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Volumn 336, Issue 2, 2005, Pages 375-385

Assembly of homotrimeric type XXI minicollagen by coexpression of prolyl 4-hydroxylase in stably transfected Drosophila melanogaster S2 cells

Author keywords

Collagen; Drosophila melanogaster S2 cells; FACIT; Minicollagen; Prolyl 4 hydroxylase; Type XXI collagen

Indexed keywords

COLLAGEN; COMPLEMENTARY DNA; HYDROXYPROLINE; ISOENZYME; PEPSIN A; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; RECOMBINANT ENZYME;

EID: 24644518652     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.08.018     Document Type: Article
Times cited : (14)

References (34)
  • 1
    • 0015624009 scopus 로고
    • The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen
    • R.A. Berg, and D.J. Prockop The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen Biochem. Biophys. Res. Commun. 52 1973 115 120
    • (1973) Biochem. Biophys. Res. Commun. , vol.52 , pp. 115-120
    • Berg, R.A.1    Prockop, D.J.2
  • 2
    • 0015862613 scopus 로고
    • Hydroxyproline content determines the denaturation temperature of chick tendon collagen
    • J. Rosenbloom, M. Harsch, and S. Jimenez Hydroxyproline content determines the denaturation temperature of chick tendon collagen Arch. Biochem. Biophys. 158 1973 478 484
    • (1973) Arch. Biochem. Biophys. , vol.158 , pp. 478-484
    • Rosenbloom, J.1    Harsch, M.2    Jimenez, S.3
  • 3
    • 0024639221 scopus 로고
    • Protein hydroxylation: Prolyl 4-hydroxylase, an enzyme with four cosubstrates and a multifunctional subunit
    • K.I. Kivirikko, R. Myllyla, and T. Pihlajaniemi Protein hydroxylation: prolyl 4-hydroxylase, an enzyme with four cosubstrates and a multifunctional subunit FASEB J. 3 1989 1609 1617
    • (1989) FASEB J. , vol.3 , pp. 1609-1617
    • Kivirikko, K.I.1    Myllyla, R.2    Pihlajaniemi, T.3
  • 4
    • 0023654667 scopus 로고
    • A single polypeptide acts both as the beta subunit of prolyl 4-hydroxylase and as a protein disulfide-isomerase
    • J. Koivu, R. Myllyla, T. Helaakoski, T. Pihlajaniemi, K. Tasanen, and K.I. Kivirikko A single polypeptide acts both as the beta subunit of prolyl 4-hydroxylase and as a protein disulfide-isomerase J. Biol. Chem. 262 1987 6447 6449
    • (1987) J. Biol. Chem. , vol.262 , pp. 6447-6449
    • Koivu, J.1    Myllyla, R.2    Helaakoski, T.3    Pihlajaniemi, T.4    Tasanen, K.5    Kivirikko, K.I.6
  • 5
    • 0023303619 scopus 로고
    • Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene
    • T. Pihlajaniemi, T. Helaakoski, K. Tasanen, R. Myllyla, M.L. Huhtala, J. Koivu, and K.I. Kivirikko Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene EMBO J. 6 1987 643 649
    • (1987) EMBO J. , vol.6 , pp. 643-649
    • Pihlajaniemi, T.1    Helaakoski, T.2    Tasanen, K.3    Myllyla, R.4    Huhtala, M.L.5    Koivu, J.6    Kivirikko, K.I.7
  • 6
    • 0026725853 scopus 로고
    • Characterization of the human prolyl 4-hydroxylase tetramer and its multifunctional protein disulfide-isomerase subunit synthesized in a baculovirus expression system
    • K. Vuori, T. Pihlajaniemi, M. Marttila, and K.I. Kivirikko Characterization of the human prolyl 4-hydroxylase tetramer and its multifunctional protein disulfide-isomerase subunit synthesized in a baculovirus expression system Proc. Natl. Acad. Sci. USA 89 1992 7467 7470
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7467-7470
    • Vuori, K.1    Pihlajaniemi, T.2    Marttila, M.3    Kivirikko, K.I.4
  • 7
    • 0029795764 scopus 로고    scopus 로고
