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Matrix metalloproteinases and the regulation of tissue remodelling
Abstract
Matrix metalloproteinases (MMPs) were discovered because of their role in amphibian metamorphosis, yet they have attracted more attention because of their roles in disease. Despite intensive scrutiny in vitro, in cell culture and in animal models, the normal physiological roles of these extracellular proteases have been elusive. Recent studies in mice and flies point to essential roles of MMPs as mediators of change and physical adaptation in tissues, whether developmentally regulated, environmentally induced or disease associated.
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MMPs are a large family of zinc-containing endoproteases whose role has been demonstrated in degrading extracellular matrix proteins and tissue remodeling.
“Matrix metalloproteinases (MMPs) are a large family of zinccontaining endoproteases whose role has been demonstrated in degrading ECM proteins and tissue remodeling (24).”
From Differential protective effects of connective tissue growth factor against Aβ neurotoxicity on neurons and glia (2017) · cites this paper as [24]
These MMPs function in several processes including neural development, tissue remodeling, and tumor progression.
“These MMPs function in several processes including neural development, tissue remodeling, and tumor progression (24,49,54,55).”
From Differential protective effects of connective tissue growth factor against Aβ neurotoxicity on neurons and glia (2017) · cites this paper as [24]
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New functions for the matrix metalloproteinases in cancer progression
Egeblad, M., & Werb, Z. (2002) · Nature Reviews Cancer · doi:10.1038/nrc745 · Cited by 6,108
Self-citationMatrix metalloproteinase-9 triggers the angiogenic switch during carcinogenesis
Bergers, G., Brekken, R., McMahon, G., Vu, T. H., Itoh, T., Tamaki, K., Tanzawa, K., Thorpe, P., Itohara, S., Werb, Z., et al. (2000) · Nature Cell Biology · doi:10.1038/35036374 · Cited by 2,797
Self-citationMatrix metalloproteinases as modulators of inflammation and innate immunity
Parks, W. C., Wilson, C. L., & López-Boado, Y. S. (2004) · Nature Reviews Immunology · doi:10.1038/nri1418 · Cited by 1,929
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Radisky, D. C., Levy, D. D., Littlepage, L. E., Liu, H., Nelson, C. M., Fata, J. E., Leake, D., Godden, E. L., Albertson, D. G., Angela Nieto, M., et al. (2005) · Nature · doi:10.1038/nature03688 · Cited by 1,284
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- Gross, J. & Lapiere, C. M. Collagenolytic activity in amphibian tissues: a tissue culture assay. Proc. Natl Acad. Sci. USA 47, 1014–1022 (1962). · DOI
- Brinckerhoff, C. E. & Matrisian, L. M. Matrix metalloproteinases: a tail of a frog that became a prince. Nature Rev. Mol. Cell Biol. 3, 207–214 (2002). · DOI
- Birkedal-Hansen, H. et al. Matrix metalloproteinases: a review. Crit. Rev. Oral. Biol. Med. 4, 197–250 (1993). · DOI
- Welgus, H. G., Kobayashi, D. K. & Jeffrey, J. J. The collagen substrate specificity of rat uterus collagenase. J. Biol. Chem. 258, 14162–14165 (1983). · DOI
- Coussens, L. M., Fingleton, B. & Matrisian, L. M. Matrix metalloproteinase inhibitors and cancer: trials and tribulations. Science 295, 2387–2392 (2002). A critical analysis of why MMP inhibitors failed as cancer therapeutics, despite great promise. · DOI · Paper page
- Stickens, D. et al. Altered endochondral bone development in matrix metalloproteinase 13-deficient mice. Development 131, 5883–5895 (2004). · DOI
- Oh, J. et al. Mutations in two matrix metalloproteinase genes, MMP-2 and MT1-MMP, are synthetic lethal in mice. Oncogene 23, 5041–5048 (2004). · DOI
- Ducharme, A. et al. Targeted deletion of matrix metalloproteinase-9 attenuates left ventricular enlargement and collagen accumulation after experimental myocardial infarction. J. Clin. Invest. 106, 55–62 (2000). · DOI
- Rudolph-Owen, L. A., Hulboy, D. L., Wilson, C. L., Mudgett, J. & Matrisian, L. M. Coordinate expression of matrix metalloproteinase family members in the uterus of normal, matrilysin-deficient, and stromelysin-1-deficient mice. Endocrinology 138, 4902–4911 (1997). · DOI
- Bode, W., Gomis-Ruth, F. X. & Stockler, W. Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'. FEBS Lett. 331, 134–140 (1993). · DOI
- Stocker, W. et al. The metzincins--topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases. Protein Science 4, 823–840 (1995). · DOI
- Rawlings, N. D., Morton, F. R. & Barrett, A. J. MEROPS: the peptidase database. Nucleic Acids Res. 34, D270–D272 (2006). · DOI
