CoChat
Sign Up
Cited by 29

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

Membrane-type I matrix metalloproteinase (MT1-MMP), lipid metabolism and therapeutic implications.

Xia, Xiao-Dan, Alabi, Adekunle, Wang, Maggie, Gu, Hong-Mei, Yang, Rui Zhe, Wang, Gui-Qing, Zhang, Da-Wei·2021·Journal of Molecular Cell Biology
DOI 10.1093/jmcb/mjab048PMC PMC8530520
Open this paper in CoChat — free account

Abstract

Lipids exert many essential physiological functions, such as serving as a structural component of biological membranes, storing energy, and regulating cell signal transduction. Dysregulation of lipid metabolism can lead to dyslipidemia related to various human diseases, such as obesity, diabetes, and cardiovascular disease. Therefore, lipid metabolism is strictly regulated through multiple mechanisms at different levels, including the extracellular matrix. Membrane-type I matrix metalloproteinase (MT1-MMP), a zinc-dependent endopeptidase, proteolytically cleaves extracellular matrix components, and non-matrix proteins, thereby regulating many physiological and pathophysiological processes. Emerging evidence supports the vital role of MT1-MMP in lipid metabolism. For example, MT1-MMP mediates ectodomain shedding of low-density lipoprotein receptor and increases plasma low-density lipoprotein cholesterol levels and the development of atherosclerosis. It also increases the vulnerability of atherosclerotic plaque by promoting collagen cleavage. Furthermore, it can cleave the extracellular matrix of adipocytes, affecting adipogenesis and the development of obesity. Therefore, the activity of MT1-MMP is strictly regulated by multiple mechanisms, such as autocatalytic cleavage, endocytosis and exocytosis, and post-translational modifications. Here, we summarize the latest advances in MT1-MMP, mainly focusing on its role in lipid metabolism, the molecular mechanisms regulating the function and expression of MT1-MMP, and their pharmacotherapeutic implications.

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 · 10.1093/jmcb/mjab048

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?

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: 129

  1. Actis Dato, 2018, The role of low-density lipoprotein receptor-related protein 1 in lipid metabolism, glucose homeostasis and inflammation, Int. J. Mol. Sci., 19, 1780, 10.3390/ijms19061780 · DOI
  2. Aikawa, 2004, The vulnerable atherosclerotic plaque: pathogenesis and therapeutic approach, Cardiovasc. Pathol., 13, 125, 10.1016/S1054-8807(04)00004-3 · DOI
  3. Alfonso-Jaume, 2004, Co-operative interactions between NFAT (nuclear factor of activated T cells) c1 and the zinc finger transcription factors Sp1/Sp3 and Egr-1 regulate MT1-MMP (membrane type 1 matrix metalloproteinase) transcription by glomerular mesangial cells, Biochem. J., 380, 735, 10.1042/bj20031281 · DOI
  4. Alkhouli, 2013, The mechanical properties of human adipose tissues and their relationships to the structure and composition of the extracellular matrix, Am. J. Physiol. Endocrinol. Metab., 305, E1427, 10.1152/ajpendo.00111.2013 · DOI
  5. Alonso-Herranz, 2020, Macrophages promote endothelial-to-mesenchymal transition via MT1-MMP/TGFβ1 after myocardial infarction, eLife, 9, e57920, 10.7554/eLife.57920 · DOI
  6. Amar, 2017, Matrix metalloproteinase collagenolysis in health and disease, Biochim. Biophys. Acta, 1864, 1940, 10.1016/j.bbamcr.2017.04.015 · DOI · Paper page
