메뉴 건너뛰기




Volumn 17, Issue 11, 1999, Pages 1116-1121

Engineering Chinese hamster ovary cells to maximize sialic acid content of recombinant glycoproteins

Author keywords

Chinese hamster ovary cells; Glycosylation; Glycosyltransferase overexpression; Recombinant protein expression

Indexed keywords

BETA N ACETYLGLUCOSAMINYLGLYCOPEPTIDE BETA 1,4 GALACTOSYLTRANSFERASE; GLYCOPROTEIN; RECOMBINANT PROTEIN; SIALIC ACID; SIALYLTRANSFERASE;

EID: 0032693972     PISSN: 10870156     EISSN: None     Source Type: Journal    
DOI: 10.1038/15104     Document Type: Article
Times cited : (177)

References (27)
  • 2
    • 0020021127 scopus 로고
    • Carbohydrate specific receptors of the liver
    • Ashwell, G. & Hartford, J. Carbohydrate specific receptors of the liver. Annu. Rev. Biochem. 51, 531-554 (1982).
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 531-554
    • Ashwell, G.1    Hartford, J.2
  • 3
    • 0028224656 scopus 로고
    • Glycosylation of recombinant proteins: Problems and prospects
    • Jenkins, N. & Curling, E.M.A. Glycosylation of recombinant proteins: problems and prospects. Enzyme Microb. Technol. 16, 354-364 (1994). 7
    • (1994) Enzyme Microb. Technol. , vol.16 , pp. 354-364
    • Jenkins, N.1    Curling, E.M.A.2
  • 4
    • 0028061380 scopus 로고
    • The effect of cell culture conditions on the oligosaccharide structures of recombinant glycoproteins
    • Andersen, D. & Goochee, C.F. The effect of cell culture conditions on the oligosaccharide structures of recombinant glycoproteins. Curr. Opin. Biotechnol. 5, 546-549 (1994 ).
    • (1994) Curr. Opin. Biotechnol. , vol.5 , pp. 546-549
    • Andersen, D.1    Goochee, C.F.2
  • 5
    • 0025721017 scopus 로고
    • Protection against endotoxic shock by a tumor necrosis factor receptor immunoadhesin
    • Ashkenazi, A. et al. Protection against endotoxic shock by a tumor necrosis factor receptor immunoadhesin. Proc. Natl. Acad. Sci. USA 88, 10535-10539 (1991).
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10535-10539
    • Ashkenazi, A.1
  • 6
    • 23444439163 scopus 로고
    • A faster and more potent form of tissue plasminogen activator
    • Keyt, B.A. et al. A faster and more potent form of tissue plasminogen activator. Proc. Natl. Acad. Sci. USA 91, 3670-3674 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3670-3674
    • Keyt, B.A.1
  • 7
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • Varki, A. Biological roles of oligosaccharides: all of the theories are correct. Glycobiology 3, 97-130 (1993).
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 8
    • 0024497455 scopus 로고
    • Survival of recombinant erythropoietin in the circulation: The role of carbohydrates
    • Fukuda, M.N., Sasaki, H., Lopez, L. & Fukada, M. Survival of recombinant erythropoietin in the circulation: the role of carbohydrates. Blood 73, 84-89 (1989).
    • (1989) Blood , vol.73 , pp. 84-89
    • Fukuda, M.N.1    Sasaki, H.2    Lopez, L.3    Fukada, M.4
  • 9
    • 0025893335 scopus 로고
    • The importance of N-and O-linked oligosaccharides for the biosynthesis and in vitro and in vivo biologic activities of erythropoietin
    • Wasley, L.C. et al. The importance of N-and O-linked oligosaccharides for the biosynthesis and in vitro and in vivo biologic activities of erythropoietin. Blood 77, 2624-2632 (1991).
    • (1991) Blood , vol.77 , pp. 2624-2632
    • Wasley, L.C.1
  • 10
    • 0021099058 scopus 로고
    • Binding of synthetic oligosaccharides to the hepatic Gal/GalNAc lectin: Dependence on fine structural features
    • Lee, Y.C. et al. Binding of synthetic oligosaccharides to the hepatic Gal/GalNAc lectin: dependence on fine structural features. J. Biol. Chem. 258, 199-202 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 199-202
    • Lee, Y.C.1
  • 12
    • 0026848764 scopus 로고
