메뉴 건너뛰기




Volumn 289, Issue 1, 2010, Pages 81-90

Differential tumor-targeting abilities of three single-domain antibody formats

Author keywords

(Chimeric) heavy chain antibody; Epidermal growth factor receptor; Single domain antibody

Indexed keywords

CHIMERIC ANTIBODY; CONTRAST MEDIUM; COPPER 1,4,7,10 TETRAAZACYCLODODECANE 1,4,7,10 TETRAACETIC ACID SINGLE DOMAIN ANTIBODY EG2; COPPER 1,4,7,10 TETRAAZACYCLODODECANE 1,4,7,10 TETRAACETIC ACID SINGLE DOMAIN ANTIBODY EG2 IMMUNOGLOBULIN FC FRAGMENT FUSION PROTEIN CU 64; COPPER 1,4,7,10 TETRAAZACYCLODODECANE 1,4,7,10 TETRAACETIC ACID SINGLE DOMAIN ANTIBODY EG2 MUTANT SHIGA TOXIN B SUBUNIT FUSION PROTEIN; EPIDERMAL GROWTH FACTOR; HYBRID PROTEIN; IMMUNOGLOBULIN HEAVY CHAIN; PROTEIN ANTIBODY; SINGLE DOMAIN ANTIBODY EG2; SINGLE DOMAIN ANTIBODY EG2 IMMUNOGLOBULIN FC FRAGMENT FUSION PROTEIN; SINGLE DOMAIN ANTIBODY EG2 MUTANT SHIGA TOXIN B SUBUNIT FUSION PROTEIN; UNCLASSIFIED DRUG;

EID: 75949097934     PISSN: 03043835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.canlet.2009.08.003     Document Type: Article
Times cited : (99)

References (45)
  • 2
    • 0023082137 scopus 로고
    • Receptors for epidermal growth factor and other polypeptide mitogens
    • Carpenter G. Receptors for epidermal growth factor and other polypeptide mitogens. Annu. Rev. Biochem. 56 (1987) 881-914
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 881-914
    • Carpenter, G.1
  • 3
    • 0020933452 scopus 로고
    • Biological effects in vitro of monoclonal antibodies to human epidermal growth factor receptors
    • Sato J.D., Kawamoto T., Le A.D., Mendelsohn J., Polikoff J., and Sato G.H. Biological effects in vitro of monoclonal antibodies to human epidermal growth factor receptors. Mol. Biol. Med. 1 (1983) 511-529
    • (1983) Mol. Biol. Med. , vol.1 , pp. 511-529
    • Sato, J.D.1    Kawamoto, T.2    Le, A.D.3    Mendelsohn, J.4    Polikoff, J.5    Sato, G.H.6
  • 4
    • 24744450185 scopus 로고    scopus 로고
    • Penetratin improves tumor retention of single-chain antibodies: a novel step toward optimization of radioimmunotherapy of solid tumors
    • Jain M., Chauhan S.C., Singh A.P., Venkatraman G., Colcher D., and Batra S.K. Penetratin improves tumor retention of single-chain antibodies: a novel step toward optimization of radioimmunotherapy of solid tumors. Cancer Res. 65 (2005) 7840-7846
    • (2005) Cancer Res. , vol.65 , pp. 7840-7846
    • Jain, M.1    Chauhan, S.C.2    Singh, A.P.3    Venkatraman, G.4    Colcher, D.5    Batra, S.K.6
  • 5
    • 0036749988 scopus 로고    scopus 로고
    • Analysis of renal handling of radiopharmaceuticals
    • Trejtnar F., and Laznicek M. Analysis of renal handling of radiopharmaceuticals. Quart. J. Nucl. Med. 46 (2002) 181-194
    • (2002) Quart. J. Nucl. Med. , vol.46 , pp. 181-194
    • Trejtnar, F.1    Laznicek, M.2
  • 6
    • 0034671309 scopus 로고    scopus 로고
    • Genetically engineered tetravalent single-chain Fv of the pancarcinoma monoclonal antibody CC49: improved biodistribution and potential for therapeutic application
    • Goel A., Colcher D., Baranowska-Kortylewicz J., Augustine S., Booth B.J., Pavlinkova G., et al. Genetically engineered tetravalent single-chain Fv of the pancarcinoma monoclonal antibody CC49: improved biodistribution and potential for therapeutic application. Cancer Res. 60 (2000) 6964-6971
