Combating trastuzumab resistance by targeting SRC, a common node downstream of multiple resistance pathways (original) (raw)

• Slamon, D.J. et al. Use of chemotherapy plus a monoclonal antibody against HER2 for metastatic breast cancer that overexpresses HER2. N. Engl. J. Med. 344, 783–792 (2001).
  Article CAS Google Scholar
• Romond, E.H. et al. Trastuzumab plus adjuvant chemotherapy for operable HER2-positive breast cancer. N. Engl. J. Med. 353, 1673–1684 (2005).
  Article CAS Google Scholar
• Vogel, C.L. et al. Efficacy and safety of trastuzumab as a single agent in first-line treatment of HER2-overexpressing metastatic breast cancer. J. Clin. Oncol. 20, 719–726 (2002).
  Article CAS Google Scholar
• Seidman, A.D. et al. Randomized phase III trial of weekly compared with every-3-weeks paclitaxel for metastatic breast cancer, with trastuzumab for all HER-2 overexpressors and random assignment to trastuzumab or not in HER-2 nonoverexpressors: final results of Cancer and Leukemia Group B protocol 9840. J. Clin. Oncol. 26, 1642–1649 (2008).
  Article CAS Google Scholar
• Lan, K.H., Lu, C.H. & Yu, D. Mechanisms of trastuzumab resistance and their clinical implications. Ann. NY Acad. Sci. 1059, 70–75 (2005).
  Article CAS Google Scholar
• Piccart, M. Circumventing de novo and acquired resistance to trastuzumab: new hope for the care of ErbB2-positive breast cancer. Clin. Breast Cancer 8 (Suppl 3), S100–S113 (2008).
  Article CAS Google Scholar
• Nagata, Y. et al. PTEN activation contributes to tumor inhibition by trastuzumab, and loss of PTEN predicts trastuzumab resistance in patients. Cancer Cell 6, 117–127 (2004).
  Article CAS Google Scholar
• Berns, K. et al. A functional genetic approach identifies the PI3K pathway as a major determinant of trastuzumab resistance in breast cancer. Cancer Cell 12, 395–402 (2007).
  Article CAS Google Scholar
• Scaltriti, M. et al. Expression of p95HER2, a truncated form of the HER2 receptor, and response to anti-HER2 therapies in breast cancer. J. Natl. Cancer Inst. 99, 628–638 (2007).
  Article CAS Google Scholar
• Moulder, S.L. et al. Epidermal growth factor receptor (HER1) tyrosine kinase inhibitor ZD1839 (Iressa) inhibits HER2/neu (erbB2)-overexpressing breast cancer cells in vitro and in vivo. Cancer Res. 61, 8887–8895 (2001).
  CAS PubMed Google Scholar
• Dua, R. et al. EGFR over-expression and activation in high HER2, ER negative breast cancer cell line induces trastuzumab resistance. Breast Cancer Res. Treat. 122, 685–697 (2009).
  Article Google Scholar
• Ritter, C.A. et al. Human breast cancer cells selected for resistance to trastuzumab in vivo overexpress epidermal growth factor receptor and ErbB ligands and remain dependent on the ErbB receptor network. Clin. Cancer Res. 13, 4909–4919 (2007).
  Article CAS Google Scholar
• Lu, Y., Zi, X., Zhao, Y., Mascarenhas, D. & Pollak, M. Insulin-like growth factor-I receptor signaling and resistance to trastuzumab (Herceptin). J. Natl. Cancer Inst. 93, 1852–1857 (2001).
  Article CAS Google Scholar
• Nahta, R., Yuan, L.X., Zhang, B., Kobayashi, R. & Esteva, F.J. Insulin-like growth factor-I receptor/human epidermal growth factor receptor 2 heterodimerization contributes to trastuzumab resistance of breast cancer cells. Cancer Res. 65, 11118–11128 (2005).
  Article CAS Google Scholar
• Shattuck, D.L., Miller, J.K., Carraway, K.L. III & Sweeney, C. Met receptor contributes to trastuzumab resistance of Her2-overexpressing breast cancer cells. Cancer Res. 68, 1471–1477 (2008).
  Article CAS Google Scholar
• Huang, X. et al. Heterotrimerization of the growth factor receptors erbB2, erbB3, and insulin-like growth factor-I receptor in breast cancer cells resistant to herceptin. Cancer Res. 70, 1204–1214 (2010).
