CoChat
Sign Up
Cited by 401

The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.

Membrane-type matrix metalloproteinases: Their functions and regulations

Itoh, Yoshifumi·2015·Matrix Biology
DOI 10.1016/j.matbio.2015.03.004
Open this paper in CoChat — free account

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1016/j.matbio.2015.03.004

Cites

5 of 5 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • MT1-MMP is highly expressed in various types of cancer cells and promotes cancer metastasis and angiogenesis.

    “It is well documented that MT1-MMP is highly expressed in various types of cancer cells and promotes cancer metastasis and angiogenesis16,44,47–50.”

    From Membrane type 1 matrix metalloproteinase promotes LDL receptor shedding and accelerates the development of atherosclerosis (2021) · cites this paper as [16]

    The MT1-MMP section identifies the enzyme as involved in cancer-cell invasion, metastasis, and angiogenesis, and says it was discovered in invasive cancer cells. The Gene and protein expression section describes MT1-MMP upregulation in particular cells under particular conditions, but does not establish that it is highly expressed across various types of cancer cells. Page numbers are unavailable in our copy. (LLM, conf=0.85)

    Experimental — accuracy not yet measured

  • MT1-MMP is highly expressed in multiple cancer cell types promoting metastasis and invasion.

    “Interestingly, MT1-MMP is also highly expressed in multiple cancer cell types promoting metastasis and invasion106,108, thus inhibiting MT1-MMP holds both promise as a therapeutic target to reduce the risk of cancer metastasis and lower plasma LDL cholesterol.”

    From Pathways and Molecular Mechanisms Governing LDL Receptor Regulation (2025) · cites this paper as [106]

    The MT1-MMP section identifies MT1-MMP as a promoter of cancer-cell invasion and metastasis. The Gene and protein expression section describes its upregulation in particular cancer cell lines under specified conditions, but does not establish that it is generally highly expressed across multiple cancer cell types. (LLM, conf=0.84)

    Experimental — accuracy not yet measured

  • MT1-MMP plays an essential role in tissue remodelling by cleaving extracellular matrix components and many non-extracellular matrix substrates.

    “MT1-MMP plays an essential role in tissue remodelling by cleaving extracellular matrix components and many non-extracellular matrix substrates16,20,21,43.”

    From Membrane type 1 matrix metalloproteinase promotes LDL receptor shedding and accelerates the development of atherosclerosis (2021) · cites this paper as [16]

  • MT1-MMP is a transmembrane protease with major and well-established functions in remodelling extracellular matrix proteins.

    “MT1-MMP is a transmembrane protease that has major and well-established functions in the remodelling of extracellular matrix proteins [57].”

    From Post-translational regulation of the low-density lipoprotein receptor provides new targets for cholesterol regulation (2024) · cites this paper as [57]

  • MT1-MMP is highly expressed in various types of cancer cells and promotes cancer metastasis and angiogenesis.

    “MT1-MMP is highly expressed in various types of cancer cells and promotes cancer metastasis and angiogenesis [57,59].”

    From Post-translational regulation of the low-density lipoprotein receptor provides new targets for cholesterol regulation (2024) · cites this paper as [57]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 189

