Zagouri et al. BMC Cancer 2010, 10:409 http://www.biomedcentral.com/1471-2407/10/409 setting, in which this study was performed. Collaborative efforts overcoming such limitations seem to be needed for further substantiation of the present findings in the future. Conclusion In conclusion, it can be said that Hsp90 expression seems decreased in ILC lesions compared to the normal adjacent breast ducts and lobules, a finding contrary to what might have been expected, given that high Hsp90 expression is a trait of invasive ductal carcinomas. Further studies adopting quantitative procedures, asses- sing mRNA levels and the pathophysiologically asso- ciated estrogen receptor status seem mandatory. Acknowledgements We would like to thank the President of the Hellenic Anticancer Institute Dr. Efstathios Fragoulis, for the technical organization of the Breast Unit and we would like to thank the Special Account for Research Grants of the University of Athens for the financial support. No conflict of interests exists. Author details 1Breast Unit, 1stDepartment of Propaedeutic Surgery, Hippokratio Hospital, School of Medicine, University of Athens, Athens, Greece. 2Department of Clinical and Therapeutics, Alexandra Hospital, School of Medicine, University of Athens, Athens, Greece. 3Department of Pathology, School of Medicine, University of Athens, Athens, Greece. Authors’ contributions All Authors have read and approved the final manuscript. Moreover, FZ: conceived the idea, participated in the design of the study and assisted in the writing of the manuscript; TS: participated in the design of the study, performed the statistical analysis and assisted in the writing of the manuscript; AN: performed the pathological evaluation; CP: evaluated critically the manuscript; AP: performed vacuum-assisted breast biopsy and open surgery and critically revised the manuscript for important scientific content; NM: performed vacuum-assisted breast biopsy and open surgery; PS: performed vacuum-assisted breast biopsy and open surgery; AL: performed the pathological evaluation; GT: performed vacuum-assisted breast biopsy and open surgery; EP: evaluated critically the manuscript; GZ: conceived of the study, participated in its design, performed vacuum- assisted breast biopsy and open surgery and evaluated critically the manuscript Competing interests The authors declare that they have no competing interests. Received: 13 November 2009 Accepted: 6 August 2010 Published: 6 August 2010 References 1. Lai BT, Chin NW, Stanek AE, Keh W, Lanks KW: Quantitation and intracellular localization of the 85 K heat shock protein by using monoclonal and polyclonal antibodies. Mol Cell Biol 1984, 4:2802-2810. 2. Whitley D, Goldberg SP, Jordan WD: Heat shock proteins: a review of the molecular chaperones. J Vasc Surg 1999, 29:748-751. 3. Beliakoff J, Whitesell L: Hsp90: an emerging target for breast cancer therapy. Anticancer Drugs 2004, 15:651-662. 4. Conroy SE, Latchman DS: Do heat shock proteins have a role in breast cancer? Br J Cancer 1996, 74:717-721. 5. Yano M, Naito Z, Tanaka S, Asano G: Expression and roles of heat shock proteins in human breast cancer. Jpn J Cancer Res 1996, 87:908-915. 6. Yano M, Naito Z, Yokoyama M, Shiraki Y, Ishiwata T, Inokuchi M, Asano G: Expression of hsp90 and cyclin D1 in human breast cancer. Cancer Lett 1999, 137:45-51. Page 6 of 6 7. Pick E, Kluger Y, Giltnane JM, Moeder C, Camp RL, Rimm DL, Kluger HM: High HSP90 expression is associated with decreased survival in breast cancer. Cancer Res 2007, 67:2932-2937. 