Atomic force microscopy study of the effect of HER 2 antibody on EGF mediated ErbB ligand-receptor interaction

Nanomedicine: Nanotechnology, Biology, and Medicine

Volumn 9, Issue 5, 2013, Pages 627-635

  Zhang, Xuejie ^a   Shi, Xiaoli ^a   Xu, Li ^a   Yuan, Jinghe ^a   Fang, Xiaohong ^a  

^a INSTITUTE OF CHEMISTRY   (China)

Author keywords

Atomic force microscopy (AFM); EGFR HER2 heterodimerization; Pertuzumab; Single molecule force spectroscopy (SMFS); Trastuzumab

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTORS; EXTRACELLULAR DOMAINS; HETERODIMERIZATION; LIGAND-RECEPTOR INTERACTIONS; MEMBRANE RECEPTORS; PERTUZUMAB; SINGLE MOLECULE FORCE SPECTROSCOPY; TRASTUZUMAB;

ATOMIC FORCE MICROSCOPY; DIMERIZATION; MOLECULES; ONCOLOGY; SPECTROSCOPY; SURFACE PLASMON RESONANCE;

MONOCLONAL ANTIBODIES;

EPIDERMAL GROWTH FACTOR; EPIDERMAL GROWTH FACTOR RECEPTOR; EPIDERMAL GROWTH FACTOR RECEPTOR 2; PERTUZUMAB; TRASTUZUMAB;

ARTICLE; ATOMIC FORCE MICROSCOPY; DIMERIZATION; HUMAN; HUMAN CELL; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; SINGLE MOLECULE FORCE SPECTROSCOPY;

ANTIBODIES, MONOCLONAL, HUMANIZED; EPIDERMAL GROWTH FACTOR; GENE EXPRESSION REGULATION, NEOPLASTIC; HEK293 CELLS; HUMANS; LIGANDS; MICROSCOPY, ATOMIC FORCE; NEOPLASMS; PROTEIN BINDING; RECEPTOR, EPIDERMAL GROWTH FACTOR; RECEPTOR, ERBB-2;

EID: 84879464278     PISSN: 15499634     EISSN: 15499642     Source Type: Journal    
DOI: 10.1016/j.nano.2012.11.005     Document Type: Article

References (46)

