Characterization of matrix metalloproteinase-26, a novel metalloproteinase widely expressed in cancer cells of epithelial origin

Марченко, Г. Н.; Ratnikov, Boris I.; Rozanov, Dmitry V.; Godzik, Adam; Deryugina, Elena I.; Strongin, Alex Y.

doi:10.1042/bj3560705

Cited by 86 publications

(60 citation statements)

References 36 publications

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“…Endometase/matrilysin-2 (MMP-26) is a member of the MMP family recently cloned by our group and others [7][8][9][10]. MMP-26 is one of the two smallest members of this family, exhibiting minimal domain structure consisting of a catalytic domain and a prodomain, which maintains the enzyme in a latent form prior to its activation.…”

Section: Introductionmentioning

confidence: 99%

“…MMP-26 is one of the two smallest members of this family, exhibiting minimal domain structure consisting of a catalytic domain and a prodomain, which maintains the enzyme in a latent form prior to its activation. Once active, MMP-26 has been shown to cleave multiple components of the ECM, including fibronectin, type IV collagen, vitronectin, gelatins, and fibrinogen, as well as non ECM proteins such as insulin-like growth factor-binding protein-1 and α-1 protease inhibitor [7][8][9][10][11]. MMP-26 is also able to activate progelatinase B (pro-MMP-9), an enzyme that plays a critical role in ECM remodeling [12].…”

Section: Introductionmentioning

confidence: 99%

“…MMP-26 mRNA is primarily expressed in epithelial cancers, such as lung, breast, endometrial, and prostate carcinomas [7][8][9][10]. Our previous studies have shown that MMP-26 expression in human prostate carcinoma is significantly higher than that in prostatitis, benign prostate hyperplasia (BPH), and normal prostate tissue [12].…”

Section: Introductionmentioning

confidence: 99%

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Coordinated peak expression of MMP-26 and TIMP-4 in preinvasive human prostate tumor

et al. 2006

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The identification of novel biomarkers for early prostate cancer diagnosis is highly important because early detection and treatment are critical for the medical management of patients. Disruption in the continuity of both the basal cell layer and basement membrane is essential for the progression of high-grade prostatic intraepithelial neoplasia (HGPIN) to invasive adenocarcinoma in human prostate. The molecules involved in the conversion to an invasive phenotype are the subject of intense scrutiny. We have previously reported that matrix metalloproteinase-26 (MMP-26) promotes the invasion of human prostate cancer cells via the cleavage of basement membrane proteins and by activating the zymogen form of MMP-9. Furthermore, we have found that tissue inhibitor of metalloproteinases-4 (TIMP-4) is the most potent endogenous inhibitor of MMP-26. Here we demonstrate higher (p<0.0001) MMP-26 and TIMP-4 expression in HGPIN and cancer, compared to non-neoplastic acini. Their expression levels are highest in HGPIN, but decline in invasive cancer (p<0.001 for each) in the same tissues. Immunohistochemical staining of serial prostate cancer tissue sections suggests colocalization of MMP-26 and TIMP-4. The present study indicates that MMP-26 and TIMP-4 may play an integral role during the conversion of HGPIN to invasive cancer and may also serve as markers for early prostate cancer diagnosis.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Coordinated peak expression of MMP-26 and TIMP-4 in preinvasive human prostate tumor

et al. 2006

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“…), some of them having important implications in cancer progression. [27][28][29][30][31][32][33][34][35][36] These independent data from the literature therefore suggest that a reorganisation of E-cadherin/b-catenin and an overexpression of MCP-1 in tumour cells are 2 events associated with cancer progression. This prompted us to investigate the potential regulation of MCP-1 by the b-catenin/TCF pathway.…”

