메뉴 건너뛰기




Volumn 289, Issue 50, 2014, Pages 34583-34594

Interaction with both domain I and III of albumin is required for optimal pH-dependent binding to the neonatal Fc receptor (FcRn)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BODY FLUIDS; MACROPHAGES; PROTEINS;

EID: 84919372179     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.587675     Document Type: Article
Times cited : (41)

References (47)
  • 3
    • 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. (2009) 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, 318-332
    • (2009) Drug Metab. Pharmacokinet. , vol.24 , pp. 318-332
    • Andersen, J.T.1    Sandlie, I.2
  • 4
    • 84855850311 scopus 로고    scopus 로고
    • Impact of albumin on drug delivery: New applications on the horizon
    • Elsadek, B., and Kratz, F. (2012) Impact of albumin on drug delivery: new applications on the horizon. J. Control. Release 157, 4-28
    • (2012) J. Control. Release , vol.157 , pp. 4-28
    • Elsadek, B.1    Kratz, F.2
  • 5
    • 84885370061 scopus 로고    scopus 로고
    • Albumin as a versatile platform for drug half-life extension
    • Sleep, D., Cameron, J., and Evans, L. R. (2013) Albumin as a versatile platform for drug half-life extension. Biochim. Biophys. Acta 1830, 5526-5534
    • (2013) Biochim. Biophys. Acta , vol.1830 , pp. 5526-5534
    • Sleep, D.1    Cameron, J.2    Evans, L.R.3
  • 6
    • 79953131275 scopus 로고    scopus 로고
    • Extending half-life by indirect targeting of the neonatal Fc receptor (FcRn) using a minimal albumin binding domain
    • Andersen, J. T., Pehrson, R., Tolmachev, V., Daba, M. B., Abrahmsén, L., and Ekblad, C. (2011) Extending half-life by indirect targeting of the neonatal Fc receptor (FcRn) using a minimal albumin binding domain. J. Biol. Chem. 286, 5234-5241
    • (2011) J. Biol. Chem. , vol.286 , pp. 5234-5241
    • Andersen, J.T.1    Pehrson, R.2    Tolmachev, V.3    Daba, M.B.4    Abrahmsén, L.5    Ekblad, C.6
  • 7
    • 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., Hayton, W. L., Pearl, D. K., Roopenian, D. C., and Anderson, C. L. (2003) The major histocompatibility complex-related Fc receptor for IgG (FcRn) binds albumin and prolongs its lifespan. J. Exp. Med. 197, 315-322
    • (2003) J. Exp. Med. , vol.197 , pp. 315-322
    • Chaudhury, C.1    Mehnaz, S.2    Robinson, J.M.3    Hayton, W.L.4    Pearl, D.K.5    Roopenian, D.C.6    Anderson, C.L.7
  • 8
    • 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. (2009) 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, 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
  • 9
    • 69949115639 scopus 로고    scopus 로고
    • Chapter 4: Multitasking by exploitation of intracellular transport functions the many faces of FcRn
    • Ward, E. S., and Ober, R. J. (2009) Chapter 4: multitasking by exploitation of intracellular transport functions the many faces of FcRn. Adv. Immunol. 103, 77-115
    • (2009) Adv. Immunol. , vol.103 , pp. 77-115
    • Ward, E.S.1    Ober, R.J.2
  • 11
    • 0024953939 scopus 로고
    • Cloning and expression of the neonatal rat intestinal Fc receptor, a major histocompatibility complex class I antigen homolog
    • Simister, N. E., and Mostov, K. E. (1989) Cloning and expression of the neonatal rat intestinal Fc receptor, a major histocompatibility complex class I antigen homolog. Cold Spring Harbor Symp. Quant. Biol. 54, 571-580
    • (1989) Cold Spring Harbor Symp. Quant. Biol. , vol.54 , pp. 571-580
    • Simister, N.E.1    Mostov, K.E.2
  • 12
    • 0028061347 scopus 로고
    • A major histocompatibility complex class I-like Fc receptor cloned from human placenta: Possible role in transfer of immunoglobulin G from mother to fetus
    • Story, C. M., Mikulska, J. E., and Simister, N. E. (1994) A major histocompatibility complex class I-like Fc receptor cloned from human placenta: possible role in transfer of immunoglobulin G from mother to fetus. J. Exp. Med. 180, 2377-2381
    • (1994) J. Exp. Med. , vol.180 , pp. 2377-2381
    • Story, C.M.1    Mikulska, J.E.2    Simister, N.E.3
  • 13
    • 77951156788 scopus 로고    scopus 로고
    • Cross-species binding analyses of mouse and human neonatal Fc receptor show dramatic differences in immunoglobulin G and albumin binding
