Significance of Coexpression of Urokinase-type Plasminogen Activator, and Matrix Metalloproteinase 3 (Stromelysin) and 9 (Gelatinase B) in Colorectal Carcinoma

Inuzuka, Kiyohisa; Osuga, Yutaka; Nagase, Hideaki; Shirouzu, Kazuo

doi:10.1006/jsre.2000.5952

Cited by 44 publications

(34 citation statements)

References 21 publications

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“…MMP-3 degrades many non-collagenous matrix components, such as fibronectin, laminin, but also denatured collagens and native collagens type III, IV and V 45 , and proteolytically activates interstitial procollagenase (proMMP-1) and progelatinase B (proMMP-9) to their active zymogens 6,46 .…”

Section: Discussionmentioning

confidence: 99%

Inhibition of Integrin αvβ6 on Cholangiocytes Blocks Transforming Growth Factor-β Activation and Retards Biliary Fibrosis Progression

et al. 2008

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Section: Discussionmentioning

confidence: 99%

Inhibition of Integrin αvβ6 on Cholangiocytes Blocks Transforming Growth Factor-β Activation and Retards Biliary Fibrosis Progression

et al. 2008

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“…Increased co-expression of MMP-3 and MMP-9 has been found in colorectal tumors. Co-expression of uPA with MMP-9 in colorectal cancers is responsible for the activation of plasminogen to plasmin [41] . Plasmin stimulates proMMP-3 to active MMP-3 which in turn promotes proMMP-9 to active MMP-9, thus, resulting in colorectal cancer progression [41] .…”

Section: Role Of Specific Mmps In Colorectal Cancermentioning

confidence: 99%

“…Co-expression of uPA with MMP-9 in colorectal cancers is responsible for the activation of plasminogen to plasmin [41] . Plasmin stimulates proMMP-3 to active MMP-3 which in turn promotes proMMP-9 to active MMP-9, thus, resulting in colorectal cancer progression [41] . Excess MMP-9 expression in colorectal cancer contributes to the inflammation related to neoplasms but not to aggressive tumors [42] .…”

Section: Role Of Specific Mmps In Colorectal Cancermentioning

confidence: 99%

Matrix metalloproteinases and gastrointestinal cancers: Impacts of dietary antioxidants

Verma

Kesh

Ganguly

et al. 2014

WJBC

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teinase (TIMP) which bind MMPs with a 1:1 stoichiometry. In addition, RECK (reversion including cysteinerich protein with kazal motifs) is a membrane bound glycoprotein that inhibits MMP-2, -9 and -14. Moreover, α2-macroglobulin mediates the uptake of several MMPs thereby inhibit their activity. Cancerous conditions increase intrinsic reactive oxygen species (ROS) through mitochondrial dysfunction leading to altered protease/ anti-protease balance. ROS, an index of oxidative stress is also involved in tumorigenesis by activation of different MAP kinase pathways including MMP induction. Oxidative stress is involved in cancer by changing the activity and expression of regulatory proteins especially MMPs. Epidemiological studies have shown that high intake of fruits that rich in antioxidants is associated with a lower cancer incidence. Evidence indicates that some antioxidants inhibit the growth of malignant cells by inducing apoptosis and inhibiting the activity of MMPs. This review is discussed in six subchapters, as follows. AbstractThe process of carcinogenesis is tightly regulated by antioxidant enzymes and matrix degrading enzymes, namely, matrix metalloproteinases (MMPs). Degradation of extracellular matrix (ECM) proteins like collagen, proteoglycan, laminin, elastin and fibronectin is considered to be the prerequisite for tumor invasion and metastasis. MMPs can degrade essentially all of the ECM components and, most MMPs also substantially contribute to angiogenesis, differentiation, proliferation and apoptosis. Hence, MMPs are important regulators of tumor growth both at the primary site and in distant metastases; thus the enzymes are considered as important targets for cancer therapy. The implications of MMPs in cancers are no longer mysterious; however, the mechanism of action is yet to be explained. Herein, our major interest is to clarify how MMPs are tied up with gastrointestinal cancers. Gastrointestinal cancer is a variety of cancer types, including the cancers of gastrointestinal tract and organs, i.e., esophagus, stomach, biliary system, pancreas, small intestine, large intestine, rectum and anus. The activity of MMPs is regulated by its endogenous inhibitor tissue inhibitor of metallopro-

