Monitoring of the tissue distribution of fibroblast growth factor containing a high mannose-type sugar chain produced in mutant yeast

Glycoconjugate Journal

Volumn 20, Issue 6, 2003, Pages 385-397

  Takamatsu, Shinji ^a   Chiba, Yasunori ^b   Ishii, Tomoko ^b   Nakayama, Ken Ichi ^b   Yokomatsu Kubota, Tomoko ^c,d   Makino, Tadashi ^c,e   Fujibayashi, Yasuhisa ^a   Jigami, Yoshifumi ^b  

^a UNIVERSITY OF FUKUI   (Japan)

^b NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

^c MITSUI CHEMICALS INC   (Japan)

^d Society for Techno Innovation of Agriculture   (Japan)

^e Research Association for Biotechnology   (Japan)

Author keywords

Fibroblast growth factor; Glycoprotein; Saccharomyces cerevisiae; Tissue distribution; Tissue targeting therapy

Indexed keywords

FIBROBLAST GROWTH FACTOR; GLYCOPROTEIN; MANNOSE; SUGAR; FUNGAL PROTEIN; HYBRID PROTEIN; MANNOSIDASE; MANNOSYL OLIGOSACCHARIDE 1,2 ALPHA MANNOSIDASE; MANNOSYL-OLIGOSACCHARIDE 1,2-ALPHA-MANNOSIDASE; MANNOSYLTRANSFERASE; MEMBRANE PROTEIN; MNN1 PROTEIN, S CEREVISIAE; OLIGOSACCHARIDE; RECOMBINANT PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN;

ARTICLE; CELL PROLIFERATION; KIDNEY; MAMMAL CELL; MUTANT; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; TISSUE DISTRIBUTION; YEAST; ANIMAL; BIOLOGICAL MODEL; BIOSYNTHESIS; CELL CULTURE; CHEMISTRY; CHO CELL; CYTOLOGY; ESCHERICHIA COLI; GENE VECTOR; GENETICS; GENOTYPE; GLYCOSYLATION; HAMSTER; MALE; METABOLISM; MOUSE; MUTATION; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRION; PROTEIN TERTIARY STRUCTURE; SACCHAROMYCES CEREVISIAE; TIME; VASCULAR ENDOTHELIUM; WESTERN BLOTTING;

BOVINAE; MAMMALIA; SACCHAROMYCES CEREVISIAE;

ANIMALS; BLOTTING, WESTERN; CELLS, CULTURED; CHO CELLS; CRICETINAE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENDOTHELIUM, VASCULAR; ESCHERICHIA COLI; FIBROBLAST GROWTH FACTORS; FUNGAL PROTEINS; GENETIC VECTORS; GENOTYPE; GLYCOPROTEINS; GLYCOSYLATION; MALE; MANNOSE; MANNOSIDASES; MANNOSYLTRANSFERASES; MEMBRANE GLYCOPROTEINS; MICE; MODELS, GENETIC; MUTATION; OLIGOSACCHARIDES; PRIONS; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; TIME FACTORS; TISSUE DISTRIBUTION;

EID: 16644389161     PISSN: 02820080     EISSN: 15734986     Source Type: Journal    
DOI: 10.1023/B:GLYC.0000033995.95412.1f     Document Type: Article

References (36)