    • Andersen, J. T., Daba, M. B., Berntzen, G., Michaelsen, T. E., and Sandlie, I. (2010) Cross-species binding analyses of mouse and human neonatal Fc receptor show dramatic differences in immunoglobulin G and albumin binding. J. Biol. Chem. 285, 4826-4836
    • (2010) J. Biol. Chem. , vol.285 , pp. 4826-4836
    • Andersen, J.T.1    Daba, M.B.2    Berntzen, G.3    Michaelsen, T.E.4    Sandlie, I.5
  • 14
    • 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. (2006) 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, 3044-3051
    • (2006) Eur. J. Immunol. , vol.36 , pp. 3044-3051
    • Andersen, J.T.1    Dee Qian, J.2    Sandlie, I.3
  • 20
    • 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. (2007) Neonatal FcR expression in bone marrow-derived cells functions to protect serum IgG from catabolism. J. Immunol. 179, 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
  • 21
    • 70350093622 scopus 로고    scopus 로고
    • An FcRn-dependent role for anti-flagellin immunoglobulin G in pathogenesis of colitis in mice
    • Kobayashi, K., Qiao, S. W., Yoshida, M., Baker, K., Lencer, W. I., and Blumberg, R. S. (2009) An FcRn-dependent role for anti-flagellin immunoglobulin G in pathogenesis of colitis in mice. Gastroenterology 137, 1746-1756
    • (2009) Gastroenterology , vol.137 , pp. 1746-1756
    • Kobayashi, K.1    Qiao, S.W.2    Yoshida, M.3    Baker, K.4    Lencer, W.I.5    Blumberg, R.S.6
  • 26
    • 33845364560 scopus 로고    scopus 로고
    • Enhanced half-life of genetically engineered human IgG1 antibodies in a humanized FcRn mouse model: Potential application in humorally mediated autoimmune disease
    • Petkova, S. B., Akilesh, S., Sproule, T. J., Christianson, G. J., Al Khabbaz, H., Brown, A. C., Presta, L. G., Meng, Y. G., and Roopenian, D. C. (2006) Enhanced half-life of genetically engineered human IgG1 antibodies in a humanized FcRn mouse model: potential application in humorally mediated autoimmune disease. Int. Immunol. 18, 1759-1769
    • (2006) Int. Immunol. , vol.18 , pp. 1759-1769
    • Petkova, S.B.1    Akilesh, S.2    Sproule, T.J.3    Christianson, G.J.4    Al Khabbaz, H.5    Brown, A.C.6    Presta, L.G.7    Meng, Y.G.8    Roopenian, D.C.9
  • 29
    • 84882393963 scopus 로고    scopus 로고
    • Single-chain variable fragment albumin fusions bind the neonatal Fc Receptor (FcRn) in a species-dependent manner: Implications for in vivo half-life evaluation of albumin fusion therapeutics
    • Andersen, J. T., Cameron, J., Plumridge, A., Evans, L., Sleep, D., and Sandlie, I. (2013) Single-chain variable fragment albumin fusions bind the neonatal Fc Receptor (FcRn) in a species-dependent manner: implications for in vivo half-life evaluation of albumin fusion therapeutics. J. Biol. Chem. 288, 24277-24285
    • (2013) J. Biol. Chem. , vol.288 , pp. 24277-24285
    • Andersen, J.T.1    Cameron, J.2    Plumridge, A.3    Evans, L.4    Sleep, D.5    Sandlie, I.6
  • 30
    • 76749138019 scopus 로고    scopus 로고
    • FcRn binding properties of an abnormal truncated analbuminemic albumin variant
    • Andersen, J. T., Daba, M. B., and Sandlie, I. (2010) FcRn binding properties of an abnormal truncated analbuminemic albumin variant. Clin. Biochem. 43, 367-372
    • (2010) Clin. Biochem. , vol.43 , pp. 367-372
    • Andersen, J.T.1    Daba, M.B.2    Sandlie, I.3
  • 33
    • 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. (2005) 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, 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
  • 34
    • 0033393536 scopus 로고    scopus 로고
    • Mapping the site on human IgG for binding of the MHC class I-related receptor
    • Kim, J. K., Firan, M., Radu, C. G., Kim, C. H., Ghetie, V., and Ward, E. S. (1999) Mapping the site on human IgG for binding of the MHC class I-related receptor, FcRn. Eur. J. Immunol. 29, 2819-2825
    • (1999) FcRn. Eur. J. Immunol. , vol.29 , pp. 2819-2825
    • Kim, J.K.1    Firan, M.2    Radu, C.G.3    Kim, C.H.4    Ghetie, V.5    Ward, E.S.6
  • 35
    • 0026530383 scopus 로고
    • Quantitative analysis of protein far UV circular dichroism spectra by neural networks
    • Böhm, G., Muhr, R., and Jaenicke, R. (1992) Quantitative analysis of protein far UV circular dichroism spectra by neural networks. Protein Eng. 5, 191-195
    • (1992) Protein Eng. , vol.5 , pp. 191-195
    • Böhm, G.1    Muhr, R.2    Jaenicke, R.3