  1. Sato, 1994, A matrix metalloproteinase expressed on the surface of invasive tumour cells, Nature, 370, 61, 10.1038/370061a0 · DOI
  2. Will, 1995, cDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment, Eur J Biochem, 231, 602, 10.1111/j.1432-1033.1995.tb20738.x · DOI
  3. Takino, 1995, Identification of the second membrane-type matrix metalloproteinase (MT-MMP-2) gene from a human placenta cDNA library. MT-MMPs form a unique membrane-type subclass in the MMP family, J Biol Chem, 270, 23013, 10.1074/jbc.270.39.23013 · DOI
  4. Puente, 1996, Molecular cloning of a novel membrane-type matrix metalloproteinase from a human breast carcinoma, Cancer Res, 56, 944
  5. Pei, 1999, Identification and characterization of the fifth membrane-type matrix metalloproteinase MT5-MMP, J Biol Chem, 274, 8925, 10.1074/jbc.274.13.8925 · DOI
  6. Llano, 1999, Identification and characterization of human MT5-MMP, a new membrane- bound activator of progelatinase a overexpressed in brain tumors [In Process Citation], Cancer Res, 59, 2570
  7. Pei, 1999, Leukolysin/MMP25/MT6-MMP: a novel matrix metalloproteinase specifically expressed in the leukocyte lineage, Cell Res, 9, 291, 10.1038/sj.cr.7290028 · DOI
  8. Velasco, 2000, Human MT6-matrix metalloproteinase: identification, progelatinase A activation, and expression in brain tumors, Cancer Res, 60, 877
  9. Zhao, 2008, Identification and role of the homodimerization interface of the glycosylphosphatidylinositol-anchored membrane type 6 matrix metalloproteinase (MMP25), J Biol Chem, 283, 35023, 10.1074/jbc.M806553200 · DOI
  10. Ohuchi, 1997, Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules, J Biol Chem, 272, 2446, 10.1074/jbc.272.4.2446 · DOI · Paper page
  11. Morrison, 2006, TIMP independence of matrix metalloproteinase (MMP)-2 activation by membrane type 2 (MT2)-MMP is determined by contributions of both the MT2-MMP catalytic and hemopexin C domains, J Biol Chem, 281, 26528, 10.1074/jbc.M603331200 · DOI
  12. Shimada, 1999, Characterization of a truncated recombinant form of human membrane type 3 matrix metalloproteinase, Eur J Biochem, 262, 907, 10.1046/j.1432-1327.1999.00459.x · DOI
  13. Hiraoka, 1998, Matrix metalloproteinases regulate neovascularization by acting as pericellular fibrinolysins, Cell, 95, 365, 10.1016/S0092-8674(00)81768-7 · DOI
  14. Hotary, 2002, Matrix metalloproteinases (MMPs) regulate fibrin-invasive activity via MT1-MMP-dependent and -independent processes, J Exp Med, 195, 295, 10.1084/jem.20010815 · DOI
  15. Butler, 1997, Membrane-type-2 matrix metalloproteinase can initiate the processing of progelatinase A and is regulated by the tissue inhibitors of metalloproteinases, Eur J Biochem, 244, 653, 10.1111/j.1432-1033.1997.t01-1-00653.x · DOI
  16. Gao, 2004, J Biol Chem, 279, 10042, 10.1074/jbc.M312100200 · DOI
  17. Folgueras, 2009, Metalloproteinase MT5-MMP is an essential modulator of neuro-immune interactions in thermal pain stimulation, Proc Natl Acad Sci U S A, 106, 16451, 10.1073/pnas.0908507106 · DOI · Paper page
  18. Ries, 2007, MMP-2, MT1-MMP, and TIMP-2 are essential for the invasive capacity of human mesenchymal stem cells: differential regulation by inflammatory cytokines, Blood, 109, 4055, 10.1182/blood-2006-10-051060 · DOI
  19. Imai, 1997, Expression of membrane-type 1 matrix metalloproteinase and activation of progelatinase A in human osteoarthritic cartilage, Am J Pathol, 151, 245
  20. Kadono, 1998, Membrane type 1-matrix metalloproteinase is involved in the formation of hepatocyte growth factor/scatter factor-induced branching tubules in madin-darby canine kidney epithelial cells, Biochem Biophys Res Commun, 251, 681, 10.1006/bbrc.1998.9531 · DOI
  21. Chun, 2006, A pericellular collagenase directs the 3-dimensional development of white adipose tissue, Cell, 125, 577, 10.1016/j.cell.2006.02.050 · DOI · Paper page
  22. Gonzalo, 2010, MT1-MMP is required for myeloid cell fusion via regulation of Rac1 signaling, Dev Cell, 18, 77, 10.1016/j.devcel.2009.11.012 · DOI
  23. Belien, 1999, Membrane-type 1 matrix metalloprotease (MT1-MMP) enables invasive migration of glioma cells in central nervous system white matter, J Cell Biol, 144, 373, 10.1083/jcb.144.2.373 · DOI
  24. Esparza, 1999, Fibronectin upregulates gelatinase B (MMP-9) and induces coordinated expression of gelatinase A (MMP-2) and its activator MT1-MMP (MMP-14) by human T lymphocyte cell lines. A process repressed through RAS/MAP kinase signaling pathways, Blood, 94, 2754, 10.1182/blood.V94.8.2754.420k09_2754_2766 · DOI
  25. Jin, 2011, MT1-MMP cleaves Dll1 to negatively regulate Notch signalling to maintain normal B-cell development, EMBO J, 30, 2281, 10.1038/emboj.2011.136 · DOI · Paper page
  26. Holmbeck, 1999, MT1-MMP-deficient mice develop dwarfism, osteopenia, arthritis, and connective tissue disease due to inadequate collagen turnover, Cell, 99, 81, 10.1016/S0092-8674(00)80064-1 · DOI · Paper page
  27. Zhou, 2000, Impaired endochondral ossification and angiogenesis in mice deficient in membrane-type matrix metalloproteinase I, Proc Natl Acad Sci U S A, 97, 4052, 10.1073/pnas.060037197 · DOI · Paper page
  28. Oblander, 2005, 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, 10.1016/j.ydbio.2004.09.033 · DOI