- Overall, C. M. Molecular determinants of metalloproteinase substrate specificity: matrix metalloproteinase substrate binding domains, modules, and exosites. Mol. Biotechnol. 22, 51–86 (2002). · DOI
- Maskos, K. Crystal structures of MMPs in complex with physiological and pharmacological inhibitors. Biochimie 87, 249–263 (2005). · DOI
- Sternlicht, M. D. & Werb, Z. How matrix metalloproteinases regulate cell behavior. Annu. Rev. Cell. Dev. Biol. 17, 463–516 (2001). · DOI · Paper page
- Streuli, C. Extracellular matrix remodelling and cellular differentiation. Curr. Opin. Cell. Biol. 11, 634–640 (1999). · DOI
- Giannelli, G., Falk-Marzillier, J., Schiraldi, O., Stetler-Stevenson, W. G. & Quaranta, V. Induction of cell migration by matrix metalloprotease-2 cleavage of laminin-5. Science 277, 225–228 (1997). Demonstration that cleavage of an ECM protein reveals a cryptic function, in this case chemokinesis. · DOI · Paper page
- Xu, J. et al. Proteolytic exposure of a cryptic site within collagen type IV is required for angiogenesis and tumor growth in vivo. J. Cell. Biol. 154, 1069–1080 (2001). · DOI
- Pilcher, B. K. et al. The activity of collagenase-1 is required for keratinocyte migration on a type I collagen matrix. J. Cell. Biol. 137, 1445–1457 (1997). · DOI
- Fowlkes, J. L., Thrailkill, K. M., Serra, D. M., Suzuki, K. & Nagase, H. Matrix metalloproteinases as insulin-like growth factor binding protein-degrading proteinases. Prog. Growth Factor Res. 6, 255–263 (1995). · DOI
- Whitelock, J. M., Murdoch, A. D., Iozzo, R. V. & Underwood, P. A. The degradation of human endothelial cell-derived perlecan and release of bound basic fibroblast growth factor by stromelysin, collagenase, plasmin, and heparanases. J. Biol. Chem. 271, 10079–10086 (1996). · DOI
- Wang, Z., Juttermann, R. & Soloway, P. D. TIMP-2 is required for efficient activation of proMMP-2 in vivo. J. Biol. Chem. 275, 26411–26415 (2000). · DOI
- Luo, D., Mari, B., Stoll, I. & Anglard, P. Alternative splicing and promoter usage generates an intracellular stromelysin 3 isoform directly translated as an active matrix metalloproteinase. J. Biol. Chem. 277, 25527–25536 (2002). · DOI
- Peschon, J. J. et al. An essential role for ectodomain shedding in mammalian development. Science 282, 1281–1284 (1998). · DOI
- Suzuki, M., Raab, G., Moses, M. A., Fernandez, C. A. & Klagsbrun, M. Matrix metalloproteinase-3 releases active heparin-binding EGF-like growth factor by cleavage at a specific juxtamembrane site. J. Biol. Chem. 272, 31730–31737 (1997). · DOI
- Montero, J. C., Yuste, L., Diaz-Rodriguez, E., Esparis-Ogando, A. & Pandiella, A. Differential shedding of transmembrane neuregulin isoforms by the tumor necrosis factor-α-converting enzyme. Mol. Cell. Neurosci. 16, 631–648 (2000). · DOI
- Sternlicht, M. D. et al. Mammary ductal morphogenesis requires paracrine activation of stromal EGFR via ADAM17-dependent shedding of epithelial amphiregulin. Development 132, 3923–3933 (2005). · DOI
- Noe, V. et al. Release of an invasion promoter E-cadherin fragment by matrilysin and stromelysin-1. J. Cell Sci. 114, 111–118 (2001). · DOI
- Kajita, M. et al. Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration. J. Cell. Biol. 153, 893–904 (2001). · DOI
- Endo, K. et al. Cleavage of syndecan-1 by membrane type matrix metalloproteinase-1 stimulates cell migration. J. Biol. Chem. 278, 40764–40770 (2003). · DOI
- Li, Q., Park, P. W., Wilson, C. L. & Parks, W. C. Matrilysin shedding of syndecan-1 regulates chemokine mobilization and transepithelial efflux of neutrophils in acute lung injury. Cell 111, 635–646 (2002). · DOI
- Senft, A. P., Korfhagen, T. R., Whitsett, J. A., Shapiro, S. D. & LeVine, A. M. Surfactant protein-D regulates soluble CD14 through matrix metalloproteinase-12. J. Immunol. 174, 4953–4959 (2005). · DOI
- Mohan, R. et al. Matrix metalloproteinase gelatinase B (MMP-9) coordinates and effects epithelial regeneration. J. Biol. Chem. 277, 2065–2072 (2002). · DOI
- Yu, Q. & Stamenkovic, I. Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-β and promotes tumor invasion and angiogenesis. Genes Dev. 14, 163–176 (2000). · DOI · Paper page
- Vu, T. H. et al. MMP-9/gelatinase B is a key regulator of growth plate angiogenesis and apoptosis of hypertrophic chondrocytes. Cell 93, 411–422 (1998). First MMP-null mutant with a tissue-remodelling phenotype and defects in development and angiogenesis. · DOI
- Colnot, C., Sidhu, S. S., Balmain, N. & Poirier, F. Uncoupling of chondrocyte death and vascular invasion in mouse galectin 3 null mutant bones. Dev. Biol. 229, 203–214 (2001). · DOI
- Ortega, N., Behonick, D. J., Colnot, C., Cooper, D. N. & Werb, Z. Galectin-3 is a downstream regulator of matrix metalloproteinase-9 function during endochondral bone formation. Mol. Biol. Cell 16, 3028–3039 (2005). · DOI
