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(PDF) Membrane type-1 matrix metalloproteinase and TIMP-2 in tumor angiogenesis
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{"work":{"id":8651888,"created_at":"2014-10-06T00:49:06.931-07:00","from_world_paper_id":127070744,"updated_at":"2025-01-31T19:34:38.058-08:00","_data":{"ai_title_tag":"MT1-MMP and TIMP-2 in Tumor Angiogenesis","grobid_abstract":"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.","publication_date":"2003,,","publication_name":"Matrix Biology","grobid_abstract_attachment_id":"48030998"},"document_type":"paper","pre_hit_view_count_baseline":null,"quality":"high","language":"en","title":"Membrane type-1 matrix metalloproteinase and TIMP-2 in tumor angiogenesis","broadcastable":true,"draft":null,"has_indexable_attachment":true,"indexable":true,"seo_quality":null}}["work"]; window.loswp.workCoauthors = [18050897]; window.loswp.locale = "en"; window.loswp.countryCode = "SG"; window.loswp.cwvAbTestBucket = ""; window.loswp.designVariant = "ds_vanilla"; window.loswp.fullPageMobileSutdModalVariant = "control"; window.loswp.useOptimizedScribd4genScript = false; window.loginModal = {}; window.loginModal.appleClientId = 'edu.academia.applesignon'; window.userInChina = "false";</script><script defer="" src="https://accounts.google.com/gsi/client"></script><div class="ds-loswp-container"><div class="ds-work-card--grid-container"><div class="ds-work-card--container js-loswp-work-card"><div class="ds-work-card--cover"><div class="ds-work-cover--wrapper"><div class="ds-work-cover--container"><button class="ds-work-cover--clickable js-swp-download-button" data-signup-modal="{"location":"swp-splash-paper-cover","attachmentId":48030998,"attachmentType":"pdf"}"><img alt="First page of “Membrane type-1 matrix metalloproteinase and TIMP-2 in tumor angiogenesis”" class="ds-work-cover--cover-thumbnail" src="https://0.academia-photos.com/attachment_thumbnails/48030998/mini_magick20190205-18919-rlyfi4.png?1549363265" /><img alt="PDF Icon" class="ds-work-cover--file-icon" src="//a.academia-assets.com/images/single_work_splash/adobe_icon.svg" /><div class="ds-work-cover--hover-container"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">download</span><p>Download Free PDF</p></div><div class="ds-work-cover--ribbon-container">Download Free PDF</div><div class="ds-work-cover--ribbon-triangle"></div></button></div></div></div><div class="ds-work-card--work-information"><h1 class="ds-work-card--work-title">Membrane type-1 matrix metalloproteinase and TIMP-2 in tumor angiogenesis</h1><div class="ds-work-card--work-authors ds-work-card--detail"><a class="ds-work-card--author js-wsj-grid-card-author ds2-5-body-md ds2-5-body-link" data-author-id="18050897" href="https://independent.academia.edu/NorEddineSounni"><img alt="Profile image of Nor Eddine Sounni" class="ds-work-card--author-avatar" src="//a.academia-assets.com/images/s65_no_pic.png" />Nor Eddine Sounni</a></div><div class="ds-work-card--detail"><p class="ds-work-card--detail ds2-5-body-sm">2003, Matrix Biology</p><div class="ds-work-card--work-metadata"><div class="ds-work-card--work-metadata__stat"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">visibility</span><p class="ds2-5-body-sm" id="work-metadata-view-count">…</p></div><div class="ds-work-card--work-metadata__stat"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">description</span><p class="ds2-5-body-sm">7 pages</p></div><div class="ds-work-card--work-metadata__stat"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">link</span><p class="ds2-5-body-sm">1 file</p></div></div><script>(async () => { const workId = 8651888; 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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.</p></div></div><div class="ds-top-related-works--grid-container"><div class="ds-related-content--container ds-top-related-works--container"><h2 class="ds-related-content--heading">Related papers</h2><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="0" data-entity-id="61170265" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/61170265/Selected_Matrix_Metalloproteinases_MMP_2_MMP_7_and_Their_Inhibitor_TIMP_2_in_Adult_and_Pediatric_Cancer">Selected Matrix Metalloproteinases (MMP-2, MMP-7) and Their Inhibitor (TIMP-2) in Adult and Pediatric Cancer</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="58536220" href="https://independent.academia.edu/NataliaMi%C4%99kus">Natalia Miękus</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Diagnostics</p><p