메뉴 건너뛰기




Volumn 4, Issue 3, 2015, Pages 141-156

Pre-clinical intravenous serum pharmacokinetics of albumin binding and non-half-life extended nanobodies®

Author keywords

Albumin; Half life extension; Nanobodies; Pharmacokinetics; Pre clinical

Indexed keywords

HLE1 NANOBODY; IRR1 HLE1 NANOBODY; IRR1 IRR1 NANOBODY; IRR1 NANOBODY; IRR2 HLE2 IRR2 NANOBODY; IRR3 HLE2 NANOBODY; IRR3 NANOBODY; NANOBODY; UNCLASSIFIED DRUG;

EID: 85108690991     PISSN: 20734468     EISSN: None     Source Type: Journal    
DOI: 10.3390/antib4030141     Document Type: Article
Times cited : (82)

References (47)
  • 2
    • 35348819390 scopus 로고    scopus 로고
    • Properties, production, and applications of camelid single-domain antibody fragments
    • Harmsen, M.M.; De Haard, H.J. Properties, production, and applications of camelid single-domain antibody fragments. Appl. Microbiol. Biotechnol. 2007, 77, 13-22.
    • (2007) Appl. Microbiol. Biotechnol. , vol.77 , pp. 13-22
    • Harmsen, M.M.1    De Haard, H.J.2
  • 3
    • 84878935042 scopus 로고    scopus 로고
    • Nanobodies: Natural single-domain antibodies
    • Muyldermans, S. Nanobodies: Natural single-domain antibodies. Ann. Rev. Biochem. 2013, 82, 775-797.
    • (2013) Ann. Rev. Biochem. , vol.82 , pp. 775-797
    • Muyldermans, S.1
  • 6
    • 0018189597 scopus 로고
    • The structural and molecular basis of glomerular filtration
    • Venkatachalam, M.A.; Rennke, H.G. The structural and molecular basis of glomerular filtration. Circul. Res. 1978, 43, 337-347.
    • (1978) Circul. Res. , vol.43 , pp. 337-347
    • Venkatachalam, M.A.1    Rennke, H.G.2
  • 7
    • 72949106918 scopus 로고    scopus 로고
    • Pharmacokinetics of biotech drugs: Peptides, proteins and monoclonal antibodies
    • Lin, J.H. Pharmacokinetics of biotech drugs: peptides, proteins and monoclonal antibodies. Curr. Drug Metab. 2009, 10, 661-691.
    • (2009) Curr. Drug Metab. , vol.10 , pp. 661-691
    • Lin, J.H.1
  • 8
    • 0018147284 scopus 로고
    • Glomerular filtration of proteins: Clearance of anionic, neutral, and cationic horseradish peroxidase in the rat
    • Rennke, H.G.; Patel, Y.; Venkatachalam, M.A. Glomerular filtration of proteins: Clearance of anionic, neutral, and cationic horseradish peroxidase in the rat. Kidney Int. 1978, 13, 278-288.
    • (1978) Kidney Int. , vol.13 , pp. 278-288
    • Rennke, H.G.1    Patel, Y.2    Venkatachalam, M.A.3
  • 9
    • 0021782306 scopus 로고
    • Serum albumin
    • Peters, T., Jr. Serum albumin. Adv. Protein Chem. 1985, 37, 161-245.
    • (1985) Adv. Protein Chem. , vol.37 , pp. 161-245
    • Peters, T.1
  • 10
    • 0026445848 scopus 로고
    • Intrarenal handling of proteins in rats using fractional micropuncture technique
    • Tojo, A.; Endou, H. Intrarenal handling of proteins in rats using fractional micropuncture technique. Am. J. Physiol. 1992, 263, F601-606.
    • (1992) Am. J. Physiol. , vol.263 , pp. F601-F606
    • Tojo, A.1    Endou, H.2
  • 11
    • 84866177934 scopus 로고    scopus 로고
    • Mechanisms of glomerular albumin filtration and tubular reabsorption
    • 2012, Article ID 481520
    • Tojo, A.; Kinugasa, S. Mechanisms of glomerular albumin filtration and tubular reabsorption. Int. J. Nephrol. 2012, 2012, Article ID 481520.
    • (2012) Int. J. Nephrol.
    • Tojo, A.1    Kinugasa, S.2
  • 12
    • 0033868831 scopus 로고    scopus 로고
    • Glomerular size and charge selectivity in the rat as revealed by FITC-ficoll and albumin