  29. Irie, 2005, Impaired alveolization in mice deficient in membrane-type matrix metalloproteinase 1 (MT1-MMP), Med Mol Morphol, 38, 43, 10.1007/s00795-004-0277-9 · DOI
  30. Holmbeck, 2004, MT1-MMP: a tethered collagenase, J Cell Physiol, 200, 11, 10.1002/jcp.20065 · DOI
  31. Chan, 2012, MT1-MMP inactivates ADAM9 to regulate FGFR2 signaling and calvarial osteogenesis, Dev Cell, 22, 1176, 10.1016/j.devcel.2012.04.014 · DOI · Paper page
  32. Wong, 2012, When MT1-MMP meets ADAMs, Cell Cycle, 11, 2793, 10.4161/cc.20949 · DOI
  33. Itoh, 2001, Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion, EMBO J, 20, 4782, 10.1093/emboj/20.17.4782 · DOI
  34. Itoh, 2008, The second dimer interface of MT1-MMP, the transmembrane domain, is essential for ProMMP-2 activation on the cell surface, J Biol Chem, 283, 13053, 10.1074/jbc.M709327200 · DOI
  35. Strongin, 1995, 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, 10.1074/jbc.270.10.5331 · DOI
  36. Itoh, 2006, MT1-MMP: A potent modifier of pericellular microenvironment, J Cell Physiol, 206, 1, 10.1002/jcp.20431 · DOI
  37. Will, 1996, The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. Regulation by TIMP-2 and TIMP-3, J Biol Chem, 271, 17119, 10.1074/jbc.271.29.17119 · DOI
  38. English, 2001, Characterization of the role of the "MT-loop": an eight-amino acid insertion specific to progelatinase A (MMP2) activating membrane-type matrix metalloproteinases, J Biol Chem, 276, 42018, 10.1074/jbc.M107783200 · DOI · Paper page
  39. Itoh, 1998, Plasma membrane-bound tissue inhibitor of metalloproteinases (TIMP)-2 specifically inhibits matrix metalloproteinase 2 (gelatinase A) activated on the cell surface, J Biol Chem, 273, 24360, 10.1074/jbc.273.38.24360 · DOI
  40. Okada, 1990, Matrix metalloproteinase 2 from human rheumatoid synovial fibroblasts. Purification and activation of the precursor and enzymic properties, Eur J Biochem, 194, 721, 10.1111/j.1432-1033.1990.tb19462.x · DOI
  41. Taniwaki, 2007, Stroma-derived matrix metalloproteinase (MMP)-2 promotes membrane type 1-MMP-dependent tumor growth in mice, Cancer Res, 67, 4311, 10.1158/0008-5472.CAN-06-4761 · DOI
  42. Knäuper, 1996, Cellular mechanisms for human procollagenase 3 (mmp 13) activation: evidence that mt1 mmp (mmp 14) and gelatinase a (mmp 2) are able to generate active enzyme, J Biol Chem, 271, 17124, 10.1074/jbc.271.29.17124 · DOI
  43. Knäuper, 2002, Cellular activation of proMMP-13 by MT1-MMP depends on the C-terminal domain of MMP-13, FEBS Lett, 532, 127, 10.1016/S0014-5793(02)03654-2 · DOI
  44. Tsunezuka, 1996, Expression of membrane-type matrix metalloproteinase 1 (MT1-MMP) in tumor cells enhances pulmonary metastasis in an experimental metastasis assay, Cancer Res, 56, 5678
  45. Hotary, 2003, Membrane type I matrix metalloproteinase usurps tumor growth control imposed by the three-dimensional extracellular matrix, Cell, 114, 33, 10.1016/S0092-8674(03)00513-0 · DOI
  46. Okada, 1997, Expression of matrix metalloproteinases during rat skin wound healing: evidence that membrane type-1 matrix metalloproteinase is a stromal activator of pro-gelatinase A, J Cell Biol, 137, 67, 10.1083/jcb.137.1.67 · DOI
  47. Sakamoto, 2009, Cytoplasmic tail of MT1-MMP regulates macrophage motility independently from its protease activity, Genes Cells, 14, 617, 10.1111/j.1365-2443.2009.01293.x · DOI
  48. Rajavashisth, 1999, Membrane type 1 matrix metalloproteinase expression in human atherosclerotic plaques: evidence for activation by proinflammatory mediators, Circulation, 99, 3103, 10.1161/01.CIR.99.24.3103 · DOI
  49. Miller, 2009, Membrane type 1 matrix metalloproteinase is a crucial promoter of synovial invasion in human rheumatoid arthritis, Arthritis Rheum, 60, 686, 10.1002/art.24331 · DOI
  50. Sabeh, 2010, Membrane-type I matrix metalloproteinase-dependent regulation of rheumatoid arthritis synoviocyte function, J Immunol, 184, 6396, 10.4049/jimmunol.0904068 · DOI
  51. Itoh, 2006, MT1-MMP: a key regulator of cell migration in tissue, IUBMB Life, 58, 589, 10.1080/15216540600962818 · DOI
  52. Hotary, 2000, Regulation of cell invasion and morphogenesis in a three-dimensional type I collagen matrix by membrane-type matrix metalloproteinases 1, 2, and 3, J Cell Biol, 149, 1309, 10.1083/jcb.149.6.1309 · DOI
  53. Sabeh, 2004, Tumor cell traffic through the extracellular matrix is controlled by the membrane-anchored collagenase MT1-MMP, J Cell Biol, 167, 769, 10.1083/jcb.200408028 · DOI
  54. Koshikawa, 2000, Role of cell surface metalloprotease MT1-MMP in epithelial cell migration over laminin-5, J Cell Biol, 148, 615, 10.1083/jcb.148.3.615 · DOI
  55. Gilles, 2001, Contribution of MT1-MMP and of human laminin-5 gamma2 chain degradation to mammary epithelial cell migration, J Cell Sci, 114, 2967, 10.1242/jcs.114.16.2967 · DOI
  56. Koshikawa, 2010, Membrane type 1-matrix metalloproteinase cleaves off the NH2-terminal portion of heparin-binding epidermal growth factor and converts it into a heparin-independent growth factor, Cancer Res, 70, 6093, 10.1158/0008-5472.CAN-10-0346 · DOI
  57. Kajita, 2001, Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration, J Cell Biol, 153, 893, 10.1083/jcb.153.5.893 · DOI
