메뉴 건너뛰기




Volumn 20, Issue 11, 2009, Pages 2021-2033

Electrospray Ionization Quadrupole Ion-Mobility Time-of-Flight Mass Spectrometry as a Tool to Distinguish the Lot-to-Lot Heterogeneity in N-Glycosylation Profile of the Therapeutic Monoclonal Antibody Trastuzumab

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE RESIDUE; COLLISION CELLS; ELECTROSPRAYS; FAST-LC; GLYCAN STRUCTURES; GLYCOFORMS; GLYCOPEPTIDES; GLYCOSYLATED; MASS SPECTRA; N-GLYCOSYLATION; PRODUCTION BATCHES; QUADRUPOLES; RAPID ANALYSIS; RELATIVE ABUNDANCE; SEPARATION FUNCTIONS; THERAPEUTIC MONOCLONAL ANTIBODIES; TIME OF FLIGHT MASS SPECTROMETRY; TRASTUZUMAB;

EID: 70349762761     PISSN: 10440305     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jasms.2009.07.017     Document Type: Article
Times cited : (119)

References (50)
  • 1
    • 0037264969 scopus 로고    scopus 로고
    • Therapeutic Antibodies for Human Diseases at the Dawn of the Twenty-First Century
    • Brekke O.H., and Sandlie I. Therapeutic Antibodies for Human Diseases at the Dawn of the Twenty-First Century. Nat. Rev. Drug Discov. 2 (2003) 52-62
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 52-62
    • Brekke, O.H.1    Sandlie, I.2
  • 3
    • 34347395733 scopus 로고    scopus 로고
    • Trastuzumab-Mechanism of Action and Use in Clinical Practice
    • Hudis C.A. Trastuzumab-Mechanism of Action and Use in Clinical Practice. N. Engl. J. Med. 357 (2007) 39-51
    • (2007) N. Engl. J. Med. , vol.357 , pp. 39-51
    • Hudis, C.A.1
  • 4
    • 13544276336 scopus 로고    scopus 로고
    • Glycosylation of Recombinant Antibody Therapeutics
    • Jefferis R. Glycosylation of Recombinant Antibody Therapeutics. Biotechnol. Prog. 21 (2005) 11-16
    • (2005) Biotechnol. Prog. , vol.21 , pp. 11-16
    • Jefferis, R.1
  • 5
    • 33749860977 scopus 로고    scopus 로고
    • Post-Translational Modifications in the Context of Therapeutic Proteins
    • Walsh G., and Jefferis R. Post-Translational Modifications in the Context of Therapeutic Proteins. Nat. Biotechnol. 24 (2006) 1241-1252
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1241-1252
    • Walsh, G.1    Jefferis, R.2
  • 7
    • 0037474543 scopus 로고    scopus 로고
    • Structural Analysis of Human IgG-Fc Glycoforms Reveals a Correlation Between Glycosylation and Structural Integrity
    • Krapp S., Mimura Y., Jefferis R., Huber R., and Sondermann P. Structural Analysis of Human IgG-Fc Glycoforms Reveals a Correlation Between Glycosylation and Structural Integrity. J. Mol. Biol. 325 (2003) 979-989
    • (2003) J. Mol. Biol. , vol.325 , pp. 979-989
    • Krapp, S.1    Mimura, Y.2    Jefferis, R.3    Huber, R.4    Sondermann, P.5
  • 8
    • 40649109261 scopus 로고    scopus 로고
    • Glycosylation Profiling of a Therapeutic Recombinant Monoclonal Antibody with Two N-Linked Glycosylation Sites Using Liquid Chromatography Coupled to a Hybrid Quadrupole Time-of-Flight Mass Spectrometer
    • Lim A., Reed-Bogan A., and Harmon B.J. Glycosylation Profiling of a Therapeutic Recombinant Monoclonal Antibody with Two N-Linked Glycosylation Sites Using Liquid Chromatography Coupled to a Hybrid Quadrupole Time-of-Flight Mass Spectrometer. Anal. Biochem. 375 (2008) 163-172