    • Ohlson, M.; Sorensson, J.; Haraldsson, B. Glomerular size and charge selectivity in the rat as revealed by FITC-ficoll and albumin. Am. J. Physiol. 2000, 279, F84-F91.
    • (2000) Am. J. Physiol. , vol.279 , pp. F84-F91
    • Ohlson, M.1    Sorensson, J.2    Haraldsson, B.3
  • 13
    • 0028846136 scopus 로고
    • Renal clearance of a recombinant granulocyte colony-stimulating factor, nartograstim, in rats
    • Kuwabara, T.; Ishikawa, Y.; Kobayashi, H.; Kobayashi, S.; Sugiyama, Y. Renal clearance of a recombinant granulocyte colony-stimulating factor, nartograstim, in rats. Pharm. Res. 1995, 12, 1466-1469.
    • (1995) Pharm. Res. , vol.12 , pp. 1466-1469
    • Kuwabara, T.1    Ishikawa, Y.2    Kobayashi, H.3    Kobayashi, S.4    Sugiyama, Y.5
  • 14
    • 1942434668 scopus 로고    scopus 로고
    • Polyethylene glycol modification of filgrastim results in decreased renal clearance of the protein in rats
    • Yang, B.B.; Lum, P.K.; Hayashi, M.M.; Roskos, L.K. Polyethylene glycol modification of filgrastim results in decreased renal clearance of the protein in rats. J. Pharm. Sci. 2004, 93, 1367-1373.
    • (2004) J. Pharm. Sci. , vol.93 , pp. 1367-1373
    • Yang, B.B.1    Lum, P.K.2    Hayashi, M.M.3    Roskos, L.K.4
  • 16
    • 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.; 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. Pharmacok. 2009, 24, 318-332.
    • (2009) Drug Metab. Pharmacok. , vol.24 , pp. 318-332
    • Andersen, J.T.1    Sandlie, I.2
  • 17
    • 85015350029 scopus 로고    scopus 로고
    • Unraveling the Interaction between FcRn and Albumin: Opportunities for Design of Albumin-Based Therapeutics
    • Sand, K.M.; Bern, M.; Nilsen, J.; Noordzij, H.T.; Sandlie, I.; Andersen, J.T. Unraveling the Interaction between FcRn and Albumin: Opportunities for Design of Albumin-Based Therapeutics. Front. Immunol. 2014, 5, 682.
    • (2014) Front. Immunol. , vol.5 , pp. 682
    • Sand, K.M.1    Bern, M.2    Nilsen, J.3    Noordzij, H.T.4    Sandlie, I.5    Andersen, J.T.6
  • 18
    • 0013518141 scopus 로고
    • Tracer experiments with I131 labeled human serum albumin: Distribution and degradation studies
    • Berson, S.A.; Yalow, R.S.; Schreiber, S.S.; Post, J. Tracer experiments with I131 labeled human serum albumin: distribution and degradation studies. J. Clin. Invest. 1953, 32, 746-768.
    • (1953) J. Clin. Invest. , vol.32 , pp. 746-768
    • Berson, S.A.1    Yalow, R.S.2    Schreiber, S.S.3    Post, J.4
  • 19
    • 0014770620 scopus 로고
    • Metabolic properties of IgG subclasses in man
    • Morell, A.; Terry, W.D.; Waldmann, T.A. Metabolic properties of IgG subclasses in man. J. Clin. Invest. 1970, 49, 673-680.
    • (1970) J. Clin. Invest. , vol.49 , pp. 673-680
    • Morell, A.1    Terry, W.D.2    Waldmann, T.A.3
  • 21
    • 38549161562 scopus 로고    scopus 로고
    • Fc-based cytokines: Prospects for engineering superior therapeutics
    • Jazayeri, J.A.; Carroll, G.J. Fc-based cytokines: Prospects for engineering superior therapeutics. BioDrugs 2008, 22, 11-26.
    • (2008) BioDrugs , vol.22 , pp. 11-26
    • Jazayeri, J.A.1    Carroll, G.J.2
  • 23
    • 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.; Abrahmsen, L.; Ekblad, C. Extending half-life by indirect targeting of the neonatal Fc receptor (FcRn) using a minimal albumin binding domain. J. Biol. Chem. 2011, 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    Abrahmsen, L.5    Ekblad, C.6
  • 26
    • 53349171633 scopus 로고    scopus 로고