  58. Nagano, 2004, Cell-matrix interaction via CD44 is independently regulated by different metalloproteinases activated in response to extracellular Ca(2+) influx and PKC activation, J Cell Biol, 165, 893, 10.1083/jcb.200310024 · DOI
  59. Endo, 2003, Cleavage of syndecan-1 by membrane type matrix metalloproteinase-1 stimulates cell migration, J Biol Chem, 278, 40764, 10.1074/jbc.M306736200 · DOI
  60. Deryugina, 2002, Processing of integrin alpha v subunit by membrane type 1 matrix metalloproteinase stimulates migration of breast carcinoma cells on vitronectin and enhances tyrosine phosphorylation of focal adhesion kinase, J Biol Chem, 277, 9749, 10.1074/jbc.M110269200 · DOI
  61. Sithu, 2007, Membrane-type 1-matrix metalloproteinase regulates intracellular adhesion molecule-1 (ICAM-1)-mediated monocyte transmigration, J Biol Chem, 282, 25010, 10.1074/jbc.M611273200 · DOI
  62. Chun, 2004, MT1-MMP-dependent neovessel formation within the confines of the three-dimensional extracellular matrix, J Cell Biol, 167, 757, 10.1083/jcb.200405001 · DOI
  63. Handsley, 2005, Metalloproteinases and their inhibitors in tumor angiogenesis, Int J Cancer, 115, 849, 10.1002/ijc.20945 · DOI
  64. Yana, 2007, Crosstalk between neovessels and mural cells directs the site-specific expression of MT1-MMP to endothelial tip cells, J Cell Sci, 120, 1607, 10.1242/jcs.000679 · DOI
  65. Sounni, 2002, MT1-MMP expression promotes tumor growth and angiogenesis through an up-regulation of vascular endothelial growth factor expression, FASEB J, 16, 555, 10.1096/fj.01-0790com · DOI
  66. Deryugina, 2002, Up-regulation of vascular endothelial growth factor by membrane-type 1 matrix metalloproteinase stimulates human glioma xenograft growth and angiogenesis, Cancer Res, 62, 580
  67. Eisenach, 2010, MT1-MMP regulates VEGF-A expression through a complex with VEGFR-2 and Src, J Cell Sci, 123, 4182, 10.1242/jcs.062711 · DOI
  68. Sakamoto, 2010, A membrane protease regulates energy production in macrophages by activating hypoxia-inducible factor-1 via a non-proteolytic mechanism, J Biol Chem, 285, 29951, 10.1074/jbc.M110.132704 · DOI
  69. Gingras, 2008, Sphingosine-1-phosphate induces the association of membrane-type 1 matrix metalloproteinase with p130Cas in endothelial cells, FEBS Lett, 582, 399, 10.1016/j.febslet.2007.12.029 · DOI
  70. Hoshino, 2009, A novel protein associated with membrane-type 1 matrix metalloproteinase binds p27(kip1) and regulates RhoA activation, actin remodeling, and matrigel invasion, J Biol Chem, 284, 27315, 10.1074/jbc.M109.041400 · DOI
  71. Shimizu-Hirota, 2012, MT1-MMP regulates the PI3Kdelta.Mi-2/NuRD-dependent control of macrophage immune function, Genes Dev, 26, 395, 10.1101/gad.178749.111 · DOI
  72. Ohtake, 2006, Multifunctional roles of MT1-MMP in myofiber formation and morphostatic maintenance of skeletal muscle, J Cell Sci, 119, 3822, 10.1242/jcs.03158 · DOI
  73. Lafleur, 2002, Endothelial tubulogenesis within fibrin gels specifically requires the activity of membrane-type-matrix metalloproteinases (MT-MMPs), J Cell Sci, 115, 3427, 10.1242/jcs.115.17.3427 · DOI
  74. Hotary, 2006, A cancer cell metalloprotease triad regulates the basement membrane transmigration program, Genes Dev, 20, 2673, 10.1101/gad.1451806 · DOI
  75. Ota, 2009, Induction of a MT1-MMP and MT2-MMP-dependent basement membrane transmigration program in cancer cells by Snail1, Proc Natl Acad Sci U S A, 106, 20318, 10.1073/pnas.0910962106 · DOI
  76. Rowe, 2009, Mesenchymal cells reactivate Snail1 expression to drive three-dimensional invasion programs, J Cell Biol, 184, 399, 10.1083/jcb.200810113 · DOI
  77. Rebustini, 2009, MT2-MMP-dependent release of collagen IV NC1 domains regulates submandibular gland branching morphogenesis, Dev Cell, 17, 482, 10.1016/j.devcel.2009.07.016 · DOI
  78. Shofuda, 2001, Membrane-type matrix metalloproteinase-1 and −3 activity in primate smooth muscle cells, FASEB J, 15, 2010, 10.1096/fj.00-0871fje · DOI
  79. Iida, 2007, Cell surface chondroitin sulfate glycosaminoglycan in melanoma: role in the activation of pro-MMP-2 (pro-gelatinase A), Biochem J, 403, 553, 10.1042/BJ20061176 · DOI
  80. Zhao, 2004, Differential inhibition of membrane type 3 (MT3)-matrix metalloproteinase (MMP) and MT1-MMP by tissue inhibitor of metalloproteinase (TIMP)-2 and TIMP-3 rgulates pro-MMP-2 activation, J Biol Chem, 279, 8592, 10.1074/jbc.M308708200 · DOI
  81. Butler, 1999, Human tissue inhibitor of metalloproteinases 3 interacts with both the N- and C-terminal domains of gelatinases A and B. Regulation by polyanions, J Biol Chem, 274, 10846, 10.1074/jbc.274.16.10846 · DOI
  82. Tatti, 2011, Membrane-type-3 matrix metalloproteinase (MT3-MMP) functions as a matrix composition-dependent effector of melanoma cell invasion, PLoS One, 6, e28325, 10.1371/journal.pone.0028325 · DOI
  83. Shi, 2008, Membrane-type MMPs enable extracellular matrix permissiveness and mesenchymal cell proliferation during embryogenesis, Dev Biol, 313, 196, 10.1016/j.ydbio.2007.10.017 · DOI · Paper page
  84. Ferraro, 2011, Membrane-type matrix metalloproteinase-3 regulates neuronal responsiveness to myelin through Nogo-66 receptor 1 cleavage, J Biol Chem, 286, 31418, 10.1074/jbc.M111.249169 · DOI