  7. Anilkumar, 2005, Palmitoylation at Cys574 is essential for MT1-MMP to promote cell migration, FASEB J., 19, 1326, 10.1096/fj.04-3651fje · DOI
  8. Attur, 2020, Membrane-type 1 matrix metalloproteinase modulates tissue homeostasis by a non-proteolytic mechanism, iScience, 23, 101789, 10.1016/j.isci.2020.101789 · DOI
  9. Barnes, 2017, Membrane-tethered metalloproteinase expressed by vascular smooth muscle cells limits the progression of proliferative atherosclerotic lesions, J. Am. Heart Assoc., 6, e003693, 10.1161/JAHA.116.003693 · DOI · Paper page
  10. Begg, 2004, Soluble LDL-R are formed by cell surface cleavage in response to phorbol esters, Eur. J. Biochem., 271, 524, 10.1046/j.1432-1033.2003.03953.x · DOI · Paper page
  11. Boon, 2016, Glycosylation of matrix metalloproteases and tissue inhibitors: present state, challenges and opportunities, Biochem. J., 473, 1471, 10.1042/BJ20151154 · DOI
  12. Bosco, 2017, A new synthetic matrix metalloproteinase inhibitor reduces human mesenchymal stem cell adipogenesis, PLoS One, 12, e0172925, 10.1371/journal.pone.0172925 · DOI
  13. Botkjaer, 2016, Development of a specific affinity-matured exosite inhibitor to MT1-MMP that efficiently inhibits tumor cell invasion in vitro and metastasis in vivo, Oncotarget, 7, 16773, 10.18632/oncotarget.7780 · DOI
  14. 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
  15. Castagnino, 2018, Coronin 1C promotes triple-negative breast cancer invasiveness through regulation of MT1-MMP traffic and invadopodia function, Oncogene, 37, 6425, 10.1038/s41388-018-0422-x · DOI
  16. Cathcart, 2016, Interleukin-6 increases matrix metalloproteinase-14 (MMP-14) levels via down-regulation of p53 to drive cancer progression, Oncotarget, 7, 61107, 10.18632/oncotarget.11243 · DOI
  17. Cauwe, 2010, Intracellular substrate cleavage: a novel dimension in the biochemistry, biology and pathology of matrix metalloproteinases, Crit. Rev. Biochem. Mol. Biol., 45, 351, 10.3109/10409238.2010.501783 · DOI
  18. Chan, 2021, Co-localisation of intra-nuclear membrane type-1 matrix metalloproteinase and hypoxia inducible factor-2α in osteosarcoma and prostate carcinoma cells, Oncol. Lett., 21, 158, 10.3892/ol.2020.12419 · DOI
  19. Chan, 2020, Site-directed MT1-MMP trafficking and surface insertion regulate AChR clustering and remodeling at developing NMJs, eLife, 9, e54379, 10.7554/eLife.54379 · DOI
  20. Chavey, 2003, Matrix metalloproteinases are differentially expressed in adipose tissue during obesity and modulate adipocyte differentiation, J. Biol. Chem., 278, 11888, 10.1074/jbc.M209196200 · DOI
  21. Chernov, 2009, Epigenetic control of the invasion-promoting MT1-MMP/MMP-2/TIMP-2 axis in cancer cells, J. Biol. Chem., 284, 12727, 10.1074/jbc.M900273200 · DOI
  22. Chevalier, 2016, TOM1L1 drives membrane delivery of MT1-MMP to promote ERBB2-induced breast cancer cell invasion, Nat. Commun., 7, 10765, 10.1038/ncomms10765 · DOI
  23. Cho, 2008, The inactive 44-kDa processed form of membrane type 1 matrix metalloproteinase (MT1-MMP) enhances proteolytic activity via regulation of endocytosis of active MT1-MMP, J. Biol. Chem., 283, 17391, 10.1074/jbc.M708943200 · DOI
  24. 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
  25. Cukier, 2017, Structure‒function relationships in reconstituted HDL: Focus on antioxidative activity and cholesterol efflux capacity, Biochim. Biophys. Acta Mol. Cell Biol. Lipids, 1862, 890, 10.1016/j.bbalip.2017.05.010 · DOI