class="ds-related-work--abstract ds2-5-body-sm">The tumor microenvironment (TME) consists of numerous biologically relevant elements. One of the most important components of the TME is the extracellular matrix (ECM). The compounds of the ECM create a network that provides structural and biochemical support to surrounding cells. The most important substances involved in the regulation of the ECM degradation process are matrix metalloproteinases (MMPs) and their endogenous inhibitors (tissue inhibitors of metalloproteinases, TIMPs). The disruption of the physiological balance between MMP activation and deactivation could lead to progression of various diseases such as cardiovascular disease, cancer, fibrosis arthritis, chronic tissue ulcers, pathologies of the nervous system (such as stroke and Alzheimer’s disease), periodontitis, and atheroma. MMP-TIMP imbalance results in matrix proteolysis associated with various pathological processes such as tumor invasion. The present review discusses the involvement of two MMPs, MMP-2 and MM...</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Selected Matrix Metalloproteinases (MMP-2, MMP-7) and Their Inhibitor (TIMP-2) in Adult and Pediatric Cancer","attachmentId":74299741,"attachmentType":"pdf","work_url":"https://www.academia.edu/61170265/Selected_Matrix_Metalloproteinases_MMP_2_MMP_7_and_Their_Inhibitor_TIMP_2_in_Adult_and_Pediatric_Cancer","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/61170265/Selected_Matrix_Metalloproteinases_MMP_2_MMP_7_and_Their_Inhibitor_TIMP_2_in_Adult_and_Pediatric_Cancer"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="1" data-entity-id="20975120" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/20975120/Tissue_Inhibitor_of_Metalloproteinase_TIMP_2_Acts_Synergistically_with_Synthetic_Matrix_Metalloproteinase_MMP_Inhibitors_but_Not_with_TIMP_4_to_Enhance_the_Membrane_Type_1_MMP_dependent_Activation_of_Pro_MMP_2">Tissue Inhibitor of Metalloproteinase (TIMP)-2 Acts Synergistically with Synthetic Matrix Metalloproteinase (MMP) Inhibitors but Not with TIMP-4 to Enhance the (Membrane Type 1)-MMP-dependent Activation of Pro-MMP-2</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="42225466" href="https://independent.academia.edu/PaulSoloway">Paul Soloway</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Journal of Biological Chemistry, 2000</p><p class="ds-related-work--abstract ds2-5-body-sm">The membrane-type 1 matrix metalloproteinase (MT1-MMP) has been shown to be a key enzyme in tumor angiogenesis and metastasis. MT1-MMP hydrolyzes a variety of extracellular matrix components and is a physiological activator of pro-MMP-2, another MMP involved in malignancy. Pro-MMP-2 activation by MT1-MMP involves the formation of an MT1-MMP⅐tissue inhibitors of metalloproteinases 2 (TIMP-2)⅐pro-MMP-2 complex on the cell surface that promotes the hydrolysis of pro-MMP-2 by a neighboring TIMP-2-free MT1-MMP. The MT1-MMP⅐TIMP-2 complex also serves to reduce the intermolecular autocatalytic turnover of MT1-MMP, resulting in accumulation of active MT1-MMP (57 kDa) on the cell surface. Evidence shown here in Timp2-null cells demonstrates that pro-MMP-2 activation by MT1-MMP requires TIMP-2. In contrast, a C-terminally deleted TIMP-2 (⌬-TIMP-2), unable to form ternary complex, had no effect. However, ⌬-TIMP-2 and certain synthetic MMP inhibitors, which inhibit MT1-MMP autocatalysis, can act synergistically with TIMP-2 in the promotion of pro-MMP-2 activation by MT1-MMP. In contrast, TIMP-4, an efficient MT1-MMP inhibitor, had no synergistic effect. These studies suggest that under certain conditions the pericellular activity of MT1-MMP in the presence of TIMP-2 can be modulated by synthetic and natural (TIMP-4) MMP inhibitors. . 1 The abbreviations used are: ECM, extracellular matrix; MMP, matrix metalloproteinase; MT-MMP, membrane type MMP; MMPI, MMP inhibitor; TIMP, tissue inhibitor of metalloproteinase; PAGE, polyacrylamide gel electrophoresis; pAb, polyclonal antibody; pfu, plaque-forming units; DMEM, Dulbecco's modified Eagle's medium.