Controlling glycation of recombinant antibody in fed-batch cell cultures

Biotechnology and Bioengineering

Volumn 108, Issue 11, 2011, Pages 2600-2610

  Yuk, Inn H ^a   Zhang, Boyan ^a   Yang, Yi ^a   Dutina, George ^a   Leach, Kimberly D ^a   Vijayasankaran, Natarajan ^a   Shen, Amy Y ^a   Andersen, Dana C ^a   Snedecor, Bradley R ^a   Joly, John C ^a  

^a GENENTECH INC   (United States)

Author keywords

CHO cell culture; Continuous feed; Glucose; Glycation; Recombinant antibody

Indexed keywords

AMINE GROUPS; BASIC PRINCIPLES; CELL CULTURE PROCESS; CHO CELL; CHRONIC DISEASE; CONTINUOUS FEED; FED BATCHES; FIRST ORDER; GLUCOSE CONCENTRATION; GLYCATION; HUMAN BODIES; NON-ENZYMATIC; RECOMBINANT ANTIBODY; RECOMBINANT MONOCLONAL ANTIBODY; RECOMBINANT PROTEIN; REDUCING SUGARS; SECOND-ORDER CHEMICAL REACTIONS; SECRETED PROTEIN; STRUCTURAL HETEROGENEITY; THERAPEUTIC ANTIBODIES;

ANIMAL CELL CULTURE; BATCH CELL CULTURE; BIOREACTORS; CHEMICAL REACTIONS; GLUCOSE; MONOCLONAL ANTIBODIES; PROTEINS;

CELLS;

GLUCOSE; MONOCLONAL ANTIBODY; RECOMBINANT HUMANIZED MONOCLONAL ANTIBODY; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; BIOREACTOR; CHO CELL; CONCENTRATION RESPONSE; CULTURE MEDIUM; FED BATCH CULTURE; NONHUMAN; PROTEIN GLYCOSYLATION; REACTION ANALYSIS;

ANIMALS; ANTIBODIES, MONOCLONAL; CELL CULTURE TECHNIQUES; CHO CELLS; CRICETINAE; GLYCOPROTEINS; GLYCOSYLATION; HUMANS; PROTEIN PROCESSING, POST-TRANSLATIONAL; RECOMBINANT PROTEINS;

EID: 80053051994     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.23218     Document Type: Article

References (38)

