메뉴 건너뛰기




Volumn 16, Issue 3, 1997, Pages 105-116

A cDNA cassette system for the synthesis of recombinant procollagens. Variants of procollagen II lacking a D-period are secreted as triple-helical monomers

Author keywords

cDNA cassettes; Recombinant type II procollagen

Indexed keywords

COLLAGEN FIBRIL; COLLAGEN TYPE 1; COLLAGEN TYPE 2; COMPLEMENTARY DNA; PROCOLLAGEN;

EID: 0030931450     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0945-053X(97)90039-1     Document Type: Article
Times cited : (17)

References (37)
  • 1
    • 0025251582 scopus 로고
    • Completion of the intronexon structure of the gene for human type II procollagen (COL2A1). Variations in the nucleotide sequences of the alleles from three chromosomes
    • Ala-Kokko L., Prockop D.J. Completion of the intronexon structure of the gene for human type II procollagen (COL2A1). Variations in the nucleotide sequences of the alleles from three chromosomes. Genomics. 8:1990;454-460.
    • (1990) Genomics , vol.8 , pp. 454-460
    • Ala-Kokko, L.1    Prockop, D.J.2
  • 3
    • 0025872761 scopus 로고
    • Sequence specific thermal stability of the collagen tripe helix
    • Bächinger H.P., Davis J.M. Sequence specific thermal stability of the collagen tripe helix. Int. J. Biol. Macromol. 13:1991;152-162.
    • (1991) Int. J. Biol. Macromol. , vol.13 , pp. 152-162
    • Bächinger, H.P.1    Davis, J.M.2
  • 4
    • 0027389056 scopus 로고
    • Thermal stability and folding of the collagen triple helix and the effects of mutations in osteogensis imprefecta on the triple helix of type I collagen
    • Bächinger H.P., Morris N.P., Davis J.M. Thermal stability and folding of the collagen triple helix and the effects of mutations in osteogensis imprefecta on the triple helix of type I collagen. Am. J. Med. Genet. 45:1993;152-162.
    • (1993) Am. J. Med. Genet. , vol.45 , pp. 152-162
    • Bächinger, H.P.1    Morris, N.P.2    Davis, J.M.3
  • 5
    • 0024467464 scopus 로고
    • Structure of cDNA clones coding for human type II procolagen. The α1(II) chain is more similar to the α(I) chain than two other a chains of fibrillar collagens
    • Baldwin C.T., Reginato A.M., Smith C., Jimenez S.A., Prockop D.J. Structure of cDNA clones coding for human type II procolagen. The α1(II) chain is more similar to the α(I) chain than two other a chains of fibrillar collagens. Biochem. J. 262:1989;521-528.
    • (1989) Biochem. J. , vol.262 , pp. 521-528
    • Baldwin, C.T.1    Reginato, A.M.2    Smith, C.3    Jimenez, S.A.4    Prockop, D.J.5
  • 6
    • 0003032298 scopus 로고
    • Molecular organization in the collagen fibril
    • D.W.L. Hukins. Deerfield Beach, FL: Verlag Chemie
    • Chapman J.A. Molecular organization in the collagen fibril. Hukins D.W.L. Connective Tissue Matrix. 1984;89-132 Verlag Chemie, Deerfield Beach, FL.
    • (1984) Connective Tissue Matrix , pp. 89-132
    • Chapman, J.A.1
  • 7
    • 0022725107 scopus 로고
    • Infuence of different tripeptides on the stability of the collagen triple helix. I. Analysis of the collagen sequence and identification of typical tripeptides
    • Dölz R., Heidemann E. Infuence of different tripeptides on the stability of the collagen triple helix. I. Analysis of the collagen sequence and identification of typical tripeptides. Biopolymers. 25:1986;1069-1080.
    • (1986) Biopolymers , vol.25 , pp. 1069-1080
    • Dölz, R.1    Heidemann, E.2
  • 9
    • 0002309794 scopus 로고
    • Folding and unfolding of collagen triple helices
    • A.M. Pearson, T.R. Dudson, & A.J. Bailey. Van Nostrand Reinhold
    • Engel J. Folding and unfolding of collagen triple helices. Pearson A.M., Dudson T.R., Bailey A.J. Advances in Meat Research. 1987;145-161 Van Nostrand Reinhold.
