A functional analysis of N-glycosylation-related genes on sialylation of recombinant erythropoietin in six commonly used mammalian cell lines

Metabolic Engineering

Volumn 12, Issue 6, 2010, Pages 526-536

  Zhang, Peiqing ^a,b   Lifen Tan, Diana ^a   Heng, Desmond ^a   Wang, Tianhua ^a   Mariati, ^a   Yang, Yuansheng ^a   Song, Zhiwei ^a  

^a AGENCY FOR SCIENCE   (Singapore)

^b NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

Author keywords

Glycogenes; Isoelectric focusing (IEF); N glycosylation; Recombinant erythropoietin (EPO); Sialic acid

Indexed keywords

GLYCOGENES; ISOELECTRIC FOCUSING; N-GLYCOSYLATION; RECOMBINANT ERYTHROPOIETIN (EPO); SIALIC ACIDS;

ACIDS; CARBOXYLIC ACIDS; CELL CULTURE; ELECTROPHORESIS; FUNCTIONAL ANALYSIS; GENES; GLYCOSYLATION; MAMMALS;

ESTERIFICATION;

GLYCOPROTEIN; GLYCOSIDASE; GLYCOSYLTRANSFERASE; LECTIN; RECOMBINANT ERYTHROPOIETIN; SIALYLTRANSFERASE;

ANIMAL CELL; ARTICLE; GENE OVEREXPRESSION; GLYCOSYLATION; MAMMAL CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SIALYLATION;

3T3 CELLS; ANIMALS; CELL LINE; CERCOPITHECUS AETHIOPS; CHO CELLS; COS CELLS; CRICETINAE; CRICETULUS; ERYTHROPOIETIN, RECOMBINANT; GLYCOPROTEINS; GLYCOSYLATION; HEK293 CELLS; HUMANS; ISOELECTRIC FOCUSING; LECTINS; MICE; N-ACETYLNEURAMINIC ACID; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; SILANES; THIOBARBITURIC ACID REACTIVE SUBSTANCES;

MAMMALIA;

EID: 78049428272     PISSN: 10967176     EISSN: 10967184     Source Type: Journal    
DOI: 10.1016/j.ymben.2010.08.004     Document Type: Article

References (44)

