen made of extended α-chains, procollagen, in geneticallydefective dermatosparaxic calves
    • Lenaers, A., Ansay, M., Nusgens, B. V. & Lapiere, C. M. (1971) Collagen made of extended α-chains, procollagen, in geneticallydefective dermatosparaxic calves. Eur. J. Biochem. 23, 533-543.
    • (1971) Eur. J. Biochem. , vol.23 , pp. 533-543
    • Lenaers, A.1    Ansay, M.2    Nusgens, B.V.3    Lapiere, C.M.4
  • 35
    • 0026327127 scopus 로고
    • Fulvic acid disturbs processing of procollagen II in articular cartilage of embryonic chicken and may also cause KashinBeck disease
    • Yang, C. L., Bodo, M., Notbohm, H., Peng, A. & Muller, P. K. (1991) Fulvic acid disturbs processing of procollagen II in articular cartilage of embryonic chicken and may also cause KashinBeck disease, Eur. J.Biochem. 202, 1141-1146.
    • (1991) Eur. J.Biochem. , vol.202 , pp. 1141-1146
    • Yang, C.L.1    Bodo, M.2    Notbohm, H.3    Peng, A.4    Muller, P.K.5
  • 36
    • 0018187844 scopus 로고
    • Partial purification and characterization of a neutral protease which cleaves the N-terininal propeptides from procollagen
    • Tuderman, L., Kivirikko, K. I. & Prockop, D. J. (1978) Partial purification and characterization of a neutral protease which cleaves the N-terininal propeptides from procollagen. Biochemistry. 17. 2948-2954.
    • (1978) Biochemistry , vol.17 , pp. 2948-2954
    • Tuderman, L.1    Kivirikko, K.I.2    Prockop, D.J.3
  • 37
    • 0021991881 scopus 로고
    • Type I procollagen N-proteinase from whole chick embryos. Cleavage of a homotrimer of pro-α1(I) chains and the requirement for procollagen with a triple-helical conformation
    • Tanzawa, K., Berger, J. & Prockop, D. J. (1985) Type I procollagen N-proteinase from whole chick embryos. Cleavage of a homotrimer of pro-α1(I) chains and the requirement for procollagen with a triple-helical conformation. J. Biol. Chem. 260, 1120- 1126.
    • (1985) J. Biol. Chem. , vol.260 , pp. 1120-1126
    • Tanzawa, K.1    Berger, J.2    Prockop, D.J.3
  • 38
    • 0027160737 scopus 로고
    • Learning how mutations in type I collagen genes cause connective tissue disease
    • Kadler, K. E. (1993) Learning how mutations in type I collagen genes cause connective tissue disease. Int. J. Exp. Pathol. 74, 319-323.
    • (1993) Int. J. Exp. Pathol. , vol.74 , pp. 319-323
    • Kadler, K.E.1
  • 39
    • 0026451141 scopus 로고
    • Identification of cross-linking sites in bovine cartilage type IX collagen reveals an anti-parallel type II-type IX molecular relationship and type IX to type IX bonding
    • Wu, J. J., Woods, P. E. & Eyre, D. R. (1992) Identification of cross-linking sites in bovine cartilage type IX collagen reveals an anti-parallel type II-type IX molecular relationship and type IX to type IX bonding. J. Biol. Chem. 267, 23007-23014.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23007-23014
    • Wu, J.J.1    Woods, P.E.2    Eyre, D.R.3
  • 40
    • 0029134143 scopus 로고
    • Structural analysis of cross-linking domains in cartilage type XI collagen. Insights on polymeric assembly
    • Wu, J. J. & Eyre, D. R. (1995) Structural analysis of cross-linking domains in cartilage type XI collagen. Insights on polymeric assembly. J. Biol. Chem. 270, 18865-18870.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18865-18870
    • Wu, J.J.1    Eyre, D.R.2


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