    • (1987) Advances in Meat Research , pp. 145-161
    • Engel, J.1
  • 11
    • 0023750874 scopus 로고
    • A synthetic model of collagen: An experimental investigation of the triple-helix stability
    • Germann H.-P., Heidemann E. A synthetic model of collagen: an experimental investigation of the triple-helix stability. Biopolymers. 27:1988;157-163.
    • (1988) Biopolymers , vol.27 , pp. 157-163
    • Germann, H.-P.1    Heidemann, E.2
  • 12
    • 0026782146 scopus 로고
    • Analysis of α1β1, α2β1 and α3β1 integrins in cell-collagen interactions: Identification of conformation dependent α1β1 binding sites in collagen I
    • Gullberg D., Gehlson K.R., Turner D.C., Ahlen K., Zijenah L.S., Barnes M.J., Rubin K. Analysis of α1β1, α2β1 and α3β1 integrins in cell-collagen interactions: identification of conformation dependent α1β1 binding sites in collagen I. EMBO J. 11:1992;3865-3873.
    • (1992) EMBO J. , vol.11 , pp. 3865-3873
    • Gullberg, D.1    Gehlson, K.R.2    Turner, D.C.3    Ahlen, K.4    Zijenah, L.S.5    Barnes, M.J.6    Rubin, K.7
  • 13
    • 0027717615 scopus 로고
    • Binding of fibromodulin and decorin to separate sites on fibrillar collagens
    • Hedbom E., Heineg→ard D. Binding of fibromodulin and decorin to separate sites on fibrillar collagens. J. Biol. Chem. 268:1993;27307-27312.
    • (1993) J. Biol. Chem. , vol.268 , pp. 27307-27312
    • Hedbom, E.1    Heinegard, D.2
  • 14
    • 0020248260 scopus 로고
    • Synthesis and investigation of collagen model peptides
    • Heidemann E., Roth W. Synthesis and investigation of collagen model peptides. Adv. Polym. Sci. 43:1983;143-153.
    • (1983) Adv. Polym. Sci. , vol.43 , pp. 143-153
    • Heidemann, E.1    Roth, W.2
  • 16
    • 0020215497 scopus 로고
    • Synthesis and physical properties of (hydroxyproline-proline-glycine) 10: Hydroxyproline in the X-position decreases the melting temperature of the collagen triple helix
    • Inouye K., Kobayashi Y., Kyogoku Y., Kishida Y., Sakakibara S., Prockop D.J. Synthesis and physical properties of (hydroxyproline-proline-glycine) 10: Hydroxyproline in the X-position decreases the melting temperature of the collagen triple helix. Arch. Biochem. Biophys. 219:1982;198-203.
    • (1982) Arch. Biochem. Biophys. , vol.219 , pp. 198-203
    • Inouye, K.1    Kobayashi, Y.2    Kyogoku, Y.3    Kishida, Y.4    Sakakibara, S.5    Prockop, D.J.6
  • 17
    • 0023748662 scopus 로고
    • Assembly of type I collagen de novo between 37 and 41 °c the process is limited by micro-unfolding of monomers
    • Kadler K.E., Hojima Y., Prockop D.J. Assembly of type I collagen de novo between 37 and 41 °C the process is limited by micro-unfolding of monomers. J. Biol. Chem. 263:1988;1517-10523.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1517-10523
    • Kadler, K.E.1    Hojima, Y.2    Prockop, D.J.3
  • 18
    • 4243355466 scopus 로고
    • The action of proteolytic enzymes on collagen
    • Kühn K., Fietzek P., Kühn J. The action of proteolytic enzymes on collagen. Biochem. Z. 344:1966;418-434.
    • (1966) Biochem. Z. , vol.344 , pp. 418-434
    • Kühn, K.1    Fietzek, P.2    Kühn, J.3
  • 19
    • 0030955414 scopus 로고    scopus 로고
    • Mutations in fibrillar collagen (types I, Ii, III and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vessels
    • Kuivaniemi H., Tromp G., Prockop D.J. Mutations in fibrillar collagen (types I, Ii, III and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vessels. Human Mutation. 9:1997;300-315.
    • (1997) Human Mutation , vol.9 , pp. 300-315
    • Kuivaniemi, H.1    Tromp, G.2    Prockop, D.J.3
