MMPs are also associated with tumor progression and con‐ tribute to tumor invasion and metastasis. MMPs are associated with five principal processes promoting tumor progression (Egeblad and Werb, 2002). First, MMPs can pro‐ mote cancer cell proliferation by three known mechanisms. These include release of cellmembrane-bound precursors of some growth factors, such as TGF-α, degradation of ECM proteins resulting in the release of peptide growth factors, or indirect proliferative signals through integrins. Second, MMPs regulate apoptosis as well as anti-apoptosis. MMP-3, -7, -9 and –11 are known to regulate apoptosis involving different signaling processes. Over‐ expression of MMP-3 is known to induce apoptosis in mammary epithelial cells by de‐ grading laminin (Alexander et al., 1996a; Witty et al., 1995) and MMP-7 cleaves FAS ligand, a ligand for the death receptor FAS, from its membrane-bound precursor. As a re‐ sult of this cleavage, a pro-apoptotic molecule is released into the surrounding microen‐ vironment (Powell et al., 1999; Mitsiades et al., 2001). MMPs can also induce apoptosis of endothelial cells or epithelial cells by shedding the adhesion molecules VE-cadherin (Her‐ ren et al., 1998), PECAM-1 (Ilan et al., 2001) and E-cadherin (Steinhusen et al., 2001). Third, MMPs are positive regulators of angiogenesis, which is required for tumor growth. MMP-2, -9 and –14 and –19 have been shown to regulate angiogenesis by promoting the availability of factors involved in angiogenesis, such as vascular endothelial growth factor (VEGF), fibroblast growth factor 2 (FGF-2) and TGF-β. These factors are required for en‐ dothelial cell proliferation and migration. Moreover, MMP-2 is required for transition to an angiogenic phenotype in a tumor model (Fang et al., 2000), suggesting that MMPs are important for maintenance of tumor growth and proliferation. Fourth, MMPs allow cancer cells to evade immune surveillance. For example, MMP-9 can cleave interleukin-2 recep‐ tor-a (IL-2Ra) from the surface of activated T lymphocytes, thereby suppressing their pro‐ liferation (Sheu et al., 2001). As a result of this suppression, tumor-specific T lymphocytes cannot infiltrate tumor cells. MMP-11 also generates a cleavage product that allows tumor cells to evade the tumor-targeted activity of natural killer cells. MMP-11 cleaves α1-protei‐ nase-inhibitor, which decreases natural killer cell cytotoxicity (Kataoka et al., 1999). Active membrane-type 1 MMP (MT1-MMP) has also been suggested to assist tumor cells in eva‐ sion of immune surveillance (Rozanov et al., 2002). Therefore, tumor cells escape immune surveillance leading to uncontrolled tumor growth. Fifth, MMPs degrade extracellular ma‐ trix components and allow tumor cells to migrate across epithelial basement membranes and metastasize to a new site. While the exact mechanism triggering MMP release by tu‐ mor cells is not yet completely understood, MMPs are the only enzymes known to de‐ grade fibrillar collagen types I, II, III and IV. MMP-2, -3, -13 and –14 promote invasion of cell lines in *in vitro* models of invasion (Lochter et al., 1997; Belien et al., 1999; Deryugina et al., 1997; Polette and Birembaut, 1998). Furthermore, MMP-2 and MMP-14 cleave lami‐ nin-5 leading to cell motility (Koshikawa et al., 2000). Proteolytic cleavage of CD44 as well as integrin αv subunit by MMP-14 promotes cell migration (Kajita et al., 2001; Deryugina, 2001). Recently, MT-MMP1 has been identified as a downstream target of the β-catenin/ Tcf4 complex in colorectal cancers, suggesting that E-cadherin-catenin signaling is impor‐ tant in regulating MT-MMP1 expression (Takahashi et al., 2002). Interestingly, MMP-14 has recently been shown to function as an integrin convertase promoting cell adhesion, migration and focal adhesion kinase phosphorylation of breast cancer cells (Ratnikov et al., 2002). These findings suggest that MMP-14 may be important in regulating cross-talk between integrin and cell-adhesion molecules. MMP-3 as well as MMP-7 cleaves E-cadher‐ in leading to tumor progression (Noe et al., 2001). The newly released E-cadherin cleav‐ age product could interfere with another unprocessed E-cadherin molecule such that Ecadherin function is impaired and, as a result, tumor-cell invasion ensues. Taken together, MMPs are important in many aspects of tumor progression in addition to tumor cell mi‐ gration and invasion.

