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Volumn 43, Issue 4-5, 2010, Pages 367-372

FcRn binding properties of an abnormal truncated analbuminemic albumin variant

Author keywords

Analbuminemia; Biodistribution; Clinical albumin variants; Enzyme linked immunosorbent assay; FcRn; Half life; IgG; Surface plasmon resonance

Indexed keywords

FC RECEPTOR; GLUTATHIONE TRANSFERASE; HUMAN SERUM ALBUMIN; IMMUNOGLOBULIN G; MUTANT PROTEIN;

EID: 76749138019     PISSN: 00099120     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.clinbiochem.2009.12.001     Document Type: Article
Times cited : (32)

References (43)
  • 2
    • 0036001387 scopus 로고    scopus 로고
    • Pharmaceutical strategies utilizing recombinant human serum albumin
    • Chuang V.T., Kragh-Hansen U., and Otagiri M. Pharmaceutical strategies utilizing recombinant human serum albumin. Pharm. Res. 19 (2002) 569-607
    • (2002) Pharm. Res. , vol.19 , pp. 569-607
    • Chuang, V.T.1    Kragh-Hansen, U.2    Otagiri, M.3
  • 3
    • 0036599564 scopus 로고    scopus 로고
    • Practical aspects of the ligand-binding and enzymatic properties of human serum albumin
    • Kragh-Hansen U., Chuang V.T., and Otagiri M. Practical aspects of the ligand-binding and enzymatic properties of human serum albumin. Biol. Pharm. Bull. 25 (2002) 695-704
    • (2002) Biol. Pharm. Bull. , vol.25 , pp. 695-704
    • Kragh-Hansen, U.1    Chuang, V.T.2    Otagiri, M.3
  • 4
    • 0037415556 scopus 로고    scopus 로고
    • The major histocompatibility complex-related Fc receptor for IgG (FcRn) binds albumin and prolongs its lifespan
    • Chaudhury C., Mehnaz S., Robinson J.M., et al. The major histocompatibility complex-related Fc receptor for IgG (FcRn) binds albumin and prolongs its lifespan. J. Exp. Med. 197 (2003) 315-322
    • (2003) J. Exp. Med. , vol.197 , pp. 315-322
    • Chaudhury, C.1    Mehnaz, S.2    Robinson, J.M.3
  • 5
    • 0028051652 scopus 로고
    • Crystal structure at 2.2 A resolution of the MHC-related neonatal Fc receptor
    • Burmeister W.P., Gastinel L.N., Simister N.E., Blum M.L., and Bjorkman P.J. Crystal structure at 2.2 A resolution of the MHC-related neonatal Fc receptor. Nature 372 (1994) 336-343
    • (1994) Nature , vol.372 , pp. 336-343
    • Burmeister, W.P.1    Gastinel, L.N.2    Simister, N.E.3    Blum, M.L.4    Bjorkman, P.J.5
  • 6
    • 0034663798 scopus 로고    scopus 로고
    • Crystal structure and immunoglobulin G binding properties of the human major histocompatibility complex-related Fc receptor
    • West Jr. A.P., and Bjorkman P.J. Crystal structure and immunoglobulin G binding properties of the human major histocompatibility complex-related Fc receptor. Biochemistry 39 (2000) 9698-9708
    • (2000) Biochemistry , vol.39 , pp. 9698-9708
    • West Jr., A.P.1    Bjorkman, P.J.2
  • 8
    • 48249148222 scopus 로고    scopus 로고
    • Dependence of antibody-mediated presentation of antigen on FcRn
    • Qiao S.W., Kobayashi K., Johansen F.E., et al. Dependence of antibody-mediated presentation of antigen on FcRn. Proc. Natl. Acad. Sci. U. S. A. 105 (2008) 9337-9342
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 9337-9342
    • Qiao, S.W.1    Kobayashi, K.2    Johansen, F.E.3
  • 9
    • 34548229364 scopus 로고    scopus 로고
    • FcRn: the neonatal Fc receptor comes of age
    • Roopenian D.C., and Akilesh S. FcRn: the neonatal Fc receptor comes of age. Nat. Rev. Immunol. 7 (2007) 715-725
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 715-725
    • Roopenian, D.C.1    Akilesh, S.2
  • 10
    • 33751196811 scopus 로고    scopus 로고
