Analysis of site-specific glycosylation in recombinant human follistatin expressed in Chinese hamster ovary cells

Biologicals

Volumn 32, Issue 2, 2004, Pages 70-77

  Hyuga, Masashi ^a   Itoh, Satsuki ^a   Kawasaki, Nana ^a   Ohta, Miyako ^a   Ishii, Akiko ^a   Hyuga, Sumiko ^a   Hayakawa, Takao ^a  

^a NATIONAL INSTITUTE OF HEALTH SCIENCES   (Japan)

Author keywords

Chinese hamster ovary; CHO; FCS; fetal calf serum; follistatin; FS; GCC; GnT; graphitized carbon column; high pH anion exchange chromatography with pulsed amperometric detection; HPAEC PAD; IEF; isoelectric focusing; LC MS; N acetylglucosaminyltransferase

Indexed keywords

ASPARAGINE; COMPLEMENTARY DNA; FOLLISTATIN; GLYCOPEPTIDE; MONOSACCHARIDE; OLIGOSACCHARIDE; RECOMBINANT PROTEIN;

ANIMAL CELL; ARTICLE; CARBOHYDRATE ANALYSIS; CHO CELL; FUCOSYLATION; GLYCOSYLATION; HUMAN; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NONHUMAN; PEPTIDE MAPPING; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; ANIMALS; ASPARAGINE; BINDING SITES; CARBOHYDRATES; CELL LINE; CHO CELLS; CHROMATOGRAPHY, LIQUID; CRICETINAE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; FOLLISTATIN; GLYCOPEPTIDES; GLYCOSYLATION; HUMANS; ISOELECTRIC FOCUSING; MASS SPECTROMETRY; MOLECULAR SEQUENCE DATA; MONOSACCHARIDES; OLIGOSACCHARIDES; PEPTIDES; RECOMBINANT PROTEINS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; TIME FACTORS;

CRICETINAE; CRICETULUS GRISEUS;

EID: 5344256264     PISSN: 10451056     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biologicals.2004.04.001     Document Type: Article

References (28)