    • Glycoprotein pharmaceuticals: Scientific and regulatory considerations, and the US orphan drug act
    • Liu, D.T.-Y. Glycoprotein pharmaceuticals: scientific and regulatory considerations, and the US Orphan Drug Act. Trends Biotechnol. 10, 114-120 (1992).
    • (1992) Trends Biotechnol. , vol.10 , pp. 114-120
    • Liu, D.T.-Y.1
  • 13
    • 0025649375 scopus 로고
    • Recombinant human interferon-γ. Differences in glycosylation and proteolytic processing lead to heterogeneity in batch culture
    • Curling, E.M. et al. Recombinant human interferon-γ. Differences in glycosylation and proteolytic processing lead to heterogeneity in batch culture. Biochem. J. 272, 333-337 (1990).
    • (1990) Biochem. J. , vol.272 , pp. 333-337
    • Curling, E.M.1
  • 14
    • 0027628305 scopus 로고
    • Glycosidase activities in Chinese hamster ovary cell lysate and cell culture supernatant
    • Gramer, M.J. & Goochee, C.F. Glycosidase activities in Chinese hamster ovary cell lysate and cell culture supernatant. Biotechnol. Prog. 9, 366-373 (1993).
    • (1993) Biotechnol. Prog. , vol.9 , pp. 366-373
    • Gramer, M.J.1    Goochee, C.F.2
  • 15
    • 0024364391 scopus 로고
    • Tissue specific expression of sialyl transferases
    • Paulson, J.C., Weinstein, J. & Schauer, A. Tissue specific expression of sialyl transferases. J. Biol. Chem. 264, 10931-10934 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 10931-10934
    • Paulson, J.C.1    Weinstein, J.2    Schauer, A.3
  • 16
    • 0026795058 scopus 로고
    • Tissue-specific alternative splicing of the βgalactoside α2,6-sialyltransferase gene
    • Wen, D.X., Svensson, E.C. & Paulson, J.C. Tissue-specific alternative splicing of the βgalactoside α2,6-sialyltransferase gene. J. Biol. Chem. 267, 2512-2518 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 2512-2518
    • Wen, D.X.1    Svensson, E.C.2    Paulson, J.C.3
  • 17
    • 0024321508 scopus 로고
    • Alteration of terminal glycosylation sequences on N-linked oligosaccharides of Chinese hamster ovary cells by expression of β-galactosideo α2,6-sialyltransferase
    • Lee, U.E., Roth, J. & Paulsen, J.C. Alteration of terminal glycosylation sequences on N-linked oligosaccharides of Chinese hamster ovary cells by expression of β-galactosideo α2,6-sialyltransferase. J. Biol. Chem. 164, 13848-13855 (1989).
    • (1989) J. Biol. Chem. , vol.164 , pp. 13848-13855
    • Lee, U.E.1    Roth, J.2    Paulsen, J.C.3
  • 18
    • 0028979967 scopus 로고
    • Construction of stable BHK-21 cells co-expressing human secretory glycoproteins and human Gal(β1-4) GlcNAc-r α2,6-sialyltransferase. α2,6-linked NeuAc is preferentially attached to the Gal(β-1-4)GlcNAc(β-1-2)Man(α-1,3)-branch of diantennary oligosaccharides from secreted recombinant βtrace protein
    • Grabenhorst, E., Hoffmann, A., Nimtz, M., Zettmeissl, G. & Conradt H.S. Construction of stable BHK-21 cells co-expressing human secretory glycoproteins and human Gal(β1-4) GlcNAc-r α2,6-sialyltransferase. α2,6-linked NeuAc is preferentially attached to the Gal(β-1-4)GlcNAc(β-1-2)Man(α-1,3)-branch of diantennary oligosaccharides from secreted recombinant βtrace protein. Eur. J. Biochem. 232, 718-725 (1995).
    • (1995) Eur. J. Biochem. , vol.232 , pp. 718-725
    • Grabenhorst, E.1    Hoffmann, A.2    Nimtz, M.3    Zettmeissl, G.4    Conradt, H.S.5
  • 19
    • 0029294124 scopus 로고
    • Tissue plasminogen activator co-expressed in Chinese hamster ovary cells with α-2,6-sialyltransferase contains NeuAc-α(2,6)Gal-β(1,4)GlcNAc linkages
    • Minch, S.L., Kallio, P.T. & Bailey, J.E. Tissue plasminogen activator co-expressed in Chinese hamster ovary cells with α-2,6-sialyltransferase contains NeuAc-α(2,6)Gal-β(1,4)GlcNAc linkages. Biotechnol. Prog. 11, 348-351 (1995).
    • (1995) Biotechnol. Prog. , vol.11 , pp. 348-351