1. Burgess A.W., Cho H.S., Eigenbrot C., Ferguson K.M., Garrett T.P., Leahy D.J., et al. An open-and-shut case? Recent insights into the activation of EGF/ ErbB receptors. Mol Cell 2003, 12:541-552.
2. Leahy D.J. A molecular view of anti-ErbB monoclonal antibody therapy. Cancer Cell 2008, 13:291-293.
3. Yarden Y. The EGFR family and its ligands in human cancer: signalling mechanisms and therapeutic opportunities. Eur J Cancer 2001, 37(Suppl. 4):S3-S8.
4. Slamon D.J., Leyland-Jones B., Shak S., Fuchs H., Paton V., Bajamonde A., et al. Use of chemotherapy plus a monoclonal antibody against HER2 for metastatic breast cancer that overexpresses HER2. N Engl J Med 2001, 344:783-792.
5. Holbro T., Hynes N.E. ErbB receptors: directing key signaling networks throughout life. Annu Rev Pharmacol Toxicol 2004, 44:195-217.
6. Cho H.S., Mason K., Ramyar K.X., Stanley A.M., Gabelli S.B., Denney D.W., et al. Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab. Nature 2003, 421:756-760.
7. Ross J.S., Fletcher J.A. The HER-2/neu oncogene in breast cancer: prognostic factor, predictive factor, and target for therapy. Stem Cells 1998, 16:413-428.
8. Slamon D.J., Clark G.M., Wong S.G., Levin W.J., Ullrich A., McGuire W.L. Human breast cancer: correlation of relapse and survival with amplification of the HER-2/neu oncogene. Science 1987, 235:177-182.
9. Yarden Y., Sliwkowski M.X. Untangling the ErbB signalling network. Nat Rev Mol Cell Biol 2001, 2:127-137.
10. Ross J., Slodkowska E., Symmans W.F., Pusztai L., Ravdin P.M., Hortobagyi G.N. The HER-2 receptor and breast cancer: ten years of targeted anti-HER-2 therapy and personalized medicine. Oncologist 2009, 14:320-368.
11. Carter P., Presta L., Gorman C.M., Ridgway J.B.B., Henner D., Wong W.L.T., et al. Humanization of an anti-p185HER2 antibody for human cancer therapy. Proc Natl Acad Sci U S A 1992, 89:4285-4289.
12. Hortobagyi G. Overview of treatment results with trastuzumab (Herceptin) in metastatic breast cancer. Semin Oncol 2001, 28(Suppl. 18):43-47.
13. Wehrman T.S., Raab W., Casipit C., Doyonnas R., Pomerantz J., Blau H. A system for quantifying dynamic protein interactions defines a role for Herceptin in modulating ErbB2 interactions. Proc Natl Acad Sci U S A 2006, 103:19063-19068.
14. Nadege G., Christel L., Julie V., Frederic P., Caroline B.M., Evelyne C., et al. Time-resolved fluorescence resonance energy transfer (TR-FRET) to analyze the disruption of EGFR/HER2 dimers. J Biol Chem 2011, 286:11337-11345.
15. Nahtaa R., Esteva F.J. Herceptin: mechanisms of action and resistance. Cancer Lett 2006, 232:123-138.
16. Vajdos F.F., Adams C.W., Breece T.N., Presta L.G., de Vos A.M., Sidhu S.S. Comprehensive functional maps of the antigen-binding site of an anti-ErbB2 antibody obtained with shotgun scanning mutagenesis. J Mol Biol 2002, 320:415-428.
17. Franklin M.C., Carey K.D., Vajdos F.F., Leahy D.J., de Vos A.M., Sliwkowski M.X. Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex. Cancer Cell 2004, 5:317-328.
18. Shi X., Xu L., Yu J., Fang X. Study of inhibition effect of Herceptin on interaction between Heregulin and ErbB Receptors HER3/HER2 by single-molecule force spectroscopy. Exp Cell Res 2009, 315:2847-2855.
19. Florin E.L., Moy V.T., Gaub H.E. Adhesion forces between individual ligand-receptor pairs. Science 1994, 264:415-417.
20. Yu J., Wang Q., Shi X., Ma X., Yang H., Chen Y.G., et al. Single-molecule force spectroscopy study of interaction between transforming growth factor β1 and its receptor in living cells. J Phys Chem B 2007, 111:13619-13625.
21. Hinterdorfer P., Dufrêne Y.F. Detection and localization of single molecular recognition events using atomic force microscopy. Nat Methods 2006, 3:347-355.
22. Yang Y., Xu Y., Xia T., Chen F., Zhang C., Liang W., et al. A single-molecule study of the inhibition effect of naringenin on transforming growth factor-β ligand-receptor binding. Chem Commun 2011, 47:5440-5442.
23. Cross S.E., Jin Y.S., Rao J., Gimzewski J.K. Nanomechanical analysis of cells from cancer patients. Nat Nanotechnol 2007, 2:780-783.