  • 36
    • 11844275385 scopus 로고    scopus 로고
    • Conferring the binding properties of the mouseMHCclass I-related receptor, FcRn, onto the human ortholog by sequential rounds of site-directed mutagenesis
    • Zhou, J., Mateos, F., Ober, R. J., and Ward, E. S. (2005) Conferring the binding properties of the mouseMHCclass I-related receptor, FcRn, onto the human ortholog by sequential rounds of site-directed mutagenesis. J. Mol. Biol. 345, 1071-1081
    • (2005) J. Mol. Biol. , vol.345 , pp. 1071-1081
    • Zhou, J.1    Mateos, F.2    Ober, R.J.3    Ward, E.S.4
  • 37
    • 84885376431 scopus 로고    scopus 로고
    • Human serum albumin isoforms: Genetic and molecular aspects and functional consequences
    • Kragh-Hansen, U., Minchiotti, L., Galliano, M., and Peters, T., Jr. (2013) Human serum albumin isoforms: genetic and molecular aspects and functional consequences. Biochim. Biophys. Acta 1830, 5405-5417
    • (2013) Biochim. Biophys. Acta , vol.1830 , pp. 5405-5417
    • Kragh-Hansen, U.1    Minchiotti, L.2    Galliano, M.3    Peters, T.4
  • 40
    • 0033062612 scopus 로고    scopus 로고
    • Crystal structure of human serum albumin at 2.5 A resolution
    • Sugio, S., Kashima, A., Mochizuki, S., Noda, M., and Kobayashi, K. (1999) Crystal structure of human serum albumin at 2.5 A resolution. Protein Eng. 12, 439-446
    • (1999) Protein Eng. , vol.12 , pp. 439-446
    • Sugio, S.1    Kashima, A.2    Mochizuki, S.3    Noda, M.4    Kobayashi, K.5
  • 41
    • 0037375585 scopus 로고    scopus 로고
    • Characterization of the electrophile binding site and substrate binding mode of the 26-kDa glutathione S-transferase from Schistosoma japonicum
    • Cardoso, R. M., Daniels, D. S., Bruns, C. M., and Tainer, J. A. (2003) Characterization of the electrophile binding site and substrate binding mode of the 26-kDa glutathione S-transferase from Schistosoma japonicum. Proteins 51, 137-146
    • (2003) Proteins , vol.51 , pp. 137-146
    • Cardoso, R.M.1    Daniels, D.S.2    Bruns, C.M.3    Tainer, J.A.4
  • 42
    • 0031852954 scopus 로고    scopus 로고
    • Unfolding of acrylodan-labeled human serum albumin probed by steadystate and time-resolved fluorescence methods
    • Flora, K., Brennan, J. D., Baker, G. A., Doody, M. A., and Bright, F. V. (1998) Unfolding of acrylodan-labeled human serum albumin probed by steadystate and time-resolved fluorescence methods. Biophys. J. 75, 1084-1096
    • (1998) Biophys. J. , vol.75 , pp. 1084-1096
    • Flora, K.1    Brennan, J.D.2    Baker, G.A.3    Doody, M.A.4    Bright, F.V.5
  • 43
    • 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. (2007) Kinetics of FcRn-mediated recycling of IgG and albumin in human: pathophysiology and therapeutic implications using a simplified mechanism-based model. Clin. Immunol. 122, 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
  • 45
    • 0031683467 scopus 로고    scopus 로고
    • Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites
    • Curry, S., Mandelkow, H., Brick, P., and Franks, N. (1998) Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nat. Struct. Biol. 5, 827-835
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 827-835
    • Curry, S.1    Mandelkow, H.2    Brick, P.3    Franks, N.4
  • 46
    • 0030806484 scopus 로고    scopus 로고
    • High-affinity binding of the neonatal Fc receptor to its IgG ligand requires receptor immobilization
    • Vaughn, D. E., and Bjorkman, P. J. (1997) High-affinity binding of the neonatal Fc receptor to its IgG ligand requires receptor immobilization. Biochemistry 36, 9374-9380
    • (1997) Biochemistry , vol.36 , pp. 9374-9380
    • Vaughn, D.E.1    Bjorkman, P.J.2
  • 47
    • 0034879134 scopus 로고    scopus 로고
    • The MHC class I-related receptor, FcRn, plays an essential role in the maternofetal transfer of γ-globulin in humans
    • Firan, M., Bawdon, R., Radu, C., Ober, R. J., Eaken, D., Antohe, F., Ghetie, V., and Ward, E. S. (2001) The MHC class I-related receptor, FcRn, plays an essential role in the maternofetal transfer of γ-globulin in humans. Int. Immunol. 13, 993-1002
    • (2001) Int. Immunol. , vol.13 , pp. 993-1002
    • Firan, M.1    Bawdon, R.2    Radu, C.3    Ober, R.J.4    Eaken, D.5    Antohe, F.6    Ghetie, V.7    Ward, E.S.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.