Low serum MMP-1 in breast cancer: a negative prognostic factor?

References

• Agarwal D, Goodison S, Nicholson B, Tarin D, Urquidi V. (2003). Expression of matrix metalloproteinase 8 (MMP-8) and tyrosinase-related protein-1 (TYRP-1) correlates with the absence of metastasis in an isogenic human breast cancer model. Differentiation 71:114–125.
   PubMed Web of Science ®Google Scholar
• Boström P, Söderström M, Vahlberg T, Söderström KO, Roberts PJ, Carpén O, Hirsimäki P. (2011). MMP-1 expression has an independent prognostic value in breast cancer. BMC Cancer 11:348.
   Google Scholar
• Cancer registry. Croatian National Institute for Public Health, 2010. Available at: http://www.hzjz.hr/rak/novo.htm Accessed on 28 February 2011.
   Google Scholar
• Decock J, Hendrickx W, Vanleeuw U, Van Belle V, Van Huffel S, Christiaens MR, Ye S, Paridaens R. (2008). Plasma MMP1 and MMP8 expression in breast cancer: protective role of MMP8 against lymph node metastasis. BMC Cancer 8:77.
   PubMed Web of Science ®Google Scholar
• Egeblad M, Werb Z. (2002). New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer 2:161–174.
   PubMed Web of Science ®Google Scholar
• Fingleton B. (2006). Matrix metalloproteinases: roles in cancer and metastasis. Front Biosci 11:479–491.
   PubMedGoogle Scholar
• Fingleton B. (2007). Matrix metalloproteinases as valid clinical targets. Curr Pharm Des 13:333–346.
   PubMed Web of Science ®Google Scholar
• Folkman J. (2004). Endogenous angiogenesis inhibitors. APMIS 112:496–507.
   PubMed Web of Science ®Google Scholar
• Fowlkes JL, Enghild JJ, Suzuki K, Nagase H. (1994). Matrix metalloproteinases degrade insulin-like growth factor-binding protein-3 in dermal fibroblast cultures. J Biol Chem 269:25742–25746.
   PubMed Web of Science ®Google Scholar
• Ghosh AK, Bhattacharyya S, Varga J. (2004). The tumor suppressor p53 abrogates Smad-dependent collagen gene induction in mesenchymal cells. J Biol Chem 279:47455–47463.
   Google Scholar
• Hanahan D, Weinberg RA. (2011). Hallmarks of cancer: the next generation. Cell 144:646–674.
   PubMed Web of Science ®Google Scholar
• Horwitz KB, McGuire WL. (1977). Progesterone and progesterone receptors in experimental breast cancer. Cancer Res 37:1733–1738.
   PubMed Web of Science ®Google Scholar
• Mañes S, Llorente M, Lacalle RA, Gómez-Moutón C, Kremer L, Mira E, Martínez-A C. (1999). The matrix metalloproteinase-9 regulates the insulin-like growth factor-triggered autocrine response in DU-145 carcinoma cells. J Biol Chem 274:6935–6945.
   PubMed Web of Science ®Google Scholar
• Marsolais D, Côté CH, Frenette J. (2007). Pifithrin-alpha, an inhibitor of p53 transactivation, alters the inflammatory process and delays tendon healing following acute injury. Am J Physiol Regul Integr Comp Physiol 292:R321–R327.
   Google Scholar
• Martin MD, Matrisian LM. (2007). The other side of MMPs: protective roles in tumor progression. Cancer Metastasis Rev 26:717–724.
   PubMed Web of Science ®Google Scholar
• Mbeunkui F, Johann DJ Jr. (2009). Cancer and the tumor microenvironment: a review of an essential relationship. Cancer Chemother Pharmacol 63:571–582.
   PubMed Web of Science ®Google Scholar
• McGowan PM, Duffy MJ. (2008). Matrix metalloproteinase expression and outcome in patients with breast cancer: analysis of a published database. Ann Oncol 19:1566–1572.
   PubMedGoogle Scholar
• McQuibban GA, Gong JH, Wong JP, Wallace JL, Clark-Lewis I, Overall CM. (2002). Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo. Blood 100:1160–1167.
   PubMed Web of Science ®Google Scholar
• Montel V, Kleeman J, Agarwal D, Spinella D, Kawai K, Tarin D. (2004). Altered metastatic behavior of human breast cancer cells after experimental manipulation of matrix metalloproteinase 8 gene expression. Cancer Res 64:1687–1694.
   PubMed Web of Science ®Google Scholar
• Noë V, Fingleton B, Jacobs K, Crawford HC, Vermeulen S, Steelant W, Bruyneel E, Matrisian LM, Mareel M. (2001). Release of an invasion promoter E-cadherin fragment by matrilysin and stromelysin-1. J Cell Sci 114:111–118.
   PubMed Web of Science ®Google Scholar
• Remacle AG, Noël A, Duggan C, McDermott E, O’Higgins N, Foidart JM, Duffy MJ. (1998). Assay of matrix metalloproteinases types 1, 2, 3 and 9 in breast cancer. Br J Cancer 77:926–931.
   PubMed Web of Science ®Google Scholar
• Rifkin DB, Mazzieri R, Munger JS, Noguera I, Sung J. (1999). Proteolytic control of growth factor availability. APMIS 107:80–85.
   PubMed Web of Science ®Google Scholar
• Sternlicht MD, Werb Z. (2001). How matrix metalloproteinases regulate cell behavior. Annu Rev Cell Dev Biol 17:463–516.
   PubMed Web of Science ®Google Scholar
• Turpeenniemi-Hujanen T. (2005). Gelatinases (MMP-2 and -9) and their natural inhibitors as prognostic indicators in solid cancers. Biochimie 87:287–297.
   PubMed Web of Science ®Google Scholar
• Vihinen P, Kähäri VM. (2002). Matrix metalloproteinases in cancer: prognostic markers and therapeutic targets. Int J Cancer 99:157–166.
   PubMed Web of Science ®Google Scholar
• Vu TH, Werb Z. (2000). Matrix metalloproteinases: effectors of development and normal physiology. Genes Dev 14:2123–2133.
   PubMed Web of Science ®Google Scholar
• Watson SA, Tierney G. (1998). Matrix metalloproteinase inhibitors: a review. BioDrugs 9:325–335.
   Google Scholar
• Zucker S, Hymowitz M, Conner C, Zarrabi HM, Hurewitz AN, Matrisian L, Boyd D, Nicolson G, Montana S. (1999). Measurement of matrix metalloproteinases and tissue inhibitors of metalloproteinases in blood and tissues. Clinical and experimental applications. Ann N Y Acad Sci 878:212–227.
   Google Scholar