    • (2000) Cancer Res. , vol.60 , pp. 6964-6971
    • Goel, A.1    Colcher, D.2    Baranowska-Kortylewicz, J.3    Augustine, S.4    Booth, B.J.5    Pavlinkova, G.6
  • 7
    • 0029890636 scopus 로고    scopus 로고
    • Minibody: a novel engineered anti-carcinoembryonic antigen antibody fragment (single-chain Fv-CH3) which exhibits rapid, high-level targeting of xenografts
    • Hu S., Shively L., Raubitschek A., Sherman M., Williams L.E., Wong J.Y., et al. Minibody: a novel engineered anti-carcinoembryonic antigen antibody fragment (single-chain Fv-CH3) which exhibits rapid, high-level targeting of xenografts. Cancer Res. 56 (1996) 3055-3061
    • (1996) Cancer Res. , vol.56 , pp. 3055-3061
    • Hu, S.1    Shively, L.2    Raubitschek, A.3    Sherman, M.4    Williams, L.E.5    Wong, J.Y.6
  • 8
    • 0035874887 scopus 로고    scopus 로고
    • High affinity restricts the localization and tumor penetration of single-chain fv antibody molecules
    • Adams G.P., Schier R., McCall A.M., Simmons H.H., Horak E.M., Alpaugh R.K., et al. High affinity restricts the localization and tumor penetration of single-chain fv antibody molecules. Cancer Res. 61 (2001) 4750-4755
    • (2001) Cancer Res. , vol.61 , pp. 4750-4755
    • Adams, G.P.1    Schier, R.2    McCall, A.M.3    Simmons, H.H.4    Horak, E.M.5    Alpaugh, R.K.6
  • 9
    • 0035712627 scopus 로고    scopus 로고
    • Multimerization of a chimeric anti-CD20 single-chain Fv-Fc fusion protein is mediated through variable domain exchange
    • Wu A.M., Tan G.J., Sherman M.A., Clarke P., Olafsen T., Forman S.J., et al. Multimerization of a chimeric anti-CD20 single-chain Fv-Fc fusion protein is mediated through variable domain exchange. Protein Eng. 14 (2001) 1025-1033
    • (2001) Protein Eng. , vol.14 , pp. 1025-1033
    • Wu, A.M.1    Tan, G.J.2    Sherman, M.A.3    Clarke, P.4    Olafsen, T.5    Forman, S.J.6
  • 10
    • 33846708242 scopus 로고    scopus 로고
    • Radioiodinated versus radiometal-labeled anti-carcinoembryonic antigen single-chain Fv-Fc antibody fragments: optimal pharmacokinetics for therapy
    • Kenanova V., Olafsen T., Williams L.E., Ruel N.H., Longmate J., Yazaki P.J., et al. Radioiodinated versus radiometal-labeled anti-carcinoembryonic antigen single-chain Fv-Fc antibody fragments: optimal pharmacokinetics for therapy. Cancer Res. 67 (2007) 718-726
    • (2007) Cancer Res. , vol.67 , pp. 718-726
    • Kenanova, V.1    Olafsen, T.2    Williams, L.E.3    Ruel, N.H.4    Longmate, J.5    Yazaki, P.J.6
  • 12
    • 4444302074 scopus 로고    scopus 로고
    • Aggregation-resistant domain antibodies selected on phage by heat denaturation
    • Jespers L., Schon O., Famm K., and Winter G. Aggregation-resistant domain antibodies selected on phage by heat denaturation. Nat. Biotechnol. 22 (2004) 1161-1165
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1161-1165
    • Jespers, L.1    Schon, O.2    Famm, K.3    Winter, G.4
  • 14
    • 0028962371 scopus 로고
    • A new antigen receptor gene family that undergoes rearrangement and extensive somatic diversification in sharks
    • Greenberg A.S., Avila D., Hughes M., Hughes A., McKinney E.C., and Flajnik M.F. A new antigen receptor gene family that undergoes rearrangement and extensive somatic diversification in sharks. Nature 374 (1995) 168-173
    • (1995) Nature , vol.374 , pp. 168-173
