The distribution of matrix metalloproteinases and tissue inhibitor of metalloproteinases in colorectal cancer

Gallegos, Nicolas; Smales, Caroline; Savage, F; Hembry, Rosalind M.; Boulos, PB

doi:10.1016/s0960-7404(10)80015-5

Cited by 18 publications

(6 citation statements)

References 31 publications

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“…In our study, we were unable to detect mRNA for MMP-2 and TIMP-2 in the prostatic stroma. Studies examining MMP and TIMP expression in other tissues indicate that the majority of human malignancies, including ovarian, colorectal, bladder, breast, and both basal-and squamous-cell carcinomas of the skin, express both MMP-2 and TIMP-2 predominantly within the stromal compartment, particularly in areas of tumor-related stroma [17][18][19][20][21][22][23]29,30]. Our findings, however, are not inconsistent with other observations.…”

Section: Discussionsupporting

confidence: 42%

“…The main component of the basement membrane is type IV collagen, and therefore the type IV collagenases (MMP-2, MMP-9) which degrade type IV collagen may play a role in metastasis. MMP-2 has been associated with aggressive disease in a number of tumors including ovarian tumors, colorectal cancers, bladder cancer, breast cancer, and both basal-and squamous-cell carcinomas of the skin [17][18][19][20][21][22][23].…”

Section: Discussionmentioning

confidence: 99%

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Localization and quantification of mRNA for matrix metalloproteinase-2 (MMP-2) and tissue inhibitor of matrix metalloproteinase-2 (TIMP-2) in human benign and malignant prostatic tissue

et al. 2000

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BACKGROUND. The family of matrix metalloproteinases (MMPs) has been shown to be involved in proteolytic degradation of the extracellular matrix, which is an essential step in tumor invasion and metastasis. MMPs are tightly regulated by the levels of active enzymes and their inhibitors, the tissue inhibitors of metalloproteinases (TIMPs). MMP-2 and its ratio to TIMP-2 have been associated with tumor recurrence and progression in a number of human malignancies. METHODS. We examined the relationship between MMP-2 and TIMP-2 mRNA expression in 42 men with malignant (n = 32) and benign (n = 10) prostates using nonisotopic in situ hybridization and Northern blot analysis. RESULTS. mRNA for MMP-2 and TIMP-2 was localized to the malignant epithelial cells of both high-and low-grade tumors in the periphery of the glands and in areas of extracapsular involvement, and to the glandular epithelium in the benign prostates. Using Northern blot analysis, the mean MMP-2 to TIMP-2 ratio was approximately one in the benign prostates and low-grade and -stage cancers. The MMP-2 to TIMP-2 ratio increased to 3.3 in the high-grade and 2.8 in the high-stage tumors. CONCLUSIONS. The results suggest a close association between MMP-2/TIMP-2 expression and local tumor invasion, with a disruption in expression of the two genes leading to disease progression. Future studies should focus on the activity of these enzymes and on the ratio of enzyme/inhibitor expression, which may become a useful prognostic marker in prostate cancer.

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Section: Discussionsupporting

confidence: 42%

Section: Discussionmentioning

confidence: 99%

Localization and quantification of mRNA for matrix metalloproteinase-2 (MMP-2) and tissue inhibitor of matrix metalloproteinase-2 (TIMP-2) in human benign and malignant prostatic tissue

et al. 2000

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“…mors, most reports focus on a single class of proteases (1)(2)(3)(4)(5)(6)(7)(8). A variety of techniques to detect proteases were used, making comparisons among the studies difficult and data reported from different studies often inconsistent.…”

Section: Introductionmentioning

confidence: 99%

A Functional Proteomics Screen of Proteases In Colorectal Carcinoma

McKerrow

Bhargava

Hansell

et al. 2000

Mol Med

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Background: Proteases facilitate several steps in cancer progression. To identify proteases most suitable for drug targeting, actual enzyme activity and not messenger RNA levels or immunoassay of protein is the ideal assay readout. Materials and Methods: An automated microtiter plate assay format was modified to allow detection of all four major classes of proteases in tissue samples. Fifteen sets of colorectal carcinoma biopsies representing primary tumor, adjacent normal colon, and liver metastases were screened for protease activity. Results: The major proteases detected were matrix metalloproteases (MMP9, MMP2, and MMP1), cathepsin B, cathepsin D, and the mast cell serine proteases, tryptase and chymase. Matrix metalloproteases were expressed at higher levels in the primary tumor than in adjacent normal tissue. The mast cell proteases, in contrast, were at very high levels in adjacent normal tissue, and not detectable in the metastases. Cathepsin B activity was significantly higher in the primary tumor, and highest in the

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“…11,12 Increased activity of MMP-3 has been reported in neoplastic conditions of humans such as breast cancer, oral squamous cell carcinomas, colorectal cancer, and pulmonary carcinomas. 31,33,34,36,37 In a model that involved the use of mice, MMP-3 was expressed in stromal cells surrounding tumors, and conversion of tumors to highly malignant forms was associated with the expression of MMP-3 mRNA in tumor cells. 29 Similar amounts of MMP-3 immunoreactivity in chondrosarcomas and chondromas of dogs found in the study reported here indicated that MMP-3 may not be involved in invasion and metastasis.…”

Section: Discussionmentioning

confidence: 99%

“…24,38,39 Because of its strong ability to hydrolyze type-II collagen and its origin in chondrocytes, MMP-13 has been targeted for diagnostic and therapeutic modalities in various arthropathies, including osteoarthritis. 9 Several studies [16][17][18]36,40,41 have revealed that MMP-13 expression is associated with invasive and metastatic tumors, including carcinomas of the breast, head, and neck, malignant melanomas, and chondrosarcomas. Those studies highlighted a role for MMP-13 in malignancy of tumors.…”

Section: Discussionmentioning

confidence: 99%

Immunohistochemical analysis of matrix metalloproteinase-1, -3, and -13 in naturally occurring cartilaginous tumors of dogs

Kuroki¹,

Kreeger²,

Cook³

et al. 2002

ajvr

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The distribution of matrix metalloproteinases and tissue inhibitor of metalloproteinases in colorectal cancer

Cited by 18 publications

References 31 publications

Localization and quantification of mRNA for matrix metalloproteinase-2 (MMP-2) and tissue inhibitor of matrix metalloproteinase-2 (TIMP-2) in human benign and malignant prostatic tissue

Localization and quantification of mRNA for matrix metalloproteinase-2 (MMP-2) and tissue inhibitor of matrix metalloproteinase-2 (TIMP-2) in human benign and malignant prostatic tissue

A Functional Proteomics Screen of Proteases In Colorectal Carcinoma

Immunohistochemical analysis of matrix metalloproteinase-1, -3, and -13 in naturally occurring cartilaginous tumors of dogs

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