Activation of the extracellular signal‐regulated protein kinase (ERK) cascade by membrane‐type‐1 matrix metalloproteinase (MT1‐MMP)

Gingras, Denis; Bousquet-Gagnon, Nathalie; Langlois, Stéphanie; Lachambre, Marie-Paule; Annabi, Borhane; Béliveau, Richard

doi:10.1016/s0014-5793(01)02985-4

Cited by 113 publications

(111 citation statements)

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“…These data indicate that the S1P-stimulated MT1-MMP -dependent EGFR transactivation involves the cytoplasmic domain of MT1-MMP and the catalytic activity of an unidentified metalloproteinase. Although BB94 inhibits MT1-MMP -dependent proMMP-2 activation (data not shown), the MMP involved is unlikely to be MMP-2 because the MT1-MMP CD20 mutant, which failed to induce EGFR transactivation, can activate pro-MMP-2 in COS-7 cells (14).…”

Section: Mt1-mmp -Dependent Egfr Transactivation Involves the Cytoplamentioning

confidence: 93%

“…The overexpression of MT1-MMP enables tumor cell growth in otherwise growthrestrictive, three-dimensional extracellular matrices (7) and promotes cell migration of a number of cancer (8)(9)(10) and endothelial cell lines (11)(12)(13). The short cytoplasmic sequence of MT1-MMP also contributes to the induction of cell migration by the enzyme (9, 10, 13) possibly through activation of the extracellular signal-regulated protein kinase (ERK) cascade (14), endocytosis and trafficking of the enzyme (15,16), and interaction with tyrosine phosphorylated caveolin-1 (17). Additional insights into the mechanisms by which MT1-MMP induces cell migration may come from our observation that MT1-MMP cooperates with the plateletderived bioactive lipid sphingosine 1-phosphate (S1P) to stimulate endothelial cell migration and morphogenic differentiation into capillary-like structures in vitro (13).…”

Section: Introductionmentioning

confidence: 99%

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Membrane-Type 1 Matrix Metalloproteinase Stimulates Cell Migration through Epidermal Growth Factor Receptor Transactivation

Langlois

Nyalendo

Tomasso

et al. 2007

Molecular Cancer Research

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Proteolysis of extracellular matrix proteins by membrane-type 1 matrix metalloproteinase (MT1-MMP) plays a pivotal role in tumor and endothelial cell migration. In addition to its proteolytic activity, several studies indicate that the proinvasive properties of MT1-MMP also involve its short cytoplasmic domain, but the specific mechanisms mediating this function have yet to be fully elucidated. Having previously shown that the serum factor sphingosine 1-phosphate stimulates MT1-MMP promigratory function through a process that involves its cytoplasmic domain, we now extend these findings to show that this cooperative interaction is permissive to cellular migration through MT1-MMP -dependent transactivation of the epidermal growth factor receptor (EGFR). In the presence of sphingosine 1-phosphate, MT1-MMP stimulates EGFR transactivation through a process that is dependent upon the cytoplasmic domain of the enzyme but not its catalytic activity. The MT1-MMP -induced EGFR transactivation also involves G i protein signaling and Src activities and leads to enhanced cellular migration through downstream extracellular signal-regulated kinase activation. The present study, thus, elucidates a novel role of MT1-MMP in signaling events mediating EGFR transactivation and provides the first evidence of a crucial role of this receptor activity in MT1-MMP promigratory function. Taken together, our results suggest that the inhibition of EGFR may represent a novel target to inhibit MT1-MMP -dependent processes associated with tumor cell invasion and angiogenesis. (Mol Cancer Res 2007;5(6):569 -83)

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Section: Mt1-mmp -Dependent Egfr Transactivation Involves the Cytoplamentioning

confidence: 93%

Section: Introductionmentioning

confidence: 99%

Membrane-Type 1 Matrix Metalloproteinase Stimulates Cell Migration through Epidermal Growth Factor Receptor Transactivation

