Abstract
An estimated 1.15 million new cases of invasive breast cancer occurred in women worldwide in the year 2002 accounting with 410,712 new deaths. The 5-year relative survival rate for localized breast cancer (cancer that has not spread to lymph nodes or other locations outside the breast) has increased from 72% in the 1940s to 97% today. However, the survival rate is lower (79%) in patients with regional spread while for women with distant metastases, the rate is 23% (cancer expected to occur in women in the United States in the year 2004). In this ultimate stage of malignant transformation, the tumors become resistant to most therapies, and the disease is almost incurable. Therefore, therapeutic interventions designed to inhibit metastatic spread of cancer cells are critical. This chapter will briefly cover recent advances in the study of tumor metastasis and the important role played by heat shock protein 25/27
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References
Asea, A., Rehli, M., Kabingu, E., Boch, J. A., Bare, O., Auron, P. E., Stevenson, M. A. and Calderwood, S. K. (2002) Novel signal transduction pathway utilized by extracellular HSP70: role of toll-like receptor (TLR) 2 and TLR4. J Biol Chem 277, 15028–15034.
Bausero, M. A., Bharti, A., Page, D. T., Perez, K. D., Eng, J. W., Ordonez, S. L., Asea, E. E., Jantschitsch, C., Kindas-Muegge, I., Ciocca, D. and Asea, A. (2006) Silencing the hsp25 gene eliminates migration capability of the highly metastatic murine 4T1 breast adenocarcinoma cell. Tumour Biol 27, 17–26.
Bausero, M. A., Page, D. T., Osinaga, E. and Asea, A. (2004) Surface expression of Hsp25 and Hsp72 differentially regulates tumor growth and metastasis. Tumour Biol 25, 243–251.
Botzler, C., Issels, R. and Multhoff, G. (1996) Heat-shock protein 72 cell-surface expression on human lung carcinoma cells in associated with an increased sensitivity to lysis mediated by adherent natural killer cells. Cancer Immunol Immunother 43, 226–230.
Botzler, C., Li, G., Issels, R. D. and Multhoff, G. (1998) Definition of extracellular localized epitopes of Hsp70 involved in an NK immune response. Cell Stress Chaperones 3, 6–11.
Cahill, C. M., Waterman, W. R., Xie, Y., Auron, P. E. and Calderwood, S. K. (1996) Transcriptional repression of the prointerleukin 1beta gene by heat shock factor 1. J. Biol. Chem. 271, 24874–24879.
Calderwood, S. K. and Asea, A. (2002) Targeting HSP70-induced thermotolerance for design of thermal sensitizers. Int J Hyperthermia 18, 597–608.
Ciocca, D. R., Green, S., Elledge, R. M., Clark, G. M., Pugh, R., Ravdin, P., Lew, D., Martino, S. and Osborne, C. K. (1998) Heat shock proteins hsp27 and hsp70: lack of correlation with response to tamoxifen and clinical course of disease in estrogen receptor-positive metastatic breast cancer (a Southwest Oncology Group Study). Clin Cancer Res 4, 1263–1266.
Ciocca, D. R. and Roig, L. M. (1995) Estrogen receptors in human nontarget tissues: biological and clinical implications. Endocr Rev 16, 35–62.
Ciocca, D. R., Rozados, V. R., Cuello Carrion, F. D., Gervasoni, S. I., Matar, P. and Scharovsky, O. G. (2003) Hsp25 and Hsp70 in rodent tumors treated with doxorubicin and lovastatin. Cell Stress Chaperones 8, 26–36.
Ciocca, D. R. and Vargas-Roig, L. M. (2002) Hsp27 as a prognostic and predictive factor in cancer. Prog Mol Subcell Biol 28, 205–218.
Cornford, P. A., Dodson, A. R., Parsons, K. F., Desmond, A. D., Woolfenden, A., Fordham, M., Neoptolemos, J. P., Ke, Y. and Foster, C. S. (2000) Heat shock protein expression independently predicts clinical outcome in prostate cancer. Cancer Res 60, 7099–7105.
Craig, E. A. and Gross, C. A. (1991) Is hsp70 the cellular thermometer? Trends Biochem Sci 16, 135–140.
De, A. K., Kodys, K. M., Yeh, B. S. and Miller-Graziano, C. (2000) Exaggerated human monocyte IL-10 concomitant to minimal TNF-alpha induction by heat-shock protein 27 (Hsp27) suggests Hsp27 is primarily an antiinflammatory stimulus. J Immunol 165, 3951–3958.
Didelot, C., Schmitt, E., Brunet, M., Maingret, L., Parcellier, A. and Garrido, C. (2006) Heat shock proteins: endogenous modulators of apoptotic cell death. Handb Exp Pharmacol, 171–198.
Egeblad, M. and Werb, Z. (2002) New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer 2, 161–174.
Elbashir, S. M., Harborth, J., Lendeckel, W., Yalcin, A., Weber, K. and Tuschl, T. (2001) Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature 411, 494–498.
Farkas, B., Hantschel, M., Magyarlaki, M., Becker, B., Scherer, K., Landthaler, M., Pfister, K., Gehrmann, M., Gross, C., Mackensen, A. and Multhoff, G. (2003) Heat shock protein 70 membrane expression and melanoma-associated marker phenotype in primary and metastatic melanoma. Melanoma Res 13, 147–152.
Fire, A., Xu, S., Montgomery, M. K., Kostas, S. A., Driver, S. E. and Mello, C. C. (1998) Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans. Nature 391, 806–811.
Gross, C., Hansch, D., Gastpar, R. and Multhoff, G. (2003a) Interaction of heat shock protein 70 peptide with NK cells involves the NK receptor CD94. Biol Chem 384, 267–279.