- Colnot, C., Thompson, Z., Miclau, T., Werb, Z. & Helms, J. A. Altered fracture repair in the absence of MMP9. Development 130, 4123–4133 (2003). · DOI
- Inada, M. et al. Critical roles for collagenase-3 (Mmp13) in development of growth plate cartilage and in endochondral ossification. Proc. Natl Acad. Sci. USA 101, 17192–17197 (2004). · DOI
- Little, C. B. et al. Matrix metalloproteinases are not essential for aggrecan turnover during normal skeletal growth and development. Mol. Cell. Biol. 25, 3388–3399 (2005). · DOI
- Holmbeck, K. et al. MT1-MMP-deficient mice develop dwarfism, osteopenia, arthritis, and connective tissue disease due to inadequate collagen turnover. Cell 99, 81–92 (1999). Demonstration that loss of an MMP decreases ECM remodelling with the surprising consequence of increased bone loss and arthritis; previously these phenotypes were thought to be the consequence of excess proteolysis. · DOI · Paper page
- Zhou, Z. et al. Impaired endochondral ossification and angiogenesis in mice deficient in membrane-type matrix metalloproteinase I. Proc. Natl Acad. Sci. USA 97, 4052–4057 (2000). · DOI · Paper page
- Ohuchi, E. et al. Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules. J. Biol. Chem. 272, 2446–2451 (1997). · DOI · Paper page
- Holmbeck, K., Bianco, P., Chrysovergis, K., Yamada, S. & Birkedal-Hansen, H. MT1-MMP-dependent, apoptotic remodeling of unmineralized cartilage: a critical process in skeletal growth. J. Cell. Biol. 163, 661–671 (2003). · DOI
- Oblander, S. A. et al. Distinctive functions of membrane type 1 matrix-metalloprotease (MT1-MMP or MMP-14) in lung and submandibular gland development are independent of its role in pro-MMP-2 activation. Dev. Biol. 277, 255–269 (2005). · DOI
- Martignetti, J. A. et al. Mutation of the matrix metalloproteinase 2 gene (MMP2) causes a multicentric osteolysis and arthritis syndrome. Nature Genet. 28, 261–265 (2001). · DOI
- Kennedy, A. M. et al. MMP13 mutation causes spondyloepimetaphyseal dysplasia, Missouri type (SEMDM O). J. Clin. Invest. 115, 2832–2842 (2005). · DOI
- Kim, J. W. et al. MMP-20 mutation in autosomal recessive pigmented hypomaturation amelogenesis imperfecta. J. Med. Genet. 42, 271–275 (2005). · DOI
- Inoue, K. et al. A crucial role for matrix metalloproteinase 2 in osteocytic canalicular formation and bone metabolism. J. Biol. Chem. 281, 33814–33824 (2006). · DOI
- Strongin, A. Y. et al. Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease. J. Biol. Chem. 270, 5331–5338 (1995). · DOI
- Sato, H. et al. A matrix metalloproteinase expressed on the surface of invasive tumor cells. Nature 370, 61–65 (1994). Discovery of the first transmembrane MMP, MMP14 (MT1-MMP). This discovery changed the concept of pericellular proteolysis. · DOI
- Sternlicht, M. D., Kouros-Mehr, H., Lu, P. & Werb, Z. Hormonal and local control of mammary branching morphogenesis. Differentiation 74, 365–381 (2006). · DOI
- Wiseman, B. S. et al. Site-specific inductive and inhibitory activities of MMP-2 and MMP-3 orchestrate mammary gland branching morphogenesis. J. Cell. Biol. 162, 1123–1133 (2003). · DOI
- Kato, T. et al. Diminished corneal angiogenesis in gelatinase A-deficient mice. FEBS Lett. 508, 187–190 (2001). · DOI
- Lambert, V. et al. MMP-2 and MMP-9 synergize in promoting choroidal neovascularization. FASEB J. 17, 2290–2292 (2003). · DOI
- Chun, T. H. et al. MT1-MMP-dependent neovessel formation within the confines of the three-dimensional extracellular matrix. J. Cell. Biol. 167, 757–767 (2004). · DOI
- Filippov, S. et al. MT1-matrix metalloproteinase directs arterial wall invasion and neointima formation by vascular smooth muscle cells. J. Exp. Med. 202, 663–671 (2005). · DOI
- Chantrain, C. F. et al. Stromal matrix metalloproteinase-9 regulates the vascular architecture in neuroblastoma by promoting pericyte recruitment. Cancer Res. 64, 1675–1686 (2004). · DOI
- Lehti, K. et al. An MT1-MMP–PDGF receptor-β axis regulates mural cell investment of the microvasculature. Genes Dev. 19, 979–991 (2005). · DOI
- Park, J. E., Keller, G. A. & Ferrara, N. The vascular endothelial growth factor (VEGF) isoforms: differential deposition into the subepithelial extracellular matrix and bioactivity of extracellular matrix-bound VEGF. Mol. Biol. Cell 4, 1317–1326 (1993). · DOI
- Bergers, G., Hanahan, D. & Coussens, L. M. Angiogenesis and apoptosis are cellular parameters of neoplastic progression in transgenic mouse models of tumorigenesis. Int. J. Dev. Biol. 42, 995–1002 (1998). Discovery that MMP-regulated bioavailability of VEGF regulated the angiogenic switch early in tumour progression.