  85. Kolkenbrock, 1999, Biochemical characterization of the catalytic domain of membrane-type 4 matrix metalloproteinase, Biol Chem, 380, 1103, 10.1515/BC.1999.137 · DOI
  86. English, 2000, Membrane type 4 matrix metalloproteinase (MMP17) has tumor necrosis factor-alpha convertase activity but does not activate pro-MMP2, J Biol Chem, 275, 14046, 10.1074/jbc.275.19.14046 · DOI
  87. Rikimaru, 2007, Establishment of an MT4-MMP-deficient mouse strain representing an efficient tracking system for MT4-MMP/MMP-17 expression in vivo using beta-galactosidase, Genes Cells, 12, 1091, 10.1111/j.1365-2443.2007.01110.x · DOI
  88. Srichai, 2011, Membrane-type 4 matrix metalloproteinase (MT4-MMP) modulates water homeostasis in mice, PLoS One, 6, e17099, 10.1371/journal.pone.0017099 · DOI
  89. Clements, 2011, Matrix metalloproteinase 17 is necessary for cartilage aggrecan degradation in an inflammatory environment, Ann Rheum Dis, 70, 683, 10.1136/ard.2010.130757 · DOI
  90. Chabottaux, 2006, Membrane-type 4 matrix metalloproteinase promotes breast cancer growth and metastases, Cancer Res, 66, 5165, 10.1158/0008-5472.CAN-05-3012 · DOI
  91. Chabottaux, 2009, Membrane-type 4 matrix metalloproteinase (MT4-MMP) induces lung metastasis by alteration of primary breast tumour vascular architecture, J Cell Mol Med, 13, 4002, 10.1111/j.1582-4934.2009.00764.x · DOI
  92. Host, 2012, The proteolytic activity of MT4-MMP is required for its pro-angiogenic and pro-metastatic promoting effects, Int J Cancer, 131, 1537, 10.1002/ijc.27436 · DOI
  93. Paye, 2014, EGFR activation and signaling in cancer cells are enhanced by the membrane-bound metalloprotease MT4-MMP, Cancer Res, 74, 6758, 10.1158/0008-5472.CAN-13-2994 · DOI
  94. Hayashita-Kinoh, 2001, Membrane-type 5 matrix metalloproteinase is expressed in differentiated neurons and regulates axonal growth, Cell Growth Differ, 12, 573
  95. Bar-Or, 2003, Analyses of all matrix metalloproteinase members in leukocytes emphasize monocytes as major inflammatory mediators in multiple sclerosis, Brain, 126, 2738, 10.1093/brain/awg285 · DOI
  96. Komori, 2004, Absence of mechanical allodynia and Abeta-fiber sprouting after sciatic nerve injury in mice lacking membrane-type 5 matrix metalloproteinase, FEBS Lett, 557, 125, 10.1016/S0014-5793(03)01458-3 · DOI
  97. Porlan, 2014, MT5-MMP regulates adult neural stem cell functional quiescence through the cleavage of N-cadherin, Nat Cell Biol, 16, 629, 10.1038/ncb2993 · DOI
  98. Kojima, 2000, Membrane-type 6 matrix metalloproteinase (MT6-MMP, MMP-25) is the second glycosyl-phosphatidyl inositol (GPI)-anchored MMP, FEBS Lett, 480, 142, 10.1016/S0014-5793(00)01919-0 · DOI
  99. Nie, 2003, Direct activation of pro-matrix metalloproteinase-2 by leukolysin/membrane-type 6 matrix metalloproteinase/matrix metalloproteinase 25 at the asn(109)-Tyr bond, Cancer Res, 63, 6758
  100. Wang, 2004, The hemopexin domain of membrane-type matrix metalloproteinase-1 (MT1-MMP) Is not required for its activation of proMMP2 on cell surface but is essential for MT1-MMP-mediated invasion in three-dimensional type I collagen, J Biol Chem, 279, 51148, 10.1074/jbc.M409074200 · DOI
  101. Starr, 2012, Biochemical characterization and N-terminomics analysis of leukolysin, the membrane-type 6 matrix metalloprotease (MMP25): chemokine and vimentin cleavages enhance cell migration and macrophage phagocytic activities, J Biol Chem, 287, 13382, 10.1074/jbc.M111.314179 · DOI
  102. Stanton, 1998, The activation of ProMMP-2 (gelatinase A) by HT1080 fibrosarcoma cells is promoted by culture on a fibronectin substrate and is concomitant with an increase in processing of MT1-MMP (MMP-14) to a 45kDa form, J Cell Sci, 111, 2789, 10.1242/jcs.111.18.2789 · DOI
  103. Yu, 1995, Complex regulation of membrane-type matrix metalloproteinase expression and matrix metalloproteinase-2 activation by concanavalin A in MDA-MB-231 human breast cancer cells, Cancer Res, 55, 3272
  104. Gervasi, 1996, Carbohydrate-mediated regulation of matrix metalloproteinase-2 activation in normal human fibroblasts and fibrosarcoma cells, Biochem Biophys Res Commun, 228, 530, 10.1006/bbrc.1996.1694 · DOI
  105. Tomasek, 1997, Gelatinase A activation is regulated by the organization of the polymerized actin cytoskeleton, J Biol Chem, 272, 7482, 10.1074/jbc.272.11.7482 · DOI
  106. Ruangpanit, 2001, Gelatinase A (MMP-2) activation by skin fibroblasts: dependence on MT1-MMP expression and fibrillar collagen form, Matrix Biol, 20, 193, 10.1016/S0945-053X(01)00135-4 · DOI
  107. Haas, 1999, Egr-1 mediates extracellular matrix-driven transcription of membrane type 1 matrix metalloproteinase in endothelium, J Biol Chem, 274, 22679, 10.1074/jbc.274.32.22679 · DOI
  108. Han, 2001, TNF-alpha stimulates activation of pro-MMP2 in human skin through NF-(kappa)B mediated induction of MT1-MMP, J Cell Biol, 114, 131
  109. Rajavashisth, 1999, Inflammatory cytokines and oxidized low density lipoproteins increase endothelial cell expression of membrane type 1-matrix metalloproteinase, J Biol Chem, 274, 11924, 10.1074/jbc.274.17.11924 · DOI