    • Improved tumor targeting of anti-epidermal growth factor receptor Nanobodies through albumin binding: Taking advantage of modular Nanobody technology
    • Tijink, B.M.; Laeremans, T.; Budde, M.; Stigter-van Walsum, M.; Dreier, T.; de Haard, H.J.; Leemans, C.R.; van Dongen, G.A. Improved tumor targeting of anti-epidermal growth factor receptor Nanobodies through albumin binding: Taking advantage of modular Nanobody technology. Mol. Cancer Therap. 2008, 7, 2288-2297.
    • (2008) Mol. Cancer Therap. , vol.7 , pp. 2288-2297
    • Tijink, B.M.1    Laeremans, T.2    Budde, M.3    Stigter-Van Walsum, M.4    Dreier, T.5    de Haard, H.J.6    Leemans, C.R.7    van Dongen, G.A.8
  • 27
    • 0028227096 scopus 로고
    • Structure of serum albumin
    • Carter, D.C.; Ho, J.X. Structure of serum albumin. Adv. Protein Chem. 1994, 45, 153-203.
    • (1994) Adv. Protein Chem. , vol.45 , pp. 153-203
    • Carter, D.C.1    Ho, J.X.2
  • 31
    • 0027275566 scopus 로고
    • Physiological Parameters in Laboratory Animals and Humans
    • Davies, B.; Morris, T. Physiological Parameters in Laboratory Animals and Humans. Pharm. Res. 1993, 10, 1093-1096.
    • (1993) Pharm. Res. , vol.10 , pp. 1093-1096
    • Davies, B.1    Morris, T.2
  • 33
    • 1842530336 scopus 로고    scopus 로고
    • An experimental model to study the in vivo survival of von Willebrand factor. Basic aspects and application to the R1205H mutation
    • Lenting, P.J.; Westein, E.; Terraube, V.; Ribba, A.S.; Huizinga, E.G.; Meyer, D.; de Groot, P.G.; Denis, C.V. An experimental model to study the in vivo survival of von Willebrand factor. Basic aspects and application to the R1205H mutation. J. Biol. Chem. 2004, 279, 12102-12109.
    • (2004) J. Biol. Chem. , vol.279 , pp. 12102-12109
    • Lenting, P.J.1    Westein, E.2    Terraube, V.3    Ribba, A.S.4    Huizinga, E.G.5    Meyer, D.6    de Groot, P.G.7    Denis, C.V.8
  • 37
    • 33745712861 scopus 로고    scopus 로고
    • The pharmacokinetics of an albumin-binding Fab (AB.Fab) can be modulated as a function of affinity for albumin
    • Nguyen, A.; Reyes, A.E., 2nd; Zhang, M.; McDonald, P.; Wong, W.L.; Damico, L.A.; Dennis, M.S. The pharmacokinetics of an albumin-binding Fab (AB.Fab) can be modulated as a function of affinity for albumin. Protein Eng. Des. Sel. 2006, 19, 291-297.
    • (2006) Protein Eng. Des. Sel. , vol.19 , pp. 291-297
    • Nguyen, A.1    Reyes, A.E.2    Zhang, M.3    McDonald, P.4    Wong, W.L.5    Damico, L.A.6    Dennis, M.S.7
  • 38
    • 8644234910 scopus 로고    scopus 로고
    • Antibody pharmacokinetics and pharmacodynamics
    • Lobo, E.D.; Hansen, R.J.; Balthasar, J.P. Antibody pharmacokinetics and pharmacodynamics. J. Pharm. Sci. 2004, 93, 2645-2668.
    • (2004) J. Pharm. Sci. , vol.93 , pp. 2645-2668
    • Lobo, E.D.1    Hansen, R.J.2    Balthasar, J.P.3
  • 39
    • 78651400009 scopus 로고    scopus 로고
    • Projecting human pharmacokinetics of therapeutic antibodies from nonclinical data: What have we learned?
    • Deng, R.; Iyer, S.; Theil, F.P.; Mortensen, D.L.; Fielder, P.J.; Prabhu, S. Projecting human pharmacokinetics of therapeutic antibodies from nonclinical data: What have we learned? mAbs 2011, 3, 61-66.
    • (2011) mAbs , vol.3 , pp. 61-66
    • Deng, R.1    Iyer, S.2    Theil, F.P.3    Mortensen, D.L.4    Fielder, P.J.5    Prabhu, S.6
  • 40
    • 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.; Roopenian, D.C. Enhanced half-life of genetically engineered human IgG1 antibodies in a humanized FcRn mouse model: potential application in humorally mediated autoimmune disease. Int. Immunol. 2006, 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