1. Robertson D.M., Klein R., de Vos F.L., McLachlan R.I., Wettenhall R.E., Hearn M.T., et al. The isolation of polypeptides with FSH suppressing activity from bovine follicular fluid which are structurally different to inhibin. Biochem Biophys Res Commun. 149:1987;744-749
2. Ueno N., Ling N., Ying S.Y., Esch F., Shimasaki S., Guillemin R. Isolation and partial characterization of follistatin: a single-chain Mr 35,000 monomeric protein that inhibits the release of follicle-stimulating hormone. Proc Natl Acad Sci USA. 84:1987;8282-8286
3. Nakamura T., Takio K., Eto Y., Shibai H., Titani K., Sugino H. Activin-binding protein from rat ovary is follistatin. Science. 247:1990;836-838
4. Kogawa K., Nakamura T., Sugino K., Takio K., Titani K., Sugino H. Activin-binding protein is present in pituitary. Endocrinology. 128:1991;1434-1440
5. Massague J. The transforming growth factor-beta family. Annu Rev Cell Biol. 6:1990;597-641
6. Kingsley D.M. The TGF-beta superfamily: new members, new receptors, and new genetic tests of function in different organisms. Genes Dev. 8:1994;133-146
7. Wada M., Shintani Y., Kosaka M., Sano T., Hizawa K., Saito S. Immunohistochemical localization of activin A and follistatin in human tissues. Endocr J. 43:1996;375-385
8. Sugino K., Kurosawa N., Nakamura T., Takio K., Shimasaki S., Ling N., et al. Molecular heterogeneity of follistatin, an activin-binding protein. Higher affinity of the carboxyl-terminal truncated forms for heparan sulfate proteoglycans on the ovarian granulosa cell. J Biol Chem. 268:1993;15579-15587
9. Patel K. Follistatin. Int J Biochem Cell Biol. 30:1998;1087-1093
10. Inouye S., Guo Y., DePaolo L., Shimonaka M., Ling N., Shimasaki S. Recombinant expression of human follistatin with 315 and 288 amino acids: chemical and biological comparison with native porcine follistatin. Endocrinology. 129:1991;815-822
11. Sumitomo S., Inouye S., Liu X.J., Ling N., Shimasaki S. The heparin binding site of follistatin is involved in its interaction with activin. Biochem Biophys Res Commun. 208:1995;1-9
12. Hashimoto O., Nakamura T., Shoji H., Shimasaki S., Hayashi Y., Sugino H. A novel role of follistatin, an activin-binding protein, in the inhibition of activin action in rat pituitary cells. Endocytotic degradation of activin and its acceleration by follistatin associated with cell-surface heparan sulfate. J Biol Chem. 272:1997;13835-13842
13. Kobata A. Structures and functions of the sugar chains of glycoproteins. Eur J Biochem. 209:1992;483-501
14. Varki A. Biological roles of oligosaccharides: all of the theories are correct. Glycobiology. 3:1993;97-130
15. Itoh S., Kawasaki N., Ohta M., Hyuga M., Hyuga S., Hayakawa T. Study on evaluating methods for the quality control of glycoprotein products. (III) - Erythropoietin products. Part 3. Bull Natl Inst Health Sci. 2001;65-69
16. Simultaneous microanalysis of N-linked oligosaccharides in a glycoprotein using microbore graphitized carbon column liquid chromatography-mass spectrometry. J Chromatogr A. 968:2002;89-100
17. Kawasaki N., Ohta M., Hyuga S., Hashimoto O., Hayakawa T. Analysis of carbohydrate heterogeneity in a glycoprotein using liquid chromatography/mass spectrometry and liquid chromatography with tandem mass spectrometry. Anal Biochem. 269:1999;297-303
18. Kawasaki N., Ohta M., Hyuga S., Hyuga M., Hayakawa T. Application of liquid chromatography/mass spectrometry and liquid chromatography with tandem mass spectrometry to the analysis of the site-specific carbohydrate heterogeneity in erythropoietin. Anal Biochem. 285:2000;82-91
19. Kawasaki N., Haishima Y., Ohta M., Itoh S., Hyuga M., Hyuga S., et al. Structural analysis of sulfated N-linked oligosaccharides in erythropoietin. Glycobiology. 11:2001;1043-1049
20. Kawasaki N., Ohta M., Itoh S., Hyuga M., Hyuga S., Hayakawa T. Usefulness of sugar mapping by liquid chromatography/mass spectrometry in comparability assessments of glycoprotein products. Biologicals. 30:2002;113-123
21. Ohta M., Kawasaki N., Hyuga S., Hyuga M., Hayakawa T. Selective glycopeptide mapping of erythropoietin by on-line high-performance liquid chromatography-electrospray ionization mass spectrometry. J Chromatogr A. 910:2001;1-11
22. Ohta M., Kawasaki N., Itoh S., Hayakawa T. Usefulness of glycopeptide mapping by liquid chromatography/mass spectrometry in comparability assessment of glycoprotein products. Biologicals. 30:2002;235-244
23. Hardy M.R., Townsend R.R., Lee Y.C. Monosaccharide analysis of glycoconjugates by anion exchange chromatography with pulsed amperometric detection. Anal Biochem. 170:1988;54-62
24. Kawasaki N., Ohta M., Hyuga S., Hyuga M., Hayakawa T. Application of liquid chromatography/mass spectrometry and liquid chromatography with tandem mass spectrometry to the analysis of the site-specific carbohydrate heterogeneity in erythropoietin. Anal Biochem. 285:2000;82-91
25. Ingrosso D., Fowler A.V., Bleibaum J., Clarke S. Specificity of endoproteinase Asp-N (Pseudomonas fragi): cleavage at glutamyl residues in two proteins. Biochem Biophys Res Commun. 162:1989;1528-1534
26. Inouye S., Ling N., Shimasaki S. Localization of the heparin binding site of follistatin. Mol Cell Endocrinol. 90:1992;1-6
27. Picard V., Ersdal-Badju E., Bock S.C. Partial glycosylation of antithrombin III asparagine-135 is caused by the serine in the third position of its N-glycosylation consensus sequence and is responsible for production of the beta-antithrombin III isoform with enhanced heparin affinity. Biochemistry. 34:1995;8433-8440
28. Bohme C., Nimtz M., Grabenhorst E., Conradt H.S., Strathmann A., Ragg H. Tyrosine sulfation and N-glycosylation of human heparin cofactor II from plasma and recombinant Chinese hamster ovary cells and their effects on heparin binding. Eur J Biochem. 269:2002;977-988