Langlois

Nyalendo

Tomasso

et al. 2007

Molecular Cancer Research

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“…[12][13][14][15] Intracellular proteins may regulate the localization and activity of MT1-MMP by interacting with its cytoplasmic tail, potentially via dileucine and tyrosine residues within this domain. [16][17][18] MT-MMP-4 and -6 are GPI-anchored. 19,20 …”

Section: Matrix Metalloproteinasesmentioning

confidence: 99%

“…12-15 Intracellular proteins may regulate the localization and activity of MT1-MMP by interacting with its cytoplasmic tail, potentially via dileucine and tyrosine residues within this domain. [16][17][18]20 Endogenous inhibitors of metalloproteinasesThe activity of MMPs can be regulated by endogenous inhibitors, which include the TIMPs, 21 a 2 -macroglobulin 22 and the membrane-anchored glycoprotein RECK (for ''reversioninducing cysteine-rich protein with kazal motifs''). 23 There are 4 vertebrate TIMPs.…”

mentioning

confidence: 99%

Metalloproteinases and their inhibitors in tumor angiogenesis

Handsley

Edwards

2005

Intl Journal of Cancer

264

211

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Angiogenesis is the process by which new blood vessels are formed from preexisting vasculature. It is an essential feature of the female reproductive cycle, embryonic development and wound repair. Angiogenesis has also been identified as a causal or contributing factor in several pathologies, including cancer, where it is a rate-limiting step during tumor progression. Matrix metalloproteinases (MMPs) are a family of soluble and membrane-anchored proteolytic enzymes that can degrade components of the extracellular matrix (ECM) as well as a growing number of modulators of cell function. Several of the MMPs, in particular the gelatinases and membrane-type 1 MMP (MT1-MMP), have been linked to angiogenesis. Potential roles for these proteases during the angiogenic process include degradation of the basement membrane and perivascular ECM components, unmasking of cryptic biologically relevant sites in ECM components, modulation of angiogenic factors and production of endogenous angiogenic inhibitors. This review brings together what is currently known about the functions of the MMPs and the closely related ADAM (a disintegrin and metalloproteinase domain) and ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) families in angiogenesis and considers how this information might be useful in manipulation of the angiogenic process, with a view to constraining tumor progression. ' 2005 Wiley-Liss, Inc.Key words: metalloproteinase; tumor; angiogenesis; tissue inhibitor of metalloproteinases; protease; extracellular matrix Angiogenesis is an essential feature of several physiologic processes such as the developmental growth of organs, wound healing and the female reproductive cycle. 1 It is also particularly significant in cancer progression, being a crucial step in the transition of a tumor from a hyperplastic but contained in situ state to a malignant phenotype. 2,3 To allow its growth beyond a certain critical size, a solid avascular tumor must develop its own blood supply in order to meet its growing metabolic requirements. 1 Vascularization of a tumor also provides a route for dissemination of the tumor cells to different sites around the body.Although angiogenesis appears to be the primary form of tumor vascularization, the malignant cells of a tumor can gain access to a blood supply through other means, such as via tumor-induced vasculogenesis, in which bone marrow-derived precursor endothelial cells contribute to the formation of tumor vessels. 4,5 Vasculogenic mimicry is another form of vessel formation that has been reported in certain tumor types, such as aggressive human uveal melanomas, prostate and breast tumors. [6][7][8] In these cases, networks of tumor cell-lined vascular channels were identified within the tumors. Finally, vessel co-option, implemented by tumor cells as a temporary means of gaining access to a blood supply, involves the tumor cells growing around and thus co-opting existing host vessels to form an initially well-vascularized tumor. 9 This review will highlight new insigh...

