MT1-MMP protects breast carcinoma cells against type I collagen-induced apoptosis

Maquoi, Erik; Assent, Delphine; Detilleux, Johann; Péqueux, Christel; Foidart, Jean‐Michel; Noël, Agnès

doi:10.1038/onc.2011.249

Cited by 58 publications

(82 citation statements)

References 63 publications

(74 reference statements)

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“…1E), and adding doxycycline to the growth medium switched off ADAM12 expression (MCF7-A12Dcyt+dox). In contrast to earlier publications (Deryugina et al, 2000;Figueira et al, 2009;Maquoi et al, 2012), we were able to detect equal levels of MMP-14 under all three experimental conditions (Fig. 1E).…”

Section: Mmp-14 Recruitment To the Tumor Cell Surface Is Stimulated Bcontrasting

confidence: 99%

“…MMP-14 is a classical transmembrane metalloproteinase and, like ADAM12, it is upregulated in human cancer (Egeblad and Werb, 2002;Figueira et al, 2009;Jiang et al, 2006;Seiki, 2003;Strongin, 2010) and accelerates tumor progression in mouse models of cancer (Fröhlich et al, 2011;Kveiborg et al, 2005;Maquoi et al, 2012;Perentes et al, 2011;Roy et al, 2011). MMP-14 degrades extracellular matrix components (i.e.…”

Section: Introductionmentioning

confidence: 99%

“…MMP-14 degrades extracellular matrix components (i.e. fibrillar collagen and gelatin), activates enzymes such as MMP-2 and MMP-13, sheds cell surface proteins (Chan et al, 2012;Egeblad and Werb, 2002;Itoh and Seiki, 2006;Koshikawa et al, 2011;Koshikawa et al, 2010), and was recently shown to prevent collagen-induced apoptosis (Maquoi et al, 2012). The activity of MMP-14 is regulated by multiple mechanisms, including activation by cell surface proteins such as tetraspanin CD151 and aVb3 integrins (Deryugina et al, 2004;Gonzalo et al, 2010;Hadler-Olsen et al, 2011;Itoh and Seiki, 2004;Yañez-Mó et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

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ADAM12 redistributes and activates MMP-14, resulting in gelatin degradation, reduced apoptosis, and increased tumor growth

Albrechtsen

Kveiborg

Stautz

et al. 2013

Journal of Cell Science

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SummaryMatrix metalloproteinases (MMPs), in particular MMP-2, MMP-9 and MMP-14, play a key role in various aspects of cancer pathology. Likewise, ADAMs (a disintegrin and metalloproteinases), including ADAM12, are upregulated in malignant tumors and contribute to the pathology of cancers. Here, we show that there is a positive correlation between MMP-14 and ADAM12 expression in human breast cancer. We demonstrated that in 293-VnR and human breast cancer cells expressing ADAM12 at the cell surface, endogenous MMP-14 was recruited to the cell surface, resulting in its activation. Subsequent to this activation, gelatin degradation was stimulated and tumor cell apoptosis was decreased, with reduced expression of the pro-apoptotic proteins BCL2L11 and BIK. The effect on gelatin degradation was abrogated by inhibition of the MMP-14 activity and appeared to be dependent on cell surface aVb3 integrin localization, but neither the catalytic activity of ADAM12 nor the cytoplasmic tail of ADAM12 were required. The significance of ADAM12-induced activation of MMP-14 was underscored by a reduction in MMP-14-mediated gelatin degradation and abolition of apoptosis-protective effects by specific monoclonal antibodies against ADAM12. Furthermore, orthotopic implantation of ADAM12-expressing MCF7 cells in nude mice produced tumors with increased levels of activated MMP-14 and confirmed that ADAM12 protects tumor cells against apoptosis, leading to increased tumor progression. In conclusion, our data suggest that a ternary protein complex composed of ADAM12, aVb3 integrin and MMP-14 at the tumor cell surface regulates the function of MMP-14. This interaction might point to a novel concept for the development of MMP-14-targeting drugs in treating cancer.

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Section: Mmp-14 Recruitment To the Tumor Cell Surface Is Stimulated Bcontrasting

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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ADAM12 redistributes and activates MMP-14, resulting in gelatin degradation, reduced apoptosis, and increased tumor growth

Albrechtsen

Kveiborg

Stautz

et al. 2013

Journal of Cell Science

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“…Recent studies have demonstrated that MT1-MMP protects cancer cells from apoptosis induced by collagen gel culture [21]. HSC-4 cells used here express mutant form of p53-R248Q [22] and lack the expression of PTEN (Fig.…”

Section: Discussionmentioning

confidence: 99%

Vinculin negatively regulates transcription of MT1-MMP through MEK/ERK pathway

Yoshimoto

Takino

et al. 2014

Biochemical and Biophysical Research Communications

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“…MT1-MMP (MMP14) has emerged as an important collagenase that cancer cells use to degrade and invade in a collagen-rich environment [9,10]. While poorly invasive breast adenocarcinoma cells undergo apoptosis when confronted with a collagen-rich environment, the production of MT1-MMP endows these cells with the capacity to escape from collagen-induced apoptosis [11]. The localized activity of MT1-MMP helps tumour cells to overcome higher collagen density found in some peritumoural stroma [12].…”

Section: Introductionmentioning

confidence: 99%

Effects of Matrix Metalloproteinase on Tumour Growth and Morphology via Haptotaxis

Cr¹,

Nn²

2016

J Bioengineer & Biomedical Sci

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A tumour invasion model has been developed to examine the influence of diffusible matrix metalloproteinases (MMPs) and the mediated proteolysis of non-diffusible, membrane type MMPs (MT-MMPs) on tumour growth and morphology via haptotaxis. Our results are the first to explore the influence of localized degradation of extracellular matrix (ECM) by MT-MMPs on the morphology of tumours growing in nutrient-rich and nutrient-poor microenvironments. Two-dimensional numerical simulation, using a level-set-based tumour host interface-capturing method, reveals that haptotaxis due to ECM degradation by MMP causes greater instability than with ECM degradation by MT-MMP in low-nutrient environments, even at low proliferation rates; whereas the resulting morphologies are similar for high apoptosis rates. Our simulation results show that while haptotaxis leads to completely different tumour growth rates and morphologies depending on proliferation and apoptosis rates in low-nutrient environment, there are no significant variations when we compare the haptotaxis due to ECM degradation by MMP and MT-MMP, except for low proliferation rates. Focusing on the differences between MMP and MT-MMP mediated effects; our study has important implications in MMP-target validation and MMP-inhibitor-drug development for anti-cancer clinical trials.

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MT1-MMP protects breast carcinoma cells against type I collagen-induced apoptosis

Cited by 58 publications

References 63 publications

ADAM12 redistributes and activates MMP-14, resulting in gelatin degradation, reduced apoptosis, and increased tumor growth

ADAM12 redistributes and activates MMP-14, resulting in gelatin degradation, reduced apoptosis, and increased tumor growth

Vinculin negatively regulates transcription of MT1-MMP through MEK/ERK pathway

Effects of Matrix Metalloproteinase on Tumour Growth and Morphology via Haptotaxis

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