    • Intracellular dissociation and reassembly of prolyl 4-hydroxylase:the alpha-subunits associated with the immunoglobulin-heavy-chain binding protein (BiP) allowing reassembly with the beta-subunit
    • D.C. John, and N.J. Bulleid Intracellular dissociation and reassembly of prolyl 4-hydroxylase:the alpha-subunits associated with the immunoglobulin- heavy-chain binding protein (BiP) allowing reassembly with the beta-subunit Biochem. J. 317 Pt 3 1996 659 665
    • (1996) Biochem. J. , vol.317 , Issue.3 PART , pp. 659-665
    • John, D.C.1    Bulleid, N.J.2
  • 8
    • 0034672132 scopus 로고    scopus 로고
    • Coexpression of alpha and beta subunits of prolyl 4-hydroxylase stabilizes the triple helix of recombinant human type X collagen
    • K. Wagner, E. Poschl, J. Turnay, J. Baik, T. Pihlajaniemi, S. Frischholz, and K. vonder Mark Coexpression of alpha and beta subunits of prolyl 4-hydroxylase stabilizes the triple helix of recombinant human type X collagen Biochem. J. 352 Pt 3 2000 907 911
    • (2000) Biochem. J. , vol.352 , Issue.3 PART , pp. 907-911
    • Wagner, K.1    Poschl, E.2    Turnay, J.3    Baik, J.4    Pihlajaniemi, T.5    Frischholz, S.6    Vonder Mark, K.7
  • 9
    • 0030732364 scopus 로고    scopus 로고
    • Assembly of human prolyl 4-hydroxylase and type III collagen in the yeast Pichia pastoris: Formation of a stable enzyme tetramer requires coexpression with collagen and assembly of a stable collagen requires coexpression with prolyl 4-hydroxylase
    • A. Vuorela, J. Myllyharju, R. Nissi, T. Pihlajaniemi, and K.I. Kivirikko Assembly of human prolyl 4-hydroxylase and type III collagen in the yeast Pichia pastoris: formation of a stable enzyme tetramer requires coexpression with collagen and assembly of a stable collagen requires coexpression with prolyl 4-hydroxylase EMBO J. 16 1997 6702 6712
    • (1997) EMBO J. , vol.16 , pp. 6702-6712
    • Vuorela, A.1    Myllyharju, J.2    Nissi, R.3    Pihlajaniemi, T.4    Kivirikko, K.I.5
  • 11
    • 0030005258 scopus 로고    scopus 로고
    • Co-expression of the alpha subunit of human prolyl 4-hydroxylase with BiP polypeptide in insect cells leads to the formation of soluble and insoluble complexes. Soluble alpha-subunit-BiP complexes have no prolyl 4-hydroxylase activity
    • J. Veijola, T. Pihlajaniemi, and K.I. Kivirikko Co-expression of the alpha subunit of human prolyl 4-hydroxylase with BiP polypeptide in insect cells leads to the formation of soluble and insoluble complexes. Soluble alpha-subunit-BiP complexes have no prolyl 4-hydroxylase activity Biochem. J. 315 2 1996 613 618
    • (1996) Biochem. J. , vol.315 , Issue.2 , pp. 613-618
    • Veijola, J.1    Pihlajaniemi, T.2    Kivirikko, K.I.3
  • 12
    • 0029006974 scopus 로고
    • Collagens: Molecular biology, diseases, and potentials for therapy
    • D.J. Prockop, and K.I. Kivirikko 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
  • 14
    • 0035937135 scopus 로고    scopus 로고
    • Cartilage oligomeric matrix protein interacts with type IX collagen; Disruptions to these interactions identify a pathogenetic mechanism in a bone dysplasia family
    • P. Holden, R.S. Meadows, K.L. Chapman, M.E. Grant, K.E. Kadler, and M.D. Briggs Cartilage oligomeric matrix protein interacts with type IX collagen; disruptions to these interactions identify a pathogenetic mechanism in a bone dysplasia family J. Biol. Chem. 2000
    • (2000) J. Biol. Chem.
    • Holden, P.1    Meadows, R.S.2    Chapman, K.L.3    Grant, M.E.4    Kadler, K.E.5    Briggs, M.D.6
