A monoclonal antibody targeting the dimer interface of epidermal growth factor receptor (EGFR)

Immunology Letters

Volumn 180, Issue , 2016, Pages 39-45

  Guo, Tujing ^a   Zhao, Lin ^a   Zhang, Yawen ^a   Liu, Guoqiang ^a   Yao, Yuanhang ^a   Li, Huangjin ^a  

^a GUANGDONG PHARMACEUTICAL UNIVERSITY   (China)

Author keywords

Anti cancer; Dimer interface; Dimerization; EGFR; Monoclonal antibody

Indexed keywords

ANTIDIMER 5G9; EPIDERMAL GROWTH FACTOR RECEPTOR; IMMUNOGLOBULIN G1; MONOCLONAL ANTIBODY; UNCLASSIFIED DRUG; ANTINEOPLASTIC AGENT; IMMUNOGLOBULIN G;

3T3 CELL LINE; ANIMAL CELL; ANIMAL TISSUE; APOPTOSIS; ARTICLE; BINDING AFFINITY; CANCER IMMUNIZATION; CANCER INHIBITION; CONFOCAL LASER SCANNING MICROSCOPY; CONTROLLED STUDY; DRUG RECEPTOR BINDING; DRUG TARGETING; FEMALE; FLOW CYTOMETRY; HELA CELL LINE; HUMAN; HUMAN CELL; HYBRIDOMA; LEWIS LUNG CARCINOMA CELL; MDA MB 231 CELL LINE; MOUSE; MYELOMA CELL; NONHUMAN; PRIORITY JOURNAL; ANIMAL; BAGG ALBINO MOUSE; BREAST TUMOR; CELL PROLIFERATION; DIMERIZATION; DRUG EFFECTS; LUNG TUMOR; METABOLISM; SIGNAL TRANSDUCTION; TUMOR CELL LINE;

ANIMALS; ANTIBODIES, MONOCLONAL; ANTINEOPLASTIC AGENTS; APOPTOSIS; BREAST NEOPLASMS; CELL LINE, TUMOR; CELL PROLIFERATION; DIMERIZATION; FEMALE; HELA CELLS; HUMANS; IMMUNOGLOBULIN G; LUNG NEOPLASMS; MICE; MICE, INBRED BALB C; RECEPTOR, EPIDERMAL GROWTH FACTOR; SIGNAL TRANSDUCTION;

EID: 84994552725     PISSN: 01652478     EISSN: 18790542     Source Type: Journal    
DOI: 10.1016/j.imlet.2016.10.011     Document Type: Article

References (23)