    • FcRn: an IgG receptor on phagocytes with a novel role in phagocytosis
    • Vidarsson G., Stemerding A.M., Stapleton N.M., et al. FcRn: an IgG receptor on phagocytes with a novel role in phagocytosis. Blood 108 (2006) 3573-3579
    • (2006) Blood , vol.108 , pp. 3573-3579
    • Vidarsson, G.1    Stemerding, A.M.2    Stapleton, N.M.3
  • 11
    • 33751211517 scopus 로고    scopus 로고
    • The conserved histidine 166 residue of the human neonatal Fc receptor heavy chain is critical for the pH-dependent binding to albumin
    • Andersen J.T., Dee Qian J., and Sandlie I. The conserved histidine 166 residue of the human neonatal Fc receptor heavy chain is critical for the pH-dependent binding to albumin. Eur. J. Immunol. 36 (2006) 3044-3051
    • (2006) Eur. J. Immunol. , vol.36 , pp. 3044-3051
    • Andersen, J.T.1    Dee Qian, J.2    Sandlie, I.3
  • 12
    • 62449200475 scopus 로고    scopus 로고
    • Conditional deletion of the MHC class I-related receptor FcRn reveals the sites of IgG homeostasis in mice
    • Montoyo H.P., Vaccaro C., Hafner M., Ober R.J., Mueller W., and Ward E.S. Conditional deletion of the MHC class I-related receptor FcRn reveals the sites of IgG homeostasis in mice. Proc. Natl. Acad. Sci. U. S. A. 106 (2009) 2788-2793
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 2788-2793
    • Montoyo, H.P.1    Vaccaro, C.2    Hafner, M.3    Ober, R.J.4    Mueller, W.5    Ward, E.S.6
  • 13
    • 39549088649 scopus 로고    scopus 로고
    • Neonatal FcR expression in bone marrow-derived cells functions to protect serum IgG from catabolism
    • Akilesh S., Christianson G.J., Roopenian D.C., and Shaw A.S. Neonatal FcR expression in bone marrow-derived cells functions to protect serum IgG from catabolism. J. Immunol. 179 (2007) 4580-4588
    • (2007) J. Immunol. , vol.179 , pp. 4580-4588
    • Akilesh, S.1    Christianson, G.J.2    Roopenian, D.C.3    Shaw, A.S.4
  • 14
    • 0037379288 scopus 로고    scopus 로고
    • The MHC class I-like IgG receptor controls perinatal IgG transport, IgG homeostasis, and fate of IgG-Fc-coupled drugs
    • Roopenian D.C., Christianson G.J., Sproule T.J., et al. The MHC class I-like IgG receptor controls perinatal IgG transport, IgG homeostasis, and fate of IgG-Fc-coupled drugs. J. Immunol. 170 (2003) 3528-3533
    • (2003) J. Immunol. , vol.170 , pp. 3528-3533
    • Roopenian, D.C.1    Christianson, G.J.2    Sproule, T.J.3
  • 15
    • 0029891262 scopus 로고    scopus 로고
    • The protection receptor for IgG catabolism is the beta2-microglobulin-containing neonatal intestinal transport receptor
    • Junghans R.P., and Anderson C.L. The protection receptor for IgG catabolism is the beta2-microglobulin-containing neonatal intestinal transport receptor. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 5512-5516
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 5512-5516
    • Junghans, R.P.1    Anderson, C.L.2
  • 16
    • 0028980061 scopus 로고
    • Requirement for a beta 2-microglobulin-associated Fc receptor for acquisition of maternal IgG by fetal and neonatal mice
    • Israel E.J., Patel V.K., Taylor S.F., Marshak-Rothstein A., and Simister N.E. Requirement for a beta 2-microglobulin-associated Fc receptor for acquisition of maternal IgG by fetal and neonatal mice. J. Immunol. 154 (1995) 6246-6251
    • (1995) J. Immunol. , vol.154 , pp. 6246-6251
    • Israel, E.J.1    Patel, V.K.2    Taylor, S.F.3    Marshak-Rothstein, A.4    Simister, N.E.5
  • 17
    • 0025666296 scopus 로고
    • Familial hypercatabolic hypoproteinemia. A disorder of endogenous catabolism of albumin and immunoglobulin
