TIMP-1 overexpression does not affect sensitivity to HER2-targeting drugs in the HER2-gene-amplified SK-BR-3 human breast cancer cell line
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  • 作者:Xiaohong Deng (1) (2)
    Louise Fogh (1)
    Ulrik Lademann (1)
    Vibeke Jensen (1)
    Jan Stenvang (1)
    Huanming Yang (2)
    Nils Brünner (1)
    Anne-Sofie Schrohl (1)
  • 关键词:TIMP ; 1 and HER2 ; Signal pathway ; HER2 cleavage ; Sensitivity to trastuzumab and lapatinib ; Breast cancer
  • 刊名:Tumor Biology
  • 出版年:2013
  • 出版时间:April 2013
  • 年:2013
  • 卷:34
  • 期:2
  • 页码:1161-1170
  • 全文大小:343KB
  • 参考文献:1. Schlessinger J. Cell signaling by receptor tyrosine kinases. Cell. 2000;103:211-5. CrossRef
    2. Slamon DJ, Godolphin W, Jones LA, Holt JA, Wong SG, Keith DE, et al. Studies of the her-2/neu proto-oncogene in human breast and ovarian cancer. Science. 1989;244:707-2. CrossRef
    3. Press MF, Bernstein L, Thomas PA, Meisner LF, Zhou JY, Ma Y, et al. Her-2/neu gene amplification characterized by fluorescence in situ hybridization: poor prognosis in node-negative breast carcinomas. J Clin Oncol. 1997;15:2894-04.
    4. Slamon DJ, Clark GM, Wong SG, Levin WJ, Ullrich A, McGuire WL. Human breast cancer: correlation of relapse and survival with amplification of the her-2/neu oncogene. Science. 1987;235:177-2. CrossRef
    5. Carter P, Presta L, Gorman CM, Ridgway JB, Henner D, Wong WL, et al. Humanization of an anti-p185her2 antibody for human cancer therapy. Proc Natl Acad Sci U S A. 1992;89:4285-. CrossRef
    6. Esteva FJ, Yu D, Hung MC, Hortobagyi GN. Molecular predictors of response to trastuzumab and lapatinib in breast cancer. Nat Rev Clin Oncol. 2010;7:98-07. CrossRef
    7. MacFarlane RJ, Gelmon KA. Lapatinib for breast cancer: a review of the current literature. Expert Opin Drug Saf. 2011;10:109-1. CrossRef
    8. Gajria D, Chandarlapaty S. Her2-amplified breast cancer: mechanisms of trastuzumab resistance and novel targeted therapies. Expert Rev Anticancer Ther. 2011;11:263-5. CrossRef
    9. Cobleigh MA, Vogel CL, Tripathy D, Robert NJ, Scholl S, Fehrenbacher L, et al. Multinational study of the efficacy and safety of humanized anti-HER2 monoclonal antibody in women who have HER2-overexpressing metastatic breast cancer that has progressed after chemotherapy for metastatic disease. J Clin Oncol. 1999;17:2639-8.
    10. Vogel CL, Cobleigh MA, Tripathy D, Gutheil JC, Harris LN, Fehrenbacher 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. 2002;20:719-6. CrossRef
    11. Gomez HL, Doval DC, Chavez MA, Ang PC, Aziz Z, Nag S, et al. Efficacy and safety of lapatinib as first-line therapy for erbb2-amplified locally advanced or metastatic breast cancer. J Clin Oncol. 2008;26:2999-005. CrossRef
    12. Talvensaari-Mattila A, Turpeenniemi-Hujanen T. High preoperative serum TIMP-1 is a prognostic indicator for survival in breast carcinoma. Breast Cancer Res Treat. 2005;89:29-4. CrossRef
    13. Kuvaja P, Talvensaari-Mattila A, Turpeenniemi-Hujanen T. High preoperative plasma TIMP-1 is prognostic for early relapse in primary breast carcinoma. Int J Cancer. 2008;123:846-1. CrossRef
    14. Wurtz SO, Moller S, Mouridsen H, Hertel PB, Friis E, Brunner N. Plasma and serum levels of tissue inhibitor of metalloproteinases-1 are associated with prognosis in node-negative breast cancer: a prospective study. Mol Cell Proteomics. 2008;7:424-0.