  26. Cupido, 2020, Inclisiran for the treatment of hypercholesterolaemia: implications and unanswered questions, Cardiovasc. Res., 116, e136, 10.1093/cvr/cvaa212 · DOI · Paper page
  27. D'Alessio, 2008, Tissue inhibitor of metalloproteinases-2 binding to membrane-type 1 matrix metalloproteinase induces MAPK activation and cell growth by a non-proteolytic mechanism, J. Biol. Chem., 283, 87, 10.1074/jbc.M705492200 · DOI
  28. de Vos, 2018, Functional analysis of a hypomorphic allele shows that MMP14 catalytic activity is the prime determinant of the Winchester syndrome phenotype, Hum. Mol. Genet., 27, 2775, 10.1093/hmg/ddy168 · DOI
  29. Decaneto, 2017, Solvent water interactions within the active site of the membrane type I matrix metalloproteinase, Phys. Chem. Chem. Phys., 19, 30316, 10.1039/C7CP05572B · DOI · Paper page
  30. Eguchi, 2008, Novel transcription-factor-like function of human matrix metalloproteinase 3 regulating the CTGF/CCN2 gene, Mol. Cell. Biol., 28, 2391, 10.1128/MCB.01288-07 · DOI
  31. Eisenach, 2012, Membrane type 1 matrix metalloproteinase (MT1-MMP) ubiquitination at Lys581 increases cellular invasion through type I collagen, J. Biol. Chem., 287, 11533, 10.1074/jbc.M111.306340 · DOI
  32. 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
  33. Esteban, 2020, Endothelial MT1-MMP targeting limits intussusceptive angiogenesis and colitis via TSP1/nitric oxide axis, EMBO Mol. Med., 12, e10862, 10.15252/emmm.201910862 · DOI
  34. Fenech, 2015, Effect of tissue inhibitor of metalloproteinases 3 on DLK1 shedding in cultured human pre-adipocytes and implications for adipose tissue remodelling, Lancet, 385(Suppl 1, S35, 10.1016/S0140-6736(15)60350-6 · DOI
  35. Fernandez-Catalan, 1998, Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor, EMBO J., 17, 5238, 10.1093/emboj/17.17.5238 · DOI · Paper page
  36. Fields, 2015, New strategies for targeting matrix metalloproteinases, Matrix Biol., 44–46, 239, 10.1016/j.matbio.2015.01.002 · DOI · Paper page
  37. Fischer, 1993, An antiviral soluble form of the LDL receptor induced by interferon, Science, 262, 250, 10.1126/science.8211145 · DOI · Paper page
  38. Gallardo-Vara, 2016, Transcription factor KLF6 upregulates expression of metalloprotease MMP14 and subsequent release of soluble endoglin during vascular injury, Angiogenesis, 19, 155, 10.1007/s10456-016-9495-8 · DOI
  39. Gifford, 2019, MT1-MMP-dependent cell migration: proteolytic and non-proteolytic mechanisms, Biochem. Soc. Trans., 47, 811, 10.1042/BST20180363 · DOI
  40. Grafinger, 2020, β1 integrin-mediated signaling regulates MT1-MMP phosphorylation to promote tumour cell invasion, J. Cell Sci., 133, jcs239152, 10.1242/jcs.239152 · DOI
  41. Gramolelli, 2018, PROX1 is a transcriptional regulator of MMP14, Sci. Rep., 8, 9531, 10.1038/s41598-018-27739-w · DOI
  42. Grossman, 2010, The intrinsic protein flexibility of endogenous protease inhibitor TIMP-1 controls its binding interface and affects its function, Biochemistry, 49, 6184, 10.1021/bi902141x · DOI · Paper page
  43. Guo, 2020, Proprotein convertase subtilisin/kexin-type 9 and lipid metabolism, Adv. Exp. Med. Biol., 1276, 137, 10.1007/978-981-15-6082-8_9 · DOI
  44. 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
  45. 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
  46. Houghton, 2015, Matrix metalloproteinases in destructive lung disease, Matrix Biol., 44–46, 167, 10.1016/j.matbio.2015.02.002 · DOI · Paper page