    • (2008) Anal. Biochem. , vol.375 , pp. 163-172
    • Lim, A.1    Reed-Bogan, A.2    Harmon, B.J.3
  • 10
    • 0024508462 scopus 로고
    • Clonal Analysis of the Glycosylation of Immunoglobulin G Secreted by Murine Hybridomas
    • Rothman R.J., Warren L., Vliegenthart J.F., and Hard K.J. Clonal Analysis of the Glycosylation of Immunoglobulin G Secreted by Murine Hybridomas. Biochemistry 28 (1989) 1377-1384
    • (1989) Biochemistry , vol.28 , pp. 1377-1384
    • Rothman, R.J.1    Warren, L.2    Vliegenthart, J.F.3    Hard, K.J.4
  • 12
    • 0034045472 scopus 로고    scopus 로고
    • Comparisons of the Glycosylation of a Monoclonal Antibody Produced Under Nominally Identical Cell Culture Conditions in Two Different Bioreactors
    • Kunkel J.P., Jan D.C., Butler M., and Jamieson J.C. Comparisons of the Glycosylation of a Monoclonal Antibody Produced Under Nominally Identical Cell Culture Conditions in Two Different Bioreactors. Biotechnol. Prog. 16 (2000) 462-470
    • (2000) Biotechnol. Prog. , vol.16 , pp. 462-470
    • Kunkel, J.P.1    Jan, D.C.2    Butler, M.3    Jamieson, J.C.4
  • 13
    • 0026641016 scopus 로고
    • Different Culture Methods Lead to Differences in Glycosylation of a Murine IgG Monoclonal Antibody
    • Patel T.P., Parekh R.B., Moellering B.J., and Prior C.P. Different Culture Methods Lead to Differences in Glycosylation of a Murine IgG Monoclonal Antibody. Biochem. J. 285 (1992) 839-845
    • (1992) Biochem. J. , vol.285 , pp. 839-845
    • Patel, T.P.1    Parekh, R.B.2    Moellering, B.J.3    Prior, C.P.4
  • 15
    • 0035922885 scopus 로고    scopus 로고
    • Metabolic Control of Recombinant Monoclonal Antibody N-Glycosylation in GS-NS0 Cells
    • Hills A.E., Patel A., Boyd P., and James D.C. Metabolic Control of Recombinant Monoclonal Antibody N-Glycosylation in GS-NS0 Cells. Biotechnol. Bioeng. 75 (2001) 239-251
    • (2001) Biotechnol. Bioeng. , vol.75 , pp. 239-251
    • Hills, A.E.1    Patel, A.2    Boyd, P.3    James, D.C.4
  • 16
    • 29144436001 scopus 로고    scopus 로고
    • Analysis of Recombinant Monoclonal Antibody Isoforms by Electrospray Ionization Mass Spectrometry as a Strategy for Streamlining Characterization of Recombinant Monoclonal Antibody Charge Heterogeneity
    • Lyubarskaya Y., Houde D., Woodard J., Murphy D., and Mhatre R. Analysis of Recombinant Monoclonal Antibody Isoforms by Electrospray Ionization Mass Spectrometry as a Strategy for Streamlining Characterization of Recombinant Monoclonal Antibody Charge Heterogeneity. Anal. Biochem. 348 (2006) 24-39
    • (2006) Anal. Biochem. , vol.348 , pp. 24-39
    • Lyubarskaya, Y.1    Houde, D.2    Woodard, J.3    Murphy, D.4    Mhatre, R.5
  • 17
    • 53149151450 scopus 로고    scopus 로고
    • Evaluation of Glycosylation for Quality Assurance of Antibody Pharmaceuticals by Capillary Electrophoresis
    • Kamoda S., and Kakehi K. Evaluation of Glycosylation for Quality Assurance of Antibody Pharmaceuticals by Capillary Electrophoresis. Electrophoresis 29 (2008) 3595-3604
    • (2008) Electrophoresis , vol.29 , pp. 3595-3604
    • Kamoda, S.1    Kakehi, K.2
  • 18
    • 2442586731 scopus 로고    scopus 로고
    • Carbohydrate Analysis of a Chimeric Recombinant Monoclonal Antibody by Capillary Electrophoresis with Laser-Induced Fluorescence Detection