  Article CAS Google Scholar
• Narayan, M. et al. Trastuzumab-induced HER reprogramming in “resistant” breast carcinoma cells. Cancer Res. 69, 2191–2194 (2009).
  Article CAS Google Scholar
• Zhang, S. & Yu, D. PI(3)king apart PTEN′s role in cancer. Clin. Cancer Res. 16, 4325–4330 (2010).
  Article CAS Google Scholar
• Liaw, D. et al. Germline mutations of the PTEN gene in Cowden disease, an inherited breast and thyroid cancer syndrome. Nat. Genet. 16, 64–67 (1997).
  Article CAS Google Scholar
• Kmiecik, T.E. & Shalloway, D. Activation and suppression of pp60c-src transforming ability by mutation of its primary sites of tyrosine phosphorylation. Cell 49, 65–73 (1987).
  Article CAS Google Scholar
• Tice, D.A., Biscardi, J.S., Nickles, A.L. & Parsons, S.J. Mechanism of biological synergy between cellular Src and epidermal growth factor receptor. Proc. Natl. Acad. Sci. USA 96, 1415–1420 (1999).
  Article CAS Google Scholar
• Ishizawar, R. & Parsons, S.J. c-Src and cooperating partners in human cancer. Cancer Cell 6, 209–214 (2004).
  Article CAS Google Scholar
• Baselga, J. & Swain, S.M. Novel anticancer targets: revisiting ERBB2 and discovering ERBB3. Nat. Rev. Cancer 9, 463–475 (2009).
  Article CAS Google Scholar
• Junttila, T.T. et al. Ligand-independent HER2/HER3/PI3K complex is disrupted by trastuzumab and is effectively inhibited by the PI3K inhibitor GDC-0941. Cancer Cell 15, 429–440 (2009).
  Article CAS Google Scholar
• Tabernero, J. et al. Phase I study of AZD0530, an oral potent inhibitor of Src kinase: First demonstration of inhibition of Src activity in human cancers. in ASCO Meeting Vol. 25, 3520 (2007).
  Google Scholar
• Reagan-Shaw, S., Nihal, M. & Ahmad, N. Dose translation from animal to human studies revisited. FASEB J. 22, 659–661 (2008).
  Article CAS Google Scholar
• Stommel, J.M. et al. Coactivation of receptor tyrosine kinases affects the response of tumor cells to targeted therapies. Science 318, 287–290 (2007).
  Article CAS Google Scholar
• Tol, J. et al. Chemotherapy, bevacizumab, and cetuximab in metastatic colorectal cancer. N. Engl. J. Med. 360, 563–572 (2009).
  Article CAS Google Scholar
• Bromann, P.A., Korkaya, H. & Courtneidge, S.A. The interplay between Src family kinases and receptor tyrosine kinases. Oncogene 23, 7957–7968 (2004).
  Article CAS Google Scholar
• Parsons, J.T. & Parsons, S.J. Src family protein tyrosine kinases: cooperating with growth factor and adhesion signaling pathways. Curr. Opin. Cell Biol. 9, 187–192 (1997).
  Article CAS Google Scholar
• Biscardi, J.S. et al. c-Src-mediated phosphorylation of the epidermal growth factor receptor on Tyr845 and Tyr1101 is associated with modulation of receptor function. J. Biol. Chem. 274, 8335–8343 (1999).
  Article CAS Google Scholar
• Karni, R., Jove, R. & Levitzki, A. Inhibition of pp60c-Src reduces Bcl-XL expression and reverses the transformed phenotype of cells overexpressing EGF and HER-2 receptors. Oncogene 18, 4654–4662 (1999).
  Article CAS Google Scholar
• Belsches-Jablonski, A.P. et al. Src family kinases and HER2 interactions in human breast cancer cell growth and survival. Oncogene 20, 1465–1475 (2001).
  Article CAS Google Scholar
• Ishizawar, R.C., Miyake, T. & Parsons, S.J. c-Src modulates ErbB2 and ErbB3 heterocomplex formation and function. Oncogene 26, 3503–3510 (2007).
  Article CAS Google Scholar
• Nautiyal, J. et al. ErbB-inhibitory protein: a modified ectodomain of epidermal growth factor receptor synergizes with dasatinib to inhibit growth of breast cancer cells. Mol. Cancer Ther. 9, 1503–1514 (2010).