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confidence: 99%

Transactivation of MCP‐1/CCL2 by β‐catenin/TCF‐4 in human breast cancer cells

Mestdagt

Polette

Butticè

et al. 2005

Intl Journal of Cancer

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The loss of E-cadherin expression and the translocation of b-catenin to the nucleus are frequently associated with the metastatic conversion of epithelial cells. In the nucleus, b-catenin binds to the TCF/LEF-1 (T-cell factor/ lymphoid enhancer factor) transcription factor family resulting in the activation of several genes, some of them having important implications in tumour progression. In our study, we investigated the potential regulation of monocyte chemotactic protein-1 (MCP-1/CCL2) expression by the b-catenin/TCF pathway. This CC-chemokine has been implicated in tumour progression events such as angiogenesis or tumour associated macrophage (TAM) infiltration. We thus demonstrated that MCP-1 expression correlates with the reorganization of the E-cadherin/b-catenin complexes. Indeed, MCP-1 was expressed by invasive breast cancer cells (MDA-MB-231, BT549 and Hs578T), which do not express E-cadherin but was not produced by noninvasive breast cancer cell lines (MCF7 and T47D) expressing high level of E-cadherin. In addition, the MCP-1 promoter was activated in BT549 breast cancer cells transfected with b-catenin and TCF-4 cDNAs. The MCP-1 mRNA level was similarly upregulated. Moreover, we showed that MCP-1 mRNA was downregulated after transfection with a siRNA against b-catenin in both BT549 and Hs578T cells. Our results therefore identify MCP-1 as a target of the b-catenin/TCF/LEF pathway in breast tumour cells, a regulation which could play a key role in breast tumour progression. ' 2005 Wiley-Liss, Inc.Key words: MCP-1; b-catenin; breast cancer Chemokines constitute a superfamily of proinflammatory cytokines that are implicated in tumour progression, modulating not only host tumour-specific immunological response but also angiogenesis or tumour cell invasion and proliferation. 1-3 Monocyte chemotactic protein-1 (MCP-1) or CCL2 is a CC-chemokine that specifically attracts monocytes and memory T cells. It has been particularly implicated in processes characterized by mononuclear cell infiltration including breast cancer. 4,5 In some models, MCP-1 has been shown to display an antitumoral effect. 6,7 Nevertheless, a large number of studies demonstrate that MCP-1 facilitates tumour progression through its ability to recruit stromal cells including tumour associated macrophages (TAMs) and endothelial cells. 7-10 A pro-angiogenic role of MCP-1 has been demonstrated in many systems, facilitating tumour growth and dissemination. 8,9,11,12 Moreover, a direct effect of MCP-1 on tumour cell migration in vitro has also been described. 13 Recently, Lebrecht et al. 14 have correlated an increased MCP-1 serum level with an advanced breast tumour stage and the presence of lymph node metastasis. In the same way, Amann et al. 15 reported a significant association between MCP-1 urinary levels and tumour stage and grade. They suggested a use of its urinary level as prognosis marker in bladder cancer. The correlation between MCP-1 expression and a poor prognosis was also demonstrated for the squamous cell carcinoma of the oeso...

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“…They have also been found to be actively involved with generating factors that can stimulate tumour cell (Stetler-Stevenson and Yu, 2001) and endothelial migration and angiogenesis needed for tumour formation (John and Tuszynski, 2001). The matrix metalloproteinase family comprises at least 20 zinc dependent endopeptidases clearly identified, with more (up to MMP-26) currently being characterised (Marchenko et al, 2001). Normally they are associated with programmed cellular events such as tissue remodelling, wound healing, uterine and breast involution and organogenesis in development (Chambers and Matrisian, 1997).…”

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confidence: 99%

Role of proteolytic enzymes in human prostate bone metastasis formation: in vivo and in vitro studies

et al. 2002

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Prostate cancers ability to invade and grow in bone marrow stroma is thought to be due in part to degradative enzymes. The formation of prostate skeletal metastases have been reproduced in vitro by growing co-cultures of prostatic epithelial cells in bone marrow stroma. Expression of urokinase plasminogen activator, matrix metalloproteinase 1 and 7 by prostatic epithelial cells were identified using immunocytochemistry. Also, in vivo tissue sections from human prostatic bone marrow metastases were stained. To establish the role of these enzymes on colony formation, inhibitory antibodies directed against urokinase plasminogen activator, matrix metalloproteinase 1 and matrix metalloproteinase 7 were added into primary prostatic epithelial cells and bone marrow stroma co-cultures. All prostatic epithelial cell cultures stained positively for matrix metalloproteinase 1, matrix metalloproteinase 7 and urokinase plasminogen activator. Generally prostatic epithelial cells derived from malignant tissues showed increased staining in comparison to epithelia derived from non-malignant tissue. In agreement with in vitro cocultures, the in vivo tissue sections of prostate bone marrow metastases showed positive staining for all three enzymes. Inhibition studies demonstrated that blocking matrix metalloproteinase 1, matrix metalloproteinase 7 and urokinase plasminogen activator function reduced the median epithelial colony area significantly in bone marrow stroma co-cultures in vitro. Using a human ex-vivo model we have shown that matrix metalloproteinase 1, matrix metalloproteinase 7 and urokinase plasminogen activator play an important role in the establishment of prostatic epithelial cells within bone marrow.

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Characterization of matrix metalloproteinase-26, a novel metalloproteinase widely expressed in cancer cells of epithelial origin

Cited by 86 publications

References 36 publications

Coordinated peak expression of MMP-26 and TIMP-4 in preinvasive human prostate tumor

Coordinated peak expression of MMP-26 and TIMP-4 in preinvasive human prostate tumor

Transactivation of MCP‐1/CCL2 by β‐catenin/TCF‐4 in human breast cancer cells

Role of proteolytic enzymes in human prostate bone metastasis formation: in vivo and in vitro studies

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