Gross, C., Koelch, W., DeMaio, A., Arispe, N. and Multhoff, G. (2003b) Cell surface-bound heat shock protein 70 (Hsp70) mediates perforin-independent apoptosis by specific binding and uptake of granzyme B. J Biol Chem 278, 41173–41181.
Gross, C., Schmidt-Wolf, I. G., Nagaraj, S., Gastpar, R., Ellwart, J., Kunz-Schughart, L. A. and Multhoff, G. (2003c) Heat shock protein 70-reactivity is associated with increased cell surface density of CD94/CD56 on primary natural killer cells. Cell Stress Chaperones 8, 348–360.
Hantschel, M., Pfister, K., Jordan, A., Scholz, R., Andreesen, R., Schmitz, G., Schmetzer, H., Hiddemann, W. and Multhoff, G. (2000) Hsp70 plasma membrane expression on primary tumor biopsy material and bone marrow of leukemic patients. Cell Stress Chaperones 5, 438–442.
Jaattela, M. (2002) Programmed cell death: many ways for cells to die decently. Ann Med 34, 480–488.
Jaattela, M., Wissing, D., Kokholm, K., Kallunki, T. and Egeblad, M. (1998) Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases. Embo J 17, 6124–6134.
Kim, S. H., Yeo, G. S., Lim, Y. S., Kang, C. D., Kim, C. M. and Chung, B. S. (1998) Suppression of multidrug resistance via inhibition of heat shock factor by quercetin in MDR cells. Exp Mol Med 30, 87–92.
Lavoie, J. N., Lambert, H., Hickey, E., Weber, L. A. and Landry, J. (1995) Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27. Mol Cell Biol 15, 505–516.
Lee, Y. J., Cho, H. N., Jeoung, D. I., Soh, J. W., Cho, C. K., Bae, S., Chung, H. Y., Lee, S. J. and Lee, Y. S. (2004) HSP25 overexpression attenuates oxidative stress-induced apoptosis: roles of ERK1/2 signaling and manganese superoxide dismutase. Free Radic Biol Med 36, 429–444.
Liang, Z., Yoon, Y., Votaw, J., Goodman, M. M., Williams, L. and Shim, H. (2005) Silencing of CXCR4 blocks breast cancer metastasis. Cancer Res 65, 967–971.
Lindquist, S. and Craig, E. A. (1988) The heat-shock proteins. Annu Rev Genet 22, 631–677.
Lirdprapamongkol, K., Sakurai, H., Kawasaki, N., Choo, M. K., Saitoh, Y., Aozuka, Y., Singhirunnusorn, P., Ruchirawat, S., Svasti, J. and Saiki, I. (2005) Vanillin suppresses in vitro invasion and in vivo metastasis of mouse breast cancer cells. Eur J Pharm Sci 25, 57–65.
Mehlen, P., Schulze-Osthoff, K. and Arrigo, A. P. (1996) Small stress proteins as novel regulators of apoptosis. Heat shock protein 27 blocks Fas/APO-1- and staurosporine-induced cell death. J Biol Chem 271, 16510–16514.
Multhoff, G., Botzler, C., Jennen, L., Schmidt, J., Ellwart, J. and Issels, R. (1997) Heat shock protein 72 on tumor cells: a recognition structure for natural killer cells. J Immunol 158, 4341–4350.
Multhoff, G. and Hightower, L. E. (1996) Cell surface expression of heat shock proteins and the immune response. Cell Stress Chaperones 1, 167–176.
Neumark, E., Sagi-Assif, O., Shalmon, B., Ben-Baruch, A. and Witz, I. P. (2003) Progression of mouse mammary tumors: MCP-1-TNFalpha cross-regulatory pathway and clonal expression of promalignancy and antimalignancy factors. Int J Cancer 106, 879–886.
Oesterreich, S., Hilsenbeck, S. G., Ciocca, D. R., Allred, D. C., Clark, G. M., Chamness, G. C., Osborne, C. K. and Fuqua, S. A. (1996) The small heat shock protein HSP27 is not an independent prognostic marker in axillary lymph node-negative breast cancer patients. Clin Cancer Res 2, 1199–1206.
Park, S. H., Lee, Y. S., Osawa, Y., Hachiya, M. and Akashi, M. (2002) Hsp25 regulates the expression of p21(Waf1/Cip1/Sdi1) through multiple mechanisms. J Biochem (Tokyo) 131, 869–875.
Rogalla, T., Ehrnsperger, M., Preville, X., Kotlyarov, A., Lutsch, G., Ducasse, C., Paul, C., Wieske, M., Arrigo, A. P., Buchner, J. and Gaestel, M. (1999) Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation. J Biol Chem 274, 18947–18956.
Smith, M. C., Luker, K. E., Garbow, J. R., Prior, J. L., Jackson, E., Piwnica-Worms, D. and Luker, G. D. (2004) CXCR4 regulates growth of both primary and metastatic breast cancer. Cancer Res 64, 8604–8612.
Soldes, O. S., Kuick, R. D., Thompson, I. A., 2nd, Hughes, S. J., Orringer, M. B., Iannettoni, M. D., Hanash, S. M. and Beer, D. G. (1999) Differential expression of Hsp27 in normal oesophagus, Barrett’s metaplasia and oesophageal adenocarcinomas. Br J Cancer 79, 595–603.
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Bausero, M.A., Asea, A. (2007). Role of Heat Shock Protein Hsp25/27 in~the~Metastatic Spread of Cancer Cells. In: Calderwood, S.K., Sherman, M.Y., Ciocca, D.R. (eds) Heat Shock Proteins in Cancer. Heat Shock Proteins, vol 2. Springer, Dordrecht. https://doi.org/10.1007/978-1-4020-6401-2_6
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DOI: https://doi.org/10.1007/978-1-4020-6401-2_6
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