  47. Hwang, 2004, A proteomic approach to identify substrates of matrix metalloproteinase-14 in human plasma, Biochim. Biophys. Acta, 1702, 79, 10.1016/j.bbapap.2004.08.001 · DOI
  48. Itoh, 2015, Membrane-type matrix metalloproteinases: their functions and regulations, Matrix Biol., 44–46, 207, 10.1016/j.matbio.2015.03.004 · DOI · Paper page
  49. Itoh, 2021, A common SNP risk variant MT1-MMP causative for Dupuytren's disease has a specific defect in collagenolytic activity, Matrix Biol., 97, 20, 10.1016/j.matbio.2021.02.003 · DOI
  50. Ji, 2019, APOE hypermethylation is significantly associated with coronary heart disease in males, Gene, 689, 84, 10.1016/j.gene.2018.11.088 · DOI
  51. Jiang, 2001, Regulation of membrane-type matrix metalloproteinase 1 activity by dynamin-mediated endocytosis, Proc. Natl Acad. Sci. USA, 98, 13693, 10.1073/pnas.241293698 · DOI
  52. Jiang, 2020, MT1-MMP deficiency leads to defective ependymal cell maturation, impaired ciliogenesis and hydrocephalus, JCI Insight, 5, e132782, 10.1172/jci.insight.132782 · DOI
  53. Johnson, 2014, Relationship of MMP-14 and TIMP-3 expression with macrophage activation and human atherosclerotic plaque vulnerability, Mediators Inflamm., 2014, 276457, 10.1155/2014/276457 · DOI
  54. Johnson, 2008, Low tissue inhibitor of metalloproteinases 3 and high matrix metalloproteinase 14 levels defines a subpopulation of highly invasive foam-cell macrophages, Arterioscler. Thromb. Vasc. Biol., 28, 1647, 10.1161/ATVBAHA.108.170548 · DOI · Paper page
  55. Kajiho, 2016, RAB2A controls MT1-MMP endocytic and E-cadherin polarized Golgi trafficking to promote invasive breast cancer programs, EMBO Rep., 17, 1061, 10.15252/embr.201642032 · DOI
  56. 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
  57. Kaneko, 2016, Selective inhibition of membrane type 1 matrix metalloproteinase abrogates progression of experimental inflammatory arthritis: synergy with tumor necrosis factor blockade, Arthritis Rheumatol., 68, 521, 10.1002/art.39414 · DOI
  58. Kim, 2008, Caveolin-1 inhibits membrane-type 1 matrix metalloproteinase activity, BMB Rep., 41, 858, 10.5483/BMBRep.2008.41.12.858 · DOI
  59. Kim, 2010, Posttranslational regulation of membrane type 1-matrix metalloproteinase (MT1-MMP) in mouse PTEN null prostate cancer cells: enhanced surface expression and differential O-glycosylation of MT1-MMP, Biochim. Biophys. Acta, 1803, 1287, 10.1016/j.bbamcr.2010.06.011 · DOI
  60. Klose, 2013, Monocyte/macrophage MMP-14 modulates cell infiltration and T-cell attraction in contact dermatitis but not in murine wound healing, Am. J. Pathol., 182, 755, 10.1016/j.ajpath.2012.11.028 · DOI · Paper page
  61. Knauper, 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
  62. 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
  63. Lagoutte, 2016, LIMK regulates tumor-cell invasion and matrix degradation through tyrosine phosphorylation of MT1-MMP, Sci. Rep., 6, 24925, 10.1038/srep24925 · DOI
  64. Lang, 2004, Crystal structure of the catalytic domain of MMP-16/MT3-MMP: characterization of MT-MMP specific features, J. Mol. Biol., 336, 213, 10.1016/j.jmb.2003.12.022 · DOI · Paper page
  65. Lehti, 2000, Regulation of membrane-type-1 matrix metalloproteinase activity by its cytoplasmic domain, J. Biol. Chem., 275, 15006, 10.1074/jbc.M910220199 · DOI · Paper page
  66. Li, 2020, Critical role of matrix metalloproteinase 14 in adipose tissue remodeling during obesity, Mol. Cell. Biol., 40, e00564, 10.1128/MCB.00564-19 · DOI
