Processing of Integrin αv Subunit by Membrane Type 1 Matrix Metalloproteinase Stimulates Migration of Breast Carcinoma Cells on Vitronectin and Enhances Tyrosine Phosphorylation of Focal Adhesion Kinase

Deryugina, Elena I.; Ratnikov, Boris I.; Postnova, Tanya I.; Rozanov, Dmitri V.; Strongin, Alex Y.

doi:10.1074/jbc.m110269200

Cited by 203 publications

(155 citation statements)

References 53 publications

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“…All clones overexpressing MT1-MMP (i) were able to activate endogenous or exogenous pro-MMP2, (ii) displayed an enhanced in vitro invasiveness through matrigel-coated filters, independently of MMP2 transfection, (iii) induced the rapid development of highly vascularized tumors when injected subcutanously in nude mice, and (iv) promoted blood vessels sprouting in the rat aortic ring assay, an in vitro model of angiogenesis (Sounni et al, 2002b). These data demonstrating, in two experimental models (Sounni et al, 2002a,b), the relation between MT1-MMP expression and an angiogenic phenotype are in accordance with the in vivo observations reported by other groups (Deryugina et al, 2002b). Since MCF7 cells are estrodiol-dependent cells, the tumorigenicity and angiogenic phenotype of MT1-MMP overexpressing clones were compared after inoculation into nude mice supplemented with estradiol pellets or into nude ovariectomized mice.…”

Section: Role Of Mt1-mmp During Tumoral Angiogenesissupporting

confidence: 86%

“…Indeed, an enhancement of VEGF at the mRNA and protein levels was concomitant with MT1-MMP overexpression in cultured cells, as well as in tumor extracts. Such a modulation of VEGF production by MT1-MMP is further supported by the study of Deryugina using glioma cells (Deryugina et al, 2002b). In contrast to MMP9 which modulates VEGF bioavailability by releasing it from the ECM (Bergers et al, 2000), MT1-MMP appears to control gene expression.…”

Section: Role Of Mt1-mmp During Tumoral Angiogenesismentioning

confidence: 90%

“…MT1-MMP displays a broad spectrum of activity against ECM components such as type I and II collagen, fibronectin, vitronectin, laminin, fibrin and proteoglycan (d 'Ortho et al, 1997;Koshikawa et al, 2000). However, it has substrates that extend beyond ECM components such as cell surface molecules including CD44 (Kajita et al, 2001), pro α V integrin (Deryugina et al, 2002b) and transglutaminase (Belkin et al, 2001). It interacts with integrins ) and participates in the α V β 8 -mediated activation of TGFβ (Mu et al, 2002).…”

Section: Membrane-associated Mmpsmentioning

confidence: 99%

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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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Section: Role Of Mt1-mmp During Tumoral Angiogenesissupporting

confidence: 86%

Section: Role Of Mt1-mmp During Tumoral Angiogenesismentioning

confidence: 90%

Section: Membrane-associated Mmpsmentioning

confidence: 99%

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

et al. 2003

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“…MMP-14-mediated processing of pro-alpha(v) integrin subunit results in the maturation of alpha(v)-beta(3) integrin facilitating invasion of these cells, without altering its interaction with ECM components. It has been proposed that the shift to invasive behaviour is due to increased activation in FAK signaling, which is implicated in numerous growth promoting pathways (Deryugina et al, 2002).…”

Section: Cell Dissociationmentioning

confidence: 99%

Matrix metalloproteinases and their tissue inhibitors direct cell fate during cancer development

2003

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Matrix metalloproteinases (MMPs) were initially recognised for their extracellular matrix (ECM)-degrading capability during tissue remodelling. Their importance was further highlighted by their role in metastasis. Clinical trials have since evaluated the potential of MMP inhibitors as anticancer therapeutics, but without success. These initial studies point to the complex, multifunctional capacity of MMPs in cancer as shown by their function, not only as strident mediators of advanced malignancies, but also as effectors of early stage tumorigenesis. Research now shows that MMPs, and their tissue inhibitors, affect tumour initiation and growth through loss of cell adhesion, evasion of apoptosis, and deregulation of cell division. The extracellular nature of the metalloproteinase axis situates it as a master regulator of cell fate.

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“…MT1-MMP is located on the plasma membrane at the leading edge of migrating osteoclasts, suggesting that its collagenolytic activity may aid the movement of the osteoclast along bone surfaces (Irie, Tsuruga, Sakakura, Muto, & Yajima, 2001), potentially via a Brownian ratchet motor mechanism as suggested by studies of MMP-1-mediated collagen proteolysis (Saffarian, Collier, Marmer, Elson, & Goldberg, 2004). MT1-MMP-mediated processing of the ␣ v subunit of ␣ v ␤ 3 integrin and shedding of the adhesion molecule CD44 has also been implicated in cell migration (Delaissé et al, 2003;Deryugina, Ratnikov, Postnova, Rozanov, & Strongin, 2002;Kajita et al, 2001). The proteolytic activity of MMP may also influence osteoclast-mediated bone turnover by affecting cell signalling.…”

Section: Bone: Altered Metabolism and Extracellular Matrix Proteolysismentioning

confidence: 99%

The role of proteases in pathologies of the synovial joint

Jones¹,

Riley²,

Buttle³

2008

The International Journal of Biochemistry & Cell Biology

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Synovial (diarthrodial) joints are employed within the body to provide skeletal mobility and have a characteristic structure adapted to provide a smooth almost frictionless surface for articulation. Pathologies of the synovial joint are an important cause of patient morbidity and can affect each of the constituent tissues. A common feature of these pathologies is degenerative changes in the structure of the tissue which is mediated, at least in part, by proteolytic activity. Most tissues of the synovial joint are composed primarily of extracellular matrix and key pathological roles in the degeneration of this matrix are performed by metalloproteinases such as matrix metallproteinases (MMPs) and a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS). However, other proteases such as cathepsin K are likely to play an important role, especially in bone turnover. In addition to the cleavage of structural proteins, proteolytic activities are employed to regulate the activity of other proteases, growth factors, cytokines and other inflammatory mediators. Proteases combine to form complex regulatory networks, the correct functioning of which is required for tissue homeostasis and the imbalance of which may be a feature of pathology. A precise understanding of the proteases involved in these networks is required for a true understanding of the associated pathology.

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Processing of Integrin αv Subunit by Membrane Type 1 Matrix Metalloproteinase Stimulates Migration of Breast Carcinoma Cells on Vitronectin and Enhances Tyrosine Phosphorylation of Focal Adhesion Kinase

Cited by 203 publications

References 53 publications

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

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

Matrix metalloproteinases and their tissue inhibitors direct cell fate during cancer development

The role of proteases in pathologies of the synovial joint

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