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Tissue Inhibitor of Metalloproteinase (TIMP)-2 Acts Synergistically with Synthetic Matrix Metalloproteinase (MMP) Inhibitors but Not with TIMP-4 to Enhance the (Membrane Type 1)-MMP-dependent Activation of Pro-MMP-2","attachmentId":41653714,"attachmentType":"pdf","work_url":"https://www.academia.edu/20975120/Tissue_Inhibitor_of_Metalloproteinase_TIMP_2_Acts_Synergistically_with_Synthetic_Matrix_Metalloproteinase_MMP_Inhibitors_but_Not_with_TIMP_4_to_Enhance_the_Membrane_Type_1_MMP_dependent_Activation_of_Pro_MMP_2","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/20975120/Tissue_Inhibitor_of_Metalloproteinase_TIMP_2_Acts_Synergistically_with_Synthetic_Matrix_Metalloproteinase_MMP_Inhibitors_but_Not_with_TIMP_4_to_Enhance_the_Membrane_Type_1_MMP_dependent_Activation_of_Pro_MMP_2"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="2" data-entity-id="4780576" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/4780576/Role_of_pericellular_proteolysis_by_membrane_type_1_matrix_metalloproteinase_in_cancer_invasion_and_angiogenesis">Role of pericellular proteolysis by membrane-type 1 matrix metalloproteinase in cancer invasion and angiogenesis</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="6161344" href="https://independent.academia.edu/YanaIkuo">Yana Ikuo</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Cancer and Metastasis Reviews, 2003</p><p class="ds-related-work--abstract ds2-5-body-sm">Membrane-type 1 matrix metalloproteinase (MT1-MMP) is an integral membrane proteinase that is frequently expressed in malignant cancer cells and has potent invasion-promoting activity. When expressed on the cell surface, MT1-MMP degrades the extracellular matrix (ECM) barrier adjacent to the cells to maintain the migration route to traverse the tissue. But MT1-MMP is not just an enzyme that degrades ECM. MT1-MMP also introduces limited cleavage into proteins at the cell-ECM interspaces and converts their functions. The target molecules are ECM components, cell adhesion molecules, and latent forms of MMPs. Through these processing events MT1-MMP modulates the migratory and invasive behavior of the cells.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Role of pericellular proteolysis by membrane-type 1 matrix metalloproteinase in cancer invasion and angiogenesis","attachmentId":49635124,"attachmentType":"pdf","work_url":"https://www.academia.edu/4780576/Role_of_pericellular_proteolysis_by_membrane_type_1_matrix_metalloproteinase_in_cancer_invasion_and_angiogenesis","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/4780576/Role_of_pericellular_proteolysis_by_membrane_type_1_matrix_metalloproteinase_in_cancer_invasion_and_angiogenesis"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="3" data-entity-id="62062239" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/62062239/Role_of_Matrix_Metalloproteinases_in_Angiogenesis_and_Cancer">Role of Matrix Metalloproteinases in Angiogenesis and Cancer</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="202011142" href="https://uacm.academia.edu/Mar%C3%ADaElizbethAlvarezS%C3%A1nchez">María Elizbeth Alvarez Sánchez</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Frontiers in Oncology</p><p class="ds-related-work--abstract ds2-5-body-sm">During angiogenesis, new vessels emerge from existing endothelial lined vessels to promote the degradation of the vascular basement membrane and remodel the extracellular matrix (ECM), followed by endothelial cell migration, and proliferation and the new generation of matrix components. Matrix metalloproteinases (MMPs) participate in the disruption, tumor neovascularization, and subsequent metastasis while tissue inhibitors of metalloproteinases (TIMPs) downregulate the activity of these MMPs. Then, the angiogenic response can be directly or indirectly mediated by MMPs through the modulation of the balance between pro-and anti-angiogenic factors. This review analyzes recent knowledge on MMPs and their participation in angiogenesis.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Role of Matrix Metalloproteinases in Angiogenesis and Cancer","attachmentId":74927098,"attachmentType":"pdf","work_url":"https://www.academia.edu/62062239/Role_of_Matrix_Metalloproteinases_in_Angiogenesis_and_Cancer","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/62062239/Role_of_Matrix_Metalloproteinases_in_Angiogenesis_and_Cancer"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="4" data-entity-id="4575338" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/4575338/Matrix_metalloproteinases_in_cancer_from_new_functions_to_improved_inhibition_strategies">Matrix metalloproteinases in cancer: from new functions to improved inhibition strategies</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="5734179" href="https://iberoamericana.academia.edu/luissanchez">luis