  67. Li, 2015, miR-181a-5p inhibits cancer cell migration and angiogenesis via downregulation of matrix metalloproteinase-14, Cancer Res., 75, 2674, 10.1158/0008-5472.CAN-14-2875 · DOI
  68. Lin, 2020, mir-22-3p/KLF6/MMP14 axis in fibro-adipogenic progenitors regulates fatty infiltration in muscle degeneration, FASEB J., 34, 12691, 10.1096/fj.202000506R · DOI
  69. Lohi, 2000, Structural analysis and promoter characterization of the human membrane-type matrix metalloproteinase-1 (MT1-MMP) gene, Gene, 242, 75, 10.1016/S0378-1119(99)00549-1 · DOI
  70. Ludwig, 2008, The cytoplasmic tail dileucine motif LL572 determines the glycosylation pattern of membrane-type 1 matrix metalloproteinase, J. Biol. Chem., 283, 35410, 10.1074/jbc.M801816200 · DOI
  71. Marchesin, 2015, ARF6–JIP3/4 regulate endosomal tubules for MT1-MMP exocytosis in cancer invasion, J. Cell Biol., 211, 339, 10.1083/jcb.201506002 · DOI · Paper page
  72. Martinez-Santibanez, 2015, Obesity-induced remodeling of the adipose tissue elastin network is independent of the metalloelastase MMP-12, Adipocyte, 4, 264, 10.1080/21623945.2015.1027848 · DOI
  73. Miyagawa, 2019, MT1-MMP recruits the ER-Golgi SNARE Bet1 for efficient MT1-MMP transport to the plasma membrane, J. Cell Biol., 218, 3355, 10.1083/jcb.201808149 · DOI
  74. Mori, 2016, New insight into the role of MMP14 in metabolic balance, PeerJ, 4, e2142, 10.7717/peerj.2142 · DOI
  75. 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
  76. Munkert, 2009, Characterization of the transcriptional regulation of the human MT1-MMP gene and association of risk reduction for focal-segmental glomerulosclerosis with two functional promoter SNPs, Nephrol. Dial. Transplant., 24, 735, 10.1093/ndt/gfn576 · DOI
  77. Nyalendo, 2007, Src-dependent phosphorylation of membrane type I matrix metalloproteinase on cytoplasmic tyrosine 573: role in endothelial and tumor cell migration, J. Biol. Chem., 282, 15690, 10.1074/jbc.M608045200 · DOI
  78. Oentaryo, 2020, Neuronal MT1-MMP mediates ECM clearance and Lrp4 cleavage for agrin deposition and signaling in presynaptic development, J. Cell Sci, 133, 10.1242/jcs.246710 · DOI
  79. 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
  80. Pacheco-Fernandez, 2020, Nucleobindin-1 regulates ECM degradation by promoting intra-Golgi trafficking of MMPs, J. Cell Biol., 219, e201907058, 10.1083/jcb.201907058 · DOI
  81. Park, 2011, Analysis of apolipoprotein A-I as a substrate for matrix metalloproteinase-14, Biochem. Biophys. Res. Commun., 409, 58, 10.1016/j.bbrc.2011.04.105 · DOI
  82. Park, 2008, Cleavage and functional loss of human apolipoprotein E by digestion of matrix metalloproteinase-14, Proteomics, 8, 2926, 10.1002/pmic.200700487 · DOI
  83. Pedersen, 2020, Protrudin-mediated ER-endosome contact sites promote MT1-MMP exocytosis and cell invasion, J. Cell Biol., 219, e202003063, 10.1083/jcb.202003063 · DOI
  84. Petrella, 2005, Identification of membrane type-1 matrix metalloproteinase as a target of hypoxia-inducible factor-2α in von Hippel‒Lindau renal cell carcinoma, Oncogene, 24, 1043, 10.1038/sj.onc.1208305 · DOI
  85. 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
  86. 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
  87. Ray, 2004, Induction of the MMP-14 gene in macrophages of the atherosclerotic plaque: role of SAF-1 in the induction process, Circ. Res., 95, 1082, 10.1161/01.RES.0000150046.48115.80 · DOI
  88. 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