  • 18
    • 0035958966 scopus 로고    scopus 로고
    • Collagenous sequence governs the trimeric assembly of collagen XII
    • M. Mazzorana, S. Cogne, D. Goldschmidt, and E. Aubert-Foucher Collagenous sequence governs the trimeric assembly of collagen XII J. Biol. Chem. 276 2001 27989 27998
    • (2001) J. Biol. Chem. , vol.276 , pp. 27989-27998
    • Mazzorana, M.1    Cogne, S.2    Goldschmidt, D.3    Aubert-Foucher, E.4
  • 19
    • 0036198822 scopus 로고    scopus 로고
    • Genomic organization and characterization of the human type XXI collagen (COL21A1) gene
    • M.Y. Chou, and H.C. Li Genomic organization and characterization of the human type XXI collagen (COL21A1) gene Genomics 79 2002 395 401
    • (2002) Genomics , vol.79 , pp. 395-401
    • Chou, M.Y.1    Li, H.C.2
  • 20
    • 0035860389 scopus 로고    scopus 로고
    • A new FACIT of the collagen family: COL21A1
    • J. Fitzgerald, and J.F. Bateman A new FACIT of the collagen family: COL21A1 FEBS Lett. 505 2001 275 280
    • (2001) FEBS Lett. , vol.505 , pp. 275-280
    • Fitzgerald, J.1    Bateman, J.F.2
  • 21
    • 0036151793 scopus 로고    scopus 로고
    • Identification and analysis of collagen alpha 1 (XXI), a novel member of the FACIT collagen family
    • D. Tuckwell Identification and analysis of collagen alpha 1 (XXI), a novel member of the FACIT collagen family Matrix Biol. 21 2002 63 66
    • (2002) Matrix Biol. , vol.21 , pp. 63-66
    • Tuckwell, D.1
  • 22
    • 0015328565 scopus 로고
    • Cell lines derived from late embryonic stages of Drosophila melanogaster
    • I. Schneider Cell lines derived from late embryonic stages of Drosophila melanogaster J. Embryol. Exp. Morphol. 27 1972 353 365
    • (1972) J. Embryol. Exp. Morphol. , vol.27 , pp. 353-365
    • Schneider, I.1
  • 23
    • 0029027133 scopus 로고
    • Characterization of a cloned locust tyramine receptor cDNA by functional expression in permanently transformed Drosophila S2 cells
    • J. Vanden Broeck, V. Vulsteke, R. Huybrechts, and A. De Loof Characterization of a cloned locust tyramine receptor cDNA by functional expression in permanently transformed Drosophila S2 cells J. Neurochem. 64 1995 2387 2395
    • (1995) J. Neurochem. , vol.64 , pp. 2387-2395
    • Vanden Broeck, J.1    Vulsteke, V.2    Huybrechts, R.3    De Loof, A.4
  • 24
    • 0024688637 scopus 로고
    • Regulated expression at high copy number allows production of a growth-inhibitory oncogene product in Drosophila Schneider cells
    • H. Johansen, A. van der Straten, R. Sweet, E. Otto, G. Maroni, and M. Rosenberg Regulated expression at high copy number allows production of a growth-inhibitory oncogene product in Drosophila Schneider cells Genes Dev. 3 1989 882 889
    • (1989) Genes Dev. , vol.3 , pp. 882-889
    • Johansen, H.1    Van Der Straten, A.2    Sweet, R.3    Otto, E.4    Maroni, G.5    Rosenberg, M.6
  • 26
    • 0020010503 scopus 로고
    • Posttranslational enzymes in the biosynthesis of collagen: Intracellular enzymes
    • K.I. Kivirikko, and R. Myllyla Posttranslational enzymes in the biosynthesis of collagen: intracellular enzymes Methods Enzymol. 82 1982 245 304
    • (1982) Methods Enzymol. , vol.82 , pp. 245-304
    • Kivirikko, K.I.1    Myllyla, R.2
  • 27
    • 0029940986 scopus 로고    scopus 로고
    • Characterization of human type III collagen expressed in a baculovirus system. Production of a protein with a stable triple helix requires coexpression with the two types of recombinant prolyl 4-hydroxylase subunit