sanchez</a></div><p class="ds-related-work--metadata ds2-5-body-xs">International Journal of Developmental Biology, 2004</p><p class="ds-related-work--abstract ds2-5-body-sm">Over the last years, the relevance of the matrix metalloproteinase (MMP) family in cancer research has grown considerably. These enzymes were initially associated with the invasive properties of tumour cells, owing to their ability to degrade all major protein components of the extracellular matrix (ECM) and basement membranes. However, further studies have demonstrated the implication of MMPs in early steps of tumour evolution, including stimulation of cell proliferation and modulation of angiogenesis. The establishment of causal relationships between MMP overproduction in tumour or stromal cells and cancer progression has prompted the development of clinical trials with a series of inhibitors designed to block the proteolytic activity of these enzymes. Unfortunately, the results derived from using broad-spectrum MMP inhibitors (MMPIs) for treating patients with advanced cancer have been disappointing in most cases. There are several putative explanations for the lack of success of these MMPIs including the recent finding that some MMPs may play a paradoxical protective role in tumour progression. These observations together with the identification of novel functions for MMPs in early stages of cancer have made necessary a reformulation of MMP inhibition strategies. A better understanding of the functional complexity of this proteolytic system and global approaches to identify the relevant MMPs which must be targeted in each individual cancer patient, will be necessary to clarify whether MMP inhibition may be part of future therapies against cancer.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Matrix metalloproteinases in cancer: from new functions to improved inhibition strategies","attachmentId":31947454,"attachmentType":"pdf","work_url":"https://www.academia.edu/4575338/Matrix_metalloproteinases_in_cancer_from_new_functions_to_improved_inhibition_strategies","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/4575338/Matrix_metalloproteinases_in_cancer_from_new_functions_to_improved_inhibition_strategies"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="5" data-entity-id="52947213" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/52947213/Membrane_Type_1_Matrix_Metalloproteinase_associated_Degradation_of_Tissue_Inhibitor_of_Metalloproteinase_2_in_Human_Tumor_Cell_Lines">Membrane Type 1 Matrix Metalloproteinase-associated Degradation of Tissue Inhibitor of Metalloproteinase 2 in Human Tumor Cell Lines</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="28195659" href="https://independent.academia.edu/NorSounni">Nor Sounni</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Journal of Biological Chemistry, 2000</p><p class="ds-related-work--abstract ds2-5-body-sm">Tissue inhibitor of metalloproteinase 2 (TIMP-2) is required for the membrane type 1 matrix metalloproteinase (MT1-MMP)-dependent activation of pro-MMP-2 on the cell surface. MT1-MMP-bound TIMP-2 has been shown to function as a receptor for secreted pro-MMP-2, resulting in the formation of a trimolecular complex. In the presence of uncomplexed active MT1-MMP, the prodomain of cell surface-associated MMP-2 is cleaved, and activated MMP-2 is released. However, the behavior of MT1-MMP-bound TIMP-2 during MMP-2 activation is currently unknown. In this study, 125 I-labeled recombinant TIMP-2 (125 I-rTIMP-2) was used to investigate the fate of TIMP-2 during pro-MMP-2 activation by HT1080 and transfected A2058 cells. HT1080 and A2058 cells transfected with MT1-MMP cDNA (but not vector-transfected A2058 cells) were able to bind 125 I-rTIMP-2, to activate pro-MMP-2, and to process MT1-MMP into an inactive 43-kDa form. Under these conditions, 125 I-rTIMP-2 bound to the cell surface was rapidly internalized and degraded in intracellular organelles through a bafilomycin A 1-sensitive mechanism, and 125 I-bearing low molecular mass fragment(s) were released in the culture medium. These different processes were inhibited by hydroxamic acid-based synthetic MMP inhibitors and rTIMP-2, but not by rTIMP-1 or cysteine, serine, or aspartic proteinase inhibitors. These results support the concept that the MT1-MMP-dependent internalization and degradation of TIMP-2 by some tumor cells might be involved in the regulation of pericellular proteolysis. Matrix metalloproteinases (MMPs), 1 also known as