1. [1] Thompson, D.M., Gill, G.N., The EGF receptor: structure, regulation, and potential role in malignancy. Cancer Surv. 4 (1985), 767–788.
2. [2] Roskoski, R. Jr., The ErbB/HER family of protein-tyrosine kinases and cancer. Pharmacol. Res. 79 (2014), 34–74.
3. [3] Lemmon, M.A., Schlessinger, J., Cell signaling by receptor tyrosine kinases. Cell 141 (2010), 1117–1134.
4. [4] Schlessinger, J., Ligand-induced, receptor-mediated dimerization and activation of EGF receptor. Cell 110 (2002), 669–672.
5. [5] Liu, P., Cleveland 4th, T.E., Bouyain, S., Byrne, P.O., Longo, P.A., Leahy, D.J., A single ligand is sufficient to activate EGFR dimers. Proc. Natl. Acad. Sci. U. S. A. 109 (2012), 1086–1096.
6. [6] Olayioye, M.A., Neve, R.M., Lane, H.A., Hynes, N.E., The ErbB signaling network: receptor heterodimerization in development and cancer. EMBO J. 19:13 (2000), 3159–3167.
7. [7] Ocaña, A., Pandiella, A., Targeting HER receptors in cancer. Curr. Pharm. Des. 19:5 (2013), 808–817.
8. [8] Reardon, D.A., Wen, P.Y., Mellinghoff, I.K., Targeted molecular therapies against epidermal growth factor receptor: past experiences and challenges. Neuro Oncol. 16:Suppl. 8 (2014), viii7–viii13.
9. [9] Seshacharyulu, P., Ponnusamy, M.P., Haridas, D., Jain, M., Ganti, A.K., Batra, S.K., Targeting the EGFR signaling pathway in cancer therapy. Expert Opin. Ther. Targets 16 (2012), 15–31.
10. [10] Capdevila, J., Elez, E., Macarulla, T., Ramos, F.J., Ruiz-Echarri, M., Tabernero, J., Anti–epidermal growth factor receptor monoclonal antibodies in cancer treatment. Cancer Treatment Rev. 35:4 (2009), 354–363.
11. [11] Gasser, M., Waaga-Gasser, A.M., Therapeutic antibodies in cancer therapy. Adv. Exp. Med. Biol. 917 (2016), 95–120.
12. [12] Sin, T.K., Wang, F., Meng, F., Wong, S.C., Cho, W.C., Siu, P.M., Chan, L.W., Yung, B.Y., Implications of microRNAs in the treatment of gefitinib-resistant non-small cell lung cancer. Int. J. Mol. Sci., 17(2), 2016, 237.
13. [13] Chong, Curtis R., Jänne, Pasi A., The quest to overcome resistance to EGFR-targeted therapies incancer. Nat. Med. 19:11 (2013), 1389–1400.
14. [14] Hrustanovic, Gorjan, Lee, Bianca J., Bivona, Trever G., Mechanisms of resistance to EGFR targeted therapies. Cancer Biol. Ther. 14:4 (2013), 304–314.
15. [15] Olayioye, M.A., Neve, R.M., Lane, H.A., Hynes, N.E., The ErbB signaling network: receptor heterodimerization in development and cancer. EMBO J. 19:13 (2000), 3159–3167.
16. [16] Morgillo, F., Woo, J.K., Kim, E.S., Hong, W.K., Lee, H.Y., Heterodimerization of insulin-like growth factor receptor/epidermal growth factor receptor and induction of survivin expression counteract the antitumor action of erlotinib. Cancer Res. 66:20 (2006), 10100–10111.
17. [17] Zhu, Lei, Zhao, Lin, Wu, Meizhi, Chen, Zhange, Huangjin Li B-cell epitope peptide vaccination targeting dimer interface of epidermal growth factor receptor(EGFR). Immunol. Lett. 153:2013 (2013), 33–40.
18. [18] Wang, M., Shi, H., Wu, D., Han, H., Zhang, J., Xing, Z., Wang, S., Li, Q., Glutaraldehyde cross-linking of immobilized thermophilic esterase on hydrophobic macroporous resin for application in poly(ε-caprolactone) synthesis. Molecules 19:7 (2014), 9838–9849.
19. [19] Riaz, A., Zhao, X., Dai, X., Li, W., Liu, L., Wan, H., Yu, Y., Wang, L., Zhou, Q., Mouse cloning and somatic cell reprogramming using electrofused blastomeres. Cell Res. 21:5 (2011 May), 770–778.
20. [20] Gagnon, P., Toh, P., Lee, J., High productivity purification of immunoglobulin G monoclonal antibodies on starch-coated magnetic nanoparticles by steric exclusion of polyethylene glycol. J. Chromatogr. A 1324 (2014), 171–180.
21. [21] Zhang, Q., Goetze, A.M., Cui, H., Wylie, J., Tillotson, B., Hewig, A., Hall, M.P., Flynn, G.C., Characterization of the co-elution of host cell proteins with monoclonal antibodiesduring protein A purification. Biotechnol Prog. Biotechnol. Prog. 32:3 (2016), 708–717.
22. [22] Manoj, J., Agarwal, R.K., Sailo, B., Wani, M.A., Singh, M.K., Evaluation of recombinant outer membrane protein C immunoassay for the detection of Salmonella enzyme-linked indirect based antibodies in poultry. Vet. World 8:August (8) (2015), 1006–10010.
23. [23] Dogra, V., Verma, S., Singh, G., Wani, A.H., Chahota, R., Dhar, P., Verma, L., Sharma, M., Development of OMP based indirect ELISA to gauge the antibody titers in bovines against Pasteurella multocida. Iran. J. Vet. Res. 16:Fall (4) (2015), 350–356.