1. Clogston CL, Hu S, Boone TC, Lu HS, Glycosidase digestion, electrophoresis and chromatographic analysis of recombinant human granulocyte colony-stimulating factor glycoforms produced in Chinese hamster ovary cells, J Chromatogr 637, 55-62 (1993).
2. Hooker AD, Goldman MH, Markham NH, James DC, Ison AP, Bull AT, Strange PG, Salmon I, Baines AJ, Jenkins N, N-Glycans of recombinant human interferon-c change during batch culture of Chinese hamster ovary cells, Biotechnol Bioeng 48, 639-48 (1995).
3. Inoue N, Takeuchi M, Ohashi H, Suzuki T, The production of recombinant human erythropoietin, Biotechnol Annu Rev 1, 297-313 (1995).
4. Mutsaers JH, Kamerling JP, Devos R, Guisez Y, Fiers W, Vliegenthart JF, Structural studies of the carbohydrate chains of human gamma-interferon, Eur J Biochem 156, 651-4 (1986).
5. Oheda M, Hase S, Ono M, Ikenaka T, Structures of the sugar chains of recombinant human granulocyte-colony-stimulating factor produced by Chinese hamster ovary cells, J Biochem (Tokyo) 103, 544-6 (1988).
6. Takeuchi M, Takasaki S, Miyazaki H, Kato T, Hoshi S, Kochibe N, Kobata A, Comparative study of the asparagine-linked sugar chains of human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells, J Biol Chem 263, 3657-63 (1988).
7. Tsuda E, Goto M, Murakami A, Akai K, Ueda M, Kawanishi G, Takahashi N, Sasaki R, Chiba H, Ishihara H, et al., Comparative structural study of N-linked oligosaccharides of urinary and recombinant erythropoietins, Biochemistry 27, 5646-54 (1988).
8. Herscovics A, Orlean P, Glycoprotein biosynthesis in yeast, Faseb J 7, 540-50 (1993).
9. Baenziger JU, Protein-specific glycosyltransferases: How and why they do it!, Faseb J 8, 1019-25 (1994).
10. Ballou CE, Isolation, characterization, and properties of Saccharomyces cerevisiae mnn mutants with nonconditional protein glycosylation defects, Methods Enzymol 185, 440-70 (1990).
11. Nakayama K, Nagasu T, Shimma Y, Kuromitsu J, Jigami Y, OCH1 encodes a novel membrane bound mannosyltransferase: Outer chain elongation of asparagine-linked oligosaccharides, Embo J 11, 2511-9 (1992).
12. Odani T, Shimma Y, Tanaka A, Jigami Y, Cloning and analysis of the MNN4 gene required for phosphorylation of N-linked oligosaccharides in Saccharomyces cerevisiae, Glycobiology 6, 805-10 (1996).
13. McKeehan WL, Wang F, Kan M, The heparan sulfate-fibroblast growth factor family: Diversity of structure and function, Prog Nucleic Acid Res Mol Biol 59, 135-76 (1998).
14. Asada M, Yoneda A, Oda Y, Ota K, Ozawa K, Fukuta K, Omae F, Asanagi M, Orikasa N, Suzuki M, Oka S, Makino T, Imamura T, Characterization of fibroblast growth factor-6 expressed by Chinese hamster ovary cells as a glycosylated mitogen for human vascular endothelial cells, Growth Factors 16, 293-303 (1999).
15. Yoneda A, Asada M, Yamamoto S, Oki J, Oda Y, Ota K, Ogi Y, Fujishima S, Imamura T, Engineering neoglycoproteins with multiple O-glycans using repetitive pentapeptide glycosylation units, Glycoconj J 18, 291-9 (2001).
16. Takamatsu S, Fukuta K, Asanagi M, Abe R, Yokomatsu T, Fujibayashi Y, Makino T, Monitoring biodistribution of glycoproteins with modified sugar chains, Biochim Biophis Acta 1622, 179-91 (2003).
17. Yoneda A, Asada M, Suzuki M, Imamura T, Introduction of an N-glycosylation cassette into proteins at random sites: Expression of neoglycosylated FGF, Biotechniques 27, 576-8, 80, 82 passim (1999).
18. Alani E, Cao L, Kleckner N, A method for gene disruption that allows repeated use of URA3 selection in the construction of multiply disrupted yeast strains, Genetics 116, 541-5 (1987).
