Contribution of matrilysin (MMP-7) to the metastatic pathway of human colorectal cancers

Adachi, Yasushi; Yamamoto, Hiroyuki; Itoh, Fumio; Hinoda, Yuji; Okada, Yasunori; Imai, Kohzoh

doi:10.1136/gut.45.2.252

Cited by 205 publications

(141 citation statements)

References 31 publications

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“…In the immunohistochemical detection of MMPs the focus has been on the analysis of MMP localisation. Correlations have been described between MMP-1 immunoreactivity and survival (Murray et al, 1996) and also between stage of disease and immunoreactivity for MMP-1 (Shiozawa et al, 2000), MMP-2 (Levy et al, 1991) and MMP-7 (Adachi et al, 1999). These studies measure MMP immunoreactivity without discrimination between latent proenzyme and activated enzyme.…”

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Tissue levels of active matrix metalloproteinase-2 and -9 in colorectal cancer

Waas

Lomme

DeGroot³

et al. 2002

Br J Cancer

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The bioactivity of matrix metalloproteinases was studied in tissues from colorectal cancer patients by means of both quantitative gelatin zymography and a fluorometric activity assay. Next to paired samples of tumour tissue and distant normal mucosa (n=73), transitional tissue was analysed from a limited (n=33) number of patients. Broad-spectrum matrix metalloproteinase activity and both the active and latent forms of the gelatinases matrix metalloproteinase-2 and -9 were higher in tumour than in normal mucosa. The ratio's between active and latent forms of matrix metalloproteinase-2 and -9 were highest in tumour tissue and normal mucosa, respectively. Matrix metalloproteinase-2 levels, both active and latent forms, correlated inversely with stage of disease, the tumours without synchronous distant metastases containing significantly (P=0.005) more active matrix metalloproteinase-2 than the others. At much lower levels of activity, the same trend was observed in distant normal mucosa. The level of latent form of matrix metalloproteinase-9 in tumour depended on tumour location. Neither the active form of matrix metalloproteinase-9 nor broad-spectrum matrix metalloproteinase activity in tumour tissue did correlate with any of the clinicopathological parameters investigated. The results demonstrate explicit differences between the activity of matrix metalloproteinase-2 and -9, indicating different roles for both gelatinases in tumour progression. Such data are necessary in order to develop rational anti-cancer therapies based on inhibition of specific matrix metalloproteinases.

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confidence: 99%

Tissue levels of active matrix metalloproteinase-2 and -9 in colorectal cancer

Waas

Lomme

DeGroot³

et al. 2002

Br J Cancer

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“…Matrilysin (MMP-7) is a member of the MMP gene family, and has proteolytic activity against a wide spectrum of substrates such as collagens, proteoglycans, elastin, laminin, fibronectin and casein (Woessner and Taplin, 1988;Miyazaki et al, 1990;Wilson and Matrisian, 1996). It is produced by malignant tumour cells such as oesophageal, gastric, colorectal, head and neck, lung, prostate and hepatocellular carcinomas (Yamamoto et al, 1997;Adachi et al, 1998;Yamashita et al, 1998;Adachi et al, 1999;Babletz et al, 1999;Yamamoto et al, 1999). Immunohistochemical studies have shown that the expression of matrilysin correlates significantly with nodal or distant metastasis in gastric and colorectal carcinomas (Adachi et al, 1998Yamashita et al, 1998).…”

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confidence: 99%

Matrilysin (MMP-7) as a significant determinant of malignant potential of early invasive colorectal carcinomas

et al. 2001

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Summary Matrix metalloproteinases play a crucial role in tumour invasion and mestasis. Matrilysin (MMP-7) has been shown to correlate with nodal or distant metastasis in colorectal carcinomas; however, its implication in early invasive colorectal carcinomas has not been determined. This study was undertaken to clarify the association of matrilysin expression with clinicopathologic parameters in early invasive colorectal carcinomas. 38 early invasive colorectal carcinomas treated by local excision or radical surgery were examined. Tumour budding was evaluated as the number of dedifferentiation units along the entire invasive margin. Matrilysin protein levels were determined using immunohistochemical study. Univariate analysis showed that matrilysin expression alone was significantly associated with distant metastasis (P = 0.0339), and both tumour budding and matrilysin expression were significantly associated with adverse outcome (P = 0.0005, 0.0341). Histological differentiation, vessel invasion, and depth of invasion were not significantly associated with either distant metastasis or adverse outcome. Multivariate analysis confirmed that tumour budding and matrilysin expression were independently associated with adverse outcome, although the significance of matrilysin expression was marginal (P = 0.0488). Tumour budding at the invasive margin and matrilysin expression are more useful in identifying high-risk groups for adverse outcome in patients with early invasive colorectal carcinomas.

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“…15,29 MMP-7 is constitutively expressed in exocrine and mucosal epithelial cells in the skin, pancreas, liver, breast, intestine, and lung. In cancers of the colon, [30][31][32][33] esophagus, 34 stomach, [34][35][36] pancreas, 37 breast 38 and prostate, 39 increased MMP-7 expression is associated with tumor invasion, cancer progression, and poor prognosis. Two mechanisms may be responsible for the enhancement of cancer invasion and metastasis by MMP-7: direct effects of MMP-7 proteinase activity and indirect effects of MMP-7, such as activation of MMP-2 and MMP-9.…”

Section: Discussionmentioning

confidence: 99%

Active matrix metalloproteinase-7 is associated with invasion in buccal squamous cell carcinoma

Chuang

Huang

et al. 2008

Modern Pathology

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Protein microarrays have shown that matrix metalloproteinase-7 is upregulated in head and neck squamous cell carcinomas, but its role in local tissue invasion is still uncertain. We investigated the expression of active matrix metalloproteinase-7, using tissue microarray, immunohistochemistry, and western blotting, in oral tissues from 24 patients with buccal squamous cell carcinoma, and correlated the findings with clinicopathological features. Normal buccal tissue samples from the same patients, obtained at sites at least 1 cm from tumor tissue, served as normal controls. Total matrix metalloproteinase-7 was detected on western blots in 9 of 15 (60%) tumor tissue samples and in 2 of 15 (13%) normal mucosal samples; this difference was significant (P ¼ 0.008). Moreover, the active matrix metalloproteinase-7 was expressed only in eight of the nine (89%) tumor samples that expressed matrix metalloproteinase-7, and in none of the normal tissue samples, regardless of the expression status of the pro-matrix metalloproteinase-7. Immunostaining of matrix metalloproteinase-7 was observed histologically in both tumor and nonneoplastic epithelium, but immunostaining of active matrix metalloproteinase-7 was present only in tumor nests. Expression of active matrix metalloproteinase-7 was associated with larger tumor size (P ¼ 0.022) and was significantly higher in buccal squamous cell carcinoma with adjacent skin or bone invasion (P ¼ 0.036). In conclusion, active matrix metalloproteinase-7 expression was associated with more aggressive buccal squamous cell carcinomas.

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Contribution of matrilysin (MMP-7) to the metastatic pathway of human colorectal cancers

Cited by 205 publications

References 31 publications

Tissue levels of active matrix metalloproteinase-2 and -9 in colorectal cancer

Tissue levels of active matrix metalloproteinase-2 and -9 in colorectal cancer

Matrilysin (MMP-7) as a significant determinant of malignant potential of early invasive colorectal carcinomas

Active matrix metalloproteinase-7 is associated with invasion in buccal squamous cell carcinoma

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