Direct Site-Specific Glycoform Identification and Quantitative Comparison of Glycoprotein Therapeutics: Imiglucerase and Velaglucerase Alfa

AAPS Journal

Volumn 17, Issue 2, 2015, Pages 405-415

  Ye, Hongping ^a   Hill, John ^b   Gucinski, Ashley C ^a   Boyne, Michael T ^a   Buhse, Lucinda F ^a  

^a CENTER FOR DRUG EVALUATION AND RESEARCH   (United States)

^b NONE   (United States)

Author keywords

imiglucerase; quantitative comparison; site specific glycoforms; velaglucerase alfa

Indexed keywords

GLUCOSYLCERAMIDASE; GLYCOPROTEIN; IMIGLUCERASE; RECOMBINANT PROTEIN; VELAGLUCERASE ALFA, HUMAN;

AMINO ACID SEQUENCE; ANIMAL; CHEMISTRY; CHO CELL LINE; COMPARATIVE STUDY; CRICETULUS; ENZYME REPLACEMENT; GLYCOSYLATION; HAMSTER; HUMAN; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; PROCEDURES;

AMINO ACID SEQUENCE; ANIMALS; CHO CELLS; CHROMATOGRAPHY, LIQUID; CRICETINAE; CRICETULUS; ENZYME REPLACEMENT THERAPY; GLUCOSYLCERAMIDASE; GLYCOPROTEINS; GLYCOSYLATION; HUMANS; MASS SPECTROMETRY; RECOMBINANT PROTEINS;

EID: 84940007856     PISSN: None     EISSN: 15507416     Source Type: Journal    
DOI: 10.1208/s12248-014-9706-4     Document Type: Article

References (35)