- Lee, S., Jilani, S. M., Nikolova, G. V., Carpizo, D. & Iruela-Arispe, M. L. Processing of VEGF-A by matrix metalloproteinases regulates bioavailability and vascular patterning in tumors. J. Cell. Biol. 169, 681–691 (2005). · DOI
- Hasebe, T., Hartman, R., Fu, L., Amano, T. & Shi, Y. B. Evidence for a cooperative role of gelatinase A and membrane type-1 matrix metalloproteinase during Xenopus laevis development. Mech. Dev. 124, 11–22 (2007). · DOI
- Harrison, M. et al. Matrix metalloproteinase genes in Xenopus development. Dev. Dyn. 231, 214–220 (2004). · DOI
- Leontovich, A. A., Zhang, J., Shimokawa, K., Nagase, H. & Sarras, M. P. Jr. A novel hydra matrix metalloproteinase (HMMP) functions in extracellular matrix degradation, morphogenesis and the maintenance of differentiated cells in the foot process. Development 127, 907–920 (2000). · DOI
- Yoong, S. et al. Characterization of the zebrafish matrix metalloproteinase 9 gene and its developmental expression pattern. Gene Expr. Patterns 7, 39–46 (2007). · DOI
- Bai, S. et al. Matrix metalloproteinase expression and function during fin regeneration in zebrafish: analysis of MT1-MMP, MMP2 and TIMP2. Matrix Biol. 24, 247–260 (2005). · DOI
- Zhang, J., Bai, S., Zhang, X., Nagase, H. & Sarras, M. P. Jr. The expression of novel membrane-type matrix metalloproteinase isoforms is required for normal development of zebrafish embryos. Matrix Biol. 22, 279–293 (2003). · DOI
- Sherwood, D. R., Butler, J. A., Kramer, J. M. & Sternberg, P. W. FOS-1 promotes basement-membrane removal during anchor-cell invasion in C. elegans. Cell 121, 951–962 (2005). · DOI
- Wada, K. et al. Cloning of three Caenorhabditis elegans genes potentially encoding novel matrix metalloproteinases. Gene 211, 57–62 (1998). · DOI
- Llano, E. et al. Structural and enzymatic characterization of Drosophila Dm2-MMP, a membrane-bound matrix metalloproteinase with tissue-specific expression. J. Biol. Chem. 277, 23321–23329 (2002). · DOI · Paper page
- Llano, E., Pendas, A. M., Aza-Blanc, P., Kornberg, T. B. & Lopez-Otin, C. Dm1-MMP, a matrix metalloproteinase from Drosophila with a potential role in extracellular matrix remodeling during neural development. J. Biol. Chem. 275, 35978–35985 (2000). · DOI · Paper page
- Page-McCaw, A., Serano, J., Sante, J. M. & Rubin, G. M. Drosophila matrix metalloproteinases are required for tissue remodeling, but not embryonic development. Dev. Cell 4, 95–106 (2003). A clear demonstration of the important role of MMPs in tissue remodelling. · DOI
- Wei, S., Xie, Z., Filenova, E. & Brew, K. Drosophila TIMP is a potent inhibitor of MMPs and TACE: similarities in structure and function to TIMP-3. Biochemistry 42, 12200–12207 (2003). · DOI
- Beitel, G. J. & Krasnow, M. A. Genetic control of epithelial tube size in the Drosophila tracheal system. Development 127, 3271–3282 (2000). · DOI
- Zhang, S. et al. An MMP liberates the Ninjurin A ectodomain to signal a loss of cell adhesion. Genes Dev. 20, 1899–1910 (2006). Demonstration that MMP cleavage regulates adhesion and signalling. · DOI
- Uhlirova, M. & Bohmann, D. JNK- and Fos-regulated MMP1 expression cooperates with Ras to induce invasive tumors in Drosophila. EMBO J. 25, 5294–5304 (2006). Following loss of MMPs, mutant tissue overproliferates, resists apoptosis, leaves its site of origin and invades other organs, ultimately causing lethality. · DOI · Paper page
- Beaucher, M., Herspberger, E., Page-McCaw, A. & Shearn, A. Metastatic ability of Drosophila tumors depends on MMP activity. Dev. Biol. 5 Dec 2006 (doi:10.1016/j.ydbio.2006.12.001). · DOI · Paper page
- Lopez-Boado, Y. S. et al. Bacterial exposure induces and activates matrilysin in mucosal epithelial cells. J. Cell. Biol. 148, 1305–1315 (2000). · DOI
- Wilson, C. L. et al. Regulation of intestinal-defensin activation by the metalloproteinase matrilysin in innate host defense. Science 286, 113–117 (1999). · DOI
- McGuire, J. K., Li, Q. & Parks, W. C. Matrilysin (matrix metalloproteinase-7) mediates E-cadherin ectodomain shedding in injured lung epithelium. Am. J. Pathol. 162, 1831–1843 (2003). · DOI
- Dunsmore, S. E. et al. Matrilysin expression and function in airway epithelium. J. Clin. Invest. 102, 1321–1331 (1998). · DOI