#### **6.6. Role of MMP in prostate cancer**

ECM at the injured site. The level as well as the tissue-specificity of MMPs can determine the degree of wound repair. For example, MMP-7 is the only MMP expressed by lung epi‐ thelial cells under conditions of tracheal damage (Dunsmore et al., 1998). In contrast, more than one MMP is required for epithelial cell migration during normal wound repair (Sud‐ beck et al., 1997). While different levels of MMP-1, -2, and –9 have been detected at the wound site, neutrophil-derived MMP-8 is the primary collagenase present in normal healing wounds. However, unregulated expression of MMP-8 is associated with chronic leg ulcers (Armstrong and Jude, 2002; Nwomeh et al., 1999). Mammary gland development and invo‐ lution is another example of a physiological process that requires tightly regulated expres‐ sion of MMPs (Lund et al., 1996).  MMPs are also associated with tumor progression and con‐ tribute to tumor invasion and metastasis. MMPs are associated with five principal processes promoting tumor progression (Egeblad and Werb, 2002). First, MMPs can pro‐ mote cancer cell proliferation by three known mechanisms. These include release of cellmembrane-bound precursors of some growth factors, such as TGF-α, degradation of ECM proteins resulting in the release of peptide growth factors, or indirect proliferative signals through integrins. Second, MMPs regulate apoptosis as well as anti-apoptosis. MMP-3, -7, -9 and –11 are known to regulate apoptosis involving different signaling processes. Over‐ expression of MMP-3 is known to induce apoptosis in mammary epithelial cells by de‐ grading laminin (Alexander et al., 1996a; Witty et al., 1995) and MMP-7 cleaves FAS ligand, a ligand for the death receptor FAS, from its membrane-bound precursor. As a re‐ sult of this cleavage, a pro-apoptotic molecule is released into the surrounding microen‐ vironment (Powell et al., 1999; Mitsiades et al., 2001). MMPs can also induce apoptosis of endothelial cells or epithelial cells by shedding the adhesion molecules VE-cadherin (Her‐ ren et al., 1998), PECAM-1 (Ilan et al., 2001) and E-cadherin (Steinhusen et al., 2001). Third, MMPs are positive regulators of angiogenesis, which is required for tumor growth. MMP-2, -9 and –14 and –19 have been shown to regulate angiogenesis by promoting the availability of factors involved in angiogenesis, such as vascular endothelial growth factor (VEGF), fibroblast growth factor 2 (FGF-2) and TGF-β. These factors are required for en‐ dothelial cell proliferation and migration. Moreover, MMP-2 is required for transition to an angiogenic phenotype in a tumor model (Fang et al., 2000), suggesting that MMPs are important for maintenance of tumor growth and proliferation. Fourth, MMPs allow cancer cells to evade immune surveillance. For example, MMP-9 can cleave interleukin-2 recep‐ tor-a (IL-2Ra) from the surface of activated T lymphocytes, thereby suppressing their pro‐ liferation (Sheu et al., 2001). As a result of this suppression, tumor-specific T lymphocytes cannot infiltrate tumor cells. MMP-11 also generates a cleavage product that allows tumor cells to evade the tumor-targeted activity of natural killer cells. MMP-11 cleaves α1-protei‐ nase-inhibitor, which decreases natural killer cell cytotoxicity (Kataoka et al., 1999). Active

activity is essential for normal cellular processes.