    • Ma S., and Nashabeh W. Carbohydrate Analysis of a Chimeric Recombinant Monoclonal Antibody by Capillary Electrophoresis with Laser-Induced Fluorescence Detection. Anal. Chem. 71 (1999) 5185-5192
    • (1999) Anal. Chem. , vol.71 , pp. 5185-5192
    • Ma, S.1    Nashabeh, W.2
  • 19
    • 34249889580 scopus 로고    scopus 로고
    • Differences in the Glycosylation Profile of a Monoclonal Antibody Produced by Hybridomas Cultured in Serum-Supplemented, Serum-Free or Chemically Defined Media
    • Serrato J.A., Hernandez V., Estrada-Mondaca S., Palomares L.A., and Ramirez O.T. Differences in the Glycosylation Profile of a Monoclonal Antibody Produced by Hybridomas Cultured in Serum-Supplemented, Serum-Free or Chemically Defined Media. Biotechnol. Appl. Biochem. 47 (2007) 113-124
    • (2007) Biotechnol. Appl. Biochem. , vol.47 , pp. 113-124
    • Serrato, J.A.1    Hernandez, V.2    Estrada-Mondaca, S.3    Palomares, L.A.4    Ramirez, O.T.5
  • 20
    • 0000117004 scopus 로고    scopus 로고
    • The Use of Electrospray Ionization Mass Spectrometry to Distinguish the Lot-to-Lot Heterogeneity of an Antigen Specific Monoclonal Antibody from a Specific Cellular Clone
    • Adamczyk M., Gebler J.C., Harrington C.A., and Sequeira A.F. The Use of Electrospray Ionization Mass Spectrometry to Distinguish the Lot-to-Lot Heterogeneity of an Antigen Specific Monoclonal Antibody from a Specific Cellular Clone. Eur. Mass Spectrom. 5 (1999) 165-168
    • (1999) Eur. Mass Spectrom. , vol.5 , pp. 165-168
    • Adamczyk, M.1    Gebler, J.C.2    Harrington, C.A.3    Sequeira, A.F.4
  • 21
    • 0035853484 scopus 로고    scopus 로고
    • Rapid Method for Monitoring Galactosylation Levels During Recombinant Antibody Production by Electrospray Mass Spectrometry with Selective-Ion Monitoring
    • Wan H.Z., Kaneshiro S., Frenz J., and Cacia J. Rapid Method for Monitoring Galactosylation Levels During Recombinant Antibody Production by Electrospray Mass Spectrometry with Selective-Ion Monitoring. J. Chromatogr. A 913 (2001) 437-446
    • (2001) J. Chromatogr. A , vol.913 , pp. 437-446
    • Wan, H.Z.1    Kaneshiro, S.2    Frenz, J.3    Cacia, J.4
  • 22
    • 30744447269 scopus 로고    scopus 로고
    • A Comparison of Three Techniques for Quantitative Carbohydrate Analysis Used in Characterization of Therapeutic Antibodies
    • Siemiatkoski J., Lyubarskaya Y., Houde D., Tep S., and Mhatre R. A Comparison of Three Techniques for Quantitative Carbohydrate Analysis Used in Characterization of Therapeutic Antibodies. Carbohydr. Res. 341 (2006) 410-419
    • (2006) Carbohydr. Res. , vol.341 , pp. 410-419
    • Siemiatkoski, J.1    Lyubarskaya, Y.2    Houde, D.3    Tep, S.4    Mhatre, R.5
  • 23
    • 33646398313 scopus 로고    scopus 로고
    • Improving Mass Accuracy of High Performance Liquid Chromatography/Electrospray Ionization Time-of-Flight Mass Spectrometry of Intact Antibodies
    • Gadgil H.S., Pipes G.D., Dillon T.M., Treuheit M.J., and Bondarenko P.V. Improving Mass Accuracy of High Performance Liquid Chromatography/Electrospray Ionization Time-of-Flight Mass Spectrometry of Intact Antibodies. J. Am. Soc. Mass Spectrom. 17 (2006) 867-872