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“…12 MMP-3 may be able to activate proMMP-9 in colorectal carcinoma resulting in cancer progression and metastasis. 13 MMP-3 is synthesized both by tumor and peritumoral stromal cells in human invasive breast carcinomas but its expression levels are approximately the same as in normal breast epithelia. 14 In mice, MMP-3 can act as a natural mammary tumor promoter.…”

mentioning

confidence: 97%

High expression levels of collagenase‐1 and stromelysin‐1 correlate with shorter disease‐free survival in human metastatic melanoma

Nikkola

Vihinen

Vlaykova

et al. 2001

Intl Journal of Cancer

119

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Matrix metalloproteinases (MMPs) are proteolytic enzymes capable of degrading extracellular matrix. Their role has been emphasized in tumor invasion, metastasis and tumor-induced angiogenesis. We studied the expression of collagenase-1 (MMP-1), stromelysin-1 (MMP-3) and collagenase-3 (MMP-13) in 70 melanoma metastases obtained from 56 patients treated with combined chemoimmunotherapy. The patients were divided into 2 groups using a cut-off point of 0% for MMP-1 expression and 20% for MMP-3 expression. We found that patients with MMP-1 positive metastases (n ‫؍‬ 38) had significantly shorter disease-free survival compared to patients with MMP-1 negative metastases (n ‫؍‬ 18) (median 11.2 vs. 17.0 months, p ‫؍‬ 0.0383). The disease-free survival of patients with high levels of MMP-3 expression in their metastases (>20% positive tumor cells, n ‫؍‬ 14) was also significantly shorter compared to patients with lower levels of expression (n ‫؍‬ 42) (median 5.1 vs. 14.0 months, p ‫؍‬ 0.0294). The expression of MMP-13 did not correlate to survival parameters. We also found that the presence of melanin, a pigment produced by melanocytes, correlated with high expression levels of MMP-1 (p ‫؍‬ 0.0002), MMP-3 (p < 0.0001) and MMP-13 (p ‫؍‬ 0.0009). The high expression levels of MMP-13 were also associated with the presence of visceral metastases (p ‫؍‬ 0.0284). Our findings suggest that MMP-1 and -3 may have a special role in melanoma metastasis formation and thus they could be used to measure the biological activity of the disease. © 2002 Wiley-Liss, Inc. Key words: MMP-1; MMP-3; MMP-13; melanin; metastatic melanoma; disease-free survivalMatrix metalloproteinases (MMPs) are a family of zinc-dependent neutral endopeptidases that can degrade essentially all extracellular matrix components. At present, the human MMP gene family contains 21 members that can be divided into subgroups of collagenases, gelatinases, stromelysins, membrane-type MMPs (MT-MMPs) and novel MMPs according to their substrate specificity and primary structure. 1,2 There are specific tissue inhibitors of metalloproteinases (TIMPs) that can inhibit the activity of MMPs. The balance between MMPs and their inhibitors is essential in many physiological conditions as well as in pathological conditions such as rheumatoid arthritis, atherosclerosis, tumor invasion, metastasis and tumor-induced neovascularization. 3,4 Members of the collagenase subgroup, i.e., collagenase-1 (MMP-1), collagenase-2 (MMP-8) and collagenase-3 (MMP-13), are only neutral proteinases capable of degrading native fibrillar collagens of types I, II, III and V. After initial cleavage by collagenases followed by denaturation the fibrillar collagens are further degraded by gelatinases. MMP-13 has exceptionally wide substrate specificity compared to other MMPs. In addition to native fibrillar collagens it degrades type IV, X and XIV collagens, tenascin, fibronectin and the aggrecan core protein. 2 Stromelysin-1 (MMP-3) was one of the first proteinases found to be associated with cancer. 5 MMP-3 ...

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Significance of Coexpression of Urokinase-type Plasminogen Activator, and Matrix Metalloproteinase 3 (Stromelysin) and 9 (Gelatinase B) in Colorectal Carcinoma

Cited by 44 publications

References 21 publications

Inhibition of Integrin αvβ6 on Cholangiocytes Blocks Transforming Growth Factor-β Activation and Retards Biliary Fibrosis Progression

Inhibition of Integrin αvβ6 on Cholangiocytes Blocks Transforming Growth Factor-β Activation and Retards Biliary Fibrosis Progression

Matrix metalloproteinases and gastrointestinal cancers: Impacts of dietary antioxidants

High expression levels of collagenase‐1 and stromelysin‐1 correlate with shorter disease‐free survival in human metastatic melanoma

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