메뉴 건너뛰기




Volumn 70, Issue 1, 2008, Pages 42-50

Glycation during storage and administration of monoclonal antibody formulations

Author keywords

Administration; Antibody; Compatibility; Formulation; Glucose; Glycation; Sucrose

Indexed keywords

BORONIC ACID DERIVATIVE; GLUCOSE; IMMUNOGLOBULIN G ANTIBODY; MONOCLONAL ANTIBODY; MONOSACCHARIDE;

EID: 50349097199     PISSN: 09396411     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejpb.2008.04.021     Document Type: Article
Times cited : (104)

References (45)
  • 1
    • 14844285410 scopus 로고    scopus 로고
    • The therapeutic antibodies market to 2008
    • Pavlou A.K., and Belsey M.J. The therapeutic antibodies market to 2008. Eur. J. Pharm. Biopharm. 59 (2005) 389-396
    • (2005) Eur. J. Pharm. Biopharm. , vol.59 , pp. 389-396
    • Pavlou, A.K.1    Belsey, M.J.2
  • 2
    • 34250376918 scopus 로고    scopus 로고
    • Protein misfolding and aggregation
    • Murphy R.M., and Kendrick B.S. Protein misfolding and aggregation. Biotechnol. Prog. 23 (2007) 548-552
    • (2007) Biotechnol. Prog. , vol.23 , pp. 548-552
    • Murphy, R.M.1    Kendrick, B.S.2
  • 4
    • 0038632059 scopus 로고    scopus 로고
    • Effect of freezing and thawing rates on denaturation of proteins in aqueous solutions
    • Cao E., Chen Y., Cui Z., and Foster P.R. Effect of freezing and thawing rates on denaturation of proteins in aqueous solutions. Biotechnol. Bioeng. 82 (2003) 684-690
    • (2003) Biotechnol. Bioeng. , vol.82 , pp. 684-690
    • Cao, E.1    Chen, Y.2    Cui, Z.3    Foster, P.R.4
  • 5
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford C. Protein denaturation. Adv. Protein Chem. 23 (1968) 121-282
    • (1968) Adv. Protein Chem. , vol.23 , pp. 121-282
    • Tanford, C.1
  • 6
    • 11844291300 scopus 로고    scopus 로고
    • Protein aggregation and its inhibition in biopharmaceutics
    • Wang W. Protein aggregation and its inhibition in biopharmaceutics. Int. J. Pharm. 289 (2005) 1-30
    • (2005) Int. J. Pharm. , vol.289 , pp. 1-30
    • Wang, W.1
  • 7
    • 15444374846 scopus 로고    scopus 로고
    • Role of arginine in the stabilization of proteins against aggregation
    • Baynes B.M., Wang D.I., and Trout B.L. Role of arginine in the stabilization of proteins against aggregation. Biochemistry 44 (2005) 4919-4925
    • (2005) Biochemistry , vol.44 , pp. 4919-4925
    • Baynes, B.M.1    Wang, D.I.2    Trout, B.L.3
  • 8
    • 0027729733 scopus 로고
    • The development of stable protein formulations: a close look at protein aggregation, deamidation, and oxidation
    • Cleland J.L., Powell M.F., and Shire S.J. The development of stable protein formulations: a close look at protein aggregation, deamidation, and oxidation. Crit. Rev. Ther. Drug Carrier Syst. 10 (1993) 307-377
    • (1993) Crit. Rev. Ther. Drug Carrier Syst. , vol.10 , pp. 307-377
    • Cleland, J.L.1    Powell, M.F.2    Shire, S.J.3
  • 9
    • 33749530357 scopus 로고    scopus 로고
    • Protein aggregation starting from the native globular state
    • Marcon G., Plakoutsi G., and Chiti F. Protein aggregation starting from the native globular state. Methods Enzymol. 413 (2006) 75-91
    • (2006) Methods Enzymol. , vol.413 , pp. 75-91
    • Marcon, G.1    Plakoutsi, G.2    Chiti, F.3
  • 10
    • 0037066786 scopus 로고    scopus 로고
    • Effect of association state and conformational stability on the kinetics of immunoglobulin light chain amyloid fibril formation at physiological pH
    • Souillac P.O., Uversky V.N., Millett I.S., Khurana R., Doniach S., and Fink A.L. Effect of association state and conformational stability on the kinetics of immunoglobulin light chain amyloid fibril formation at physiological pH. J. Biol. Chem. 277 (2002) 12657-12665