    • Waldmann T.A., and Terry W.D. Familial hypercatabolic hypoproteinemia. A disorder of endogenous catabolism of albumin and immunoglobulin. J. Clin. Invest. 86 (1990) 2093-2098
    • (1990) J. Clin. Invest. , vol.86 , pp. 2093-2098
    • Waldmann, T.A.1    Terry, W.D.2
  • 18
    • 33645531322 scopus 로고    scopus 로고
    • Familial hypercatabolic hypoproteinemia caused by deficiency of the neonatal Fc receptor, FcRn, due to a mutant beta2-microglobulin gene
    • Wani M.A., Haynes L.D., Kim J., et al. Familial hypercatabolic hypoproteinemia caused by deficiency of the neonatal Fc receptor, FcRn, due to a mutant beta2-microglobulin gene. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 5084-5089
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 5084-5089
    • Wani, M.A.1    Haynes, L.D.2    Kim, J.3
  • 19
    • 49149111627 scopus 로고    scopus 로고
    • Mutations and polymorphisms of the gene of the major human blood protein, serum albumin
    • Minchiotti L., Galliano M., Kragh-Hansen U., and Peters Jr. T. Mutations and polymorphisms of the gene of the major human blood protein, serum albumin. Hum. Mutat. 29 (2008) 1007-1016
    • (2008) Hum. Mutat. , vol.29 , pp. 1007-1016
    • Minchiotti, L.1    Galliano, M.2    Kragh-Hansen, U.3    Peters Jr., T.4
  • 20
    • 76749094251 scopus 로고    scopus 로고
    • http://www.albumin.org.
  • 21
    • 0029783551 scopus 로고    scopus 로고
    • Mutations in a specific human serum albumin thyroxine binding site define the structural basis of familial dysalbuminemic hyperthyroxinemia
    • Petersen C.E., Ha C.E., Jameson D.M., and Bhagavan N.V. Mutations in a specific human serum albumin thyroxine binding site define the structural basis of familial dysalbuminemic hyperthyroxinemia. J. Biol. Chem. 271 (1996) 19110-19117
    • (1996) J. Biol. Chem. , vol.271 , pp. 19110-19117
    • Petersen, C.E.1    Ha, C.E.2    Jameson, D.M.3    Bhagavan, N.V.4
  • 23
    • 34547621791 scopus 로고    scopus 로고
    • Analbuminemia produced by a novel splicing mutation
    • Dolcini L., Caridi G., Dagnino M., et al. Analbuminemia produced by a novel splicing mutation. Clin. Chem. 53 (2007) 1549-1552
    • (2007) Clin. Chem. , vol.53 , pp. 1549-1552
    • Dolcini, L.1    Caridi, G.2    Dagnino, M.3
  • 24
    • 36649020460 scopus 로고    scopus 로고
    • A receptor-mediated mechanism to support clinical observation of altered albumin variants
    • Andersen J.T., and Sandlie I. A receptor-mediated mechanism to support clinical observation of altered albumin variants. Clin. Chem. 53 (2007) 2216
    • (2007) Clin. Chem. , vol.53 , pp. 2216
    • Andersen, J.T.1    Sandlie, I.2
  • 25
    • 17444398577 scopus 로고    scopus 로고
    • Prolonged and increased expression of soluble Fc receptors, IgG and a TCR-Ig fusion protein by transiently transfected adherent 293E cells
    • Berntzen G., Lunde E., Flobakk M., Andersen J.T., Lauvrak V., and Sandlie I. Prolonged and increased expression of soluble Fc receptors, IgG and a TCR-Ig fusion protein by transiently transfected adherent 293E cells. J. Immunol. Methods 298 (2005) 93-104
    • (2005) J. Immunol. Methods , vol.298 , pp. 93-104
    • Berntzen, G.1    Lunde, E.2    Flobakk, M.3    Andersen, J.T.4    Lauvrak, V.5    Sandlie, I.6
  • 26
    • 0343852701 scopus 로고    scopus 로고
    • Conformational stability of pGEX-expressed Schistosoma japonicum glutathione S-transferase: a detoxification enzyme and fusion-protein affinity tag
    • Kaplan W., Husler P., Klump H., Erhardt J., Sluis-Cremer N., and Dirr H. Conformational stability of pGEX-expressed Schistosoma japonicum glutathione S-transferase: a detoxification enzyme and fusion-protein affinity tag. Protein Sci. 6 (1997) 399-406