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 867-872
    • Gadgil, H.S.1    Pipes, G.D.2    Dillon, T.M.3    Treuheit, M.J.4    Bondarenko, P.V.5
  • 24
    • 31844447560 scopus 로고    scopus 로고
    • Impact of Variable Domain Glycosylation on Antibody Clearance: an LC/MS Characterization
    • Huang L., Biolsi S., Bales K.R., and Kuchibhotla U. Impact of Variable Domain Glycosylation on Antibody Clearance: an LC/MS Characterization. Anal. Biochem. 349 (2006) 197-207
    • (2006) Anal. Biochem. , vol.349 , pp. 197-207
    • Huang, L.1    Biolsi, S.2    Bales, K.R.3    Kuchibhotla, U.4
  • 25
    • 34548409568 scopus 로고    scopus 로고
    • Contrasting Glycosylation Profiles Between Fab and Fc of a Human IgG Protein Studied by Electrospray Ionization Mass Spectrometry
    • Mimura Y., Ashton P.R., Takahashi N., Harvey D.J., and Jefferis R. Contrasting Glycosylation Profiles Between Fab and Fc of a Human IgG Protein Studied by Electrospray Ionization Mass Spectrometry. J. Immunol. Methods 326 (2007) 116-126
    • (2007) J. Immunol. Methods , vol.326 , pp. 116-126
    • Mimura, Y.1    Ashton, P.R.2    Takahashi, N.3    Harvey, D.J.4    Jefferis, R.5
  • 28
    • 0029142762 scopus 로고
    • Rapid Profiling of Carbohydrate Glycoforms in Monoclonal Antibodies Using MALDI/TOF Mass Spectrometry
    • Kroon D.J., Freedy J., Burinsky D.J., and Sharma B. Rapid Profiling of Carbohydrate Glycoforms in Monoclonal Antibodies Using MALDI/TOF Mass Spectrometry. J. Pharm. Biomed. Anal. 13 (1995) 1049-1054
    • (1995) J. Pharm. Biomed. Anal. , vol.13 , pp. 1049-1054
    • Kroon, D.J.1    Freedy, J.2    Burinsky, D.J.3    Sharma, B.4
  • 29
    • 0037445404 scopus 로고    scopus 로고
    • Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry of Carbohydrates and Glycoconjugates
    • Harvey D.J. Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry of Carbohydrates and Glycoconjugates. Int. J. Mass Spectrom. 226 (2003) 1-35
    • (2003) Int. J. Mass Spectrom. , vol.226 , pp. 1-35
    • Harvey, D.J.1
  • 30
    • 34748837881 scopus 로고    scopus 로고
    • Analysis of N-Glycans from Recombinant Immunoglobulin G by On-Line Reversed-Phase High-Performance Liquid Chromatography/Mass Spectrometry
    • Chen X., and Flynn G.C. Analysis of N-Glycans from Recombinant Immunoglobulin G by On-Line Reversed-Phase High-Performance Liquid Chromatography/Mass Spectrometry. Anal. Biochem. 370 (2007) 147-161
    • (2007) Anal. Biochem. , vol.370 , pp. 147-161
    • Chen, X.1    Flynn, G.C.2
  • 31
    • 29044447751 scopus 로고    scopus 로고
    • Reversed-Phase Liquid Chromatography/Mass Spectrometry Analysis of Reduced Monoclonal Antibodies in Pharmaceutics
    • Rehder D.S., Dillon T.M., Pipes G.D., and Bondarenko P.V. Reversed-Phase Liquid Chromatography/Mass Spectrometry Analysis of Reduced Monoclonal Antibodies in Pharmaceutics. J. Chromatogr. A 1102 (2006) 164-175
    • (2006) J. Chromatogr. A , vol.1102 , pp. 164-175
    • Rehder, D.S.1    Dillon, T.M.2    Pipes, G.D.3    Bondarenko, P.V.4
  • 32
    • 12244254420 scopus 로고    scopus 로고
    • Site-Specific Characterization of the N-Linked Oligosaccharides of a Murine Immunoglobulin M by High-Performance Liquid Chromatography/Electrospray Mass Spectrometry