- Bullard, K. M. et al. Impaired wound contraction in stromelysin-1-deficient mice. Ann. Surg. 230, 260–265 (1999). · DOI
- Haas, T. L. & Madri, J. A. Extracellular matrix-driven matrix metalloproteinase production in endothelial cells: implications for angiogenesis. Trends Cardiovasc. Med. 9, 70–77 (1999). · DOI
- Haro, H. et al. Matrix metalloproteinase-3-dependent generation of a macrophage chemoattractant in a model of herniated disc resorption. J. Clin. Invest. 105, 133–141 (2000). · DOI
- Wang, M. et al. Matrix metalloproteinase deficiencies affect contact hypersensitivity: stromelysin-1 deficiency prevents the response and gelatinase B deficiency prolongs the response. Proc. Natl Acad. Sci. USA 96, 6885–6889 (1999). · DOI
- Zheng, T. et al. Inducible targeting of IL-13 to the adult lung causes matrix metalloproteinase- and cathepsin-dependent emphysema. J. Clin. Invest. 106, 1081–1093 (2000). · DOI
- Kumagai, K. et al. Inhibition of matrix metalloproteinases prevents allergen-induced airway inflammation in a murine model of asthma. J. Immunol. 162, 4212–4219 (1999). · DOI
- Overall, C. M., McQuibban, G. A. & Clark-Lewis, I. Discovery of chemokine substrates for matrix metalloproteinases by exosite scanning: a new tool for degradomics. Biol. Chem. 383, 1059–1066 (2002). · DOI
- Van den Steen, P. E., Proost, P., Wuyts, A., Van Damme, J. & Opdenakker, G. Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-α and leaves RANTES and MCP-2 intact. Blood 96, 2673–2681 (2000). · DOI
- D'Haese, A. et al. In vivo neutrophil recruitment by granulocyte chemotactic protein-2 is assisted by gelatinase B/MMP-9 in the mouse. J. Interferon Cytokine Res. 20, 667–674 (2000). · DOI
- Corry, D. B. et al. Decreased allergic lung inflammatory cell egression and increased susceptibility to asphyxiation in MMP2-deficiency. Nature Immunol. 3, 347–353 (2002). · DOI
- Corry, D. B. et al. Overlapping and independent contributions of MMP2 and MMP9 to lung allergic inflammatory cell egression through decreased CC chemokines. FASEB J. 18, 995–997 (2004). · DOI
- Greenlee, K. J. et al. Proteomic identification of in vivo substrates for matrix metalloproteinases 2 and 9 reveals a mechanism for resolution of inflammation. J. Immunol. 177, 7312–7321 (2006). · DOI
- Liu, Z. et al. The serpin α1-proteinase inhibitor is a critical substrate for gelatinase B/MMP-9 in vivo. Cell 102, 647–655 (2000). · DOI
- McQuibban, G. A. et al. Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3. Science 289, 1202–1206 (2000). First demonstration that a main role of MMPs is to regulate chemokine activity and therefore the chemoattraction of immune cells. · DOI
- McQuibban, G. A. et al. Matrix metalloproteinase activity inactivates the CXC chemokine stromal cell-derived factor-1. J. Biol. Chem. 276, 43503–43508 (2001). · DOI
- McQuibban, G. A. et al. Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo. Blood 100, 1160–1167 (2002). · DOI
- Van Den Steen, P. E. et al. Gelatinase B/MMP-9 and neutrophil collagenase/MMP-8 process the chemokines human GCP-2/CXCL6, ENA-78/CXCL5 and mouse GCP-2/LIX and modulate their physiological activities. Eur. J. Biochem. 270, 3739–3749 (2003). · DOI
- Van Lint, P. et al. Resistance of collagenase-2 (matrix metalloproteinase-8)-deficient mice to TNF-induced lethal hepatitis. J. Immunol. 175, 7642–7649 (2005). · DOI
- Balbin, M. et al. Loss of collagenase-2 confers increased skin tumor susceptibility to male mice. Nature Genet. 35, 252–257 (2003). · DOI
- Weathington, N. M. et al. A novel peptide CXCR ligand derived from extracellular matrix degradation during airway inflammation. Nature Med. 12, 317–323 (2006). · DOI
- Asahi, M. et al. Effects of matrix metalloproteinase-9 gene knock-out on the proteolysis of blood-brain barrier and white matter components after cerebral ischemia. J. Neurosci. 21, 7724–7732 (2001). · DOI · Paper page
- Lee, M. M. et al. Tissue inhibitor of metalloproteinase 1 regulates resistance to infection. Infect. Immun. 73, 661–665 (2005). · DOI
- Vermaelen, K. Y. et al. Matrix metalloproteinase-9-mediated dendritic cell recruitment into the airways is a critical step in a mouse model of asthma. J. Immunol. 171, 1016–1022 (2003). · DOI
