P95 HER2 fragments and breast cancer outcome

References

• Slamon DJ, Godolphin W, Jones LA, et al. Studies of the HER-2/neu protooncogene in human breast and ovarian cancer. Science 1989;244:707-12
   PubMed Web of Science ®Google Scholar
• Slamon DJ, Clark GM, Wong SG, et al. Human breast cancer: correlation of relapse and survival with amplification of the HER-2/neu oncogene. Science 1987;235:177-82
   PubMed Web of Science ®Google Scholar
• Tsé C, Gauchez AS, Jacot W, Lamy PJ. HER2 shedding and serum HER2 extracellular domain: biology and clinical utility in breast cancer. Cancer Treat Rev 2012;38:133-42
   PubMed Web of Science ®Google Scholar
• Baselga J, Tripathy D, Mendelsohn J, et al. Phase II study of weekly intravenous recombinant humanized anti-p185HER2 monoclonal antibody in patients with HER2/neu-overexpressing metastatic breast cancer. J Clin Oncol 1996;14:737-44
   PubMed Web of Science ®Google Scholar
• Cobleigh MA, Vogel CL, Tripathy D, et al. Multinational study of the efficacy and safety of humanized anti-HER2 monoclonal antibody in women who have HER-2 overexpressing metastatic breast cancer that has progresssed after chemotherapy for metastatic disease. J Clin Oncol 1999;17:2639-48
   PubMed Web of Science ®Google Scholar
• Vogel CL, Cobleigh MA, Tripathy D, et al. Efficacy and safety of trastuzumab as a single agent in first-line treatment of HER2-overexpressing metastatic breast cancer. J Clin Oncol 2002;20:719-26
   PubMed Web of Science ®Google Scholar
• Nahta R, Esteva FJ. HER2 therapy: molecular mechanisms of trastuzumab resistance. Breast Cancer Res 2006;8:215
   PubMed Web of Science ®Google Scholar
• Lin YL, Clinton GM. A soluble protein related to the HER-2 proto-oncogene product is released from human breast carcinoma cells. Oncogene 1991;6:639-43
   PubMed Web of Science ®Google Scholar
• Pupa SM, Menard S, Morelli D, et al. The extracellular domain of the c-erbB-2 oncoprotein is released from tumor cells by proteolytic cleavage. Oncogene 1993;8:2917-23
   PubMed Web of Science ®Google Scholar
• Zabrecky J R, Lam T, McKenzie SJ, Carney W. The extracellular domain of p185/neu is released from the surface of human breast carcinoma cells, SK-BR-3. J Biol Chem 1991;266:1716-20
   PubMedGoogle Scholar
• Molina MA, Sáez R, Ramsey EE, et al. NH(2)-terminal truncated HER-2 protein but not full-length receptor is associated with nodal metastasis in human breast cancer. Clin Cancer Res 2002;8:347-53
   PubMed Web of Science ®Google Scholar
• Brandt-Rauf PW. The c-erb transmembrane growth factor receptors as serum biomarkers in human cancer studies. Mutat Res 1995;333:203-8
   PubMed Web of Science ®Google Scholar
• Anido J, Scaltriti M, Bech Serra JJ, et al. Biosynthesis of tumorigenic HER2 C-terminal fragments by alternative initiation of translation. EMBOJ 2006;25:3234-44
   PubMed Web of Science ®Google Scholar
• Scaltriti M, Rojo F, Ocaña A, 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 2007;99:628-38
   PubMed Web of Science ®Google Scholar
• Scaltriti M, Chandarlapaty S, Prudkin L, et al. Clinical benefit of lapatinib-based therapy in patients with human epidermal growth factor receptor 2-positive breast tumors coexpressing the truncated p95HER2 receptor. Clin Cancer Res 2010;16:2688-95
   PubMed Web of Science ®Google Scholar
• Sanderson MP, Dempsey PJ, Dunbar AJ. Control of ErbB signaling through metalloprotease mediated ectodomain shedding of EGF-like factors. Growth Factors 2006;24:121-36
   PubMed Web of Science ®Google Scholar
• Pedersen K, Angelini PD, Laos S, et al. A naturally occurring HER2 carboxy-terminal fragment promotes mammary tumor growth and metastasis. Mol Cell Biol 2009;29:3319-31
   PubMed Web of Science ®Google Scholar
• Christianson TA, Doherty JK, Lin YJ, et al. NH2-terminally truncated HER-2/neu protein: relationship with shedding of the extracellular domain and with prognostic factors in breast cancer. Cancer Res 1998;58:5123-9
   PubMed Web of Science ®Google Scholar
• Molina MA, Codony-Servat J, Albanell J, et al. Trastuzumab (HerceptinR), a humanized anti-HER-2 receptor monoclonal antibody, inhibits basal and activated HER-2 ectodomain cleavage in breast cancer cells. Cancer Res 2001;15:4744-9
   Google Scholar
• Staverosky JA, Muldoon LL, Guo S, et al. Herstatin, an autoinhibitor of the epidermal growth factor receptor family, blocks the intracranial growth of glioblastoma. Clin Cancer Res 2005;11:335-40
   PubMed Web of Science ®Google Scholar
• Doherty JK, Bond C, Jardim A, et al. The HER-2/neu receptor tyrosine kinase gene encodes a secreted autoinhibitor. Proc Natl Acad Sci USA 1999;96:10869-74
   PubMed Web of Science ®Google Scholar