    • Wang F., Nakouzi A., Angeletti R.H., and Casadevall A. Site-Specific Characterization of the N-Linked Oligosaccharides of a Murine Immunoglobulin M by High-Performance Liquid Chromatography/Electrospray Mass Spectrometry. Anal. Biochem. 314 (2003) 266-280
    • (2003) Anal. Biochem. , vol.314 , pp. 266-280
    • Wang, F.1    Nakouzi, A.2    Angeletti, R.H.3    Casadevall, A.4
  • 33
    • 0031553988 scopus 로고    scopus 로고
    • Characterization of Monoclonal Antibody Glycosylation: Comparison of Expression Systems and Identification of Terminal Alpha-Linked Galactose
    • Sheeley D.M., Merrill B.M., and Taylor L.C. Characterization of Monoclonal Antibody Glycosylation: Comparison of Expression Systems and Identification of Terminal Alpha-Linked Galactose. Anal. Biochem. 247 (1997) 102-110
    • (1997) Anal. Biochem. , vol.247 , pp. 102-110
    • Sheeley, D.M.1    Merrill, B.M.2    Taylor, L.C.3
  • 34
    • 33646873090 scopus 로고    scopus 로고
    • Approaches to the Study of N-Linked Glycoproteins in Human Plasma Using Lectin Affinity Chromatography and Nano-HPLC Coupled to Electrospray Linear Ion Trap-Fourier Transform Mass Spectrometry
    • Wang Y., Wu S.L., and Hancock W.S. Approaches to the Study of N-Linked Glycoproteins in Human Plasma Using Lectin Affinity Chromatography and Nano-HPLC Coupled to Electrospray Linear Ion Trap-Fourier Transform Mass Spectrometry. Glycobiology 16 (2006) 514-523
    • (2006) Glycobiology , vol.16 , pp. 514-523
    • Wang, Y.1    Wu, S.L.2    Hancock, W.S.3
  • 36
    • 33845570516 scopus 로고    scopus 로고
    • Identification of N-Terminal Modification for Recombinant Monoclonal Antibody Light Chain Using Partial Reduction and Quadrupole Time-of-Flight Mass Spectrometry
    • Yu L., Remmele Jr. R.L., and He B. Identification of N-Terminal Modification for Recombinant Monoclonal Antibody Light Chain Using Partial Reduction and Quadrupole Time-of-Flight Mass Spectrometry. Rapid Commun. Mass Spectrom. 20 (2006) 3674-3680
    • (2006) Rapid Commun. Mass Spectrom. , vol.20 , pp. 3674-3680
    • Yu, L.1    Remmele Jr., R.L.2    He, B.3
  • 37
    • 38349085042 scopus 로고    scopus 로고
    • Determination of N-Glycosylation Sites and Site Heterogeneity in a Monoclonal Antibody by Electrospray Quadrupole Ion-Mobility Time-of-Flight Mass Spectrometry
    • Olivova P., Chen W., Chakraborty A.B., and Gebler J.C. Determination of N-Glycosylation Sites and Site Heterogeneity in a Monoclonal Antibody by Electrospray Quadrupole Ion-Mobility Time-of-Flight Mass Spectrometry. Rapid Commun. Mass Spectrom. 22 (2008) 29-40
    • (2008) Rapid Commun. Mass Spectrom. , vol.22 , pp. 29-40
    • Olivova, P.1    Chen, W.2    Chakraborty, A.B.3    Gebler, J.C.4
  • 38
    • 23844499696 scopus 로고    scopus 로고
    • A Rapid Sample Preparation Method For Mass Spectrometric Characterization of N-Linked Glycans
    • Yu Y.Q., Gilar M., Kaska J., and Gebler J.C. A Rapid Sample Preparation Method For Mass Spectrometric Characterization of N-Linked Glycans. Rapid Commun. Mass Spectrom. 19 (2005) 2331-2336
    • (2005) Rapid Commun. Mass Spectrom. , vol.19 , pp. 2331-2336
    • Yu, Y.Q.1    Gilar, M.2    Kaska, J.3    Gebler, J.C.4