- Lanone, S. et al. Overlapping and enzyme-specific contributions of matrix metalloproteinases-9 and-12 in IL-13-induced inflammation and remodeling. J. Clin. Invest. 110, 463–474 (2002). · DOI
- Pyo, R. et al. Targeted gene disruption of matrix metalloproteinase-9 (gelatinase B) suppresses development of experimental abdominal aortic aneurysms. J. Clin. Invest. 105, 1641–1649 (2000). · DOI
- Lelongt, B. et al. Matrix metalloproteinase 9 protects mice from anti-glomerular basement membrane nephritis through its fibrinolytic activity. J. Exp. Med. 193, 793–802 (2001). · DOI
- McMillan, S. J. et al. Matrix metalloproteinase-9 deficiency results in enhanced allergen-induced airway inflammation. J. Immunol. 172, 2586–2594 (2004). · DOI
- Hautamaki, R. D., Kobayashi, D. K., Senior, R. M. & Shapiro, S. D. Requirement for macrophage elastase for cigarette smoke-induced emphysema in mice. Science 277, 2002–2004 (1997). · DOI
- Morris, D. G. et al. Loss of integrin α(v)β6-mediated TGF-β activation causes Mmp12-dependent emphysema. Nature 422, 169–173 (2003). · DOI
- Liu, Z. et al. Synergy between a plasminogen cascade and MMP-9 in autoimmune disease. J. Clin. Invest. 115, 879–887 (2005). · DOI
- Esparza, J., Kruse, M., Lee, J., Michaud, M. & Madri, J. A. MMP-2 null mice exhibit an early onset and severe experimental autoimmune encephalomyelitis due to an increase in MMP-9 expression and activity. FASEB J. 18, 1682–1691 (2004). · DOI
- Lopez-Otin, C. & Overall, C. M. Protease degradomics: a new challenge for proteomics. Nature Rev. Mol. Cell Biol. 3, 509–519 (2002). · DOI · Paper page
- Sottrup-Jensen, L. & Birkedal-Hansen, H. Human fibroblast collagenase-α-macroglobulin interactions. Localization of cleavage sites in the bait regions of five mammalian a-macroglobulins. J. Biol. Chem. 264, 393–401 (1989). · DOI
- Chase, A. J. & Newby, A. C. Regulation of matrix metalloproteinase (matrixin) genes in blood vessels: a multi-step recruitment model for pathological remodelling. J. Vasc. Res. 40, 329–343 (2003). · DOI
- Leeman, M. F., Curran, S. & Murray, G. I. The structure, regulation, and function of human matrix metalloproteinase-13. Crit. Rev. Biochem. Mol. Biol. 37, 149–166 (2002). · DOI
- Ortega, N. & Werb, Z. New functional roles for non-collagenous domains of basement membrane collagens. J. Cell Sci. 115, 4201–4214 (2002). · DOI
- Nyberg, P., Xie, L. & Kalluri, R. Endogenous inhibitors of angiogenesis. Cancer Res. 65, 3967–3979 (2005). · DOI
- Kalluri, R. Basement membranes: structure, assembly and role in tumour angiogenesis. Nature Rev. Cancer 3, 422–433 (2003). · DOI
- Sund, M. et al. Function of endogenous inhibitors of angiogenesis as endothelium-specific tumor suppressors. Proc. Natl Acad. Sci. USA 102, 2934–2939 (2005). · DOI
- Larrain, J. et al. BMP-binding modules in chordin: a model for signalling regulation in the extracellular space. Development 127, 821–830 (2000). · DOI
- De Robertis, E. M. Spemann's organizer and self-regulation in amphibian embryos. Nature Rev. Mol. Cell Biol. 7, 296–302 (2006). · DOI · Paper page
- Hamano, Y. et al. Physiological levels of tumstatin, a fragment of collagen IV α3 chain, are generated by MMP-9 proteolysis and suppress angiogenesis via αV β3 integrin. Cancer Cell 3, 589–601 (2003). Shows the molecular mechanisms that underlie the function of new bioactive molecules generated from extracellular matrix by MMPs. · DOI
- Houghton, A. M. et al. Macrophage elastase (matrix metalloproteinase-12) suppresses growth of lung metastases. Cancer Res. 66, 6149–6155 (2006). · DOI
- Fjeldstad, K. & Kolset, S. O. Decreasing the metastatic potential in cancers--targeting the heparan sulfate proteoglycans. Curr. Drug Targets 6, 665–682 (2005). · DOI
- Gu, Z. et al. A highly specific inhibitor of matrix metalloproteinase-9 rescues laminin from proteolysis and neurons from apoptosis in transient focal cerebral ischemia. J. Neurosci. 25, 6401–6408 (2005). · DOI
- Trackman, P. C. Diverse biological functions of extracellular collagen processing enzymes. J. Cell Biochem. 96, 927–937 (2005). · DOI