1. Akama T.O., Nakagawa H., Wong N.K., Sutton-Smith M., Dell A., Morris H.R., Nakayama J., Nishimura S.I., Pai A., Moremen K.W., Marth J.D., Fukuda M.N. Essential and mutually compensatory roles of alpha-mannosidase II and alpha-mannosidase IIx in N-glycan processing in vivo in mice. Proc. Natl. Acad. Sci. USA. 2006, 103:8983-8988.
2. Apweiler R., Hermjakob H., Sharon N. On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim. Biophys. Acta 1999, 1473:4-8.
3. Bragonzi A., Distefano G., Buckberry L.D., Acerbis G., Foglieni C., Lamotte D., Campi G., Marc A., Soria M.R., Jenkins N., Monaco L. A new Chinese hamster ovary cell line expressing alpha 2,6-sialyltransferase used as universal host for the production of human-like sialylated recombinant glycoproteins. Biochim. Biophys. Acta 2000, 1474:273-282.
4. Brockhausen I., Narasimhan S., Schachter H. The biosynthesis of highly branched N-glycans-studies on the sequential pathway and functional-role of N-acetylglucosaminyltransferases I, II, III, IV, V and VI. Biochimie 1988, 70:1521-1533.
5. Chan K.F., Zhang P., Song Z. Identification of essential amino acid residues in the hydrophilic loop regions of the CMP-sialic acid transporter and UDP-galactose transporter. Glycobiology 2010, 20:689-701.
6. Chen P., Harcum S.W. Effects of elevated ammonium on glycosylation gene expression in CHO cells. Metab. Eng. 2006, 8:123-132.
7. Chen W., Stanley P. Five Lec1 CHO cell mutants have distinct Mgat1 gene mutations that encode truncated N-acetylglucosaminyltransferase. Glycobiology 2003, 13:43-50.
8. Chitlaru T., Kronman C., Zeevi M., Kam M., Harel A., Ordentlich A., Velan B., Shafferman A. Modulation of circulatory residence of recombinant acetylcholinesterase through biochemical or genetic manipulation of sialylation levels. Biochem. J. 1998, 336:647-658.
9. Comelli E.M., Head S.R., Gilmartin T., Whisenant T., Haslam S.M., North S.J., Wong N.K., Kudo T., Narimatsu H., Esko J.D., Drickamer K., Dell A., Paulson J.C. A focused microarray approach to functional glycomics: transcriptional regulation of the glycome. Glycobiology 2006, 16:117-131.
10. Deutscher S.L., Hirschberg C.B. Mechanism of galactosylation in the Golgi apparatus. A Chinese hamster ovary cell mutant deficient in translocation of UDP-galactose across Golgi vesicle membranes. J. Biol. Chem. 1986, 261:96-100.
11. Goh J.S.Y., Zhang P., Chan K.F., Lee M.M., Lim S.F., Song Z. RCA-I-resistant CHO mutant cells have dysfunctional GnT I and expression of normal GnT I in these mutants enhances sialylation of recombinant erythropoietin. Metab. Eng. 2010, 12:360-368.
12. Hammond K.S., Papermaster D.S. Fluorometric assay of sialic acid in the picomole range: a modification of the thiobarbituric acid assay. Anal. Biochem. 1976, 74:292-297.
13. Harduin-Lepers A., Vallejo-Ruiz V., Krzewinski-Recchi M.A., Samyn-Petit B., Julien S., Delannoy P. The human sialyltransferase family. Biochimie 2001, 83:727-737.
14. Helenius A., Aebi M. Intracellular functions of N-linked glycans. Science 2001, 291:2364-2369.
15. Hennet T. The galactosyltransferase family. Cell Mol. Life Sci. 2002, 59:1081-1095.
16. Herscovics A. Importance of glycosidases in mammalian glycoprotein biosynthesis. Biochim. Biophys. Acta 1999, 1473:96-107.
17. Herscovics A. Structure and function of Class I alpha 1,2-mannosidases involved in glycoprotein synthesis and endoplasmic reticulum quality control. Biochimie 2001, 83:757-762.
18. Hirschberg C.B., Robbins P.W., Abeijon C. Transporters of nucleotide sugars, ATP, and nucleotide sulfate in the endoplasmic reticulum and Golgi apparatus. Annu. Rev. Biochem. 1998, 67:49-69.
19. Jeong Y.T., Choi O., Son Y.D., Yeol-Park S., Kim J.H. Enhanced sialylation of recombinant erythropoietin in genetically engineered Chinese-hamster ovary cells. Biotechnol. Appl. Biochem. 2009, 52:283-291.
20. Lasne F., de Ceaurriz J. Recombinant erythropoietin in urine. Nature 2000, 405:635.
21. Lasne F., Martin L., Crepin N., de Ceaurriz J. Detection of isoelectric profiles of erythropoietin in urine: differentiation of natural and administered recombinant hormones. Anal. Biochem. 2002, 311:119-126.
22. Lasne F., Thioulouse J., Martin L., de Ceaurriz J. Detection of recombinant human erythropoietin in urine for doping analysis: interpretation of isoelectric profiles by discriminant analysis. Electrophoresis 2007, 28:1875-1881.
23. Lee E.U., Roth J., Paulson J.C. Alteration of terminal glycosylation sequences on N-linked oligosaccharides of Chinese-Hamster ovary cells by expression of beta-galactoside alpha-2,6-sialyltransferase. J. Biol. Chem. 1989, 264:13848-13855.