    • (2002) J. Biol. Chem. , vol.277 , pp. 12657-12665
    • Souillac, P.O.1    Uversky, V.N.2    Millett, I.S.3    Khurana, R.4    Doniach, S.5    Fink, A.L.6
  • 11
    • 0029817942 scopus 로고    scopus 로고
    • Adsorption of recombinant human granulocyte colony stimulating factor (rhG-CSF) to polyvinyl chloride, polypropylene, and glass: effect of solvent additives
    • Johnston T.P. Adsorption of recombinant human granulocyte colony stimulating factor (rhG-CSF) to polyvinyl chloride, polypropylene, and glass: effect of solvent additives. PDA J. Pharm. Sci. Technol. 50 (1996) 238-245
    • (1996) PDA J. Pharm. Sci. Technol. , vol.50 , pp. 238-245
    • Johnston, T.P.1
  • 12
    • 0033991650 scopus 로고    scopus 로고
    • Adsorption characteristics of mixed monolayers of a globular protein and a non-ionic surfactant
    • Miller R., Fainerman V.B., Makievski A.V., Kragel J., and Wustneck R. Adsorption characteristics of mixed monolayers of a globular protein and a non-ionic surfactant. Colloids Surf. A 161 (2000) 151-157
    • (2000) Colloids Surf. A , vol.161 , pp. 151-157
    • Miller, R.1    Fainerman, V.B.2    Makievski, A.V.3    Kragel, J.4    Wustneck, R.5
  • 15
    • 1842291518 scopus 로고    scopus 로고
    • Metal-catalyzed oxidation of histidine in human growth hormone. Mechanism, isotope effects, and inhibition by a mild denaturing alcohol
    • Zhao F., Ghezzo-Schoneich E., Aced G.I., Hong J., Milby T., and Schoneich C. Metal-catalyzed oxidation of histidine in human growth hormone. Mechanism, isotope effects, and inhibition by a mild denaturing alcohol. J. Biol. Chem. 272 (1997) 9019-9029
    • (1997) J. Biol. Chem. , vol.272 , pp. 9019-9029
    • Zhao, F.1    Ghezzo-Schoneich, E.2    Aced, G.I.3    Hong, J.4    Milby, T.5    Schoneich, C.6
  • 16
    • 0037165646 scopus 로고    scopus 로고
    • Methionine oxidation inhibits fibrillation of human alpha-synuclein in vitro
    • Uversky V.N., Yamin G., Souillac P.O., Goers J., Glaser C.B., and Fink A.L. Methionine oxidation inhibits fibrillation of human alpha-synuclein in vitro. FEBS Lett. 517 (2002) 239-244
    • (2002) FEBS Lett. , vol.517 , pp. 239-244
    • Uversky, V.N.1    Yamin, G.2    Souillac, P.O.3    Goers, J.4    Glaser, C.B.5    Fink, A.L.6
  • 19
    • 0034854492 scopus 로고    scopus 로고
    • Effect of moisture on the stability of a lyophilized humanized monoclonal antibody formulation
    • Breen E.D., Curley J.G., Overcashier D.E., Hsu C.C., and Shire S.J. Effect of moisture on the stability of a lyophilized humanized monoclonal antibody formulation. Pharm. Res. 18 (2001) 1345-1353
    • (2001) Pharm. Res. , vol.18 , pp. 1345-1353
    • Breen, E.D.1    Curley, J.G.2    Overcashier, D.E.3    Hsu, C.C.4    Shire, S.J.5
  • 20
    • 24944512327 scopus 로고    scopus 로고
    • Identification and characterization of deamidation sites in the conserved regions of human immunoglobulin gamma antibodies
    • Chelius D., Rehder D.S., and Bondarenko P.V. Identification and characterization of deamidation sites in the conserved regions of human immunoglobulin gamma antibodies. Anal. Chem. 77 (2005) 6004-6011
    • (2005) Anal. Chem. , vol.77 , pp. 6004-6011
    • Chelius, D.1    Rehder, D.S.2    Bondarenko, P.V.3
  • 21
    • 0028827624 scopus 로고
    • Characterization of erythropoietin dimerization
    • DePaolis A.M., Advani J.V., and Sharma B.G. Characterization of erythropoietin dimerization. J. Pharm. Sci. 84 (1995) 1280-1284
    • (1995) J. Pharm. Sci. , vol.84 , pp. 1280-1284
    • DePaolis, A.M.1    Advani, J.V.2    Sharma, B.G.3
  • 22
    • 0022251563 scopus 로고