  • 41
    • 39149100941 scopus 로고    scopus 로고
    • Preclinical pharmacokinetics, interspecies scaling, and tissue distribution of humanized monoclonal anti-IL-13 antibodies with different IL-13 neutralization mechanisms
    • Vugmeyster, Y.; Szklut, P.; Tchistiakova, L.; Abraham, W.; Kasaian, M.; Xu, X. Preclinical pharmacokinetics, interspecies scaling, and tissue distribution of humanized monoclonal anti-IL-13 antibodies with different IL-13 neutralization mechanisms. Int. Immunopharm. 2008, 8, 477-483.
    • (2008) Int. Immunopharm. , vol.8 , pp. 477-483
    • Vugmeyster, Y.1    Szklut, P.2    Tchistiakova, L.3    Abraham, W.4    Kasaian, M.5    Xu, X.6
  • 42
    • 0032962265 scopus 로고    scopus 로고
    • Preclinical pharmacokinetics, interspecies scaling, and tissue distribution of a humanized monoclonal antibody against vascular endothelial growth factor
    • Lin, Y.S.; Nguyen, C.; Mendoza, J.L.; Escandon, E.; Fei, D.; Meng, Y.G.; Modi, N.B. Preclinical pharmacokinetics, interspecies scaling, and tissue distribution of a humanized monoclonal antibody against vascular endothelial growth factor. J. Pharm. Exp. Therap. 1999, 288, 371-378.
    • (1999) J. Pharm. Exp. Therap. , vol.288 , pp. 371-378
    • Lin, Y.S.1    Nguyen, C.2    Mendoza, J.L.3    Escandon, E.4    Fei, D.5    Meng, Y.G.6    Modi, N.B.7
  • 43
    • 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.; Ward, E.S. Differences in promiscuity for antibody-FcRn interactions across species: implications for therapeutic antibodies. Int. Immunol. 2001, 13, 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
  • 44
    • 84860490555 scopus 로고    scopus 로고
    • The TITAN trial--assessing the efficacy and safety of an anti-von Willebrand factor Nanobody in patients with acquired thrombotic thrombocytopenic purpura
    • Holz, J.B. The TITAN trial--assessing the efficacy and safety of an anti-von Willebrand factor Nanobody in patients with acquired thrombotic thrombocytopenic purpura. Transf. Apheresis Sci. 2012, 46, 343-346.
    • (2012) Transf. Apheresis Sci. , vol.46 , pp. 343-346
    • Holz, J.B.1
  • 46
    • 84892429610 scopus 로고    scopus 로고
    • Twenty-four weeks of treatment with a novel anti-IL6 receptor nanobody (ALX-0061) resulted in 84% ACR20 improvement and 58% DAS28 remission in a phase I/II study in RA
    • Holz, J.B.; Sargentini-Maier, L.; De Bruyn, S.; Gachályi, B.; Udvaros, I.; Rojkovich, B.; Bruk, S.; Sramek, P.; Korkosz, M.; Krause, K.; et al. Twenty-four weeks of treatment with a novel anti-IL6 receptor nanobody (ALX-0061) resulted in 84% ACR20 improvement and 58% DAS28 remission in a phase I/II study in RA. Ann. Rheumat. Dis. 2013, 72, 64.
    • (2013) Ann. Rheumat. Dis. , vol.72 , pp. 64
    • Holz, J.B.1    Sargentini-Maier, L.2    De Bruyn, S.3    Gachályi, B.4    Udvaros, I.5    Rojkovich, B.6    Bruk, S.7    Sramek, P.8    Korkosz, M.9    Krause, K.10
  • 47
    • 0030767656 scopus 로고    scopus 로고
    • Selection and identification of single domain antibody fragments from camel heavy-chain antibodies
    • Arbabi Ghahroudi, M.; Desmyter, A.; Wyns, L.; Hamers, R.; Muyldermans, S. Selection and identification of single domain antibody fragments from camel heavy-chain antibodies. FEBS Lett. 1997, 414, 521-526.
    • (1997) FEBS Lett. , vol.414 , pp. 521-526
    • Arbabi Ghahroudi, M.1    Desmyter, A.2    Wyns, L.3    Hamers, R.4    Muyldermans, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.