  110. Kadono, 1998, Transformation of epithelial Madin-Darby canine kidney cells with p60(v-src) induces expression of membrane-type 1 matrix metalloproteinase and invasiveness, Cancer Res, 58, 2240
  111. Cha, 2000, Identification of cis-acting promoter elements that support expression of membrane-type 1 matrix metalloproteinase (MT1-MMP) in v-src transformed Madin-Darby canine kidney cells, Clin Exp Metastasis, 18, 675, 10.1023/A:1013190118556 · DOI
  112. Petrella, 2005, Identification of membrane type-1 matrix metalloproteinase as a target of hypoxia-inducible factor-2 alpha in von Hippel-Lindau renal cell carcinoma, Oncogene, 24, 1043, 10.1038/sj.onc.1208305 · DOI
  113. Petrella, 2006, Tumor cell invasion of von Hippel Lindau renal cell carcinoma cells is mediated by membrane type-1 matrix metalloproteinase, Mol Cancer, 5, 66, 10.1186/1476-4598-5-66 · DOI
  114. Carver, 2001, The mouse snail gene encodes a key regulator of the epithelial-mesenchymal transition, Mol Cell Biol, 21, 8184, 10.1128/MCB.21.23.8184-8188.2001 · DOI · Paper page
  115. Shofuda, 1998, Role of tissue inhibitor of metalloproteinases-2 (TIMP-2) in regulation of pro-gelatinase A activation catalyzed by membrane-type matrix metalloproteinase-1 (MT1-MMP) in human cancer cells, J Biochem, 124, 462, 10.1093/oxfordjournals.jbchem.a022136 · DOI
  116. Zhu, 2011, Transcriptional upregulation of MT2-MMP in response to hypoxia is promoted by HIF-1alpha in cancer cells, Mol Carcinog, 50, 770, 10.1002/mc.20678 · DOI
  117. Szabova, 2005, Expression pattern of four membrane-type matrix metalloproteinases in the normal and diseased mouse mammary gland, J Cell Physiol, 205, 123, 10.1002/jcp.20385 · DOI
  118. Uzui, 2002, Increased expression of membrane type 3-matrix metalloproteinase in human atherosclerotic plaque: role of activated macrophages and inflammatory cytokines, Circulation, 106, 3024, 10.1161/01.CIR.0000041433.94868.12 · DOI
  119. Grant, 1999, Overview of expression of matrix metalloproteinases (MMP-17, MMP-18, and MMP-20) in cultured human cells, Matrix Biol, 18, 145, 10.1016/S0945-053X(99)00003-7 · DOI
  120. Gauthier, 2003, Expression of membrane type-4 matrix metalloproteinase (metalloproteinase-17) by human eosinophils, Int J Biochem Cell Biol, 35, 1667, 10.1016/S1357-2725(03)00136-5 · DOI
  121. Romanic, 2001, Upregulated expression of human membrane type-5 matrix metalloproteinase in kidneys from diabetic patients, Am J Physiol Renal Physiol, 281, F309, 10.1152/ajprenal.2001.281.2.F309 · DOI
  122. Dong, 2001, Expression of membrane-type matrix metalloproteinases 4, 5, and 6 in mouse corneas infected with P. aeruginosa, Invest Ophthalmol Vis Sci, 42, 3223
  123. Itoh, 2011, Dimerization of MT1-MMP during cellular invasion detected by fluorescence resonance energy transfer, Biochem J, 440, 319, 10.1042/BJ20110424 · DOI
  124. Nakahara, 1997, Transmembrane/cytoplasmic domain-mediated membrane type 1-matrix metalloprotease docking to invadopodia is required for cell invasion, Proc Natl Acad Sci U S A, 94, 7959, 10.1073/pnas.94.15.7959 · DOI
  125. Poincloux, 2009, Matrix invasion by tumour cells: a focus on MT1-MMP trafficking to invadopodia, J Cell Sci, 122, 3015, 10.1242/jcs.034561 · DOI
  126. Mori, 2002, CD44 directs membrane-type 1 matrix metalloproteinase to lamellipodia by associating with its hemopexin-like domain, EMBO J, 21, 3949, 10.1093/emboj/cdf411 · DOI · Paper page
  127. Suenaga, 2005, CD44 binding through the hemopexin-like domain is critical for its shedding by membrane-type 1 matrix metalloproteinase, Oncogene, 24, 859, 10.1038/sj.onc.1208258 · DOI
  128. Monsky, 1994, A potential marker protease of invasiveness, seprase, is localized on invadopodia of human malignant melanoma cells, Cancer Res, 54, 5702
  129. Murphy, 2011, The 'ins' and 'outs' of podosomes and invadopodia: characteristics, formation and function, Nat Rev Mol Cell Biol, 12, 413, 10.1038/nrm3141 · DOI
  130. Yu, 2012, N-WASP coordinates the delivery and F-actin-mediated capture of MT1-MMP at invasive pseudopods, J Cell Biol, 199, 527, 10.1083/jcb.201203025 · DOI
  131. Wang, 2012, Invasive matrix degradation at focal adhesions occurs via protease recruitment by a FAK-p130Cas complex, J Cell Biol, 196, 375, 10.1083/jcb.201105153 · DOI
  132. Li, 2008, Molecular dissection of the structural machinery underlying the tissue-invasive activity of membrane type-1 matrix metalloproteinase, Mol Biol Cell, 19, 3221, 10.1091/mbc.E08-01-0016 · DOI
  133. Woskowicz, 2013, MT-LOOP-dependent localization of membrane type I matrix metalloproteinase (MT1-MMP) to the cell adhesion complexes promotes cancer cell invasion, J Biol Chem, 288, 35126, 10.1074/jbc.M113.496067 · DOI
  134. Buschman, 2009, The novel adaptor protein Tks4 (SH3PXD2B) is required for functional podosome formation, Mol Biol Cell, 20, 1302, 10.1091/mbc.E08-09-0949 · DOI
  135. Wiesner, 2010, KIF5B and KIF3A/KIF3B kinesins drive MT1-MMP surface exposure, CD44 shedding, and extracellular matrix degradation in primary macrophages, Blood, 116, 1559, 10.1182/blood-2009-12-257089 · DOI
  136. West, 2008, TLR ligand-induced podosome disassembly in dendritic cells is ADAM17 dependent, J Cell Biol, 182, 993, 10.1083/jcb.200801022 · DOI