1. Angyal SJ. 1984. The composition of reducing sugars in solution. Adv Carbohydr Chem Biochem 42: 15-68.
2. Banks DD, Hambly DM, Scavezze JL, Siska CC, Stackhouse NL, Gadgil HS. 2009. The effect of sucrose hydrolysis on the stability of protein therapeutics during accelerated formulation studies. J Pharm Sci 98: 4501-4510.
3. Booth AA, Khalifah RG, Todd P, Hudson BG. 1997. In vitro kinetic studies of formation of antigenic advanced glycation end products (AGEs). J Biol Chem 272: 5430-5437.
4. Brady LJ, Martinez T, Balland A. 2007. Characterization of nonenzymatic glycation on a monoclonal antibody. Anal Chem 79: 9403-9413.
5. Brownlee M. 1995. Advanced protein glycosylation in diabetes and aging. Ann Rev Med 46: 223-234.
6. Brownlee M. 2001. Biochemistry and molecular cell biology of diabetic complications. Nature 414: 813-820.
7. Bunn HF, Higgins PJ. 1981. Reaction of monosaccharides with proteins: Possible evolutionary significance. Science 213: 222-224.
8. Bunn HF, Haney DN, Gabbay KH, Gallop PM. 1975. Further identification of the nature and linkage of the carbohydrate in hemoglobin A1c. Biochem Biophys Res Commun 67: 102-109.
9. Chapra SC, Canale RP. 1988. Numerical methods for engineers. 2nd edition. New York: McGraw-Hill.
10. Fahrner RL, Whitney DH, Vanderlaan M, Blank GS. 1999. Performance comparison of protein A affinity-chromatography sorbents for purifying recombinant monoclonal antibodies. Biotechnol Appl Biochem 30: 121-128.
11. Fischer S, Hoernschemeyer J, Mahler HC. 2008. Glycation during storage and administration of monoclonal antibody formulations. Eur J Pharm Biopharm 70: 42-50.
12. Gadgil HS, Bondarenko PV, Treuheit MJ, Ren D. 2007. Screening and sequencing of glycated proteins by neutral loss scan LC/MS/MS method. Anal Chem 79: 5991-5999.
13. Gugliucci A, Allard MF. 1996. Glycation of hepatocyte cytosolic proteins in streptozotocin-induced diabetic rates. Biochem Biophys Res Commun 229: 952-958.
14. Guo D, Gao A, Michels DA, Feeney L, Eng M, Chan B, Laird MW, Zhang B, Yu C, Joly J, Snedecor B, Shen A. 2010. Mechanisms of unintended amino acid sequence changes in recombinant mononoclonal antibodies expressed in Chinese Hamster Ovary (CHO) cells. Biotechol Bioeng 107: 163-171.
15. Harris RJ. 2005. Heterogeneity of recombinant antibodies: Linking structure to function. Dev Biol (Basel) 122: 117-127.
16. Hayward LD, Angyal SJ. 1977. A symmetry rule for the circular dichroism of reducing sugars, and the proportion of carbonyl forms in aqueous solutions thereof. Carbohydr Res 53: 13-20.
17. Hipkiss AR, Michaelis J, Syrris P. 1995. Non-enzymatic glycosylation of the dipeptide L-carnosine, a potential anti-protein-cross-linking agent. FEBS Lett 371: 81-85.
18. Khalifah RG, Todd P, Booth A, Yang SX, Mott JD, Hudson BG. 1996. Kinetics of nonenzymatic glycation of ribonuclease A leading to advanced glycation end products. Paradoxical inhibition by ribose leads to facile isolation of protein intermediate for rapid post-Amadori studies. Biochemistry 35: 4645-4654.
19. Kurien BT, Scofield RH. 2008. Autoimmunity and oxidatively modified autoantigens. Autoimmunity Rev 7: 567-573.
20. Kwak EJ, Lim SI. 2004. The effect of sugar, amino acid, metal ion, and NaCl on model Maillard reaction under pH control. Amino Acids 27: 85-90.
21. Lee BS, Krishnanchettiar S, Lateef SS, Gupta S. 2007. Analyses of the in vitro non-enzymatic glycation of peptides/proteins by matrix-assisted laser desorption/ionization mass spectrometry. Int J Mass Spectrom 260: 67-74.
22. Ling X, Sakashita N, Takeya M, Nagai R, Horiuchi S, Takahashi K. 1998. Immunohistochemical distribution and subcellular localization of three distinct specific molecular structures of advanced glycation end products in human tissues. Lab Invest 78: 1591-1606.
23. Lucas BK, Giere LM, DeMarco RA, Shen A, Chisholm V, Crowley CW. 1996. High-level production of recombinant proteins in CHO cells using a dicistronic DHFR intron expression vector. Nucleic Acids Res 24: 1774-1779.
24. Maillard LC. 1912. Action des amines sur les sucres: Formation des mélanoïdines par voie méthodique. C R Acad Sci 154: 66-68.
25. Miranda HV, Outeiro TF. 2010. The sour side of neurodegenerative disorders: The effects of protein glycation. J Pathol 221: 13-25.
26. Monnier VM. 2006. The fructosamine 3-kinase knockout mouse: A tool for testing the glycation hypothesis of intracellular protein damage in diabetes and aging. Biochem J 399: e11-e13.
27. 13C NMR investigation of nonenzymatic glucosylation of protein. J Biol Chem 258: 14279-14283.
28. O'Callaghan PM, McLeod J, Pybus LP, Lovelady CS, Wilkinson SJ, Racher AJ, Porter A, James DC. 2010. Cell line-specific control of recombinant monoclonal antibody production by CHO cells. Biotechnol Bioeng 106: 938-951.
29. Quan C, Alcala E, Petkovska I, Matthews D, Canova-Davis E, Taticek R, Ma S. 2008. A study in glycation of a therapeutic recombinant humanized monoclonal antibody: Where it is, how it got there, and how it affects charge-based behavior. Anal Biochem 373: 179-191.
30. Rendell M, Nierenberg J, Brannan C, Valentine JL, Stephen PM, Dodds S, Mercer P, Smith PK, Walder J. 1986. Inhibition of glycation of albumin and hemoglobin by acetylation in vitro and in vivo. J Lab Clin Med 108: 286-293.
31. Schleicher E, Wieland OH. 1986. Kinetic analysis of glycation as a tool for assessing the half-life of proteins. Biochim Biophys Acta 884: 199-205.
32. Sensi M, Pricci F, de Rossi MG, Morano S, di Marlo U. 1989. D-lysine effectively decreases the non-enzymatic glycation of proteins in vitro. Clin Chem 35: 384-387.
33. Shilton BH, Campbell RL, Walton DJ. 1993. Site specificity of glycation of horse liver alcohol dehydrogenase in vitro. Eur J Biochem 215: 567-572.
34. Tarelli E, Corran PH, Bingham BR, Mollison H, Wait R. 1994. Lysine vasopressin undergoes rapid glycation in the presence of reducing sugars. J Pharm Biomed Anal 12: 1355-1361.
35. Vrdoljak A, Trescec A, Benko B, Hecimovic D, Simic M. 2004. In vitro glycation of human immunoglobulin G. Clin Chim Acta 345: 105-111.
36. Watkins NG, Thorpe SR, Baynes JW. 1985. Glycation of amino groups in protein. J Biol Chem 260: 10629-10636.
37. Watkins NG, Neglia-Fisher CI, Dyer DG, Thorpe SR, Baynes JW. 1987. Effect of phosphate on the kinetics and specificity of glycation of protein. J Biol Chem 262: 7207-7212.
38. Zhang B, Yang Y, Yuk I, Pai R, McKay P, Eigenbrot C, Dennis M, Katta V, Francissen KC. 2008. Unveiling a glycation hot spot in a recombinant humanized monoclonal antibody. Anal Chem 80: 2379-2390.