1. Kacher Y, Brumshtein B, Boldin-Adamsky S, Toker L, Shainskaya A, Silman I, et al. Acid beta-glucosidase: insights from structural analysis and relevance to Gaucher disease therapy. Biol Chem. 2008;389(11):1361–9. doi:10.1515/BC.2008.163.
2. Beutler E, Grabowski GA. Gaucher disease. In: Scriver CR, Sly WS, editors. The metabolic and molecular bases of inherited disease. New Yourk: McGraw-Hill Inc.; 2001. p. 3635–68.
3. Edmunds T. β-Glucocerebrosidase ceredase and Cerezyme. In: McGrath BM, Walsh G, editors. Directory of therapeutic enzymes. Boca Raton: CRC Press; 2006. p. 117.
4. Brumshtein B, Salinas P, Peterson B, Chan V, Silman I, Sussman JL, et al. Characterization of gene-activated human acid-beta-glucosidase: crystal structure, glycan composition, and internalization into macrophages. Glycobiology. 2010;20(1):24–32. doi:10.1093/glycob/cwp138.
5. Aerts JM, Yasothan U, Kirkpatrick P. Velaglucerase alfa. Nat Rev Drug Discov. 2010;9(11):837–8. doi:10.1038/nrd3311.
6. Hollak CE, vom Dahl S, Aerts JM, Belmatoug N, Bembi B, Cohen Y, et al. Force majeure: therapeutic measures in response to restricted supply of imiglucerase (Cerezyme) for patients with Gaucher disease. Blood Cells Mol Dis. 2010;44(1):41–7. doi:10.1016/j.bcmd.2009.09.006.
7. Wei RR, Hughes H, Boucher S, Bird JJ, Guziewicz N, Van Patten SM, et al. X-ray and biochemical analysis of N370S mutant human acid beta-glucosidase. J Biol Chem. 2011;286(1):299–308. doi:10.1074/jbc.M110.150433.
8. Van Patten SM, Hughes H, Huff MR, Piepenhagen PA, Waire J, Qiu H, et al. Effect of mannose chain length on targeting of glucocerebrosidase for enzyme replacement therapy of Gaucher disease. Glycobiology. 2007;17(5):467–78. doi:10.1093/glycob/cwm008.
9. Brooks SA. Appropriate glycosylation of recombinant proteins for human use: implications of choice of expression system. Mol Biotechnol. 2004;28(3):241–55. doi:10.1385/MB:28:3:241.
10. Warnock JN, Al-Rubeai M. Bioreactor systems for the production of biopharmaceuticals from animal cells. Biotechnol Appl Biochem. 2006;45(Pt 1):1–12. doi:10.1042/BA20050233.
11. Mukovozov I, Sabijicl T, Hortelano G, Ofosu FA. Factors that contribute to the immunogenicity of therapeutic recombinant human proteins. Thromb Haemost. 2008;99(5):874–82. doi:10.1160/Th07-11-0654.
12. Haller CA, Cosenza ME, Sullivan JT. Safety issues specific to clinical development of protein therapeutics. Clin Pharmacol Ther. 2008;84(5):624–7. doi:10.1038/clpt.2008.158.
13. Kawasaki N, Itoh S, Hashii N, Takakura D, Qin Y, Huang X, et al. The significance of glycosylation analysis in development of biopharmaceuticals. Biol Pharm Bull. 2009;32(5):796–800.
14. Rudd PM, Elliott T, Cresswell P, Wilson IA, Dwek RA. Glycosylation and the immune system. Science. 2001;291(5512):2370–6.
15. Liszewski K. Exploiting post-translational modifications. Genet Eng News. 2005;25(1):22.
16. Dwek RA, Butters TD, Platt FM, Zitzmann N. Targeting glycosylation as a therapeutic approach. Nat Rev Drug Discov. 2002;1(1):65–75. doi:10.1038/Nrd708.
17. Helenius A, Aebi M. Intracellular functions of N-linked glycans. Science. 2001;291(5512):2364–9.
18. Okuyama N, Ide Y, Nakano M, Nakagawa T, Yamanaka K, Moriwaki K, et al. Fucosylated haptoglobin is a novel marker for pancreatic cancer: a detailed analysis of the oligosaccharide structure and a possible mechanism for fucosylation. Int J Cancer. 2006;118(11):2803–8. doi:10.1002/ijc.21728.
19. Kyselova Z, Mechref Y, Al Bataineh MM, Dobrolecki LE, Hickey RJ, Vinson J, et al. Alterations in the serum glycome due to metastatic prostate cancer. J Proteome Res. 2007;6(5):1822–32. doi:10.1021/pr060664t.
20. Kayser V, Chennamsetty N, Voynov V, Forrer K, Helk B, Trout BL. Glycosylation influences on the aggregation propensity of therapeutic monoclonal antibodies. Biotechnol J. 2011;6(1):38–44. doi:10.1002/biot.201000091.
21. Sola RJ, Griebenow K. Glycosylation of therapeutic proteins: an effective strategy to optimize efficacy. BioDrugs. 2010;24(1):9–21. doi:10.2165/11530550-000000000-00000.
22. Berg-Fussman A, Grace ME, Ioannou Y, GA G. Human acid β-glucosidase N-glycosylation site occupancy and the effect of glycosylation on enzymatic activity. J Biol Chem. 1993;268(20):14861–66.
23. Varki A, Kornfeld S. The spectrum of anionic oligosaccharides released by endo-beta-N-acetylglucosaminidase H from glycoproteins. Structural studies and interactions with the phosphomannosyl receptor. J Biol Chem. 1983;258(5):2808–18.
24. Raju TS, Briggs JB, Chamow SM, Winkler ME, Jones AJ. Glycoengineering of therapeutic glycoproteins: in vitro galactosylation and sialylation of glycoproteins with terminal N-acetylglucosamine and galactose residues. Biochemistry. 2001;40(30):8868–76.
25. Salinas PA, Miller MJC, Lin MX, Savickas PJ, Thomas JJ. Mass spectrometry-based characterization of acidic glycans on protein therapeutics. Int J Mass Spectrom. 2012;312:122–34. doi:10.1016/j.ijms.2011.06.017.
26. Takasaki S, Murray GJ, Furbish FS, Brady RO, Barranger JA, Kobata A. Structure of the N-asparagine-linked oligosaccharide units of human placental beta-glucocerebrosidase. J Biol Chem. 1984;259(16):10112–7.
27. Tekoah Y, Tzaban S, Kizhner T, Hainrichson M, Gantman A, Golembo M, et al. Glycosylation and functionality of recombinant ss-glucocerebrosidase from various production systems. Bioscience reports. 2013;33(5):doi:10.1042/BSR2013008.
28. Ye H, Boyne 2nd MT, Buhse LF, Hill J. Direct approach for qualitative and quantitative characterization of glycoproteins using tandem mass tags and an LTQ Orbitrap XL electron transfer dissociation hybrid mass spectrometer. Anal Chem. 2013;85(3):1531–9. doi:10.1021/ac3026465.
29. Peterman SM, Mulholland JJ. A novel approach for identification and characterization of glycoproteins using a hybrid linear ion trap/FT-ICR mass spectrometer. J Am Soc Mass Spectrom. 2006;17(2):168–79. doi:10.1016/j.jasms.2005.10.008.
30. http://ca.expasy.org/tools/glycomod, (6/2/2014).
31. https://prosightptm2.northwestern.edu, (6/2/2014).
32. Dvir H, Harel M, McCarthy AA, Toker L, Silman I, Futerman AH, et al. X-ray structure of human acid-beta-glucosidase, the defective enzyme in Gaucher disease. EMBO Rep. 2003;4(7):704–9. doi:10.1038/sj.embor.embor873.
33. Morelle W, Canis K, Chirat F, Faid V, Michalski JC. The use of mass spectrometry for the proteomic analysis of glycosylation. Proteomics. 2006;6(14):3993–4015. doi:10.1002/pmic.200600129.
34. Alley Jr WR, Mechref Y, Novotny MV. Characterization of glycopeptides by combining collision-induced dissociation and electron-transfer dissociation mass spectrometry data. Rapid Commun Mass Spectrom. 2009;23(1):161–70. doi:10.1002/rcm.3850.
35. Viner RI, Zhang T, Second T, Zabrouskov V. Quantification of post-translationally modified peptides of bovine alpha-crystallin using tandem mass tags and electron transfer dissociation. J Proteomics. 2009;72(5):874–85. doi:10.1016/j.jprot.2009.02.005.