Downregulation of EGFR by a novel multivalent nanobody-liposome platform

Journal of Controlled Release

Volumn 145, Issue 2, 2010, Pages 165-175

  Oliveira, Sabrina ^a,b   Schiffelers, Raymond M ^a   van der Veeken, Joris ^a   van der Meel, Roy ^a   Vongpromek, Ranitha ^b   van Bergen en Henegouwen, Paul M P ^b   Storm, Gert ^a   Roovers, Rob C ^b  

^a UTRECHT UNIVERSITY   (Netherlands)

^b UTRECHT UNIVERSITY   (Netherlands)

Author keywords

Downregulation; EGFR; Liposomes; Nanobody; VHH

Indexed keywords

ANTI-EGFR; ANTIGEN-BINDING; CELL SURFACES; CETUXIMAB; DOWNREGULATION; ECTODOMAIN; EPIDERMAL GROWTH FACTOR RECEPTORS; IN-VITRO; IN-VIVO; LIGAND BINDING; NANOBODIES; RECEPTOR ACTIVATION; SINGLE CHAIN VARIABLE FRAGMENTS; TUMOR CELLS; TUMOR THERAPY;

CELL MEMBRANES; CELL PROLIFERATION; DEGRADATION; LIGANDS; MONOCLONAL ANTIBODIES; PHOSPHOLIPIDS; TUMORS;

LIPOSOMES;

ANTINEOPLASTIC AGENT; CETUXIMAB; EGA1 NANOBODY; EPIDERMAL GROWTH FACTOR RECEPTOR; LIPOSOME; MACROGOL; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ANTIGEN BINDING; ANTINEOPLASTIC ACTIVITY; ARTICLE; CANCER CELL CULTURE; CANCER INHIBITION; CELL SURFACE; CONCENTRATION RESPONSE; CONTROLLED STUDY; FEMALE; HEAD AND NECK CARCINOMA; HUMAN; HUMAN CELL; IN VITRO STUDY; IN VIVO STUDY; INTERNALIZATION; LIGAND BINDING; MOLECULAR RECOGNITION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; RECEPTOR BLOCKING; RECEPTOR DOWN REGULATION; SOLID TUMOR; SQUAMOUS CELL CARCINOMA;

ANIMALS; CARCINOMA, SQUAMOUS CELL; CELL LINE, TUMOR; CELL PROLIFERATION; DOWN-REGULATION; EPITOPES; FEMALE; FLUORESCENT ANTIBODY TECHNIQUE, DIRECT; HEAD AND NECK NEOPLASMS; HUMANS; LIGANDS; LIPOSOMES; MICE; MICE, INBRED BALB C; MICE, NUDE; PROTEIN BINDING; RECEPTOR, EPIDERMAL GROWTH FACTOR; TUMOR BURDEN; XENOGRAFT MODEL ANTITUMOR ASSAYS;

EID: 77954034976     PISSN: 01683659     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jconrel.2010.03.020     Document Type: Article

References (28)