  89. Remacle, 2006, O-glycosylation regulates autolysis of cellular membrane type-1 matrix metalloproteinase (MT1-MMP), J. Biol. Chem., 281, 16897, 10.1074/jbc.M600295200 · DOI
  90. 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
  91. Romani, 2019, Extracellular matrix mechanical cues regulate lipid metabolism through Lipin-1 and SREBP, Nat. Cell Biol., 21, 338, 10.1038/s41556-018-0270-5 · DOI
  92. Rozanov, 2001, Mutation analysis of membrane type-1 matrix metalloproteinase (MT1-MMP). The role of the cytoplasmic tail Cys574, the active site Glu240, and furin cleavage motifs in oligomerization, processing, and self-proteolysis of MT1-MMP expressed in breast carcinoma cells, J. Biol. Chem., 276, 25705, 10.1074/jbc.M007921200 · DOI
  93. Rozanov, 2003, Membrane type-1 matrix metalloproteinase functions as a proprotein self-convertase. Expression of the latent zymogen in Pichia pastoris, autolytic activation, and the peptide sequence of the cleavage forms, J. Biol. Chem., 278, 8257, 10.1074/jbc.M213246200 · DOI · Paper page
  94. Sathyamoorthy, 2015, Membrane type 1 matrix metalloproteinase regulates monocyte migration and collagen destruction in tuberculosis, J. Immunol., 195, 882, 10.4049/jimmunol.1403110 · DOI
  95. Sato, 2020, Vasoactive intestinal peptide derived from liver mesenchymal cells mediates tight junction assembly in mouse intrahepatic bile ducts, Hepatol. Commun., 4, 235, 10.1002/hep4.1459 · DOI
  96. Sato, 2010, Coordinate action of membrane-type matrix metalloproteinase-1 (MT1-MMP) and MMP-2 enhances pericellular proteolysis and invasion, Cancer Sci., 101, 843, 10.1111/j.1349-7006.2010.01498.x · DOI
  97. Sato, 1994, A matrix metalloproteinase expressed on the surface of invasive tumour cells, Nature, 370, 61, 10.1038/370061a0 · DOI
  98. Sato-Kusubata, 2011, Adipogenic histone mark regulation by matrix metalloproteinase 14 in collagen-rich microenvironments, Mol. Endocrinol., 25, 745, 10.1210/me.2010-0429 · DOI
  99. Schneider, 2008, Matrix-metalloproteinase-14 deficiency in bone-marrow-derived cells promotes collagen accumulation in mouse atherosclerotic plaques, Circulation, 117, 931, 10.1161/CIRCULATIONAHA.107.707448 · DOI · Paper page
  100. Shimohiro, 2014, Association between serum soluble low-density lipoprotein receptor levels and metabolic factors in healthy Japanese individuals, J. Clin. Lab. Anal., 29, 52, 10.1002/jcla.21727 · DOI · Paper page
  101. Shiryaev, 2013, A monoclonal antibody interferes with TIMP-2 binding and incapacitates the MMP-2-activating function of multifunctional, pro-tumorigenic MMP-14/MT1-MMP, Oncogenesis, 2, e80, 10.1038/oncsis.2013.44 · DOI · Paper page
  102. Sneeggen, 2019, WDFY2 restrains matrix metalloproteinase secretion and cell invasion by controlling VAMP3-dependent recycling, Nat. Commun., 10, 2850, 10.1038/s41467-019-10794-w · DOI
  103. Springer, 2018, GalNAc‒siRNA conjugates: leading the way for delivery of RNAi therapeutics, Nucleic Acid Ther., 28, 109, 10.1089/nat.2018.0736 · DOI · Paper page
  104. 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 45 kDa form, J. Cell Sci, 111, 2789, 10.1242/jcs.111.18.2789 · DOI
  105. Tam, 2004, Characterization of the distinct collagen binding, helicase and cleavage mechanisms of matrix metalloproteinase 2 and 14 (gelatinase A and MT1-MMP): the differential roles of the MMP hemopexin c domains and the MMP-2 fibronectin type II modules in collagen triple helicase activities, J. Biol. Chem., 279, 43336, 10.1074/jbc.M407186200 · DOI · Paper page