  • 43
    • 14744293331 scopus 로고    scopus 로고
    • Trap for MAbs: Characterization of Intact Monoclonal Antibodies Using Reversed-Phase HPLC On-Line with Ion-Trap Mass Spectrometry
    • Le J.C., and Bondarenko P.V. Trap for MAbs: Characterization of Intact Monoclonal Antibodies Using Reversed-Phase HPLC On-Line with Ion-Trap Mass Spectrometry. J. Am. Soc. Mass Spectrom. 16 (2005) 307-311
    • (2005) J. Am. Soc. Mass Spectrom. , vol.16 , pp. 307-311
    • Le, J.C.1    Bondarenko, P.V.2
  • 44
    • 37749019972 scopus 로고    scopus 로고
    • Quantitative Aspects of the Analysis of the Monoclonal Antibody Trastuzumab Using High-Performance Liquid Chromatography Coupled with Electrospray Mass Spectrometry
    • Damen C.W., Rosing H., Schellens J.H., and Beijnen J.H. Quantitative Aspects of the Analysis of the Monoclonal Antibody Trastuzumab Using High-Performance Liquid Chromatography Coupled with Electrospray Mass Spectrometry. J. Pharm. Biomed. Anal. 46 (2008) 449-455
    • (2008) J. Pharm. Biomed. Anal. , vol.46 , pp. 449-455
    • Damen, C.W.1    Rosing, H.2    Schellens, J.H.3    Beijnen, J.H.4
  • 45
    • 0027462384 scopus 로고
    • Selective Identification and Differentiation of N- and O-Linked Oligosaccharides in Glycoproteins by Liquid Chromatography-Mass Spectrometry
    • Carr S.A., Huddleston M.J., and Bean M.F. Selective Identification and Differentiation of N- and O-Linked Oligosaccharides in Glycoproteins by Liquid Chromatography-Mass Spectrometry. Protein Sci. 2 (1993) 183-196
    • (1993) Protein Sci. , vol.2 , pp. 183-196
    • Carr, S.A.1    Huddleston, M.J.2    Bean, M.F.3
  • 46
    • 0027586797 scopus 로고
    • Collisional Fragmentation of Glycopeptides by Electrospray Ionization LC/MS and LC/MS/MS: Methods for Selective Detection of Glycopeptides in Protein Digests
    • Huddleston M.J., Bean M.F., and Carr S.A. Collisional Fragmentation of Glycopeptides by Electrospray Ionization LC/MS and LC/MS/MS: Methods for Selective Detection of Glycopeptides in Protein Digests. Anal. Chem. 65 (1993) 877-884
    • (1993) Anal. Chem. , vol.65 , pp. 877-884
    • Huddleston, M.J.1    Bean, M.F.2    Carr, S.A.3
  • 47
    • 0038826106 scopus 로고    scopus 로고
    • Using Optimized Collision Energies and High Resolution, High Accuracy Fragment Ion Selection to Improve Glycopeptide Detection by Precursor Ion Scanning
    • Jebanathirajah J., Steen H., and Roepstorff P. Using Optimized Collision Energies and High Resolution, High Accuracy Fragment Ion Selection to Improve Glycopeptide Detection by Precursor Ion Scanning. J. Am. Soc. Mass Spectrom. 14 (2003) 777-784
    • (2003) J. Am. Soc. Mass Spectrom. , vol.14 , pp. 777-784
    • Jebanathirajah, J.1    Steen, H.2    Roepstorff, P.3
  • 49
    • 35548961447 scopus 로고    scopus 로고
    • A Mechanistic Perspective of Monoclonal Antibodies in Cancer Therapy Beyond Target-Related Effects
    • Strome S.E., Sausville E.A., and Mann D. A Mechanistic Perspective of Monoclonal Antibodies in Cancer Therapy Beyond Target-Related Effects. Oncologist 12 (2007) 1084-1095
    • (2007) Oncologist , vol.12 , pp. 1084-1095
    • Strome, S.E.1    Sausville, E.A.2    Mann, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.