1. Oliveira S., van Bergen en Henegouwen P.M.P., Storm G., Schiffelers R.M. Molecular biology of epidermal growth factor receptor inhibition for cancer therapy. Expert Opin. Biol. Ther. 2006, 6(6):605-617.
2. Ciardiello F., Tortora G. EGFR antagonists in cancer treatment. N. Engl. J. Med. 2008, 358(11):1160-1174.
3. Harandi A., Zaidi A.S., Stocker A.M., Laber D.A. Clinical efficacy and toxicity of anti-EGFR therapy in common cancers. J. Oncol. 2009, 567486.
4. Perez-Torres M., Guix M., Gonzalez A., Arteaga C.L. Epidermal growth factor receptor (EGFR) antibody down-regulates mutant receptors and inhibits tumors expressing EGFR mutations. J. Biol. Chem. 2006, 281(52):40183-40192.
5. Friedman L.M., Rinon A., Schechter B., Lyass L., Lavi S., Bacus S.S., Sela M., Yarden Y. Synergistic down-regulation of receptor tyrosine kinases by combinations of mAbs: implications for cancer immunotherapy. PNAS 2005, 102(6):1915-1920.
6. Torchilin V.P. Recent advances with liposomes as pharmaceutical carriers. Nat. Rev. Drug Discov. 2005, 4(2):145-160.
7. Hamers-Casterman C., Atarhouch T., Muyldermans S., Robinson G., Hamers C., Songa E.B., Bendahman N., Hamers R. Naturally occurring antibodies devoid of light chains. Nature 1993, 363(6428):446-448.
8. Muyldermans S., Atarhouch T., Saldanha J., Barbosa J.A., Hamers R. Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains. Protein Eng. 1994, 7(9):1129-1135.
9. Dolk E., van Vliet C., Perez J.M., Vriend G., Darbon H., Ferrat G., Cambillau C., Frenken L.G., Verrips T. Induced refolding of a temperature denatured llama heavy-chain antibody fragment by its antigen. Proteins 2005, 59(3):555-564.
10. De Genst E., Saerens D., Muyldermans S., Conrath K. Antibody repertoire development in camelids. Dev. Comp. Immunol. 2006, 30(1-2):187-198.
11. Roovers R.C., van Dongen G.A., van Bergen en Henegouwen P.M. Nanobodies in therapeutic applications. Curr. Opin. Mol. Ther. 2007, 9(4):327-335.
12. Roovers R.C., Laeremans T., Huang L., Taeye S.D., Verkleij A.J., Revets H., Haard H.J.D., van Bergen en Henegouwen P.M.P. Efficient inhibition of EGFR signalling and of tumour growth by antagonistic anti-EGFR nanobodies. Cancer Immunol. Immunother. 2007, 56(3):303-317.
13. Hofman E.G., Ruonala M.O., Bader A.N., van den Heuvel D., Voortman J., Roovers R.C., Verkleij A.J., Gerritsen H.C., van Bergen en Henegouwen P.M. EGF induces coalescence of different lipid rafts. J. Cell Sci. 2008, 121(15):2519-2528.
14. Gainkam L.O., Huang L., Caveliers V., Keyaerts M., Hernot S., Vaneycken I., Vanhove C., Revets H., De Baetselier P., Lahoutte T. Comparison of the biodistribution and tumor targeting of two 99mTc-labeled anti-EGFR nanobodies in mice, using pinhole SPECT/micro-CT. J. Nucl. Med. 2008, 49(5):788-795.
15. Murthy U., Basu A., Rodeck U., Herlyn M., Ross A.H., Das M. Binding of an antagonistic monoclonal antibody to an intact and fragmented EGF-receptor polypeptide. Arch. Biochem. Biophys. 1987, 252(2):549-560.
16. De Haard H.J., Bezemer S., Ledeboer A.M., Müller W.H., Boender P.J., Moineau S., Coppelmans M.C., Verkleij A.J., Frenken L.G., Verrips C.T. Llama antibodies against a lactococcal protein located at the tip of the phage tail prevent phage infection. J. Bacteriol. 2005, 187(13):4531-4541.
17. Roovers R.C., Henderikx P., Helfrich W., van der Linden E., Reurs A., de-Bruïne A.P., Arends J.W., de-Leij L., Hoogenboom H.R. High-affinity recombinant phage antibodies to the pan-carcinoma marker epithelial glycoprotein-2 for tumour targeting. Br. J. Cancer 1998, 78(11):1407-1416.
18. Schiffelers R.M., Koning G.A., ten-Hagen T.L., Fens M.H., Schraa A.J., Janssen A.P., Kok R.J., Molema G., G.S.G. Anti-tumor efficacy of tumor vasculature-targeted liposomal doxorubicin. J. Control. Release 2003, 91(1-2):115-122.
19. Rouser G., Fleisner S., Yamamoto A. Two-dimensional thin layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots. Lipids 1970, 5(5):494-496.
20. Marks J.D., Hoogenboom H.R., Bonnert T.P., McCafferty J., Griffiths A.D., Winter G. By-passing immunization. Human antibodies from V-gene libraries displayed on phage. J. Mol. Biol. 1991, 222(3):581-597.
21. Skehan P., Storeng R., Scudiero D., Monks A., McMahon J., Vistica D., Warren J.T., Bokesch H., Kenney S., Boyd M.R. New colorimetric cytotoxicity assay for anticancer-drug screening. J. Natl. Cancer Inst. 1990, 82(13):1107-1112.
22. Sorkin A., Helin K., Waters C.M., Carpenter G., Beguinot L. Multiple autophosphorylation sites of the epidermal growth factor receptor are essential for receptor kinase activity and internalization. Contrasting significance of tyrosine 992 in the native and truncated receptors. J. Biol. Chem. 1992, 267(12):8672-8678.
23. Wang Q., Villeneuve G., Wang Z. Control of epidermal growth factor receptor endocytosis by receptor dimerization, rather than receptor kinase activation. EMBO Rep. 2005, 6(10):942-948.
24. Jaramillo M.L., Leon Z., Grothe S., Paul-Roc B., Abulrob A., O'Connor-McCourt M. Effect of the anti-receptor ligand-blocking 225 monoclonal antibody on EGF receptor endocytosis and sorting. Exp. Cell Res. 2006, 312(15):2778-2790.
25. Yoshimori T., Noda T. Toward unraveling membrane biogenesis in mammalian autophagy. Curr. Opin. Cell Biol. 2008, 20(4):401-407.
26. Maeda H., Wu J., Sawa T., Matsumura Y., Hori K. Tumor vascular permeability and the EPR effect in macromolecular therapeutics: a review. J. Control. Release 2000, 65(1-2):271-284.
27. Morgillo F., Kim W.Y., Kim E.S., Ciardiello F., Hong W.K., Lee H.Y. Implication of the insulin-like growth factor-IR pathway in the resistance of non-small cell lung cancer cells to treatment with gefitinib. Clin. Cancer Res. 2007, 13(9):2795-2803.
28. van der Veeken J., Oliveira S., Schiffelers R., Storm G., van Bergen en Henegouwen P.M.P., Roovers R. Crosstalk between epidermal growth factor receptor- and insulin-like growth factor-1 receptor signaling: implications for cancer therapy. Curr. Cancer Drug Targets 2009, 9(6):748-760.