  137. Varon, 2006, Transforming growth factor beta induces rosettes of podosomes in primary aortic endothelial cells, Mol Cell Biol, 26, 3582, 10.1128/MCB.26.9.3582-3594.2006 · DOI
  138. Albrechtsen, 2013, ADAM12 redistributes and activates MMP-14, resulting in gelatin degradation, reduced apoptosis and increased tumor growth, J Cell Sci, 126, 4707, 10.1242/jcs.129510 · DOI
  139. Bravo-Cordero, 2007, MT1-MMP proinvasive activity is regulated by a novel Rab8-dependent exocytic pathway, EMBO J, 26, 1499, 10.1038/sj.emboj.7601606 · DOI
  140. Wiesner, 2013, A specific subset of RabGTPases controls cell surface exposure of MT1-MMP, extracellular matrix degradation and three-dimensional invasion of macrophages, J Cell Sci, 126, 2820, 10.1242/jcs.122358 · DOI
  141. Weaver, 2014, Basal localization of MT1-MMP is essential for epithelial cell morphogenesis in 3D collagen matrix, J Cell Sci, 127, 1203, 10.1242/jcs.135236 · DOI · Paper page
  142. Itoh, 1999, Membrane type 4 matrix metalloproteinase (MT4-MMP, MMP-17) is a glycosylphosphatidylinositol-anchored proteinase, J Biol Chem, 274, 34260, 10.1074/jbc.274.48.34260 · DOI
  143. Cross, 1990, Glycolipid anchoring of plasma membrane proteins, Annu Rev Cell Biol, 6, 1, 10.1146/annurev.cb.06.110190.000245 · DOI
  144. Varma, 1998, GPI-anchored proteins are organized in submicron domains at the cell surface, Nature, 394, 798, 10.1038/29563 · DOI · Paper page
  145. Uekita, 2001, Cytoplasmic tail-dependent internalization of membrane-type 1 matrix metalloproteinase is important for its invasion-promoting activity, J Cell Biol, 155, 1345, 10.1083/jcb.200108112 · DOI
  146. Jiang, 2001, Regulation of membrane-type matrix metalloproteinase 1 activity by dynamin-mediated endocytosis, Proc Natl Acad Sci U S A, 98, 13693, 10.1073/pnas.241293698 · DOI
  147. Anilkumar, 2005, Palmitoylation at Cys574 is essential for MT1-MMP to promote cell migration, FASEB J, 19, 1326, 10.1096/fj.04-3651fje · DOI
  148. Labrecque, 2004, Src-mediated tyrosine phosphorylation of caveolin-1 induces its association with membrane type 1 matrix metalloproteinase, J Biol Chem, 279, 52132, 10.1074/jbc.M409617200 · DOI
  149. Remacle, 2003, Membrane type I-matrix metalloproteinase (MT1-MMP) is internalised by two different pathways and is recycled to the cell surface, J Cell Sci, 116, 3905, 10.1242/jcs.00710 · DOI
  150. Wang, 2004, Co-recycling of MT1-MMP and MT3-MMP through the trans-Golgi network. Identification of DKV582 as a recycling signal, J Biol Chem, 279, 9331, 10.1074/jbc.M312369200 · DOI
  151. Wang, 2004, Mint-3 regulates the retrieval of the internalized membrane-type matrix metalloproteinase, MT5-MMP, to the plasma membrane by binding to its carboxyl end motif EWV, J Biol Chem, 279, 20461, 10.1074/jbc.M400264200 · DOI · Paper page
  152. Itoh, 2006, Cell surface collagenolysis requires homodimerization of the membrane-bound collagenase MT1-MMP, Mol Biol Cell, 17, 5390, 10.1091/mbc.E06-08-0740 · DOI
  153. Tochowicz, 2011, The dimer interface of the membrane type 1 matrix metalloproteinase hemopexin domain: crystal structure and biological functions, J Biol Chem, 286, 7587, 10.1074/jbc.M110.178434 · DOI
  154. Remacle, 2012, Novel MT1-MMP small-molecule inhibitors based on insights into hemopexin domain function in tumor growth, Cancer Res, 72, 2339, 10.1158/0008-5472.CAN-11-4149 · DOI
  155. Brew, 2010, The tissue inhibitors of metalloproteinases (TIMPs): an ancient family with structural and functional diversity, Biochim Biophys Acta, 1803, 55, 10.1016/j.bbamcr.2010.01.003 · DOI
  156. Sohail, 2008, MT4-(MMP17) and MT6-MMP (MMP25), A unique set of membrane-anchored matrix metalloproteinases: properties and expression in cancer, Cancer Metastasis Rev, 27, 289, 10.1007/s10555-008-9129-8 · DOI
  157. Caterina, 2000, Inactivating mutation of the mouse tissue inhibitor of metalloproteinases-2(Timp-2) gene alters proMMP-2 activation, J Biol Chem, 275, 21422, 10.1074/jbc.M001271200 · DOI
  158. English, 2006, Individual Timp deficiencies differentially impact pro-MMP-2 activation, J Biol Chem, 281, 10337, 10.1074/jbc.M512009200 · DOI · Paper page
  159. Oh, 2001, The membrane-anchored MMP inhibitor RECK is a key regulator of extracellular matrix integrity and angiogenesis, Cell, 107, 789, 10.1016/S0092-8674(01)00597-9 · DOI · Paper page
  160. Takahashi, 1998, Regulation of matrix metalloproteinase-9 and inhibition of tumor invasion by the membrane-anchored glycoprotein RECK, Proc Natl Acad Sci U S A, 95, 13221, 10.1073/pnas.95.22.13221 · DOI
  161. Nakada, 2001, Suppression of membrane-type 1 matrix metalloproteinase (MMP)-mediated MMP-2 activation and tumor invasion by testican 3 and its splicing variant gene product, N-Tes, Cancer Res, 61, 8896
  162. Miyamori, 2001, Claudin promotes activation of pro-matrix metalloproteinase-2 mediated by membrane-type matrix metalloproteinases, J Biol Chem, 276, 28204, 10.1074/jbc.M103083200 · DOI
  163. Matsuda, 2003, Clusterin, an abundant serum factor, is a possible negative regulator of MT6-MMP/MMP-25 produced by neutrophils, J Biol Chem, 278, 36350, 10.1074/jbc.M301509200 · DOI
  164. Lehti, 1998, Proteolytic processing of membrane-type-1 matrix metalloproteinase is associated with gelatinase A activation at the cell surface, Biochem J, 334, 345, 10.1042/bj3340345 · DOI