    15. Schrohl AS, Look MP, Meijer-van Gelder ME, Foekens JA, Brunner N. Tumor tissue levels of tissue inhibitor of metalloproteinases-1 (TIMP-1) and outcome following adjuvant chemotherapy in premenopausal lymph node-positive breast cancer patients: a retrospective study. BMC Cancer. 2009;9:322. CrossRef
    16. Schrohl AS, Meijer-van Gelder ME, Holten-Andersen MN, Christensen IJ, Look MP, Mouridsen HT, et al. Primary tumor levels of tissue inhibitor of metalloproteinases-1 are predictive of resistance to chemotherapy in patients with metastatic breast cancer. Clin Cancer Res. 2006;12:7054-. CrossRef
    17. Ejlertsen B, Jensen MB, Nielsen KV, Balslev E, Rasmussen BB, Willemoe GL, et al. HER2, TOP2a, and TIMP-1 and responsiveness to adjuvant anthracycline-containing chemotherapy in high-risk breast cancer patients. J Clin Oncol. 2010;28:984-0. CrossRef
    18. Lipton A, Leitzel K, Chaudri-Ross HA, Evans DB, Ali SM, Demers L, et al. Serum TIMP-1 and response to the aromatase inhibitor letrozole versus tamoxifen in metastatic breast cancer. J Clin Oncol. 2008;26:2653-. CrossRef
    19. Jung KK, Liu XW, Chirco R, Fridman R, Kim HR. Identification of cd63 as a tissue inhibitor of metalloproteinase-1 interacting cell surface protein. EMBO J. 2006;25:3934-2. CrossRef
    20. Fu ZY, Lv JH, Ma CY, Yang DP, Wang T. Tissue inhibitor of metalloproteinase-1 decreased chemosensitivity of MDA-435 breast cancer cells to chemotherapeutic drugs through the PI3K/AKT/NF-κB pathway. Biomed Pharmacother. 2011;65:163-. CrossRef
    21. Liu XW, Bernardo MM, Fridman R, Kim HR. Tissue inhibitor of metalloproteinase-1 protects human breast epithelial cells against intrinsic apoptotic cell death via the focal adhesion kinase/phosphatidylinositol 3-kinase and MAPK signaling pathway. J Biol Chem. 2003;278:40364-2. CrossRef
    22. Vazquez-Martin A, Oliveras-Ferraros C, Cufi S, Del Barco S, Martin-Castillo B, Menendez JA. Lapatinib, a dual HER1/HER2 tyrosine kinase inhibitor, augments basal cleavage of HER2 extracellular domain (ECD) to inhibit HER2-driven cancer cell growth. J Cell Physiol. 2011;226:52-. CrossRef
    23. Liu PC, Liu X, Li Y, Covington M, Wynn R, Huber R, et al. Identification of adam10 as a major source of HER2 ectodomain sheddase activity in HER2 overexpressing breast cancer cells. Cancer Biol Ther. 2006;5:657-4. CrossRef
    24. Amour A, Knight CG, Webster A, Slocombe PM, Stephens PE, Knauper V, et al. The in vitro activity of adam-10 is inhibited by TIMP-1 and TIMP-3. FEBS Lett. 2000;473:275-. CrossRef
    25. Codony-Servat J, Albanell J, Lopez-Talavera JC, Arribas J, Baselga J. Cleavage of the HER2 ectodomain is a pervanadate-activable process that is inhibited by the tissue inhibitor of metalloproteases-1 in breast cancer cells. Cancer Res. 1999;59:1196-01.
    26. Holten-Andersen MN, Murphy G, Nielsen HJ, Pedersen AN, Christensen IJ, Hoyer-Hansen G, et al. Quantitation of TIMP-1 in plasma of healthy blood donors and patients with advanced cancer. Br J Cancer. 1999;80:495-03. CrossRef
    27. Thaysen-Andersen M, Thogersen IB, Nielsen HJ, Lademann U, Brunner N, Enghild JJ, et al. Rapid and individual-specific glycoprofiling of the low abundance n-glycosylated protein tissue inhibitor of metalloproteinases-1. Mol Cell Proteomics. 2007;6:638-7. CrossRef
    28. Sorensen IV, Fenger C, Winther H, Foged NT, Lademann U, Brunner N, et al. Characterization of anti-TIMP-1 monoclonal antibodies for immunohistochemical localization in formalin-fixed, paraffin-embedded tissue. J Histochem Cytochem. 2006;54:1075-6. CrossRef
    29. Cedergreen N, Ritz C, Streibig JC. Improved empirical models describing hormesis. Environ Toxicol Chem. 2005;24:3166-2. CrossRef
    30. Ghedini GC, Ciravolo V, Tortoreto M, Giuffre S, Bianchi F, Campiglio M, et al. Shed HER2 extracellular domain in HER2-mediated tumor growth and in trastuzumab susceptibility. J Cell Physiol. 2010;225:256-5. CrossRef
    31. Mukai H. Treatment strategy for HER2-positive breast cancer. Int J Clin Oncol. 2010;15:335-0. CrossRef