  • 20
    • 0025309761 scopus 로고
    • Unfolding intermediates in the triple helix to coil transition of bovine type XI collagen and human type V collagen α1(2)α2 and α1α2α3
    • Morris N.P., Watt S.L., Davis J.M., Bächinger H.P. Unfolding intermediates in the triple helix to coil transition of bovine type XI collagen and human type V collagen α1(2)α2 and α1α2α3. J. Biol. Chem. 265:1990;10081-10087.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10081-10087
    • Morris, N.P.1    Watt, S.L.2    Davis, J.M.3    Bächinger, H.P.4
  • 21
    • 0000002353 scopus 로고
    • Self-assembly of rod-like particles in two dimensions: A simple model of collagen fibrillogenesis
    • Parkinson J., Kadler K.E., Bass A. Self-assembly of rod-like particles in two dimensions: a simple model of collagen fibrillogenesis. Physical Rev. E. 50:1994;2963-2966.
    • (1994) Physical Rev. e , vol.50 , pp. 2963-2966
    • Parkinson, J.1    Kadler, K.E.2    Bass, A.3
  • 22
    • 0003096348 scopus 로고
    • Molecular and aggregate structures of the collagens
    • K.A. Piez, & A.H. Reddi. New York: Elsevier
    • Piez K.A. Molecular and aggregate structures of the collagens. Piez K.A., Reddi A.H. Extracellylar Matrix Biochemistry. 1984;1-40 Elsevier, New York.
    • (1984) Extracellylar Matrix Biochemistry , pp. 1-40
    • Piez, K.A.1
  • 23
    • 0020348367 scopus 로고
    • Stability of proteins, Proteins which do not present a single cooperative system
    • Privalov P.L. Stability of proteins, Proteins which do not present a single cooperative system. Adv. Proteins Chem. 35:1982;1-104.
    • (1982) Adv. Proteins Chem. , vol.35 , pp. 1-104
    • Privalov, P.L.1
  • 24
    • 0002751244 scopus 로고
    • Assembly of collagen fibrils de novo from soluble precursors: Polymerization and copolymerization of procollagen, pN-collagen, and mutated collagens
    • P.D. Yurchenco, D.E. Birk, & R.P. Mecham. New York: Academic Press
    • Prockop D.J., Hulmes D.J.S. Assembly of collagen fibrils de novo from soluble precursors: Polymerization and copolymerization of procollagen, pN-collagen, and mutated collagens. Yurchenco P.D., Birk D.E., Mecham R.P. Extracellular Matrix Assembly and Structure. 1994;47-90 Academic Press, New York.
    • (1994) Extracellular Matrix Assembly and Structure , pp. 47-90
    • Prockop, D.J.1    Hulmes, D.J.S.2
  • 25
    • 0029006974 scopus 로고
    • Collagens: Molecular biology, diseases, and potentials for therapy
    • Prockop D.J., Kivirikko K.I. Collagens: molecular biology, diseases, and potentials for therapy. Annu. Rev. Biochem. 64:1995;403-434.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 403-434
    • Prockop, D.J.1    Kivirikko, K.I.2
  • 26
    • 0002786470 scopus 로고
    • Intracellular steps in the biosynthesis of collagen
    • G.N. Ramachandran, & A.H. Reddi. New York: Plenum
    • Prockop D.J., Berg R.A., Kiviriko K.I., Uitto J. Intracellular steps in the biosynthesis of collagen. Ramachandran G.N., Reddi A.H. Biochemistry of Collagen. 1976;163-278 Plenum, New York.
    • (1976) Biochemistry of Collagen , pp. 163-278
    • Prockop, D.J.1    Berg, R.A.2    Kiviriko, K.I.3    Uitto, J.4
  • 27
    • 84985727156 scopus 로고
    • Triple helix-coil transition of covalently bridged collagen-like peptides
    • Roth W., Heidemann E. Triple helix-coil transition of covalently bridged collagen-like peptides. Biopolymers. 19:1980;1909-1917.
    • (1980) Biopolymers , vol.19 , pp. 1909-1917
    • Roth, W.1    Heidemann, E.2
  • 28
    • 0020612083 scopus 로고
    • Conformational stability of type I collagen triple helix: Evidence for temporary and local relaxation of the protein conformation using a proteolytic probe