24. Almqvist N., Bhatia R., Primbs G., Desai N., Banerjee S., Lal R. Elasticity and adhesion force mapping reveals real-time clustering of growth factor receptors and associated changes in local cellular rheological properties. Biophys J 2004, 86:1753-1762.
25. Lee S., Mandic J., Van Vliet K.J. Chemomechanical mapping of ligand-receptor binding kinetics on cells. Proc Natl Acad Sci U S A 2007, 104:9609-9614.
26. Dickson R.B., Huff K.K., Spencer E.M., Lippman M.E. Induction of epidermal growth factor-related polypeptides by 17-beta-estradiol in MCF-7 human-breast cancer-cells. Endocrinology 1986, 118:138-142.
27. Foreman S.K., Jones S.M., Shank B.B., Kurten R.C. EGF receptor downregulation depends on a trafficking motif in the distal tyrosine kinase domain. Am J Physiol Cell Physiol 2001, 282:420-433.
28. Lanteri M., Ollier L., Giordanengo V., Lefebvre J.C. Designing a HER2/neu promoter to drive α 1, 3galactosyltransferase expression for targeted anti-α Gal antibody-mediated tumor cell killing. Breast Cancer Res 2005, 7:R487-R494.
29. Yang H., Yu J., Fu G., Shi X., Xiao L., Chen Y., et al. Interaction between single molecules of Mac-1 and ICAM-1 in living cells: an atomic force microscopy study. Exp Cell Res 2007, 313:3497-3504.
30. Hinterdorfer P., Kienberger F., Raab A., Gruber H.J., Baumgartner W., Kada G., et al. Poly(ethylene glycol): an ideal spacer for molecular recognition force microscopy/spectroscopy. Single Mol 2000, 1:99-103.
31. Kienberger F., Pastushenko V.P., Kada G., Gruber H.J., Riener C., Schindler H., et al. Static and dynamical properties of single poly(ethylene glycol) molecules investigated by force spectroscopy. Single Mol 2000, 1:123-128.
32. Benoit M., Gabriel D., Gerisch G., Gaub H.E. Discrete interactions in cell adhesion measured by single-molecule force spectroscopy. Nat Cell Biol 2000, 2:313-317.
33. Baumgartner W., Hinterdorfer P., Schindler H.W. Data analysis of interaction forces measured with the atomic force microscope. Ultramicroscopy 2000, 82:85-89.
34. Baumgartner W., Hinterdorfer P., Ness W., Raab A., Vestweber D., Schindler H., et al. Cadherin interaction probed by atomic force microscopy. Proc Natl Acad Sci U S A 2000, 97:4005-4010.
35. Olayioye M.A., Neve R.M., Lane H.A., Hynes N.E. The ErbB signaling network: receptor heterodimerization in development and cancer. EMBO J 2000, 19:3159-3167.
36. Schlessinger J. Ligand-induced, receptor-mediated dimerization and activation of EGF receptor. Cell 2002, 110:669-672.
37. Bell G.I. Models for the specific adhesion of cells to cells. Science 1978, 200:618-627.
38. Merkel R., Nassoy P., Leung A., Ritchie K., Evans E. Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy. Nature 1999, 397:50-53.
39. De Paris R., Strunz T., Oroszlan K., Güntherodt H.-J., Hegner M. Force spectroscopy and dynamics of the biotin-avidin bond studied by scanning force microscopy. Single Mol 2000, 4:285-290.
40. Strunz T., Oroszlan K., Schumakovitch I., Güntherodt H.J., Hegner M. Model energy landscapes and the force-induced dissociation of ligand-receptor bonds. Biophys J 2000, 79:1206-1212.
41. Zhou M., Felder S., Rubinstein M., Hurwitz D., Ullrich A., Lax I., et al. Real-time measurements of kinetics of EGF binding to soluble EGF receptor monomers and dimers support the dimerization model for receptor activation. Biochemistry 1993, 32:8193-8198.
42. Bieri O., Wirz J., Hellrung B., Schutkowski M., Drewello M., Kiefhaber T. The speed limit for protein folding measured by triplet-triplet energy transfer. Proc Natl Acad Sci U S A 1999, 96:9597-9601.
43. Ge L., Jin G., Fang X. Investigation of interaction between bivalent aptamer and thrombin by AFM. Langmuir 2012, 28:707-713.
44. Nunes J.M., Hensen U., Ge L., Lipinsky M., Helenius J., Grubmüller H., et al. A "force buffer" protecting immunoglobulin titin. Angew Chem Int Ed Engl 2010, 49:3528-3531.
45. Agus D.B., Akita R.W., Fox W.D., Lewis G.D., Higgins B., Pisacane P.I., et al. Targeting ligand-activated ErbB2 signaling inhibits breast and prostate tumor growth. Cancer Cell 2002, 2:127-137.
46. Takai N., Jain A., Kawamata N. 2C4, a monoclonal antibody against HER2, disrupts the HER kinase signaling pathway and inhibits ovarian carcinoma cell growth. Cancer 2005, 104:2701-2708.