메뉴 건너뛰기




Volumn 17, Issue 1, 2015, Pages 237-244

Impact of Glycation on Antibody Clearance

Author keywords

mannose receptor; mass spectrometry; pharmacokinetics; surface plasmon resonance

Indexed keywords

2 IMINO 2 METHOXYETHYL 1 THIOMANNOSIDE; IGG MONOCLONAL ANTIBODY; MANNOSE; MANNOSE RECEPTOR; MANNOSIDE; MONOCLONAL ANTIBODY; UNCLASSIFIED DRUG; CELL SURFACE RECEPTOR; IMMUNOGLOBULIN G; LECTIN; MANNOSE BINDING LECTIN;

EID: 84922103487     PISSN: None     EISSN: 15507416     Source Type: Journal    
DOI: 10.1208/s12248-014-9694-4     Document Type: Article
Times cited : (18)

References (22)
  • 1
    • 0037040350 scopus 로고    scopus 로고
    • Mannose receptor-mediated regulation of serum glycoprotein homeostasis
    • COI: 1:CAS:528:DC%2BD38XhvFClt7o%3D
    • Lee SJ, Evers S, Roeder D, Parlow AF, Risteli J, Risteli L, et al. Mannose receptor-mediated regulation of serum glycoprotein homeostasis. Science (New York). 2002;295(5561):1898–901.
    • (2002) Science (New York) , vol.295 , Issue.5561 , pp. 1898-1901
    • Lee, S.J.1    Evers, S.2    Roeder, D.3    Parlow, A.F.4    Risteli, J.5    Risteli, L.6
  • 2
    • 79958837668 scopus 로고    scopus 로고
    • High-mannose glycans on the Fc region of therapeutic IgG antibodies increase serum clearance in humans
    • COI: 1:CAS:528:DC%2BC3MXnsFWlur8%3D, PID: 21421994
    • Goetze AM, Liu YD, Zhang Z, Shah B, Lee E, Bondarenko PV, et al. High-mannose glycans on the Fc region of therapeutic IgG antibodies increase serum clearance in humans. Glycobiology. 2011;21(7):949–59.
    • (2011) Glycobiology , vol.21 , Issue.7 , pp. 949-959
    • Goetze, A.M.1    Liu, Y.D.2    Zhang, Z.3    Shah, B.4    Lee, E.5    Bondarenko, P.V.6
  • 3
    • 0344947889 scopus 로고    scopus 로고
    • Mannose receptor and its putative ligands in normal murine lymphoid and nonlymphoid organs: In situ expression of mannose receptor by selected macrophages, endothelial cells, perivascular microglia, and mesangial cells, but not dendritic cells
    • COI: 1:CAS:528:DyaK1MXktVentLk%3D, PID: 10377192
    • Linehan SA, Martinez-Pomares L, Stahl PD, Gordon S. Mannose receptor and its putative ligands in normal murine lymphoid and nonlymphoid organs: In situ expression of mannose receptor by selected macrophages, endothelial cells, perivascular microglia, and mesangial cells, but not dendritic cells. J Exp Med. 1999;189(12):1961–72.
    • (1999) J Exp Med , vol.189 , Issue.12 , pp. 1961-1972
    • Linehan, S.A.1    Martinez-Pomares, L.2    Stahl, P.D.3    Gordon, S.4
  • 4
    • 0026508876 scopus 로고
    • Contribution to ligand binding by multiple carbohydrate-recognition domains in the macrophage mannose receptor
    • COI: 1:CAS:528:DyaK38Xot1Shug%3D%3D, PID: 1730714
    • Taylor ME, Bezouska K, Drickamer K. Contribution to ligand binding by multiple carbohydrate-recognition domains in the macrophage mannose receptor. J Biol Chem. 1992;267(3):1719–26.
    • (1992) J Biol Chem , vol.267 , Issue.3 , pp. 1719-1726
    • Taylor, M.E.1    Bezouska, K.2    Drickamer, K.3
  • 5
    • 43049176187 scopus 로고    scopus 로고
    • Extended and bent conformations of the mannose receptor family
    • COI: 1:CAS:528:DC%2BD1cXltFyhu7k%3D, PID: 18193159
    • Llorca O. Extended and bent conformations of the mannose receptor family. Cell Mol Life Sci: CMLS. 2008;65(9):1302–10.
    • (2008) Cell Mol Life Sci : CMLS , vol.65 , Issue.9 , pp. 1302-1310
    • Llorca, O.1
  • 7
    • 0026482265 scopus 로고
    • Advanced Glycosylation: Chemistry, Biology, and Implications for Diabetes and Aging
    • Bucola R, Cerami A. Advanced Glycosylation: Chemistry, Biology, and Implications for Diabetes and Aging. Adv Pharmacol. 1992;23:1–33.
    • (1992) Adv Pharmacol , vol.23 , pp. 1-33
    • Bucola, R.1    Cerami, A.2
  • 8
    • 84862907501 scopus 로고    scopus 로고
    • Rates and impact of human antibody glycation in vivo
    • COI: 1:CAS:528:DC%2BC38Xoslaksw%3D%3D, PID: 21930650
