Regulation of membrane type-matrix metalloproteinases

Hernandez-Barrantes, Sonia; Bernardo, M. Margarida; Tóth, Márta; Fridman, Rafael

doi:10.1006/scbi.2001.0421

Cited by 159 publications

(133 citation statements)

References 64 publications

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“…PMA treatment increased the levels of the degraded MT1-MMP in HT1080 cells. The existence of these full-length and degraded species of MT1-MMP is in agreement with our earlier findings (28) and the results published by others (32). Importantly, these data, which agree well with those of the MMP-2 activation studies, indicate similar levels of the full-length, catalytically potent MT1-MMP in HT1080 and MCF-MT cells.…”

Section: Transfected Breast Carcinoma Cells Express Physiologicallysupporting

confidence: 93%

“…MCF7 cells were supplemented in these assays with external pro-MMP-2 in amounts that were similar to those naturally synthesized by HT1080 cells. To promote the activation of MMP-2, HT1080 cells were stimulated with PMA (5 ng/ml) (31,32). Our data indicate that the efficiency of MMP-2 activation by the transfected MCF-MT cells is highly similar to that of HT1080 cells (Fig.…”

Section: Transfected Breast Carcinoma Cells Express Physiologicallysupporting

confidence: 51%

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Cellular Membrane Type-1 Matrix Metalloproteinase (MT1-MMP) Cleaves C3b, an Essential Component of the Complement System

Rozanov

Savinov

Golubkov

et al. 2004

Journal of Biological Chemistry

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Section: Transfected Breast Carcinoma Cells Express Physiologicallysupporting

confidence: 93%

Section: Transfected Breast Carcinoma Cells Express Physiologicallysupporting

confidence: 51%

Cellular Membrane Type-1 Matrix Metalloproteinase (MT1-MMP) Cleaves C3b, an Essential Component of the Complement System

Rozanov

Savinov

Golubkov

et al. 2004

Journal of Biological Chemistry

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“…MT-MMPs have a well-known function in promoting cell migration, invasion, experimental metastasis and angiogenesis. 39 Therefore, it is not surprising that one of the tumor destructive functions of TNF/IFNg could be downregulation of two of the most important membrane associated MMPs. Unlike TIMP-1, TIMP-2 is a strong inhibitor of MMP-14 and MMP-16 and therefore could thus help TNF/IFNg in inhibiting those two MT-MMPs and in destroying the tumor and preventing it to relapse.…”

Section: Discussionmentioning

confidence: 99%

The use of tissue inhibitors of matrix metalloproteinases to increase the efficacy of a tumor necrosis factor/interferonγ antitumor therapy

et al. 2007

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Owing to its impressive ability to kill tumor cells, especially in combination with interferon-g (IFNg), tumor necrosis factor (TNF) is widely appreciated as being a potential systemic therapeutic for the treatment of cancer. On the other hand, owing to its proinflammatory activities, administration of TNF leads to many systemic side effects and eventually to a potentially lethal systemic inflammatory response syndrome (SIRS). However, systemic treatment of tumor-bearing mice with TNF/IFNg in combination with BB-94 (a broad-spectrum metalloproteinase inhibitor) confers protection against TNF/IFNg-induced mortality, whereas preserving the antitumor activity. In this study, we investigated the effect of the adenoviral delivery of human tissue inhibitors of matrix metalloproteinase (hTIMP)-1 and hTIMP-2 genes on the outcome of TNF/IFNg antitumor therapy. The dose of adenovirus was limited to 10 8 PFU per mouse owing to the additive toxicity of combining it with TNF/IFNg therapy. Nevertheless, this dose was sufficient to achieve highly efficient adenoviral transfer and expression of hTIMP-1 and hTIMP-2 in the liver, but not the tumor. Treatment with this low dose of AdhTIMP-1 or AdhTIMP-2 was not enough to protect the host against the toxic effects of TNF/IFNg. However, it was sufficient to show a synergistic effect of hTIMPs with TNF/IFNg such that tumors regressed significantly faster. Interestingly, only AdTIMP-2 was able to prevent relapses after treatment.

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“…Each of the individual templates was efficiently transcribed and translated in vitro and generated comparable amounts of the 35 S-labeled MT1-CAT species of the expected size (Fig. 3A).…”

Section: Synthesis Of Mmps In the Cell-free System And C1qmentioning

confidence: 99%

Non-proteolytic, Receptor/Ligand Interactions Associate Cellular Membrane Type-1 Matrix Metalloproteinase with the Complement Component C1q

Rozanov

Sikora

Godzik

et al. 2004

Journal of Biological Chemistry

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Matrix metalloproteinases (MMPs)1 constitute a family of zinc enzymes that are capable of cleaving a wide range of extracellular matrix proteins and soluble and cell surface-associated regulatory proteins (1). MT1-MMP, a prototypic member of a membrane-anchored MMP subfamily, is distinguished from soluble MMPs by the existence of a C-terminal transmembrane domain that associates the protease with the lipid membrane bilayer and a cytoplasmic tail that interacts with the intracellular milieu (2). Currently, six membrane-type MMPs are known: MT1-, MT2-, MT3-, MT4-, MT5-and MT6-MMP (1). In contrast to the soluble MMPs, MT1-MMP is ideally positioned for regulating pericellular proteolysis (3, 4). Our prior studies and the results of other investigations have revealed a key role for MT1-MMP in carcinogenesis and malignancy and demonstrated that MT1-MMP is a likely centerpiece of malignant transformation and that MT1-MMP contributes directly to tumor cell migration, invasion, and metastasis (5-9). Proteolysis of matrix alone, however, does not fully explain the important and unique role of MT1-MMP in tumor growth and malignant progression and, in particular, in metastasis.

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Regulation of membrane type-matrix metalloproteinases

Cited by 159 publications

References 64 publications

Cellular Membrane Type-1 Matrix Metalloproteinase (MT1-MMP) Cleaves C3b, an Essential Component of the Complement System

Cellular Membrane Type-1 Matrix Metalloproteinase (MT1-MMP) Cleaves C3b, an Essential Component of the Complement System

The use of tissue inhibitors of matrix metalloproteinases to increase the efficacy of a tumor necrosis factor/interferonγ antitumor therapy

Non-proteolytic, Receptor/Ligand Interactions Associate Cellular Membrane Type-1 Matrix Metalloproteinase with the Complement Component C1q

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