662 Advances in Prostate Cancer

Growth factors and receptor kinases can also influence transcriptional regulation of MMPs. MMPs have been shown to play a significant role in prostate cancer metastasis (Wood et al., 1997; Sehgal et al, 1998; Pajouh et al, 1991; Powell et al, 1993). Moreover, recent evidence suggests an increase in MMP-2 and TIMP-2 ratio is associated with high-grade and highstage prostate tumors (Still et al., 2000). MMP expression could be induced by two possible mechanisms. First, prostate stromal cells could secrete growth factors such as epidermal growth factor (EGF) and induce expression of downstream effectors such as metalloprotei‐ nases. Growth factors and their receptors have been shown to be key components of tumor development and progression (Sundareshan et al., 1999). Epidermal growth factor receptor (EGFR) expression in bladder cancer cells, for example, is associated with high tumor stage and grade (Nutt et al., 1998). EGF has been shown to induce the AP-1 transcriptional regula‐ tory complex, which transcriptionally activates MMP-1 expression and MMP-3 expression in fibroblasts. EGFR stimulation promotes both breast cancer cell migration (Price et al., 1999) and induces MMP-1 expresssion (Nutt and Lunec, 1996). Second, MMP expression is also regulated by E-cadherin expression (Nawrocki-Raby et al., 2003). Restoration of E-cad‐ herin expression in E-cadherin negative Dunning rat prostate tumor cells inhibits *in vitro* invasion and MMP-2 activity in these cells (Luo et al., 1999).

#### **7. Concluding remarks**

The cellular localization of E-cadherin and the catenin proteins has a significant role in regu‐ lating cancer progression. β-, γ- and p120ctn proteins are important components of the E-cad‐ herin-catenin signal transduction pathway. Elucidating the mechanisms of nuclear localization or nuclear retention of β-, γ- and p120ctn proteins, may help us to understand the role of these catenins in regulating E-cadherin downstream signaling events associated with prostate cancer invasion.

nases and their inhibitors at the maternal-embryonic boundary during mouse em‐

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#### **Acknowledgements**

This project was supported by a grant from NIH (CA97132) to JSN. The authors wish to thank Dr. Christina Voelkel-Johnson and Lucille London for carefully reading the manuscript.

#### **Author details**

Anuradha K. Murali and James S. Norris

\*Address all correspondence to<EMAIL_ADDRESS>
Microbiology and Immunology, Medical University of South Carolina, Charleston, USA

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**7. Concluding remarks**

664 Advances in Prostate Cancer

prostate cancer invasion.

**Acknowledgements**

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**Author details**

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Anuradha K. Murali and James S. Norris

\*Address all correspondence to<EMAIL_ADDRESS>
nal of Cell Science, 107, 3655-3663.

The cellular localization of E-cadherin and the catenin proteins has a significant role in regu‐ lating cancer progression. β-, γ- and p120ctn proteins are important components of the E-cad‐ herin-catenin signal transduction pathway. Elucidating the mechanisms of nuclear localization or nuclear retention of β-, γ- and p120ctn proteins, may help us to understand the role of these catenins in regulating E-cadherin downstream signaling events associated with

This project was supported by a grant from NIH (CA97132) to JSN. The authors wish to thank Dr. Christina Voelkel-Johnson and Lucille London for carefully reading the

Microbiology and Immunology, Medical University of South Carolina, Charleston, USA

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692 Advances in Prostate Cancer

## *Edited by Gerhard Hamilton*

Prostate cancer is one of the most common types of cancer in men and its treatment was constricted to surgery for confined state and androgen ablation for advanced disease until new options have become available. The present book covers a broad range of novel aspects of prostate cancer diagnosis, treatment and patient care, as well as new research on relevant cell biology. In detail, this special volume focusses on supportive modalities for prostate cancer patients, appropriate selection of novel therapeutic regimens, including inhibitors of steroidal synthesis, cytotoxic agents, as well as intermittent androgen suppression and the roles of prostate cancer stem cells and inflammatory processes.

Photo by wildpixel / iStock

Advances in Prostate Cancer

Advances in Prostate Cancer

*Edited by Gerhard Hamilton*