- Fukui, N. et al. Processing of type II procollagen amino propeptide by matrix metalloproteinases. J. Biol. Chem. 277, 2193–2201 (2002). · DOI
- Dusek, R. L. et al. The differentiation-dependent desmosomal cadherin desmoglein 1 is a novel caspase-3 target that regulates apoptosis in keratinocytes. J. Biol. Chem. 281, 3614–3624 (2006). · DOI
- Illman, S. A., Lehti, K., Keski-Oja, J. & Lohi, J. Epilysin (MMP-28) induces TGF-β mediated epithelial to mesenchymal transition in lung carcinoma cells. J. Cell Sci. 119, 3856–3865 (2006). · DOI
- Duong, T. D. & Erickson, C. A. MMP-2 plays an essential role in producing epithelial-mesenchymal transformations in the avian embryo. Dev. Dyn. 229, 42–53 (2004). · DOI
- Song, W., Jackson, K. & McGuire, P. G. Degradation of type IV collagen by matrix metalloproteinases is an important step in the epithelial-mesenchymal transformation of the endocardial cushions. Dev. Biol. 227, 606–617 (2000). · DOI
- Sternlicht, M. D. et al. The stromal proteinase MMP3/stromelysin-1 promotes mammary carcinogenesis. Cell 98, 137–146 (1999). Demonstrates that MMPs not only facilitate cell invasion, but can also initiate tumour progression directly. · DOI
- Takahashi, C. et al. Regulation of matrix metalloproteinase-9 and inhibition of tumor invasion by the membrane-anchored glycoprotein RECK. Proc. Natl Acad. Sci. USA 95, 13221–13226 (1998). · DOI
- Fernandez-Patron, C., Radomski, M. W. & Davidge, S. T. Vascular matrix metalloproteinase-2 cleaves big endothelin-1 yielding a novel vasoconstrictor. Circ. Res. 85, 906–911 (1999). · DOI
- Xu, J., Park, P. W., Kheradmand, F. & Corry, D. B. Endogenous attenuation of allergic lung inflammation by syndecan-1. J. Immunol. 174, 5758–5765 (2005). · DOI
- Hinkle, C. L. et al. Multiple metalloproteinases process protransforming growth factor-α (proTGF-α). Biochemistry 42, 2127–2136 (2003). · DOI
- Sahin, U. et al. Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands. J. Cell. Biol. 164, 769–779 (2004). · DOI
- Ii, M., Yamamoto, H., Adachi, Y., Maruyama, Y. & Shinomura, Y. Role of matrix metalloproteinase-7 (matrilysin) in human cancer invasion, apoptosis, growth, and angiogenesis. Exp. Biol. Med. 231, 20–27 (2006). · DOI
- Zhang, K. et al. HIV-induced metalloproteinase processing of the chemokine stromal cell derived factor-1 causes neurodegeneration. Nature Neurosci. 6, 1064–1071 (2003). Shows that MMPs regulate survival factors and excess activity can lead to cell death. · DOI
- Mizgerd, J. P., Spieker, M. R. & Doerschuk, C. M. Early response cytokines and innate immunity: essential roles for TNF receptor 1 and type I IL-1 receptor during Escherichia coli pneumonia in mice. J. Immunol. 166, 4042–4048 (2001). · DOI
- Xu, H., Uysal, K. T., Becherer, J. D., Arner, P. & Hotamisligil, G. S. Altered tumor necrosis factor-α (TNF-α) processing in adipocytes and increased expression of transmembrane TNF-α in obesity. Diabetes 51, 1876–1883 (2002). · DOI
- Chun, T. H. et al. A pericellular collagenase directs the 3-dimensional development of white adipose tissue. Cell 125, 577–591 (2006). This study shows that MMPs contribute to the architectural context of cells and argues that this might be necessary for the conversion of pre-adipocytes to adipocytes. · DOI · Paper page
- Alexander, C. M., Selvarajan, S., Mudgett, J. & Werb, Z. Stromelysin-1 regulates adipogenesis during mammary gland involution. J. Cell. Biol. 152, 693–703 (2001). · DOI
- Gerber, H. P. & Ferrara, N. Angiogenesis and bone growth. Trends Cardiovasc. Med. 10, 223–228 (2000). · DOI
- Harper, J. & Klagsbrun, M. Cartilage to bone — angiogenesis leads the way. Nature Med. 5, 617–618 (1999). · DOI
- Itoh, T. et al. Unaltered secretion of β-amyloid precursor protein in gelatinase A (matrix metalloproteinase 2)-deficient mice. J. Biol. Chem. 272, 22389–22392 (1997). · DOI
- Kheradmand, F., Rishi, K. & Werb, Z. Signaling through the EGF receptor controls lung morphogenesis in part by regulating MT1-MMP-mediated activation of gelatinase A/MMP2. J. Cell Sci. 115, 839–848 (2002). · DOI
- VanSaun, M., Herrera, A. A. & Werle, M. J. Structural alterations at the neuromuscular junctions of matrix metalloproteinase 3 null mutant mice. J. Neurocytol. 32, 1129–1142 (2003). · DOI