• Aigner A, Juhl H, Malerczyk C, et al. Expression of a truncated 100 kDa HER2 splice variant acts as an endogenous inhibitor of tumour cell proliferation. Oncogene 2001;20:2101-11
   PubMed Web of Science ®Google Scholar
• Penuel E, Akita RW, Sliwkowski MX. Identification of a region within the ErbB2/HER2 intracellular domain that is necessary for ligand-independent association. J Biol Chem 2002;277:28468-73
   Google Scholar
• Duffy MJ, McKiernan E, O’Donovan N, McGowan PM. Role of ADAMs in cancer formation and progression. Clin Cancer Res 2009;15:1140-4
   PubMed Web of Science ®Google Scholar
• Burns DM, He C, Li Y, et al. Conversion of an MMP-potent scaffold to an MMP-selective HER-2 sheddase inhibitor via scaffold hybridization and subtle P1’ permutations. Bioorg Med Chem Lett 2008;18:560-4
   PubMedGoogle Scholar
• Recupero D, Daniele L, Marchiò C, et al. Spontaneous and pronase-induced HER2 truncation increases the trastuzumab binding capacity of breast cancer tissues and cell lines. J Pathol 2013;229:390-9
   PubMedGoogle Scholar
• Burgess AW, Cho HS, Eigenbrot C, et al. An openand-shut case? Recent insights into the activation of EGF/ErbB receptors. Mol Cell 2003;12:541-52
   PubMed Web of Science ®Google Scholar
• Lemmon MA. Ligand-induced ErbB receptor dimerization. Exp Cell Res 2009;315:638-48
   PubMed Web of Science ®Google Scholar
• Carney WP, Neumann R, Lipton A, et al. Potential clinical utility of serum HER-2/neu oncoprotein concentrations in patients with breast cancer. Clin Chem 2003;49:1579-98
   PubMedGoogle Scholar
• Ali SM, Carney WP, Esteva FJ, et al. Serum HER-2/neu and relative resistance to trastuzumab-based therapy in patients with metastatic breast cancer. Cancer 2008;113:1294-301
   PubMed Web of Science ®Google Scholar
• Carney WP, Bernhardt D, Jasani B. Circulating HER2 extra cellular domain: a specific and quantitative biomarker of prognostic value in all breast cancer patients? Biomark Cancer 2013;5:31-9
   PubMedGoogle Scholar
• Zhang X, Gureasko J, Shen K, et al. An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. Cell 2006;125:1137-49
   PubMed Web of Science ®Google Scholar
• Xia W, Liu LH, Ho P, Spector NL. Truncated ErbB2 receptor (p95ErbB2) is regulated by heregulin through heterodimer formation with ErbB3 yet remains sensitive to the dual EGFR/ErbB2 kinase inhibitor GW572016. Oncogene 2004;23:646-53
   PubMed Web of Science ®Google Scholar
• Sáez R, Molina MA, Ramsey EE, et al. Albanell J. p95HER-2 predicts worse outcome in patients with HER-2-positive breast cancer. Clin Cancer Res 2006;12:424-31
   PubMed Web of Science ®Google Scholar
• Montemurro F, Prat A, Rossi V, et al. Potential biomarkers of long-term benefit from single-agent trastuzumab or lapatinib in HER2-positive metastatic breast cancer. Mol Oncol 2014;8:20-6
   PubMedGoogle Scholar
• Sperinde J, Jin X, Banerjee J, et al. Quantitation of p95HER2 in paraffin sections by using a p95-specific antibody and correlation with outcome in a cohort of trastuzumab-treated breast cancer patients. Clin Cancer Res 2010;16:4226-35
   PubMed Web of Science ®Google Scholar
• Duchnowska R, Sperinde J, Chenna A, et al. Quantitative measurements of tumoral p95her2 protein expression in metastatic breast cancer patients treated with trastuzumab: independent validation of the p95her2 clinical cutoff. Clin Cancer Res 2014. Epub ahead of print
   Google Scholar
• Kocar M, Bozkurtlar E, Telli F, et al. Serdar turhal N. p95-HER2 and trastuzumab resistance in metastatic breast cancer; is immunohistochemistry appropriate? J BUON 2014;19:245-9
   PubMedGoogle Scholar
• Lipton A, Goodman L, Leitzel K, et al. HER3, p95HER2, and HER2 protein expression levels define multiple subtypes of HER2-positive metastatic breast cancer. Breast Cancer Res Treat 2013;141:43-53
   PubMed Web of Science ®Google Scholar
• Han SW, Cha Y, Paquet A, et al. Correlation of HER2, p95HER2 and HER3 expression and treatment outcome of lapatinib plus capecitabine in her2-positive metastatic breast cancer. PLoS One 2012;7:e39943
   Web of Science ®Google Scholar
• Loibl S, Bruey J, Von Minckwitz G, German Breast Group. Validation of p95 as a predictive marker for trastuzumab-based therapy in primary HER2-positive breast cancer: A translational investigation from the neoadjuvant GeparQuattro study. J Clin Oncol 2011;29:suppl;abstr 530
   Google Scholar
• Modi S, D’ Andrea G, Norton L, et al. A phase I study of cetuximab/paclitaxel in patients with advanced-stage breast cancer. Clin Breast Cancer 2006;7:270-7
   PubMed Web of Science ®Google Scholar
• Chandarlapaty S, Scaltriti M, Angelini P, et al. Inhibitors of HSP90 block p95-HER2 signaling in trastuzumab-resistant tumors and suppress their growth. Oncogene 2010;29:325-34
   PubMed Web of Science ®Google Scholar