    • Greenberg, A.S.1    Avila, D.2    Hughes, M.3    Hughes, A.4    McKinney, E.C.5    Flajnik, M.F.6
  • 17
    • 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., and Muyldermans S. Selection and identification of single domain antibody fragments from camel heavy-chain antibodies. FEBS Lett. 414 (1997) 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
  • 18
    • 64149084018 scopus 로고    scopus 로고
    • Pentabody-mediated antigen delivery induces antigen-specific mucosal immune response
    • Li S., Zheng W., Kuolee R., Hirama T., Henry M., Makvandi-Nejad S., et al. Pentabody-mediated antigen delivery induces antigen-specific mucosal immune response. Mol. Immunol. 46 (2009) 1718-1726
    • (2009) Mol. Immunol. , vol.46 , pp. 1718-1726
    • Li, S.1    Zheng, W.2    Kuolee, R.3    Hirama, T.4    Henry, M.5    Makvandi-Nejad, S.6
  • 19
    • 0030250670 scopus 로고    scopus 로고
    • Affinity improvement of single antibody VH domains: residues in all three hypervariable regions affect antigen binding
    • Davies J., and Riechmann L. Affinity improvement of single antibody VH domains: residues in all three hypervariable regions affect antigen binding. Immunotechnology 2 (1996) 169-179
    • (1996) Immunotechnology , vol.2 , pp. 169-179
    • Davies, J.1    Riechmann, L.2
  • 23
    • 33845718899 scopus 로고    scopus 로고
    • An enediyne-energized single-domain antibody-containing fusion protein shows potent antitumor activity
    • Miao Q.F., Liu X.Y., Shang B.Y., Ouyang Z.G., and Zhen Y.S. An enediyne-energized single-domain antibody-containing fusion protein shows potent antitumor activity. Anticancer Drugs 18 (2007) 127-137
    • (2007) Anticancer Drugs , vol.18 , pp. 127-137
    • Miao, Q.F.1    Liu, X.Y.2    Shang, B.Y.3    Ouyang, Z.G.4    Zhen, Y.S.5
  • 26
    • 44149088593 scopus 로고    scopus 로고
    • Comparison of the biodistribution and tumor targeting of Two 99mTc-labeled Anti-EGFR nanobodies in mice, using pinhole SPECT/micro-CT
    • Gainkam L.O., Huang L., Caveliers V., Keyaerts M., Hernot S., Vaneycken I., et al. Comparison of the biodistribution and tumor targeting of Two 99mTc-labeled Anti-EGFR nanobodies in mice, using pinhole SPECT/micro-CT. J. Nucl. Med. 49 (2008) 788-795
    • (2008) J. Nucl. Med. , vol.49 , pp. 788-795
    • Gainkam, L.O.1    Huang, L.2    Caveliers, V.3    Keyaerts, M.4    Hernot, S.5    Vaneycken, I.6
  • 27
    • 43249091515 scopus 로고    scopus 로고
    • SPECT imaging with (99 m)Tc-labeled EGFR-specific nanobody for in vivo monitoring of EGFR expression
    • Huang L., Gainkam L.O., Caveliers V., Vanhove C., Keyaerts M., De Baetselier P., et al. SPECT imaging with (99 m)Tc-labeled EGFR-specific nanobody for in vivo monitoring of EGFR expression. Mol. Imaging Biol. 10 (2008) 167-175
    • (2008) Mol. Imaging Biol. , vol.10 , pp. 167-175
    • Huang, L.1    Gainkam, L.O.2    Caveliers, V.3    Vanhove, C.4    Keyaerts, M.5    De Baetselier, P.6
  • 28
    • 0028145271 scopus 로고
    • The extracellular domain of the epidermal growth factor receptor, Studies on the affinity and stoichiometry of binding, receptor dimerization and a binding-domain mutant
    • Brown P.M., Debanne M.T., Grothe S., Bergsma D., Caron M., Kay C., et al. The extracellular domain of the epidermal growth factor receptor, Studies on the affinity and stoichiometry of binding, receptor dimerization and a binding-domain mutant. Eur. J. Biochem. 225 (1994) 223-233