    32. Baselga J, Swain SM. Novel anticancer targets: revisiting ERBB2 and discovering ERBB3. Nat Rev Cancer. 2009;9:463-5. CrossRef
    33. Junttila TT, Li G, Parsons K, Phillips GL, Sliwkowski MX. Trastuzumab-dm1 (t-dm1) retains all the mechanisms of action of trastuzumab and efficiently inhibits growth of lapatinib insensitive breast cancer. Breast Cancer Res Treat. 2011;128:347-6. CrossRef
    34. Junttila TT, Akita RW, Parsons K, Fields C, Lewis Phillips GD, Friedman LS, et al. Ligand-independent HER2/HER3/PI3K complex is disrupted by trastuzumab and is effectively inhibited by the PI3K inhibitor GDC-0941. Cancer Cell. 2009;15:429-0. CrossRef
    35. Pedersen K, Angelini PD, Laos S, Bach-Faig A, Cunningham MP, Ferrer-Ramon C, et al. A naturally occurring HER2 carboxy-terminal fragment promotes mammary tumor growth and metastasis. Mol Cell Biol. 2009;29:3319-1. CrossRef
    36. Scaltriti M, Rojo F, Ocana A, Anido J, Guzman M, Cortes J, 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;99:628-8. CrossRef
    37. Pupa SM, Menard S, Morelli D, Pozzi B, De Palo G, Colnaghi MI. The extracellular domain of the c-ERBB-2 oncoprotein is released from tumor cells by proteolytic cleavage. Oncogene. 1993;8:2917-3.
    38. Parra-Palau JL, Pedersen K, Peg V, Scaltriti M, Angelini PD, Escorihuela M, et al. A major role of p95/611-CTF, a carboxy-terminal fragment of HER2, in the down-modulation of the estrogen receptor in HER2-positive breast cancers. Cancer Res. 2010;70:8537-6. CrossRef
    39. Aigner A, Juhl H, Malerczyk C, Tkybusch A, Benz CC, Czubayko F. Expression of a truncated 100 kDa HER2 splice variant acts as an endogenous inhibitor of tumour cell proliferation. Oncogene. 2001;20:2101-1. CrossRef
    40. Arribas J, Baselga J, Pedersen K, Parra-Palau JL. P95her2 and breast cancer. Cancer Res. 2011;71:1515-. CrossRef
    41. Citri A, Yarden Y. EGF-ERBB signalling: towards the systems level. Nat Rev Mol Cell Biol. 2006;7:505-6. CrossRef
    42. Tsai HP, Chen SC, Chien HT, Jan YY, Chao TC, Chen MF, et al. Relationships between serum HER2 ECD, TIMP-1 and clinical outcomes in Taiwanese breast cancer. World J Surg Oncol. 2012;10:42. CrossRef
  • 作者单位:Xiaohong Deng (1) (2)
    Louise Fogh (1)
    Ulrik Lademann (1)
    Vibeke Jensen (1)
    Jan Stenvang (1)
    Huanming Yang (2)
    Nils Brünner (1)
    Anne-Sofie Schrohl (1)

    1. Department of Pathobiology and Sino-Danish Breast Cancer Research Centre, Institute of Veterinary Disease Biology, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark
    2. Beijing Genomics Institute and Sino-Danish Breast Cancer Research Centre, Shenzhen, China
  • ISSN:1423-0380
文摘
Tissue inhibitor of metalloproteinases-1 (TIMP-1) has been suggested as a marker of prognosis and response to treatment in breast cancer. In vitro, TIMP-1 can regulate shedding of the extracellular domain of HER2 and signalling via the Akt pathway, and we hypothesize that TIMP-1 therefore can affect sensitivity to the HER2-targeting drugs trastuzumab and lapatinib. SK-BR-3 human breast cancer cells were stably transfected with TIMP-1, characterized with regard to TIMP-1 protein expression, proliferation, and functionality of the secreted TIMP-1, and the sensitivity to trastuzumab and lapatinib was studied in five selected single-cell subclones expressing TIMP-1 protein at various levels plus the parental SK-BR-3 cell line. Both trastuzumab and lapatinib reduced cell viability, as determined by MTT assay, but the sensitivity to the drugs was not associated with the expression level of TIMP-1 protein. Western blotting showed that the activation of Akt, PTEN, and HER2 as well as ADAM10 was similar in all clones. In conclusion, in this model, TIMP-1 overexpression does not affect HER2 cleavage by ADAM10 or signalling via the Akt pathway, and TIMP-1 does not influence sensitivity to trastuzumab and lapatinib.

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