24. Lim S.F., Lee M.M., Zhang P., Song Z. The Golgi CMP-sialic acid transporter: a new CHO mutant provides functional insights. Glycobiology 2008, 18:851-860.
25. Lubke T., Marquardt T., Etzioni A., Hartmann E., von Figura K., Korner C. Complementation cloning identifies CDG-IIc, a new type of congenital disorders of glycosylation, as a GDP-fucose transporter deficiency. Nat. Genet. 2001, 28:73-76.
26. Marth J.D., Grewal P.K. Mammalian glycosylation in immunity. Nat. Rev. Immunol. 2008, 8:874-887.
27. Morell A.G., Gregoriadis G., Scheinberg I.H., Hickman J., Ashwell G. The role of sialic acid in determining the survival of glycoproteins in the circulation. J. Biol. Chem. 1971, 246:1461-1467.
28. Nairn A.V., York W.S., Harris K., Hall E.M., Pierce J.M., Moremen K.W. Regulation of glycan structures in animal tissues-transcript profiling of glycan-related genes. J. Biol. Chem. 2008, 283:17298-17313.
29. Oelmann S., Stanley P., Gerardy-Schahn R. Point mutations identified in Lec8 Chinese hamster ovary glycosylation mutants that inactivate both the UDP-galactose and CMP-sialic acid transporters. J. Biol. Chem. 2001, 276:26291-26300.
30. Okajima T., Fukumoto S., Miyazaki H., Ishida H., Kiso M., Furukawa K., Urano T., Furukawa K. Molecular cloning of a novel alpha2,3-sialyltransferase (ST3Gal VI) that sialylates type II lactosamine structures on glycoproteins and glycolipids. J. Biol. Chem. 1999, 274:11479-11486.
31. Park S.S., Park J., Ko J., Chen L., Meriage D., Crouse-Zeineddini J., Wong W., Kerwin B.A. Biochemical assessment of erythropoietin products from Asia versus US Epoetin alfa manufactured by Amgen. J. Pharm. Sci. 2009, 98:1688-1699.
32. Parodi A.J. Protein glucosylation and its role in protein folding. Annu. Rev. Biochem. 2000, 69:69-93.
33. Pelletier M.F., Marcil A., Sevigny G., Jakob C.A., Tessier D.C., Chevet E., Menard R., Bergeron J.J.M., Thomas D.Y. The heterodimeric structure of glucosidase II is required for its activity, solubility, and localization in vivo. Glycobiology 2000, 10:815-827.
34. Puck T.T. Development of the Chinese hamster ovary (CHO) cell for use in somatic cell genetics. Molecular Cell Genetics 1985, 37-64. John Wiley and Sons, New York. M.M. Gottesman (Ed.).
35. Ray M.K., Yang J., Sundaram S., Stanley P. A novel glycosylation phenotype expressed by Lec23, a Chinese hamster ovary mutant deficient in alpha-glucosidase I. J. Biol. Chem. 1991, 266:22818-22825.
36. Rozen S., Skaletsky H. Primer3 onx the WWW for general users and for biologist programmers. Bioinformatics Methods and Protocols in the Series Methods in Molecular Biology 2000, 365-386. Humana Press Inc., Totowa (NJ). S. Krawetz, S. Misener (Eds.).
37. Schriebl K., Trummer E., Weik R., Lattenmayer C., Muller D., Kunert R., Katinger H., Vorauer-Uhl K. Applicability of different fluorescent dyes for isoform quantification on linear IPG gels. Electrophoresis 2007, 28:2100-2107.
38. Sinclair A.M., Elliott S. Glycoengineering: the effect of glycosylation on the properties of therapeutic proteins. J. Pharm. Sci. 2005, 94:1626-1635.
39. Stanley P. Biological consequences of overexpressing or eliminating N-acetylglucosaminyltransferase-TIII in the mouse. Biochim. Biophys. Acta 2002, 1573:363-368.
40. Trombetta E.S., Simons J.F., Helenius A. Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit. J. Biol. Chem. 1996, 271:27509-27516.
41. Wang Y., Schachter H., Marth J.D. Mice with a homozygous deletion of the Mgat2 gene encoding UDP-N-acetylglucosamine: alpha-6-d-mannoside beta 1,2-N-acetylglucosaminyltransferase II: a model for congenital disorder of glycosylation type IIa. Biochim. Biophys. Acta 2002, 1573:301-311.
42. Weikert S., Papac D., Briggs J., Cowfer D., Tom S., Gawlitzek M., Lofgren J., Mehta S., Chisholm V., Modi N., Eppler S., Carroll K., Chamow S., Peers D., Berman P., Krummen L. Engineering Chinese hamster ovary cells to maximize sialic acid content of recombinant glycoproteins. Nat. Biotechnol. 1999, 17:1116-1121.
43. Wong N.S.C., Yap M.G.S., Wang +D.I.C. Enhancing recombinant glycoprotein sialylation through CMP-sialic acid transporter over expression in Chinese hamster ovary cells. Biotechnol. Bioeng. 2006, 93:1005-1016.
44. Yoshida A., Minowa M.T., Takamatsu S., Hara T., Ikenaga H., Takeuchi M. A novel second isoenzyme of the human UDP-N-acetylglucosamine:alpha1,3-d-mannoside beta1,4-N-acetylglucosaminyltransferase family: cDNA cloning, expression, and chromosomal assignment. Glycoconjugate J. 1998, 15:1115-1123.