matrix-* This work was supported by grants from the Communauté Française de Belgique (Actions de Recherche Concertées), the Caisse Générale d'Epargne et de Retraite-Assurances (1996-1999), the Association contre le Cancer, the Association Sportive contre le Cancer, the Loterie Nationale,</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Membrane Type 1 Matrix Metalloproteinase-associated Degradation of Tissue Inhibitor of Metalloproteinase 2 in Human Tumor Cell Lines","attachmentId":69963295,"attachmentType":"pdf","work_url":"https://www.academia.edu/52947213/Membrane_Type_1_Matrix_Metalloproteinase_associated_Degradation_of_Tissue_Inhibitor_of_Metalloproteinase_2_in_Human_Tumor_Cell_Lines","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/52947213/Membrane_Type_1_Matrix_Metalloproteinase_associated_Degradation_of_Tissue_Inhibitor_of_Metalloproteinase_2_in_Human_Tumor_Cell_Lines"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="6" data-entity-id="24732818" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/24732818/Beneficial_and_detrimental_influences_of_tissue_inhibitor_of_metalloproteinase_1_TIMP_1_in_tumor_progression">Beneficial and detrimental influences of tissue inhibitor of metalloproteinase-1 (TIMP-1) in tumor progression</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="47678741" href="https://independent.academia.edu/EliseLambert">Elise Lambert</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Biochimie, 2005</p><p class="ds-related-work--abstract ds2-5-body-sm">Tissue inhibitor of metalloproteinase-1 (TIMP-1) is one representative of the natural matrix metalloproteinase (MMP) inhibitor family, encompassing four members. It inhibits all MMPs, except several MT-MMPs, and a disintegrin with a metalloproteinase domain (ADAM)-10 with Kis < nM. Unexpectedly, its upregulation was associated to poor clinical outcome for several cancer varieties. Such finding might be related to the growth-promoting and survival activities of TIMP-1 for normal and cancer cells. In most cases, such properties are MMPindependent and binding of TIMP-1 to an unknown receptor system can trigger JAK (or FAK)/PI 3 kinase/Akt/bad-bclX 2 (erythroid, myeloid, epithelial cell lines) or Ras/Raf1/FAK (osteosarcoma cell line) signaling pathways. The relationship between viral infection and TIMP-1 expression is here underlined. Thus, TIMP-1 might display a dual influence on tumor progression; either beneficial by inhibiting MMPs as MMP-9 and by impairing angiogenesis or detrimental by favoring cancer cells growth or survival. We consider that the proMMP-9/TIMP-1 balance is of critical importance in early events of tumor progression, and might show promise as diagnostic and prognostic marker of malignancy.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Beneficial and detrimental influences of tissue inhibitor of metalloproteinase-1 (TIMP-1) in tumor progression","attachmentId":45062737,"attachmentType":"pdf","work_url":"https://www.academia.edu/24732818/Beneficial_and_detrimental_influences_of_tissue_inhibitor_of_metalloproteinase_1_TIMP_1_in_tumor_progression","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/24732818/Beneficial_and_detrimental_influences_of_tissue_inhibitor_of_metalloproteinase_1_TIMP_1_in_tumor_progression"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="7" data-entity-id="29918319" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/29918319/Molecular_mechanisms_of_tissue_inhibitor_of_metalloproteinase_2_in_the_tumor_microenvironment">Molecular mechanisms of tissue inhibitor of metalloproteinase 2 in the tumor microenvironment</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="56693857" href="https://independent.academia.edu/SandraJensentaubman">Sandra M Jensen</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Molecular and Cellular Therapies, 2014</p><p class="ds-related-work--abstract ds2-5-body-sm">There has been a recent paradigm shift in the way we target cancer, drawing a greater focus on the role of the tumor microenvironment (TME) in cancer development, progression and metastasis. Within the TME, there is a crosstalk in signaling and communication between the malignant cells and the surrounding extracellular matrix. Matrix metalloproteinases (MMPs) are zinc-dependent endoproteases that have the ability to degrade the matrix surrounding a tumor and mediate tumor growth, angiogenesis and metastatic disease. Their endogenous inhibitors, the Tissue Inhibitors of Metalloproteinases (TIMPs), primarily function to prevent degradation of the ECM via inhibition of MMPs. However, recent studies demonstrate that TIMP family members also possess MMP-independent functions. One TIMP member in particular, TIMP-2, has many distinct properties and functions, that occur independent of MMP inhibition, including the inhibition of tumor growth and reduction of angiogenesis through decreased endothelial cell proliferation and migration. The MMP-independent molecular mechanisms and signaling pathways elicited by TIMP-2 in the TME are described in this review.