    • Goetze AM, Liu YD, Arroll T, Chu L, Flynn GC. Rates and impact of human antibody glycation in vivo. Glycobiology. 2012;22(2):221–34.
    • (2012) Glycobiology , vol.22 , Issue.2 , pp. 221-234
    • Goetze, A.M.1    Liu, Y.D.2    Arroll, T.3    Chu, L.4    Flynn, G.C.5
  • 9
    • 0017169872 scopus 로고
    • Correlation of glucose regulation and hemoglobin AIc in diabetes mellitus
    • COI: 1:STN:280:DyaE283itVehtw%3D%3D, PID: 934240
    • Koenig RJ, Peterson CM, Jones RL, Saudek C, Lehrman M, Cerami A. Correlation of glucose regulation and hemoglobin AIc in diabetes mellitus. N Engl J Med. 1976;295(8):417–20.
    • (1976) N Engl J Med , vol.295 , Issue.8 , pp. 417-420
    • Koenig, R.J.1    Peterson, C.M.2    Jones, R.L.3    Saudek, C.4    Lehrman, M.5    Cerami, A.6
  • 10
    • 0023484114 scopus 로고
    • Non-enzymic glycation of individual plasma proteins in normoglycemic and hyperglycemic patients
    • COI: 1:CAS:528:DyaL1cXltlOgtQ%3D%3D, PID: 3690840
    • Austin GE, Mullins RH, Morin LG. Non-enzymic glycation of individual plasma proteins in normoglycemic and hyperglycemic patients. Clin Chem. 1987;33(12):2220–4.
    • (1987) Clin Chem , vol.33 , Issue.12 , pp. 2220-2224
    • Austin, G.E.1    Mullins, R.H.2    Morin, L.G.3
  • 11
    • 79955577669 scopus 로고    scopus 로고
    • Characterization of site-specific glycation during process development of a human therapeutic monoclonal antibody
    • COI: 1:CAS:528:DC%2BC3MXlslCgtrw%3D, PID: 21287557
    • Miller AK, Hambly DM, Kerwin BA, Treuheit MJ, Gadgil HS. Characterization of site-specific glycation during process development of a human therapeutic monoclonal antibody. J Pharm Sci. 2011;100(7):2543–50.
    • (2011) J Pharm Sci , vol.100 , Issue.7 , pp. 2543-2550
    • Miller, A.K.1    Hambly, D.M.2    Kerwin, B.A.3    Treuheit, M.J.4    Gadgil, H.S.5
  • 12
    • 41849111333 scopus 로고    scopus 로고
    • Unveiling a glycation hot spot in a recombinant humanized monoclonal antibody
    • COI: 1:CAS:528:DC%2BD1cXisFGgtbs%3D, PID: 18307322
    • Zhang B, Yang Y, Yuk I, Pai R, McKay P, Eigenbrot C, et al. Unveiling a glycation hot spot in a recombinant humanized monoclonal antibody. Anal Chem. 2008;80(7):2379–90.
    • (2008) Anal Chem , vol.80 , Issue.7 , pp. 2379-2390
    • Zhang, B.1    Yang, Y.2    Yuk, I.3    Pai, R.4    McKay, P.5    Eigenbrot, C.6
  • 13
    • 0027332915 scopus 로고
    • Glycation increases the vascular clearance rate of IgG in mice
    • COI: 1:CAS:528:DyaK2cXlt1aluw%3D%3D, PID: 8252805
    • Kennedy DM, Skillen AW, Self CH. Glycation increases the vascular clearance rate of IgG in mice. Clin Exp Immunol. 1993;94(3):447–51.
    • (1993) Clin Exp Immunol , vol.94 , Issue.3 , pp. 447-451
    • Kennedy, D.M.1    Skillen, A.W.2    Self, C.H.3
  • 14
    • 33847611596 scopus 로고    scopus 로고
    • Downstream processing of monoclonal antibodies—Application of platform approaches
    • COI: 1:CAS:528:DC%2BD2sXislWmu7Y%3D, PID: 17046339
    • Shukla AA, Hubbard B, Tressel T, Guhan S, Low D. Downstream processing of monoclonal antibodies—Application of platform approaches. J Chromatogr B Analyt Technol Biomed Life Sci. 2007;848(1):28–39.
    • (2007) J Chromatogr B Analyt Technol Biomed Life Sci , vol.848 , Issue.1 , pp. 28-39
    • Shukla, A.A.1    Hubbard, B.2    Tressel, T.3    Guhan, S.4    Low, D.5
  • 15
    • 0017201417 scopus 로고
    • 2-Imino-2-methoxyethyl 1-thioglycosides: New reagents for attaching sugars to proteins
    • COI: 1:CAS:528:DyaE28XlvVylu7Y%3D, PID: 963012
    • Lee YC, Stowell CP, Krantz MJ. 2-Imino-2-methoxyethyl 1-thioglycosides: New reagents for attaching sugars to proteins. Biochemistry. 1976;15(18):3956–63.
    • (1976) Biochemistry , vol.15 , Issue.18 , pp. 3956-3963
    • Lee, Y.C.1    Stowell, C.P.2    Krantz, M.J.3
  • 16
    • 84863879204 scopus 로고    scopus 로고