19. Ito H, Fukuda Y, Murata K, Kimura A, Transformation of intact yeast cells treated with alkali cations, J Bacteriol 153, 163-8 (1983).
20. Kainuma M, Ishida N, Yoko-o T, Yoshioka S, Takeuchi M, Kawakita M, Jigami Y, Coexpression of alphal,2 galactosyltransferase and UDP-galactose transporter efficiently galactosylates N- and O-glycans in Saccharomyces cerevisiae, Glycobiology 9, 133-41 (1999).
21. Chiba Y, Suzuki M, Yoshida S, Yoshida A, Ikenaga H, Takeuchi M, Jigami Y, Ichishima E, Production of human compatible high mannose-type (Man5GlcNAc2) sugar chains in Saccharomyces cerevisiae, J Biol Chem 273, 26298-304 (1998).
22. Yoneda A, Asada M, Oda Y, Suzuki M, Imamura T, Engineering of an FGF-proteoglycan fusion protein with heparin-independent, mitogenic activity, Nat Biotechnol 18, 641-4 (2000).
23. Gavel Y, von Heijne G, Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: Implications for protein engineering, Protein Eng 3, 433-42 (1990).
24. Nakai K, Kanehisa M, Prediction of in-vivo modification sites of proteins from their primary structures, J Biochem (Tokyo) 104, 693-9 (1988).
25. Shakin-Eshleman SH, Wunner WH, Spitalnik SL, Efficiency of N-linked core glycosylation at asparagine-319 of rabies virus glycoprotein is altered by deletions C-terminal to the glycosylation sequon, Biochemistry 32, 9465-72 (1993).
26. Nilsson IM, von Heijne G, Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane, J Biol Chem 268, 5798-801 (1993).
27. Lee YC, Lee RT, Carbohydrate-protein interactions: Basis of glycobiology, Acc Chem Res. 28, 321-7 (1995).
28. Pricer WE, Jr., Ashwell G, The binding of desialylated glycoproteins by plasma membranes of rat liver, J Biol Chem 246, 4825-33 (1971).
29. Schlesinger P, Rodman JS, Frey M, Lang S, Stahl P, Clearance of lysosomal hydrolases following intravenous infusion. The role of liver in the clearance of beta-glucuronidase and N-acetyl-beta-D-glucosaminidase, Arch Biochem Biophys 177, 606-14 (1976).
30. Farquhar MG, Editorial: The primary glomerular filtration barrier-basement membrane or epithelial slits?, Kidney Int 8, 197-211 (1975).
31. Kinoshita H, Ohnishi N, Ichikawa F, Kato M, Tokura S, Iida S, Ochi N, Okazaki A, Therapeutic peptides and Proteins. In Current Communications In Molecular Biology, edited by (Cold Spring Harbor Laboratory, New York, 1989), pp. 123-7.
32. Wileman T, Boshans RL, Schlesinger P, Stahl P, Monensin inhibits recycling of macrophage mannose-glycoprotein receptors and ligand delivery to lysosomes, Biochem J 220, 665-75 (1984).
33. Feige JJ, Baird A, Glycosylation of the basic fibroblast growth factor receptor. The contribution of carbohydrate to receptor function, J Biol Chem 263, 14023-9 (1988).
34. Baird A, Esch F, Mormede P, Ueno N, Ling N, Bohlen P, Ying SY, Wehrenberg WB, Guillemin R, Molecular characterization of fibroblast growth factor: Distribution and biological activities in various tissues, Recent Prog Horm Res 42, 143-205 (1986).
35. Zhang R, Cai H, Fatima N, Buczko E, Dufau ML, Functional glycosylation sites of the rat luteinizing hormone receptor required for ligand binding, J Biol Chem 270, 21722-8 (1995).
36. Chiba Y, Sakuraba H, Kotani M, Kase R, Kobayashi K, Takeuchi M, Ogasawara S, Maruyama Y, Nakajima T, Takaoka Y, Jigami Y, Production in yeast of alpha-galactosidase A, a lysosomal enzyme applicable to enzyme replacement therapy for Fabry disease, Glycobiology 12, 821-8 (2002).