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“…Whether MT1-MMP exerts this effect directly or indirectly remains to be elucidated. It is likely that MT1-MMP transduces an intracellular signal through its cytoplasmic C-terminal domain (Gingras et al, 2001) or interaction with integrin (Deryugina et al, 2002a). Interestingly, in an in vivo murine model, TIMP-2-mediated inhibition of tumor growth and angiogenesis was associated with a down-regulation of VEGF expression in tumor cells (Hajitou et al, 2001).…”

Section: Role Of Mt1-mmp During Tumoral Angiogenesismentioning

confidence: 99%

Membrane type-1 matrix metalloproteinase and TIMP-2 in tumor angiogenesis

et al. 2003

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The matrix metalloproteinases (MMPs) constitute a multigene family of over 23 secreted and cell-surface associated enzymes that cleave or degrade various pericellular substrates. In addition to virtually all extracellular matrix (ECM) compounds, their targets include other proteinases, chemotactic molecules, latent growth factors, growth factor-binding proteins and cell surface molecules. The MMP activity is controlled by the physiological tissue inhibitors of MMPs (TIMPs). There is much evidence that MMPs and their inhibitors play a key role during extracellular remodeling in physiological situations and in cancer progression. They have other functions that promoting tumor invasion. Indeed, they regulate early stages of tumor progression such as tumor growth and angiogenesis. Membrane type MMPs (MT-MMPs) constitute a new subset of cell surface-associated MMPs. The present review will focus on MT1-MMP which plays a major role at least, in the ECM remodeling, directly by degrading several of its components, and indirectly by activating pro-MMP2. As our knowledge on the field of MT1-MMP biology has grown, the unforeseen complexities of this enzyme and its interaction with its inhibitor TIMP-2 have emerged, often revealing unexpected mechanisms of action.Keywords: MT1-MMP ; tumoral angiogenesis ; vascular endothelial growth factor ; protease inhibitors ; estradiol MMP structure and functionsMatrix metalloproteinases (MMPs) are a broad family of zinc-binding endopeptidases that play a key role in the extracellular matrix (ECM) degradation associated with cancer cell invasion, metastasis and angiogenesis (Egeblad and Werb, 2002;McCawley and Matrisian, 2000). At present, more than 21 human MMPs and the homologues from other species have been identified (Egeblad and Werb, 2002). The MMP family can be segregated into two groups, the soluble type and the membrane-type MMPs (MT-MMPs and MMP23). Although initially classified according to their substrate specificity (McCawley and Matrisian, 2000), the MMP classification is now based on their structure (Egeblad and Werb, 2002). The 'minimal-domain MMPs' (MMP7 and MMP26) contains (i) a signal peptide that directs them to the endoplasmic reticulum, (ii) a propeptide, with a zinc-interacting thiol (SH) group that maintains the proMMP in a latent form (zymogen), and (iii) a catalytic domain containing the highly conserved Zn 2+ binding site (HEXGHXXGXXHS/T) (Fig. 1). With the exception of MMP23, all other MMPs display a prolinerich hinge region that links the catalytic domain to the hemopexin/vitronectin-like domain. This C-terminal domain influences substrate specificity and the binding to tissue inhibitors of MMPs (TIMPs) and cell surface molecules. The hemopexin-containing MMPs are further distinguished by the presence of specific insert(s). The gelatin-binding MMPs (MMP2 and MMP9 or gelatinases) contain inserts that resemble the collagen-binding type II repeats of fibronectin. The membrane type (MT)-MMPs have a single pass transmembrane domain and a short cytoplasmic...

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Activation of the extracellular signal‐regulated protein kinase (ERK) cascade by membrane‐type‐1 matrix metalloproteinase (MT1‐MMP)

Cited by 113 publications

References 37 publications

Membrane-Type 1 Matrix Metalloproteinase Stimulates Cell Migration through Epidermal Growth Factor Receptor Transactivation

Membrane-Type 1 Matrix Metalloproteinase Stimulates Cell Migration through Epidermal Growth Factor Receptor Transactivation

Metalloproteinases and their inhibitors in tumor angiogenesis

Membrane type-1 matrix metalloproteinase and TIMP-2 in tumor angiogenesis

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