    • National Research Council (U.S.). Committee for the Update of the Guide for the Care and Use of Laboratory Animals, , National Academies Press (U.S.). Guide for the care and use of laboratory animals. 8th ed. Washington, D.C.: National Academies Press; xxv, 220 p. p
    • National Research Council (U.S.). Committee for the Update of the Guide for the Care and Use of Laboratory Animals, Institute for Laboratory Animal Research (U.S.), National Academies Press (U.S.). Guide for the care and use of laboratory animals. 8th ed. Washington, D.C.: National Academies Press; 2011. xxv, 220 p. p.
    • (2011) Institute for Laboratory Animal Research (U.S.)
  • 17
    • 79960209111 scopus 로고    scopus 로고
    • Pichia pastoris-produced mucin-type fusion proteins with multivalent O-glycan substitution as targeting molecules for mannose-specific receptors of the immune system
    • COI: 1:CAS:528:DC%2BC3MXoslOrt7c%3D, PID: 21474492
    • Gustafsson A, Sjoblom M, Strindelius L, Johansson T, Fleckenstein T, Chatzissavidou N, et al. Pichia pastoris-produced mucin-type fusion proteins with multivalent O-glycan substitution as targeting molecules for mannose-specific receptors of the immune system. Glycobiology. 2011;21(8):1071–86.
    • (2011) Glycobiology , vol.21 , Issue.8 , pp. 1071-1086
    • Gustafsson, A.1    Sjoblom, M.2    Strindelius, L.3    Johansson, T.4    Fleckenstein, T.5    Chatzissavidou, N.6
  • 18
    • 70349131525 scopus 로고    scopus 로고
    • Gas-phase oligosaccharide nonreducing end (GONE) sequencing and structural analysis by reversed phase HPLC/mass spectrometry with polarity switching
    • COI: 1:CAS:528:DC%2BD1MXhtFGkur%2FN, PID: 19631557
    • Chen X, Flynn GC. Gas-phase oligosaccharide nonreducing end (GONE) sequencing and structural analysis by reversed phase HPLC/mass spectrometry with polarity switching. J Am Soc Mass Spectrom. 2009;20(10):1821–33.
    • (2009) J Am Soc Mass Spectrom , vol.20 , Issue.10 , pp. 1821-1833
    • Chen, X.1    Flynn, G.C.2
  • 19
    • 0021100426 scopus 로고
    • 13C NMR investigation of nonenzymatic glucosylation of protein. Model studies using RNase A
    • COI: 1:CAS:528:DyaL2cXitlKq, PID: 6643480
    • Neglia CI, Cohen HJ, Garber AR, Ellis PD, Thorpe SR, Baynes JW. 13C NMR investigation of nonenzymatic glucosylation of protein. Model studies using RNase A. J Biol Chem. 1983;258(23):14279–83.
    • (1983) J Biol Chem , vol.258 , Issue.23 , pp. 14279-14283
    • Neglia, C.I.1    Cohen, H.J.2    Garber, A.R.3    Ellis, P.D.4    Thorpe, S.R.5    Baynes, J.W.6
  • 20
    • 0037495999 scopus 로고    scopus 로고
    • The structure of the sugar residue in glycated human serum albumin and its molecular recognition by phenylboronate
    • COI: 1:CAS:528:DC%2BD3sXksFemuro%3D, PID: 12772293
    • Rohovec J, Maschmeyer T, Aime S, Peters JA. The structure of the sugar residue in glycated human serum albumin and its molecular recognition by phenylboronate. Chemistry. 2003;9(10):2193–9.
    • (2003) Chemistry , vol.9 , Issue.10 , pp. 2193-2199
    • Rohovec, J.1    Maschmeyer, T.2    Aime, S.3    Peters, J.A.4
  • 21
    • 0034647695 scopus 로고    scopus 로고
    • Structure of a C-type carbohydrate recognition domain from the macrophage mannose receptor
    • COI: 1:CAS:528:DC%2BD3cXkvFGisLY%3D, PID: 10779515
    • Feinberg H, Park-Snyder S, Kolatkar AR, Heise CT, Taylor ME, Weis WI. Structure of a C-type carbohydrate recognition domain from the macrophage mannose receptor. J Biol Chem. 2000;275(28):21539–48.
    • (2000) J Biol Chem , vol.275 , Issue.28 , pp. 21539-21548
    • Feinberg, H.1    Park-Snyder, S.2    Kolatkar, A.R.3    Heise, C.T.4    Taylor, M.E.5    Weis, W.I.6
  • 22
    • 0037136405 scopus 로고    scopus 로고
    • The mannose receptor family
    • COI: 1:CAS:528:DC%2BD38XmvVagsbc%3D, PID: 12223280
    • East L, Isacke CM. The mannose receptor family. Biochim Biophys Acta. 2002;1572(2–3):364–86.
    • (2002) Biochim Biophys Acta , vol.1572 , Issue.2-3 , pp. 364-386
    • East, L.1    Isacke, C.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.