    • Glycation of amino groups in protein. Studies on the specificity of modification of RNase by glucose
    • Watkins N.G., Thorpe S.R., and Baynes J.W. Glycation of amino groups in protein. Studies on the specificity of modification of RNase by glucose. J. Biol. Chem. 260 (1985) 10629-10636
    • (1985) J. Biol. Chem. , vol.260 , pp. 10629-10636
    • Watkins, N.G.1    Thorpe, S.R.2    Baynes, J.W.3
  • 23
    • 1842679358 scopus 로고    scopus 로고
    • Peptide and amino acid glycation: new insights into the Maillard reaction
    • Horvat S., and Jakas A. Peptide and amino acid glycation: new insights into the Maillard reaction. J. Pept. Sci. 10 (2004) 119-137
    • (2004) J. Pept. Sci. , vol.10 , pp. 119-137
    • Horvat, S.1    Jakas, A.2
  • 24
    • 22444447985 scopus 로고    scopus 로고
    • Degradation products of proteins damaged by glycation, oxidation and nitration in clinical type 1 diabetes
    • Ahmed N., Babaei-Jadidi R., Howell S.K., Beisswenger P.J., and Thornalley P.J. Degradation products of proteins damaged by glycation, oxidation and nitration in clinical type 1 diabetes. Diabetologia 48 (2005) 1590-1603
    • (2005) Diabetologia , vol.48 , pp. 1590-1603
    • Ahmed, N.1    Babaei-Jadidi, R.2    Howell, S.K.3    Beisswenger, P.J.4    Thornalley, P.J.5
  • 25
    • 0032029363 scopus 로고    scopus 로고
    • AGEs and their interaction with AGE-receptors in vascular disease and diabetes mellitus. I. The AGE concept
    • Bierhaus A., Hofmann M.A., Ziegler R., and Nawroth P.P. AGEs and their interaction with AGE-receptors in vascular disease and diabetes mellitus. I. The AGE concept. Cardiovas. Res. 37 (1998) 586-600
    • (1998) Cardiovas. Res. , vol.37 , pp. 586-600
    • Bierhaus, A.1    Hofmann, M.A.2    Ziegler, R.3    Nawroth, P.P.4
  • 26
    • 0028908348 scopus 로고
    • Advanced protein glycosylation in diabetes and aging
    • Brownlee .M. Advanced protein glycosylation in diabetes and aging. Annu. Rev. Med. 46 (1995) 223-234
    • (1995) Annu. Rev. Med. , vol.46 , pp. 223-234
    • Brownlee, .M.1
  • 27
    • 0035135246 scopus 로고    scopus 로고
    • Advanced glycation end-products: a review
    • Singh .R., Barden A., Mori T., and Beilin L. Advanced glycation end-products: a review. Diabetologia 44 (2001) 129-146
    • (2001) Diabetologia , vol.44 , pp. 129-146
    • Singh, .R.1    Barden, A.2    Mori, T.3    Beilin, L.4
  • 28
    • 0034263945 scopus 로고    scopus 로고
    • The role of mass spectrometry in the study of non-enzymatic protein glycation in diabetes
    • Lapolla A., Fedele D., and Traldi P. The role of mass spectrometry in the study of non-enzymatic protein glycation in diabetes. Mass Spectrom. Rev. 19 (2000) 279-304
    • (2000) Mass Spectrom. Rev. , vol.19 , pp. 279-304
    • Lapolla, A.1    Fedele, D.2    Traldi, P.3
  • 29
    • 0035787070 scopus 로고    scopus 로고
    • Protein glycation, diabetes, and aging
    • Ulrich P., and Cerami A. Protein glycation, diabetes, and aging. Recent Prog. Horm. Res. 56 (2001) 1-21
    • (2001) Recent Prog. Horm. Res. , vol.56 , pp. 1-21
    • Ulrich, P.1    Cerami, A.2
  • 30
    • 0031725628 scopus 로고    scopus 로고
    • Diabetes, advanced glycation endproducts and vascular disease
    • Wautier J.L., and Guillausseau P.J. Diabetes, advanced glycation endproducts and vascular disease. Vasc. Med. 3 (1998) 131-137
    • (1998) Vasc. Med. , vol.3 , pp. 131-137
    • Wautier, J.L.1    Guillausseau, P.J.2
  • 31
    • 0037133280 scopus 로고    scopus 로고
    • Advanced glycation end products activate endothelium through signal-transduction receptor RAGE: a mechanism for amplification of inflammatory responses