    • (1994) Eur. J. Biochem. , vol.225 , pp. 223-233
    • Brown, P.M.1    Debanne, M.T.2    Grothe, S.3    Bergsma, D.4    Caron, M.5    Kay, C.6
  • 30
    • 0642342122 scopus 로고    scopus 로고
    • Phage display technology for identifying specific antigens on brain endothelial cells
    • Tanha J., Muruganandam A., and Stanimirovic D. Phage display technology for identifying specific antigens on brain endothelial cells. Methods Mol. Med. 89 (2003) 435-449
    • (2003) Methods Mol. Med. , vol.89 , pp. 435-449
    • Tanha, J.1    Muruganandam, A.2    Stanimirovic, D.3
  • 32
    • 4143139848 scopus 로고    scopus 로고
    • A pentavalent single-domain antibody approach to tumor antigen discovery and the development of novel proteomics reagents
    • Zhang J., Li Q., Nguyen T.D., Tremblay T.L., Stone E., To R., et al. A pentavalent single-domain antibody approach to tumor antigen discovery and the development of novel proteomics reagents. J. Mol. Biol. 341 (2004) 161-169
    • (2004) J. Mol. Biol. , vol.341 , pp. 161-169
    • Zhang, J.1    Li, Q.2    Nguyen, T.D.3    Tremblay, T.L.4    Stone, E.5    To, R.6
  • 33
    • 0037082158 scopus 로고    scopus 로고
    • High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells
    • Durocher Y., Perret S., and Kamen A. High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells. Nucleic Acids Res. 30 (2002) E9
    • (2002) Nucleic Acids Res. , vol.30
    • Durocher, Y.1    Perret, S.2    Kamen, A.3
  • 34
  • 35
    • 20344377891 scopus 로고    scopus 로고
    • Transient gene expression in HEK293 cells: peptone addition posttransfection improves recombinant protein synthesis
    • Pham P.L., Perret S., Cass B., Carpentier E., St-Laurent G., Bisson L., et al. Transient gene expression in HEK293 cells: peptone addition posttransfection improves recombinant protein synthesis. Biotechnol. Bioeng. 90 (2005) 332-344
    • (2005) Biotechnol. Bioeng. , vol.90 , pp. 332-344
    • Pham, P.L.1    Perret, S.2    Cass, B.3    Carpentier, E.4    St-Laurent, G.5    Bisson, L.6
  • 36
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill S.C., and Von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182 (1989) 319-326
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 37
    • 0037223094 scopus 로고    scopus 로고
    • HIV mucosal vaccine: nasal immunization with gp160-encapsulated hemagglutinating virus of Japan-liposome induces antigen-specific CTLs and neutralizing antibody responses
    • Sakaue G., Hiroi T., Nakagawa Y., Someya K., Iwatani K., Sawa Y., et al. HIV mucosal vaccine: nasal immunization with gp160-encapsulated hemagglutinating virus of Japan-liposome induces antigen-specific CTLs and neutralizing antibody responses. J. Immunol. 170 (2003) 495-502
    • (2003) J. Immunol. , vol.170 , pp. 495-502
    • Sakaue, G.1    Hiroi, T.2    Nakagawa, Y.3    Someya, K.4    Iwatani, K.5    Sawa, Y.6
  • 38
    • 0032539645 scopus 로고    scopus 로고
    • Structure of the shiga-like toxin I B-pentamer complexed with an analogue of its receptor Gb3
    • Ling H., Boodhoo A., Hazes B., Cummings M.D., Armstrong G.D., Brunton J.L., et al. Structure of the shiga-like toxin I B-pentamer complexed with an analogue of its receptor Gb3. Biochemistry 37 (1998) 1777-1788
    • (1998) Biochemistry , vol.37 , pp. 1777-1788