    • Ryhänen L., Zaragoza E.J., Uitto J. Conformational stability of type I collagen triple helix: evidence for temporary and local relaxation of the protein conformation using a proteolytic probe. Arch. Biochem. Biophys. 223:1983;562-571.
    • (1983) Arch. Biochem. Biophys. , vol.223 , pp. 562-571
    • Ryhänen, L.1    Zaragoza, E.J.2    Uitto, J.3
  • 30
    • 0028321612 scopus 로고
    • Mapping the heparin-binding sites on type I collagen monomers and fibrils
    • San Antonio J.D., Lander A.D., Karnovsky M.J., Slayter H.S. Mapping the heparin-binding sites on type I collagen monomers and fibrils. J. Cell Biol. 125:1994;1179-1188.
    • (1994) J. Cell Biol. , vol.125 , pp. 1179-1188
    • San Antonio, J.D.1    Lander, A.D.2    Karnovsky, M.J.3    Slayter, H.S.4
  • 31
    • 0027441145 scopus 로고
    • Deletion of a large domain in recombinant human procollagen II does not alter the thermal stability of the triple helix
    • Sieron A.L., Ferrala A., Ala-Kokko L., Prockop D.J. Deletion of a large domain in recombinant human procollagen II does not alter the thermal stability of the triple helix. J. Biol. Chem. 268:1993;21232-21237.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21232-21237
    • Sieron, A.L.1    Ferrala, A.2    Ala-Kokko, L.3    Prockop, D.J.4
  • 32
    • 0026744083 scopus 로고
    • Helical model of nucleation and propagation to account for the growth of nucleation and propagation to account for the growth of type I collagen fibrils from symmetrical pointed tips: A special example of self-assembly of rod-like monomers
    • Silver D., Millet J., Harrison R., Prockop D.J. Helical model of nucleation and propagation to account for the growth of nucleation and propagation to account for the growth of type I collagen fibrils from symmetrical pointed tips: A special example of self-assembly of rod-like monomers. Proc. Natl. Acad. Sci. USA. 89:1992;9860-9864.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9860-9864
    • Silver, D.1    Millet, J.2    Harrison, R.3    Prockop, D.J.4
  • 35
    • 0025792023 scopus 로고
    • Collagen family of proteins
    • van der Rest M., Garrone R. Collagen family of proteins. FASEB J. 5:1991;2814-2823.
    • (1991) FASEB J. , vol.5 , pp. 2814-2823
    • Van Der Rest, M.1    Garrone, R.2
  • 36
    • 0025166689 scopus 로고
    • Mutations that substitute serine for glycine α1-598 and glycine α1-631 in type I procollagen. Effects on thermal unfolding of the triple helix are position-specific and demonstrate that the protein unfolds through a series of cooperative blocks
    • Westerhausen A., Kishi J., Prockop D.J. Mutations that substitute serine for glycine α1-598 and glycine α1-631 in type I procollagen. Effects on thermal unfolding of the triple helix are position-specific and demonstrate that the protein unfolds through a series of cooperative blocks. J. Biol. Chem. 265:1990;13995-14000.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13995-14000
    • Westerhausen, A.1    Kishi, J.2    Prockop, D.J.3
  • 37
    • 0028169452 scopus 로고
    • Identification of integrin α2β1 as cell surface receptor for the carboxyl-terminal propeptide of type I procollagen
    • Weston S.A., Hulmes D.J.S., Mould A.P., Watson R.B., Humphries M.J. Identification of integrin α2β1 as cell surface receptor for the carboxyl-terminal propeptide of type I procollagen. J. Biol. Chem. 269:1994;20982-20986.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20982-20986
    • Weston, S.A.1    Hulmes, D.J.S.2    Mould, A.P.3    Watson, R.B.4    Humphries, M.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.