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Molecular mechanisms of tissue inhibitor of metalloproteinase 2 in the tumor microenvironment","attachmentId":50377968,"attachmentType":"pdf","work_url":"https://www.academia.edu/29918319/Molecular_mechanisms_of_tissue_inhibitor_of_metalloproteinase_2_in_the_tumor_microenvironment","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/29918319/Molecular_mechanisms_of_tissue_inhibitor_of_metalloproteinase_2_in_the_tumor_microenvironment"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="8" data-entity-id="8651906" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/8651906/Expression_of_membrane_type_1_matrix_metalloproteinase_MT1_MMP_in_A2058_melanoma_cells_is_associated_with_MMP_2_activation_and_increased_tumor_growth_and_vascularization">Expression of membrane type 1 matrix metalloproteinase (MT1-MMP) in A2058 melanoma cells is associated with MMP-2 activation and increased tumor growth and vascularization</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="18050897" href="https://independent.academia.edu/NorEddineSounni">Nor Eddine Sounni</a></div><p class="ds-related-work--metadata ds2-5-body-xs">International Journal of Cancer, 2002</p><p class="ds-related-work--abstract ds2-5-body-sm">Membrane-type metalloproteinase-1 (MT1-MMP) is a transmembrane metalloproteinase overexpressed in tumors, which plays a major role in the first step of pro-MMP-2 activation, leading to the generation of an intermediate 62 kDa species. The second step of MMP-2 activation that yields to the mature form is less understood and could involve an autocatalytic process and/or the activity of the plasminogen/plasmin system. Human melanoma A2058 cells, which express MMP-2 only in its pro-form, were used to determine the role of MT1-MMP during pericellular proteolysis and tumor progression. The induction of MT1-MMP overexpression by MT1-MMP cDNA transfection initiated the first step of MMP-2 activation. We provide evidence that a cooperation between the plasminogen/plasmin system and MT1-MMP endowed the cells with the ability to fully activate MMP-2 and with enhanced invasive properties in vitro. When injected subcutaneously in nude mice, MT1-MMP expressing clones induced rapid tumor growth and high tumor vascularization, while the control clones were poorly or not tumorigenic. Our data provide the first demonstration, in an experimental model, that MT1-MMP expression by tumor cells promotes tumor vascularization. © 2001 Wiley-Liss, Inc.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Expression of membrane type 1 matrix metalloproteinase (MT1-MMP) in A2058 melanoma cells is associated with MMP-2 activation and increased tumor growth and vascularization","attachmentId":48031064,"attachmentType":"pdf","work_url":"https://www.academia.edu/8651906/Expression_of_membrane_type_1_matrix_metalloproteinase_MT1_MMP_in_A2058_melanoma_cells_is_associated_with_MMP_2_activation_and_increased_tumor_growth_and_vascularization","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/8651906/Expression_of_membrane_type_1_matrix_metalloproteinase_MT1_MMP_in_A2058_melanoma_cells_is_associated_with_MMP_2_activation_and_increased_tumor_growth_and_vascularization"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="9" data-entity-id="115941610" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/115941610/Matrix_Metalloproteinases_and_Cancer_Roles_in_Threat_and_Therapy">Matrix Metalloproteinases and Cancer - Roles in Threat and Therapy</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="294997153" href="https://independent.academia.edu/LalitaYadav54">Lalita Yadav</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Asian Pacific Journal of Cancer Prevention, 2014</p><p class="ds-related-work--abstract ds2-5-body-sm">Matrix metalloproteinases (MMPs) are a family of zinc dependent extracellular matrix (ECM) remodelling endopeptidases having the ability to