    • Ling, H.1    Boodhoo, A.2    Hazes, B.3    Cummings, M.D.4    Armstrong, G.D.5    Brunton, J.L.6
  • 39
    • 27644472628 scopus 로고    scopus 로고
    • Correlation of pharmacokinetics with the antitumor activity of Cetuximab in nude mice bearing the GEO human colon carcinoma xenograft
    • Luo F.R., Yang Z., Dong H., Camuso A., McGlinchey K., Fager K., et al. Correlation of pharmacokinetics with the antitumor activity of Cetuximab in nude mice bearing the GEO human colon carcinoma xenograft. Cancer Chemother. Pharmacol. 56 (2005) 455-464
    • (2005) Cancer Chemother. Pharmacol. , vol.56 , pp. 455-464
    • Luo, F.R.1    Yang, Z.2    Dong, H.3    Camuso, A.4    McGlinchey, K.5    Fager, K.6
  • 40
    • 0037444270 scopus 로고    scopus 로고
    • Theoretical analysis of antibody targeting of tumor spheroids: importance of dosage for penetration, and affinity for retention
    • Graff C.P., and Wittrup K.D. Theoretical analysis of antibody targeting of tumor spheroids: importance of dosage for penetration, and affinity for retention. Cancer Res. 63 (2003) 1288-1296
    • (2003) Cancer Res. , vol.63 , pp. 1288-1296
    • Graff, C.P.1    Wittrup, K.D.2
  • 41
    • 0034662638 scopus 로고    scopus 로고
    • Targeting and therapy of carcinoembryonic antigen-expressing tumors in transgenic mice with an antibody-interleukin 2 fusion protein
    • Xu X., Clarke P., Szalai G., Shively J.E., Williams L.E., Shyr Y., et al. Targeting and therapy of carcinoembryonic antigen-expressing tumors in transgenic mice with an antibody-interleukin 2 fusion protein. Cancer Res. 60 (2000) 4475-4484
    • (2000) Cancer Res. , vol.60 , pp. 4475-4484
    • Xu, X.1    Clarke, P.2    Szalai, G.3    Shively, J.E.4    Williams, L.E.5    Shyr, Y.6
  • 43
    • 0037314439 scopus 로고    scopus 로고
    • Comparison of recombinant derivatives of chimeric TNT-3 antibody for the radioimaging of solid tumors
    • Khawli L.A., Biela B., Hu P., and Epstein A.L. Comparison of recombinant derivatives of chimeric TNT-3 antibody for the radioimaging of solid tumors. Hybrid Hybridom. 22 (2003) 1-9
    • (2003) Hybrid Hybridom. , vol.22 , pp. 1-9
    • Khawli, L.A.1    Biela, B.2    Hu, P.3    Epstein, A.L.4
  • 44
    • 0020572242 scopus 로고
    • Radiolabeled fragments of monoclonal antibodies against carcinoembryonic antigen for localization of human colon carcinoma grafted into nude mice
    • Buchegger F., Haskell C.M., Schreyer M., Scazziga B.R., Randin S., Carrel S., et al. Radiolabeled fragments of monoclonal antibodies against carcinoembryonic antigen for localization of human colon carcinoma grafted into nude mice. J. Exp. Med. 158 (1983) 413-427
    • (1983) J. Exp. Med. , vol.158 , pp. 413-427
    • Buchegger, F.1    Haskell, C.M.2    Schreyer, M.3    Scazziga, B.R.4    Randin, S.5    Carrel, S.6
  • 45
    • 1642364974 scopus 로고    scopus 로고
    • Crystal structure of HEL4, a soluble, refoldable human V(H) single domain with a germ-line scaffold
    • Jespers L., Schon O., James L.C., Veprintsev D., and Winter G. Crystal structure of HEL4, a soluble, refoldable human V(H) single domain with a germ-line scaffold. J. Mol. Biol. 337 (2004) 893-903
    • (2004) J. Mol. Biol. , vol.337 , pp. 893-903
    • Jespers, L.1    Schon, O.2    James, L.C.3    Veprintsev, D.4    Winter, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.