    • (1997) Protein Sci. , vol.6 , pp. 399-406
    • Kaplan, W.1    Husler, P.2    Klump, H.3    Erhardt, J.4    Sluis-Cremer, N.5    Dirr, H.6
  • 27
    • 0030842771 scopus 로고    scopus 로고
    • Glutathione S-transferase can be used as a C-terminal, enzymatically active dimerization module for a recombinant protease inhibitor, and functionally secreted into the periplasm of Escherichia coli
    • Tudyka T., and Skerra A. Glutathione S-transferase can be used as a C-terminal, enzymatically active dimerization module for a recombinant protease inhibitor, and functionally secreted into the periplasm of Escherichia coli. Protein Sci. 6 (1997) 2180-2187
    • (1997) Protein Sci. , vol.6 , pp. 2180-2187
    • Tudyka, T.1    Skerra, A.2
  • 28
    • 0035210960 scopus 로고    scopus 로고
    • Differences in promiscuity for antibody-FcRn interactions across species: implications for therapeutic antibodies
    • Ober R.J., Radu C.G., Ghetie V., and Ward E.S. Differences in promiscuity for antibody-FcRn interactions across species: implications for therapeutic antibodies. Int. Immunol. 13 (2001) 1551-1559
    • (2001) Int. Immunol. , vol.13 , pp. 1551-1559
    • Ober, R.J.1    Radu, C.G.2    Ghetie, V.3    Ward, E.S.4
  • 29
    • 39149118917 scopus 로고    scopus 로고
    • A strategy for bacterial production of a soluble functional human neonatal Fc receptor
    • Andersen J.T., Justesen S., Berntzen G., et al. A strategy for bacterial production of a soluble functional human neonatal Fc receptor. J. Immunol. Methods 331 (2008) 39-49
    • (2008) J. Immunol. Methods , vol.331 , pp. 39-49
    • Andersen, J.T.1    Justesen, S.2    Berntzen, G.3
  • 30
    • 48249147883 scopus 로고    scopus 로고
    • Ligand binding and antigenic properties of a human neonatal Fc receptor with mutation of two unpaired cysteine residues
    • Andersen J.T., Justesen S., Fleckenstein B., et al. Ligand binding and antigenic properties of a human neonatal Fc receptor with mutation of two unpaired cysteine residues. FEBS J. 275 (2008) 4097-4110
    • (2008) FEBS J. , vol.275 , pp. 4097-4110
    • Andersen, J.T.1    Justesen, S.2    Fleckenstein, B.3
  • 31
    • 33646108139 scopus 로고    scopus 로고
    • Oxidation of Arg-410 promotes the elimination of human serum albumin
    • Iwao Y., Anraku M., Yamasaki K., et al. Oxidation of Arg-410 promotes the elimination of human serum albumin. Biochim. Biophys. Acta 1764 (2006) 743-749
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 743-749
    • Iwao, Y.1    Anraku, M.2    Yamasaki, K.3
  • 32
    • 61649120342 scopus 로고
    • Altered chain-length and glycosylation modify the pharmacokinetics of human serum albumin
    • Iwao Y., Hiraike M., Kragh-Hansen U., et al. Altered chain-length and glycosylation modify the pharmacokinetics of human serum albumin. Biochim. Biophys. Acta 2009 (1794) 634-641
    • (1794) Biochim. Biophys. Acta , vol.2009 , pp. 634-641
    • Iwao, Y.1    Hiraike, M.2    Kragh-Hansen, U.3
  • 33
    • 36849084017 scopus 로고    scopus 로고
    • Changes of net charge and alpha-helical content affect the pharmacokinetic properties of human serum albumin
    • Iwao Y., Hiraike M., Kragh-Hansen U., et al. Changes of net charge and alpha-helical content affect the pharmacokinetic properties of human serum albumin. Biochim. Biophys. Acta 1774 (2007) 1582-1590
    • (2007) Biochim. Biophys. Acta , vol.1774 , pp. 1582-1590
    • Iwao, Y.1    Hiraike, M.2    Kragh-Hansen, U.3
  • 34
    • 0034666718 scopus 로고    scopus 로고