    • Basta G., Lazzerini G., Massaro M., Simoncini T., Tanganelli P., Fu C., Kislinger T., Stern D.M., Schmidt A.M., and De Caterina R. Advanced glycation end products activate endothelium through signal-transduction receptor RAGE: a mechanism for amplification of inflammatory responses. Circulation 105 (2002) 816-822
    • (2002) Circulation , vol.105 , pp. 816-822
    • Basta, G.1    Lazzerini, G.2    Massaro, M.3    Simoncini, T.4    Tanganelli, P.5    Fu, C.6    Kislinger, T.7    Stern, D.M.8    Schmidt, A.M.9    De Caterina, R.10
  • 33
    • 0035745275 scopus 로고    scopus 로고
    • Effect of glycation on basic fibroblast growth factor induced angiogenesis and activation of associated signal transduction pathways in vascular endothelial cells: possible relevance to wound healing in diabetes
    • Duraisamy Y., Slevin M., Smith N., Bailey J., Zweit J., Smith C., Ahmed N., and Gaffney J. Effect of glycation on basic fibroblast growth factor induced angiogenesis and activation of associated signal transduction pathways in vascular endothelial cells: possible relevance to wound healing in diabetes. Angiogenesis 4 (2001) 277-288
    • (2001) Angiogenesis , vol.4 , pp. 277-288
    • Duraisamy, Y.1    Slevin, M.2    Smith, N.3    Bailey, J.4    Zweit, J.5    Smith, C.6    Ahmed, N.7    Gaffney, J.8
  • 37
    • 33644619972 scopus 로고    scopus 로고
    • Heterogeneity of recombinant antibodies: linking structure to function
    • Harris .R.J. Heterogeneity of recombinant antibodies: linking structure to function. Dev. Biol. (Basel) 122 (2005) 117-127
    • (2005) Dev. Biol. (Basel) , vol.122 , pp. 117-127
    • Harris, .R.J.1
  • 39
    • 0024120758 scopus 로고
    • Use of lyoprotectants in the freeze-drying of a model protein, ribonuclease A
    • Townsend M.W., and DeLuca P.P. Use of lyoprotectants in the freeze-drying of a model protein, ribonuclease A. J. Parenter. Sci. Technol. 42 (1988) 190-199
    • (1988) J. Parenter. Sci. Technol. , vol.42 , pp. 190-199
    • Townsend, M.W.1    DeLuca, P.P.2
  • 41
    • 50349089126 scopus 로고    scopus 로고
    • Rowe R.C., Sheskey P.J., and Owen S.C. (Eds), Pharmaceutical Press and American Pharmacists Association
    • In: Rowe R.C., Sheskey P.J., and Owen S.C. (Eds). Pharmaceutical Excipients (2007), Pharmaceutical Press and American Pharmacists Association
    • (2007) Pharmaceutical Excipients
  • 42
    • 37749041309 scopus 로고    scopus 로고
    • 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
    • Quan C., Alcala E., Petkovska I., Matthews D., Canova-Davis E., Taticek R., and Ma S. 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 (2008) 179-191
    • (2008) Anal. Biochem. , vol.373 , pp. 179-191
    • Quan, C.1    Alcala, E.2    Petkovska, I.3    Matthews, D.4    Canova-Davis, E.5    Taticek, R.6    Ma, S.7
  • 44
    • 50349095374 scopus 로고    scopus 로고
    • H. Liu, H. Flores, M. Maier, B. Zhang, M. Cromwell, Effect of protein glycation on the stability of a humanized monoclonal antibody, in: 232nd ACS National Meeting, San Francisco, CA, United States, 2006.
    • H. Liu, H. Flores, M. Maier, B. Zhang, M. Cromwell, Effect of protein glycation on the stability of a humanized monoclonal antibody, in: 232nd ACS National Meeting, San Francisco, CA, United States, 2006.
  • 45
    • 12444315061 scopus 로고    scopus 로고
    • Effect of phosphate buffer on the kinetics of glycation of proteins
    • Gil H., Salcedo D., and Romero R. Effect of phosphate buffer on the kinetics of glycation of proteins. J. Phys. Org. Chem. 18 (2005) 183-186
    • (2005) J. Phys. Org. Chem. , vol.18 , pp. 183-186
    • Gil, H.1    Salcedo, D.2    Romero, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.