degrade almost all components of extracellular matrix and implicated in various physiological as well as pathological processes. Carcinogenesis is a multistage process in which alteration of the microenvironment is required for conversion of normal tissue to a tumour. Extracellular matrix remodelling proteinases such as MMPs are principal mediators of alterations observed in the microenvironment during carcinogenesis and according to recent concepts not only have roles in invasion or late stages of cancer but also in regulating initial steps of carcinogenesis in a favourable or unfavourable manner. Establishment of relationships between MMP overproduction and cancer progression has stimulated the development of inhibitors that block proteolytic activity of these enzymes. In this review we discuss the MMP general structure, classification, regulation roles in relation to hallmarks of cancer and as targets for therapeutic intervention.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Matrix Metalloproteinases and Cancer - Roles in Threat and Therapy","attachmentId":112208651,"attachmentType":"pdf","work_url":"https://www.academia.edu/115941610/Matrix_Metalloproteinases_and_Cancer_Roles_in_Threat_and_Therapy","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/115941610/Matrix_Metalloproteinases_and_Cancer_Roles_in_Threat_and_Therapy"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div></div></div><div class="ds-sticky-ctas--wrapper js-loswp-sticky-ctas hidden"><div class="ds-sticky-ctas--grid-container"><div class="ds-sticky-ctas--container"><button class="ds2-5-button js-swp-download-button" data-signup-modal="{"location":"continue-reading-button--sticky-ctas","attachmentId":48030998,"attachmentType":"pdf","workUrl":null}">See full PDF</button><button class="ds2-5-button ds2-5-button--secondary js-swp-download-button" data-signup-modal="{"location":"download-pdf-button--sticky-ctas","attachmentId":48030998,"attachmentType":"pdf","workUrl":null}"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">download</span>Download PDF</button></div></div></div><div class="ds-below-fold--grid-container"><div class="ds-work--container js-loswp-embedded-document"><div class="attachment_preview" data-attachment="Attachment_48030998" style="display: none"><div class="js-scribd-document-container"><div class="scribd--document-loading js-scribd-document-loader" style="display: block;"><img alt="Loading..." src="//a.academia-assets.com/images/loaders/paper-load.gif" /><p>Loading Preview</p></div></div><div style="text-align: center;"><div class="scribd--no-preview-alert js-preview-unavailable"><p>Sorry, preview is currently unavailable. 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data-collection-position="11" data-entity-id="47914397" data-sort-order="default"><a class="ds-related-work--title js-related-work-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/47914397/Impaired_tyrosine_phosphorylation_of_membrane_type_1_matrix_metalloproteinase_reduces_tumor_cell_proliferation_in_three_dimensional_matrices_and_abrogates_tumor_growth_in_mice">Impaired tyrosine phosphorylation of membrane type 1-matrix metalloproteinase reduces tumor cell proliferation in three-dimensional matrices and abrogates tumor growth in mice</a><div class="ds-related-work--metadata"><a class="js-related-work-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="37591436" href="https://independent.academia.edu/EdithBeaulieu">Edith Beaulieu</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Carcinogenesis, 2008</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" 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href="https://www.academia.edu/47914397/Impaired_tyrosine_phosphorylation_of_membrane_type_1_matrix_metalloproteinase_reduces_tumor_cell_proliferation_in_three_dimensional_matrices_and_abrogates_tumor_growth_in_mice"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-related-work-sidebar-card" data-collection-position="12" data-entity-id="25251599" data-sort-order="default"><a class="ds-related-work--title js-related-work-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/25251599/Matrix_metalloproteinases_and_tumor_metastasis">Matrix metalloproteinases and tumor metastasis</a><div class="ds-related-work--metadata"><a class="js-related-work-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="48531460" href="https://independent.academia.edu/ElenaDeryugina">Elena Deryugina</a></div><p 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