    • Minch, S.L.1    Kallio, P.T.2    Bailey, J.E.3
  • 20
    • 0030425381 scopus 로고    scopus 로고
    • Genetic engineering of α2,6 sialyltransferase in recombinant cho cells and its effect on the sialylation of recombinant interferon-γ
    • Monaco, L. et al. Genetic engineering of α2,6 sialyltransferase in recombinant CHO cells and its effect on the sialylation of recombinant interferon-γ. Cytotechnology 22, 197-203 (1996).
    • (1996) Cytotechnology , vol.22 , pp. 197-203
    • Monaco, L.1
  • 21
    • 0027201584 scopus 로고
    • Cloning and expression of human Gal beta 1,3(4)GlcNAc alpha 2,3-sialyltransferase
    • Kitagawa, H. & Paulson, J.C. Cloning and expression of human Gal beta 1,3(4)GlcNAc alpha 2,3-sialyltransferase. Biochem. Biophys. Res. Commun. 194, 375-382 (1993).
    • (1993) Biochem. Biophys. Res. Commun. , vol.194 , pp. 375-382
    • Kitagawa, H.1    Paulson, J.C.2
  • 22
    • 0024273824 scopus 로고
    • Identification of the full-length coding sequence for human galactosyltransferase (βN-acetyl-glucosaminide: β-1,4-galactosyltransferase)
    • Masri, K.A., Appert, H.E. & Fukuda, M.N. Identification of the full-length coding sequence for human galactosyltransferase (βN-acetyl-glucosaminide: β-1,4-galactosyltransferase) Biochem. Biophys. Res. Commun. 157, 657-663 (1988).
    • (1988) Biochem. Biophys. Res. Commun. , vol.157 , pp. 657-663
    • Masri, K.A.1    Appert, H.E.2    Fukuda, M.N.3
  • 23
    • 0030009435 scopus 로고    scopus 로고
    • High level production of recombinant proteins in CHO cells using a dicistronic DHFR intron expression vector
    • Lucas, B.K. et al. High level production of recombinant proteins in CHO cells using a dicistronic DHFR intron expression vector. Nucleic Acids Res. 24, 1774-1779 (1996).
    • (1996) Nucleic Acids Res. , vol.24 , pp. 1774-1779
    • Lucas, B.K.1
  • 24
    • 0023394797 scopus 로고
    • Functional analysis of a retroviral host-range mutant: Altered long terminal repeat sequences allow expression in embryonal carcinoma cells
    • Hilberg, F., Stocking, C., Ostertag, W. & Grez, M. Functional analysis of a retroviral host-range mutant: altered long terminal repeat sequences allow expression in embryonal carcinoma cells. Proc. Natl. Acad. Sci. USA 84, 5232-5236 (1987).
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5232-5236
    • Hilberg, F.1    Stocking, C.2    Ostertag, W.3    Grez, M.4
  • 25
    • 0029115046 scopus 로고
    • Rapid quantitative determination of sialic acids in glycoproteins by high-performance liquid chromatography with a sensitive fluorescence detection
    • Anumula, K.R. Rapid quantitative determination of sialic acids in glycoproteins by high-performance liquid chromatography with a sensitive fluorescence detection. Anal. Biochem. 230, 24-30 (1995).
    • (1995) Anal. Biochem. , vol.230 , pp. 24-30
    • Anumula, K.R.1
  • 26
    • 0031799347 scopus 로고    scopus 로고
    • A high-throughput microscale method to release N-linked oligosaccharides from glycoproteins for matrix-assisted laser desorption/ionization time-of-flight mass spectrometric analysis
    • Papac, D.I., Briggs, J.B., Chin, E.T. & Jones, A.J.S. A high-throughput microscale method to release N-linked oligosaccharides from glycoproteins for matrix-assisted laser desorption/ionization time-of-flight mass spectrometric analysis. Glycobiology 8, 445-454 (1998).
    • (1998) Glycobiology , vol.8 , pp. 445-454
    • Papac, D.I.1    Briggs, J.B.2    Chin, E.T.3    Jones, A.J.S.4
  • 27
    • 0003178579 scopus 로고
    • Software for the statistical analysis of non-linear models
    • Statistical Consultants PCNONLIN and NONLIN84: Software for the statistical analysis of non-linear models. The Amer. Stat. 40, 52-60 (1986).
    • (1986) The Amer. Stat. , vol.40 , pp. 52-60


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.