    • Modulation of clearance of recombinant serum albumin by either glycosylation or truncation
    • Sheffield W.P., Marques J.A., Bhakta V., and Smith I.J. Modulation of clearance of recombinant serum albumin by either glycosylation or truncation. Thromb. Res. 99 (2000) 613-621
    • (2000) Thromb. Res. , vol.99 , pp. 613-621
    • Sheffield, W.P.1    Marques, J.A.2    Bhakta, V.3    Smith, I.J.4
  • 35
    • 37549036732 scopus 로고    scopus 로고
    • Fcgamma receptors as regulators of immune responses
    • Nimmerjahn F., and Ravetch J.V. Fcgamma receptors as regulators of immune responses. Nat. Rev. Immunol. 8 (2008) 34-47
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 34-47
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 36
    • 33644872801 scopus 로고    scopus 로고
    • Albumin turnover: FcRn-mediated recycling saves as much albumin from degradation as the liver produces
    • Kim J., Bronson C.L., Hayton W.L., et al. Albumin turnover: FcRn-mediated recycling saves as much albumin from degradation as the liver produces. Am. J. Physiol. Gastrointest. Liver Physiol. 290 (2006) G352-G360
    • (2006) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.290
    • Kim, J.1    Bronson, C.L.2    Hayton, W.L.3
  • 37
    • 33846050957 scopus 로고    scopus 로고
    • Kinetics of FcRn-mediated recycling of IgG and albumin in human: pathophysiology and therapeutic implications using a simplified mechanism-based model
    • Kim J., Hayton W.L., Robinson J.M., and Anderson C.L. Kinetics of FcRn-mediated recycling of IgG and albumin in human: pathophysiology and therapeutic implications using a simplified mechanism-based model. Clin. Immunol. 122 (2007) 146-155
    • (2007) Clin. Immunol. , vol.122 , pp. 146-155
    • Kim, J.1    Hayton, W.L.2    Robinson, J.M.3    Anderson, C.L.4
  • 38
    • 64149109989 scopus 로고    scopus 로고
    • Impact of methionine oxidation on the binding of human IgG1 to FcRn and Fcgamma receptors
    • Bertolotti-Ciarlet A., Wang W., Lownes R., et al. Impact of methionine oxidation on the binding of human IgG1 to FcRn and Fcgamma receptors. Mol. Immunol. 46 (2009) 1878-1882
    • (2009) Mol. Immunol. , vol.46 , pp. 1878-1882
    • Bertolotti-Ciarlet, A.1    Wang, W.2    Lownes, R.3
  • 39
    • 59949104434 scopus 로고    scopus 로고
    • Methionine oxidation in human IgG2 Fc decreases binding affinities to protein A and FcRn
    • Pan H., Chen K., Chu L., Kinderman F., Apostol I., and Huang G. Methionine oxidation in human IgG2 Fc decreases binding affinities to protein A and FcRn. Protein Sci. 18 (2009) 424-433
    • (2009) Protein Sci. , vol.18 , pp. 424-433
    • Pan, H.1    Chen, K.2    Chu, L.3    Kinderman, F.4    Apostol, I.5    Huang, G.6
  • 41
    • 70350438004 scopus 로고    scopus 로고
    • The versatile MHC class I-related FcRn protects IgG and albumin from degradation: implications for development of new diagnostics and therapeutics
    • Andersen J.T., and Sandlie I. The versatile MHC class I-related FcRn protects IgG and albumin from degradation: implications for development of new diagnostics and therapeutics. Drug Metab. Pharmacokinet. 24 (2009) 318-332
    • (2009) Drug Metab. Pharmacokinet. , vol.24 , pp. 318-332
    • Andersen, J.T.1    Sandlie, I.2
  • 42
    • 56949084877 scopus 로고    scopus 로고
    • Albumin as a drug carrier: design of prodrugs, drug conjugates and nanoparticles
    • Kratz F. Albumin as a drug carrier: design of prodrugs, drug conjugates and nanoparticles. J. Control. Release 132 (2008) 171-183
    • (2008) J. Control. Release , vol.132 , pp. 171-183
    • Kratz, F.1


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