- Larsen, P. H., Wells, J. E., Stallcup, W. B., Opdenakker, G. & Yong, V. W. Matrix metalloproteinase-9 facilitates remyelination in part by processing the inhibitory NG2 proteoglycan. J. Neurosci. 23, 11127–11135 (2003). · DOI
- Galis, Z. S. et al. Targeted disruption of the matrix metalloproteinase-9 gene impairs smooth muscle cell migration and geometrical arterial remodeling. Circ. Res. 91, 852–859 (2002). · DOI
- Masson, R. et al. In vivo evidence that the stromelysin-3 metalloproteinase contributes in a paracrine manner to epithelial cell malignancy. J. Cell. Biol. 140, 1535–1541 (1998). · DOI
- Wells, J. E. et al. An adverse role for matrix metalloproteinase 12 after spinal cord injury in mice. J. Neurosci. 23, 10107–10115 (2003). · DOI
- Uchinami, H., Seki, E., Brenner, D. A. & D'Armiento, J. Loss of MMP 13 attenuates murine hepatic injury and fibrosis during cholestasis. Hepatology 44, 420–429 (2006). · DOI
- Deguchi, J. O. et al. Matrix metalloproteinase-13/collagenase-3 deletion promotes collagen accumulation and organization in mouse atherosclerotic plaques. Circulation 112, 2708–2715 (2005). · DOI
- Holmbeck, K. et al. The metalloproteinase MT1-MMP is required for normal development and maintenance of osteocyte processes in bone. J. Cell Sci. 118, 147–156 (2005). · DOI
- Beertsen, W. et al. On the role of MT1-MMP, a matrix metalloproteinase essential to collagen remodeling, in murine molar eruption and root growth. Eur. J. Oral Sci. 110, 445–451 (2002). · DOI
- Atkinson, J. J. et al. Membrane-type 1 matrix metalloproteinase is required for normal alveolar development. Dev. Dyn. 232, 1079–1090 (2005). · DOI
- Pendas, A. M. et al. Diet-induced obesity and reduced skin cancer susceptibility in matrix metalloproteinase 19-deficient mice. Mol. Cell. Biol. 24, 5304–5313 (2004). · DOI
- Caterina, J. J. et al. Enamelysin (matrix metalloproteinase 20)-deficient mice display an amelogenesis imperfecta phenotype. J. Biol. Chem. 277, 49598–49604 (2002). · DOI
- Komori, K. et al. Absence of mechanical allodynia and Aβ-fiber sprouting after sciatic nerve injury in mice lacking membrane-type 5 matrix metalloproteinase. FEBS Lett. 557, 125–128 (2004). · DOI
- Zhou, H. E., Zhang, X. & Nothnick, W. B. Disruption of the TIMP-1 gene product is associated with accelerated endometrial gland formation during early postnatal uterine development. Biol. Reprod. 71, 534–539 (2004). · DOI
- Chaillan, F. A. et al. Involvement of tissue inhibition of metalloproteinases-1 in learning and memory in mice. Behav. Brain Res. 173, 191–198 (2006). · DOI
- Mohammed, F. F. et al. Metalloproteinase inhibitor TIMP-1 affects hepatocyte cell cycle via HGF activation in murine liver regeneration. Hepatology 41, 857–867 (2005). · DOI
- Jaworski, D. M., Soloway, P., Caterina, J. & Falls, W. A. Tissue inhibitor of metalloproteinase-2 (TIMP-2)-deficient mice display motor deficits. J. Neurobiol. 66, 82–94 (2006). · DOI
- Fata, J. E. et al. Accelerated apoptosis in the TIMP-3-deficient mammary gland. J. Clin. Invest. 108, 831–841 (2001). · DOI
- Gill, S. E., Pape, M. C., Khokha, R., Watson, A. J. & Leco, K. J. A null mutation for tissue inhibitor of metalloproteinases-3 (TIMP-3) impairs murine bronchiole branching morphogenesis. Dev. Biol. 261, 313–323 (2003). · DOI
- Cruz-Munoz, W. et al. Enhanced metastatic dissemination to multiple organs by melanoma and lymphoma cells in Timp-3−/− mice. Oncogene 25, 6489–6496 (2006). · DOI
- English, J. L. et al. Individual Timp deficiencies differentially impact pro-MMP-2 activation. J. Biol. Chem. 281, 10337–10346 (2006). · DOI · Paper page
- Godenschwege, T. A., Pohar, N., Buchner, S. & Buchner, E. Inflated wings, tissue autolysis and early death in tissue inhibitor of metalloproteinases mutants of Drosophila. Eur. J. Cell Biol. 79, 495–501 (2000). · DOI
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Metadata
- Authors
- Page-McCaw, A., Ewald, A. J., & Werb, Z.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2007-03
- Volume
- 8
- Issue
- 3
- Pages
- 221-233
- ISSN
- 1471-0072
- 1471-0080
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