  Article CAS Google Scholar
• Wang, S.E. et al. Transforming growth factor beta induces clustering of HER2 and integrins by activating Src-focal adhesion kinase and receptor association to the cytoskeleton. Cancer Res. 69, 475–482 (2009).
  Article CAS Google Scholar
• Seoane, S., Montero, J.C., Ocana, A. & Pandiella, A. Effect of multikinase inhibitors on caspase-independent cell death and DNA damage in HER2-overexpressing breast cancer cells. J. Natl. Cancer Inst. 102, 1432–1446 (2010).
  Article CAS Google Scholar
• Lu, C.H. et al. Preclinical testing of clinically applicable strategies for overcoming trastuzumab resistance caused by PTEN deficiency. Clin. Cancer Res. 13, 5883–5888 (2007).
  Article CAS Google Scholar
• LoPiccolo, J., Blumenthal, G.M., Bernstein, W.B. & Dennis, P.A. Targeting the PI3K/AKT/mTOR pathway: effective combinations and clinical considerations. Drug Resist. Updat. 11, 32–50 (2008).
  Article CAS Google Scholar
• Johnson, D. et al. Regulation of both apoptosis and cell survival by the v-Src oncoprotein. Cell Death Differ. 7, 685–696 (2000).
  Article CAS Google Scholar
• Webb, D.J. et al. FAK-Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly. Nat. Cell Biol. 6, 154–161 (2004).
  Article CAS Google Scholar
• Ren, Z. & Schaefer, T.S. ErbB-2 activates Stat3α in a Src- and JAK2-dependent manner. J. Biol. Chem. 277, 38486–38493 (2002).
  Article CAS Google Scholar
• Kennedy, S.G. et al. The PI 3-kinase/Akt signaling pathway delivers an anti-apoptotic signal. Genes Dev. 11, 701–713 (1997).
  Article CAS Google Scholar
• Olayioye, M.A., Badache, A., Daly, J.M. & Hynes, N.E. An essential role for Src kinase in ErbB receptor signaling through the MAPK pathway. Exp. Cell Res. 267, 81–87 (2001).
  Article CAS Google Scholar
• Tan, M., Li, P., Sun, M., Yin, G. & Yu, D. Upregulation and activation of PKC alpha by ErbB2 through Src promotes breast cancer cell invasion that can be blocked by combined treatment with PKCα and Src inhibitors. Oncogene 25, 3286–3295 (2006).
  Article CAS Google Scholar
• Bowman, T. et al. Stat3-mediated Myc expression is required for Src transformation and PDGF-induced mitogenesis. Proc. Natl. Acad. Sci. USA 98, 7319–7324 (2001).
  Article CAS Google Scholar
• Franke, T.F., Hornik, C.P., Segev, L., Shostak, G.A. & Sugimoto, C. PI3K/Akt and apoptosis: size matters. Oncogene 22, 8983–8998 (2003).
  Article CAS Google Scholar
• Chang, F. et al. Regulation of cell cycle progression and apoptosis by the Ras/Raf/MEK/ERK pathway. Int. J. Oncol. (Review) 22, 469–480 (2003).
  CAS Google Scholar
• Al Zaid Siddiquee, K. & Turkson, J. STAT3 as a target for inducing apoptosis in solid and hematological tumors. Cell Res. 18, 254–267 (2008).
  Article CAS Google Scholar
• Zhang, X.H. et al. Latent bone metastasis in breast cancer tied to Src-dependent survival signals. Cancer Cell 16, 67–78 (2009).
  Article CAS Google Scholar
• Boyer, B., Bourgeois, Y. & Poupon, M.F. Src kinase contributes to the metastatic spread of carcinoma cells. Oncogene 21, 2347–2356 (2002).
  Article CAS Google Scholar
• Nahta, R., Takahashi, T., Ueno, N.T., Hung, M.C. & Esteva, F.J. P27kip1 down-regulation is associated with trastuzumab resistance in breast cancer cells. Cancer Res. 64, 3981–3986 (2004).
  Article CAS Google Scholar
• Lee, G.Y., Kenny, P.A., Lee, E.H. & Bissell, M.J. Three-dimensional culture models of normal and malignant breast epithelial cells. Nat. Methods 4, 359–365 (2007).
  Article CAS Google Scholar