    • A. Lamberg, T. Helaakoski, J. Myllyharju, S. Peltonen, H. Notbohm, T. Pihlajaniemi, and K.I. Kivirikko Characterization of human type III collagen expressed in a baculovirus system. Production of a protein with a stable triple helix requires coexpression with the two types of recombinant prolyl 4-hydroxylase subunit J. Biol. Chem. 271 1996 11988 11995
    • (1996) J. Biol. Chem. , vol.271 , pp. 11988-11995
    • Lamberg, A.1    Helaakoski, T.2    Myllyharju, J.3    Peltonen, S.4    Notbohm, H.5    Pihlajaniemi, T.6    Kivirikko, K.I.7
  • 28
    • 0039056496 scopus 로고    scopus 로고
    • Location of type XV collagen in human tissues and its accumulation in the interstitial matrix of the fibrotic kidney
    • P.M. Hagg, P.O. Hagg, S. Peltonen, H. Autio-Harmainen, and T. Pihlajaniemi Location of type XV collagen in human tissues and its accumulation in the interstitial matrix of the fibrotic kidney Am. J. Pathol. 150 1997 2075 2086
    • (1997) Am. J. Pathol. , vol.150 , pp. 2075-2086
    • Hagg, P.M.1    Hagg, P.O.2    Peltonen, S.3    Autio-Harmainen, H.4    Pihlajaniemi, T.5
  • 29
    • 0030758359 scopus 로고    scopus 로고
    • Expression of wild-type and modified proalpha chains of human type I procollagen in insect cells leads to the formation of stable [alpha1(I)]2alpha2(I) collagen heterotrimers and [alpha1(I)]3 homotrimers but not [alpha2(I)]3 homotrimers
    • J. Myllyharju, A. Lamberg, H. Notbohm, P.P. Fietzek, T. Pihlajaniemi, and K.I. Kivirikko Expression of wild-type and modified proalpha chains of human type I procollagen in insect cells leads to the formation of stable [alpha1(I)]2alpha2(I) collagen heterotrimers and [alpha1(I)]3 homotrimers but not [alpha2(I)]3 homotrimers J. Biol. Chem. 272 1997 21824 21830
    • (1997) J. Biol. Chem. , vol.272 , pp. 21824-21830
    • Myllyharju, J.1    Lamberg, A.2    Notbohm, H.3    Fietzek, P.P.4    Pihlajaniemi, T.5    Kivirikko, K.I.6
  • 30
    • 0031973115 scopus 로고    scopus 로고
    • Expression and characterization of recombinant human type II collagens with low and high contents of hydroxylysine and its glycosylated forms
    • M. Nokelainen, T. Helaakoski, J. Myllyharju, H. Notbohm, T. Pihlajaniemi, P.P. Fietzek, and K.I. Kivirikko Expression and characterization of recombinant human type II collagens with low and high contents of hydroxylysine and its glycosylated forms Matrix Biol. 16 1998 329 338
    • (1998) Matrix Biol. , vol.16 , pp. 329-338
    • Nokelainen, M.1    Helaakoski, T.2    Myllyharju, J.3    Notbohm, H.4    Pihlajaniemi, T.5    Fietzek, P.P.6    Kivirikko, K.I.7
  • 33
    • 33646286416 scopus 로고    scopus 로고
    • Hsp47: A collagen-specific molecular chaperone
    • K. Nagata Hsp47: a collagen-specific molecular chaperone Trends Biochem. Sci. 21 1996 22 26
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 22-26
    • Nagata, K.1
  • 34
    • 0002079883 scopus 로고
    • Hydroxylation of proline and lysine residues in collagens and other animal and plant proteins
    • J.J. Harding M.J.C. Crabbe CRC Press Boca Raton, FL
    • K.I. Kivirikko, R. Myllyla, and T. Pihlajaniemi Hydroxylation of proline and lysine residues in collagens and other animal and plant proteins J.J. Harding M.J.C. Crabbe Post-translational Modifications of Proteins 1992 CRC Press Boca Raton, FL 1 51
    • (1992) Post-translational Modifications of Proteins , pp. 1-51
    • Kivirikko, K.I.1    Myllyla, R.2    Pihlajaniemi, T.3


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