Matrix metalloproteinases at cancer tumor–host interface

Noël, Agnès; Jost, Maud; Maquoi, Erik

doi:10.1016/j.semcdb.2007.05.011

Cited by 212 publications

(195 citation statements)

References 112 publications

(147 reference statements)

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“…Matrix metalloproteinases (MMPs) play critical roles in cell invasion. 21 We examined MMP activities by gelatin zymography on conditioned media with or without TSAHC treatment. MMP2 and MMP9 activities were higher in SNU449Tp cells compared to those in SNU449Cp cells.…”

Section: Resultsmentioning

confidence: 99%

Blockade of four-transmembrane L6 family member 5 (TM4SF5)-mediated tumorigenicity in hepatocytes by a synthetic chalcone derivative

et al. 2008

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We previously reported that the four-transmembrane L6 family member 5 (TM4SF5) was highly expressed in hepatocarcinoma, induced morphological elongation and epithelialmesenchymal transition, and caused abnormal cell growth in multilayers in vitro and tumor formation in vivo. In this study, we identified a synthetic compound, 4 -(p-toluenesulfonylamido)-4-hydroxychalcone (TSAHC) that antagonized both the TM4SF5-mediated multilayer growth and TM4SF5-enhanced migration/invasion. TSAHC treatment induced multilayer-growing cells to grow in monolayers, recovering contact inhibition without accompanying apoptosis, and inhibited chemotactic migration and invasion. E pithelial monolayer integrity is maintained by integrin-mediated cell adhesion between the cell and the extracellular matrix (ECM) and by E-cadherin-mediated contact between adjacent cells. 1 Epithelial-mesenchymal transition (EMT) through loss of cellcell contacts disrupts monolayer integrity and alters cell-ECM interactions. 2 Tumor cells disseminated from primary tumors via loss of cell adhesion and contact can migrate to and invade distal tissues. 3 We recently reported that TM4SF5-mediated EMT results in a loss of contact inhibition and multilayer growth. 4 Therefore, altered cell adhesion and contact may lead to both a loss of contact inhibition and a dissemination of metastatic cells from the primary tumor. 5 Integrin-mediated cell adhesion reorganizes actin filaments 6 through activation of diverse intracellular signaling molecules, including focal adhesion kinase (FAK), Rho guanosine triphosphatases (RhoA, Rac1, and CDC42), and others, 7 which are critical for cellular morphology and migration. 8 TM4SF proteins (i.e., tetraspanins or tetraspans) are a group of membrane proteins with four transmembrane

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Section: Resultsmentioning

confidence: 99%

Blockade of four-transmembrane L6 family member 5 (TM4SF5)-mediated tumorigenicity in hepatocytes by a synthetic chalcone derivative

et al. 2008

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“…16 However, it has been verified that these enzymes may also change cell proliferation, adhesion, and migration, not only by degrading the extracellular matrix but also by favoring the release of growth factors and the generation of certain cleavage fragments or functional proteins in this space. 17 Some MMPs are synthesized by tumor cells, such as MMP-7, while others are produced predominantly by stromal cells, including MMP-2 and 9. Tumor cells can also stimulate the surrounding stromal cells and synthesize these enzymes in a paracrine manner via the secretion of interleukins, interferons, EMMPRIN (extracellular inducer of MMPs), and growth factors.…”

Section: Zinc and Metalloproteinases Of The Extracellular Matrixmentioning

confidence: 99%

Zinc and metalloproteinases 2 and 9: What is their relation with breast cancer?

Holanda

Oliveira²,

Cruz³

et al. 2017

Rev. Assoc. Med. Bras.

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Zinc is the catalytic component of proteins that regulate responses to DNA damage, intracellular signaling enzymes, and matrix metalloproteinases, which are important proteins in carcinogenesis. The objective of this review is to bring current information on the participation of zinc and matrix metalloproteinases types 2 and 9 in mechanisms involved in the pathogenesis of breast cancer. We conducted a literature review, in consultation with the PubMed, Lilacs, and Scielo databases. The zinc and cysteine residues are structural elements shared by all members of the family of matrix metalloproteinases, and these proteins appear to be involved in the propagation of various types of neoplasms, including breast cancer. Moreover, transported zinc is likely to be used for the metalation of the catalytic domain of the newly synthesized metalloproteinases before the latter are secreted. Accordingly, increase in zinc concentrations in cellular compartments and the reduction of this trace element in the blood of patients with breast cancer appear to alter the activity of metalloproteinases 2 and 9, contributing to the occurrence of malignancy. Thus, it is necessary to carry out further studies with a view to clarify the role of zinc and metalloproteinases 2 and 9 in the pathogenesis of breast cancer.

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“…To date, type I collagenolytic activity is confined to a small subset of proteinases belonging to either the cysteine proteinase or matrix metalloproteinase (MMP) families (BirkedalHansen, 1987;Nagase et al, 2006;Sabeh et al, 2009a). MMPs are zinc-dependent endopeptidases that play crucial roles in cancer progression (Noe¨l et al, 2008;Kessenbrock et al, 2010), not only by degrading physical ECM barriers, but also by regulating the processing of an increasing panel of molecular mediators of signaling events (Lopez-Otin and Hunter, 2010;Rodrı´guez et al, 2010). They thus represent the most prominent family of proteinases associated with tumorigenesis (Kessenbrock et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2011

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As invading breast carcinoma cells breach their underlying basement membrane, they become confronted with a dense three-dimensional reactive stroma dominated by type I collagen. To develop metastatic capabilities, invading tumor cells must acquire the capacity to negotiate this novel microenvironment. Collagen influences the fate of epithelial cells by inducing apoptosis. However, the mechanisms used by invading tumor cells to evade collagen-induced apoptosis remain to be defined. We demonstrate that membrane type-1 matrix metalloproteinase (MT1-MMP/MMP-14) confers breast cancer cells with the ability to escape apoptosis when embedded in a collagen gel and after orthotopic implantation in vivo. In the absence of MMP-14-dependent proteolysis, type I collagen triggers apoptosis by inducing the expression of the pro-apoptotic Bcl-2-interacting killer in luminallike breast cancer cells. These findings reveal a new mechanism whereby MMP-14 activity promotes tumor progression by circumventing apoptosis.

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Matrix metalloproteinases at cancer tumor–host interface

Cited by 212 publications

References 112 publications

Blockade of four-transmembrane L6 family member 5 (TM4SF5)-mediated tumorigenicity in hepatocytes by a synthetic chalcone derivative

Blockade of four-transmembrane L6 family member 5 (TM4SF5)-mediated tumorigenicity in hepatocytes by a synthetic chalcone derivative

Zinc and metalloproteinases 2 and 9: What is their relation with breast cancer?

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

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