  165. Toth, 2002, Complex pattern of membrane type 1 matrix metalloproteinase shedding. Regulation by autocatalytic cells surface inactivation of active enzyme, J Biol Chem, 277, 26340, 10.1074/jbc.M200655200 · DOI · Paper page
  166. Osenkowski, 2004, Processing, shedding, and endocytosis of membrane type 1-matrix metalloproteinase (MT1-MMP), J Cell Physiol, 200, 2, 10.1002/jcp.20064 · DOI
  167. Harayama, 1999, Shedding of membrane type 1 matrix metalloproteinase in a human breast carcinoma cell line, Jpn J Cancer Res, 90, 942, 10.1111/j.1349-7006.1999.tb00839.x · DOI
  168. Wang, 2001, Shedding of membrane type matrix metalloproteinase 5 by a furin-type convertase: a potential mechanism for down-regulation, J Biol Chem, 276, 35953, 10.1074/jbc.M103680200 · DOI
  169. Kang, 2001, Subcellular distribution and cytokine- and chemokine-regulated secretion of leukolysin/MT6-MMP/MMP-25 in neutrophils, J Biol Chem, 276, 21960, 10.1074/jbc.M007997200 · DOI
  170. Coussens, 2002, Matrix metalloproteinase inhibitors and cancer: trials and tribulations, Science, 295, 2387, 10.1126/science.1067100 · DOI · Paper page
  171. Zucker, 2000, Critical appraisal of the use of matrix metalloproteinase inhibitors in cancer treatment, Oncogene, 19, 6642, 10.1038/sj.onc.1204097 · DOI
  172. Davies, 1993, Activity of type IV collagenases in benign and malignant breast disease, Br J Cancer, 67, 1126, 10.1038/bjc.1993.207 · DOI
  173. Devy, 2009, Selective inhibition of matrix metalloproteinase-14 blocks tumor growth, invasion, and angiogenesis, Cancer Res, 69, 1517, 10.1158/0008-5472.CAN-08-3255 · DOI
  174. Koshikawa, 2005, Membrane-type matrix metalloproteinase-1 (MT1-MMP) is a processing enzyme for human laminin gamma 2 chain, J Biol Chem, 280, 88, 10.1074/jbc.M411824200 · DOI
  175. d'Ortho, 1997, Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases, Eur J Biochem, 250, 751, 10.1111/j.1432-1033.1997.00751.x · DOI
  176. Belkin, 2001, Matrix-dependent proteolysis of surface transglutaminase by membrane-type metalloproteinase regulates cancer cell adhesion and locomotion, J Biol Chem, 276, 18415, 10.1074/jbc.M010135200 · DOI
  177. Rozanov, 2004, The low density lipoprotein receptor-related protein LRP is regulated by membrane type-1 matrix metalloproteinase (MT1-MMP) proteolysis in malignant cells, J Biol Chem, 279, 4260, 10.1074/jbc.M311569200 · DOI · Paper page
  178. Deryugina, 2000, Functional activation of integrin alpha V beta 3 in tumor cells expressing membrane-type 1 matrix metalloproteinase, Int J Cancer, 86, 15, 10.1002/(SICI)1097-0215(20000401)86:1<15::AID-IJC3>3.0.CO;2-B · DOI
  179. Rozanov, 2004, Cellular membrane type-1 matrix metalloproteinase (MT1-MMP) cleaves C3b, an essential component of the complement system, J Biol Chem, 279, 46551, 10.1074/jbc.M405284200 · DOI
  180. Egawa, 2006, Membrane type 1 matrix metalloproteinase (MT1-MMP/MMP-14) cleaves and releases a 22-kDa extracellular matrix metalloproteinase inducer (EMMPRIN) fragment from tumor cells, J Biol Chem, 281, 37576, 10.1074/jbc.M606993200 · DOI
  181. Aoki, 2005, Cleavage of apolipoprotein E by membrane-type matrix metalloproteinase-1 abrogates suppression of cell proliferation, J Biochem, 137, 95, 10.1093/jb/mvi009 · DOI
  182. Liu, 2010, The membrane type matrix metalloproteinase MMP14 mediates constitutive shedding of MHC class I chain-related molecule A independent of A disintegrin and metalloproteinases, J Immunol, 184, 3346, 10.4049/jimmunol.0903789 · DOI
  183. Velasco-Loyden, 2004, The shedding of betaglycan is regulated by pervanadate and mediated by membrane type matrix metalloprotease-1, J Biol Chem, 279, 7721, 10.1074/jbc.M306499200 · DOI
  184. Tam, 2004, Membrane protease proteomics: Isotope-coded affinity tag MS identification of undescribed MT1-matrix metalloproteinase substrates, Proc Natl Acad Sci U S A, 101, 6917, 10.1073/pnas.0305862101 · DOI · Paper page
  185. Butler, 2008, Pharmacoproteomics of a metalloproteinase hydroxamate inhibitor in breast cancer cells: dynamics of membrane type 1 matrix metalloproteinase-mediated membrane protein shedding, Mol Cell Biol, 28, 4896, 10.1128/MCB.01775-07 · DOI
  186. Takino, 2003, Cleavage of metastasis suppressor gene product KiSS-1 protein/metastin by matrix metalloproteinases, Oncogene, 22, 4617, 10.1038/sj.onc.1206542 · DOI
  187. Wang, 1999, Catalytic activities and substrate specificity of the human membrane type 4 matrix metalloproteinase catalytic domain, J Biol Chem, 274, 33043, 10.1074/jbc.274.46.33043 · DOI
  188. English, 2001, Catalytic activities of membrane-type 6 matrix metalloproteinase (MMP25), FEBS Lett, 491, 137, 10.1016/S0014-5793(01)02150-0 · DOI
  189. Shiryaev, 2009, Matrix metalloproteinase proteolysis of the myelin basic protein isoforms is a source of immunogenic peptides in autoimmune multiple sclerosis, PLoS One, 4, e4952, 10.1371/journal.pone.0004952 · DOI

Cited by

Sorted by citations

Metadata

Authors
Itoh, Y.
Venue
Matrix Biology
Publisher
Elsevier BV
Published
2015-05
Volume
44-46
Pages
207-223
ISSN
0945-053X
DOI
10.1016/j.matbio.2015.03.004
Cited by
401
References
5
Language
en
Licence

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review