Role of matrix metalloproteinases in melanoma cell invasion

Hofmann, U.; Houben, Roland; Bröcker, Eva‐B.; Becker, Jürgen C.

doi:10.1016/j.biochi.2005.01.013

Cited by 149 publications

(160 citation statements)

References 85 publications

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“…Furthermore, it is well-established that melanoma cell invasion depends on MMP expression and activity especially MMP-2 and MMP-9 (26). Both MMP are highly expressed in melanoma cells, and a direct relationship between melanoma progression and MMP expression and activity has been well-established in many studies (26). Moreover, inhibition of MMP activity has been previously investigated as a new therapeutic strategy to control metastatic spreading.…”

Section: Discussionmentioning

confidence: 99%

Metformin Blocks Melanoma Invasion and Metastasis Development in AMPK/p53-Dependent Manner

Cerezo

Tichet

Abbe

et al. 2013

Molecular Cancer Therapeutics

181

139

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Metformin was reported to inhibit the proliferation of many cancer cells, including melanoma cells. In this report, we investigated the effect of metformin on melanoma invasion and metastasis development. Using different in vitro approaches, we found that metformin inhibits cell invasion without affecting cell migration and independently of antiproliferation action. This inhibition is correlated with modulation of expression of proteins involved in epithelial-mesenchymal transition such as Slug, Snail, SPARC, fibronectin, and Ncadherin and with inhibition of MMP-2 and MMP-9 activation. Furthermore, our data indicate that this process is dependent on activation of AMPK and tumor suppressor protein p53. Finally, we showed that metformin inhibits melanoma metastasis development in mice using extravasation and metastasis models. The presented data reinforce the fact that metformin might be a good candidate for clinical trial in melanoma treatment.

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Section: Discussionmentioning

confidence: 99%

Metformin Blocks Melanoma Invasion and Metastasis Development in AMPK/p53-Dependent Manner

Cerezo

Tichet

Abbe

et al. 2013

Molecular Cancer Therapeutics

181

139

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“…Distant metastasis is associated with degradation of basement membranes and remodeling of the extracellular matrix (ECM) by matrix metalloproteinases (MMPs),that operates with a large number of non-matrix proteins necessary for neo angiogenesis, MMPs concentration are observed to be low in many invasive, metastatic tumors. The potent anti tumorigenic activity of apo A-I is attributed to inhibition of tumor-associated angiogenesis and concomitant reduction in MMP-9 protein levels and activity, a critical matrix degrading enzyme whose action culminates in the availability of pro-angiogenic factors [45].…”

Section: Anti Tumor Activity Of Apo A-imentioning

confidence: 99%

Apolipoprotein A-I: A Molecule of Diverse Function

2015

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“…1 The neovascularisation process is sustained by the secretion of various angiogenic cytokines [i.e., vascular endothelial growth factor A (VEGF-A), fibroblast growth factor 2, placental growth factor 1 and -2, interleukin 8 and transforming growth factor 1], integrin overexpression and release of high amounts of metalloproteinases (MMPs). 2,3 Highly malignant cells, because of their ability to dedifferentiate and acquire characteristics of other cell types, form de novo vascular networks (vasculogenic mimicry), the presence of which predicts poor prognosis in melanoma patients. 4 This mechanism, that can contribute to new vessel formation and favour tumour growth and invasion, has been extensively studied utilizing melanoma cell lines, although it is also observed in a variety of other tumour types, including carcinomas, sarcomas, glioblastoma and astrocytoma.…”

mentioning

confidence: 99%

Cilengitide downmodulates invasiveness and vasculogenic mimicry of neuropilin 1 expressing melanoma cells through the inhibition of αvβ5 integrin

Ruffini

Graziani

Levati

et al. 2014

Intl Journal of Cancer

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During melanoma progression, tumour cells show increased adhesiveness to the vascular wall, invade the extracellular matrix (ECM) and frequently form functional channels similar to vascular vessels (vasculogenic mimicry). These properties are mainly mediated by the interaction of integrins with ECM components. Since we had previously identified neuropilin 1 (NRP-1), a coreceptor of vascular endothelial growth factor A (VEGF-A), as an important determinant of melanoma aggressiveness, aims of this study were to identify the specific integrins involved in the highly invasive phenotype of NRP-1 expressing cells and to investigate their role as targets to counteract melanoma progression. Melanoma aggressiveness was evaluated in vitro as cell ability to migrate through an ECM layer and to form tubule-like structures using transfected cells. Integrins relevant to these processes were identified using specific blocking antibodies. The avb5 integrin was found to be responsible for about 80% of the capability of NRP-1 expressing cells to adhere on vitronectin. In these cells avb5 expression level was twice higher than in low-invasive control cells and contributed to the ability of melanoma cells to form tubule-like structures on matrigel. Cilengitide, a potent inhibitor of am integrins activation, reduced ECM invasion, vasculogenic mimicry and secretion of VEGF-A and metalloproteinase 9 by melanoma cells. In conclusion, we demonstrated that amb5 integrin is involved in the highly aggressive phenotype of melanoma cells expressing NRP-1. Moreover, we identified a novel mechanism that contributes to the antimelanoma activity of the av integrin inhibitor cilengitide based on the inhibition of vasculogenic mimicry.

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Role of matrix metalloproteinases in melanoma cell invasion

Cited by 149 publications

References 85 publications

Metformin Blocks Melanoma Invasion and Metastasis Development in AMPK/p53-Dependent Manner

Metformin Blocks Melanoma Invasion and Metastasis Development in AMPK/p53-Dependent Manner

Apolipoprotein A-I: A Molecule of Diverse Function

Cilengitide downmodulates invasiveness and vasculogenic mimicry of neuropilin 1 expressing melanoma cells through the inhibition of αvβ5 integrin

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