8. Kim LS, Lee HS, Choi JW, Kang HJ, Price JE: The role of heat shock protein 90/70 as potential molecular therapeutic targets in breast cancer. Proceedings of the 90th annual meeting of the American Association for Cancer Research: 16-20 April 2005, Anaheim, CA Philadelphia, PA; AACR 2005, 2346. 9. Miyata Y: Hsp90 inhibitor geldanamycin and its derivatives as novel cancer chemotherapeutic agents. Curr Pharm Des 2005, 11:1131-1138. 10. Bagatell R, Whitesell L: Altered Hsp90 function in cancer: a unique therapeutic opportunity. Mol Cancer Ther 2004, 3:1021-1030. 11. Sõti C, Nagy E, Giricz Z, Vígh L, Csermely P, Ferdinandy P: Heat shock proteins as emerging therapeutic targets. Br J Pharmacol 2005, 146:769-780. 12. Workman P, Burrows F, Neckers L, Rosen N: Drugging the cancer chaperone HSP90: combinatorial therapeutic exploitation of oncogene addiction and tumor stress. Ann N Y Acad Sci 2007, 1113:202-216. 13. Holmes JL, Sharp SY, Hobbs S, Workman P: Silencing of HSP90 cochaperone AHA1 expression decreases client protein activation and increases cellular sensitivity to the HSP90 inhibitor 17-allylamino-17- demethoxygeldanamycin. Cancer Res 2008, 68:1188-1197. 14. Zagouri F, Nonni A, Sergentanis TN, Papadimitriou CA, Michalopoulos NV, Lazaris AC, Patsouris E, Zografos GC: Heat shock protein90 in lobular neoplasia of the breast. BMC Cancer 2008, 8:312. 15. Schreer I, Luttges J: Precursor lesions of invasive breast cancer. Eur J Radiol 2005, 54:62-71. 16. Sastre-Garau X, Jouve M, Asselain B, Vincent-Salomon A, Beuzeboc P, Dorval T, Durand JC, Fourquet A, Pouillart P: Infiltrating lobular carcinoma of the breast. Clinicopathologic analysis of 975 cases with reference to data on conservative therapy and metastatic patterns. Cancer 1996, 77:113-120. 17. Harvey JM, Clark GM, Osborne CK, Allred DC: Estrogen receptor status by immunohistochemistry is superior to the ligand-binding assay for predicting response to adjuvant endocrine therapy in breast cancer. J Clin Oncol 1999, 17:1474-81. 18. Mann GB, Fahey VD, Feleppa F, Buchanan MR: Reliance on hormone receptor assays of surgical specimens may compromise outcome in patients with breast cancer. J Clin Oncol 2005, 23:5148-5154. 19. O’Malley FP, Peder SE: Invasive carcinomas: Special types in Breast Pathology Elsevier 2006. 20. Modi S, Stopeck AT, Gordon MS, Mendelson D, Solit DB, Bagatell R, Ma W, Wheler J, Rosen N, Norton L, Cropp GF, Johnson RG, Hannah AL, Hudis CA: Combination of trastuzumab and tanespimycin (17-AAG, KOS-953) is safe and active in trastuzumab-refractory HER-2 overexpressing breast cancer: a phase I dose-escalation study. J Clin Oncol 2007, 25:5410-7. 21. Powers MV, Workman P: Targeting of multiple signalling pathways by heat shock protein 90 molecular chaperone inhibitors. Endocr Relat Cancer 2006, 13:S125-35. 22. Solit DB, Rosen N: Hsp90: a novel target for cancer therapy. Curr Top Med Chem 2006, 6:1205-14. 23. Zhang H, Chung D, Yang YC, Neely L, Tsurumoto S, Fan J, Zhang L, Biamonte M, Brekken J, Lundgren K, Burrows F: Identification of new biomarkers for clinical trials of Hsp90 inhibitors. Mol Cancer Ther 2006, 5:1256-64. 24. Diehl MC, Idowu MO, Kimmelshue K, York TP, Elmore LW, Holt SE: Elevated expression of nuclear Hsp90 in invasive breast tumors. Cancer Biol Ther 2009, 8:1952-61. 25. Gebhard B, Schütz G, Ecker RC, Steiner GE, Rudas M, Gnant M, Oehler R: MHC-class-I expression in human breast cancer correlates with nuclear localization of the 90 kDa heat-shock-protein. Anticancer Res 1999, 19:5293-5297. Pre-publication history The pre-publication history for this paper can be accessed here: http://www.biomedcentral.com/1471-2407/10/409/prepub doi:10.1186/1471-2407-10-409 Cite this article as: Zagouri et al.: Decreased Hsp90 expression in infiltrative lobular carcinoma: an immunohistochemical study. BMC Cancer 2010 10:409.