  106. Tam, 2002, Collagen binding properties of the membrane type-1 matrix metalloproteinase (MT1-MMP) hemopexin C domain. The ectodomain of the 44-kDa autocatalytic product of MT1-MMP inhibits cell invasion by disrupting native type I collagen cleavage, J. Biol. Chem., 277, 39005, 10.1074/jbc.M206874200 · DOI
  107. 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
  108. Tomita, 2000, Granulocyte‒macrophage colony-stimulating factor upregulates matrix metalloproteinase-2 (MMP-2) and membrane type-1 MMP (MT1-MMP) in human head and neck cancer cells, Cancer Lett., 156, 83, 10.1016/S0304-3835(00)00446-8 · DOI
  109. 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
  110. Udi, 2015, Inhibition mechanism of membrane metalloprotease by an exosite-swiveling conformational antibody, Structure, 23, 104, 10.1016/j.str.2014.10.012 · DOI
  111. Van Doren, 2017, Peripheral membrane associations of matrix metalloproteinases, Biochim. Biophys. Acta Mol. Cell Res., 1864, 1964, 10.1016/j.bbamcr.2017.04.013 · DOI · Paper page
  112. Veniant, 2001, Lipoprotein size and atherosclerosis susceptibility in Apoe−/− and Ldlr−/− mice, Arterioscler. Thromb. Vasc. Biol., 21, 1567, 10.1161/hq1001.097780 · DOI
  113. Vinay, 2021, Genetic association of MMP14 promoter variants and their functional significance in gallbladder cancer pathogenesis, J. Hum. Genet
  114. Wang, 2020, TGFβ attenuates cartilage extracellular matrix degradation via enhancing FBXO6-mediated MMP14 ubiquitination, Ann. Rheum. Dis., 79, 1111, 10.1136/annrheumdis-2019-216911 · DOI
  115. 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
  116. Williams, 2011, Phosphorylation of membrane type 1-matrix metalloproteinase (MT1-MMP) and its vesicle-associated membrane protein 7 (VAMP7)-dependent trafficking facilitate cell invasion and migration, J. Biol. Chem., 286, 43405, 10.1074/jbc.M111.297069 · DOI
  117. Williams, 2014, SNAP23, Syntaxin4, and vesicle-associated membrane protein 7 (VAMP7) mediate trafficking of membrane type 1-matrix metalloproteinase (MT1-MMP) during invadopodium formation and tumor cell invasion, Mol. Biol. Cell, 25, 2061, 10.1091/mbc.e13-10-0582 · DOI
  118. 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
  119. Wu, 2004, Glycosylation broadens the substrate profile of membrane type 1 matrix metalloproteinase, J. Biol. Chem., 279, 8278, 10.1074/jbc.M311870200 · DOI
  120. Xu, 2013, miR133a suppresses cell proliferation, migration and invasion in human lung cancer by targeting MMP14, Oncol. Rep., 30, 1398, 10.3892/or.2013.2548 · DOI
  121. Yu, 2021, Local protein synthesis of neuronal MT1-MMP for agrin-induced presynaptic development, Development, 148, dev199000, 10.1242/dev.199000 · DOI
  122. 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
  123. Yu, 2018, Cholesterol transport system: an integrated cholesterol transport model involved in atherosclerosis, Prog. Lipid Res., 73, 65, 10.1016/j.plipres.2018.12.002 · DOI
  124. Zarrabi, 2011, Inhibition of matrix metalloproteinase 14 (MMP-14)-mediated cancer cell migration, J. Biol. Chem., 286, 33167, 10.1074/jbc.M111.256644 · DOI · Paper page
  125. Zhang, 2012, microRNA-9 targets matrix metalloproteinase 14 to inhibit invasion, metastasis, and angiogenesis of neuroblastoma cells, Mol. Cancer Ther., 11, 1454, 10.1158/1535-7163.MCT-12-0001 · DOI
  126. Zhang, 1992, Spontaneous hypercholesterolemia and arterial lesions in mice lacking apolipoprotein E, Science, 258, 468, 10.1126/science.1411543 · DOI · Paper page
  127. Zheng, 2016, miRNA-337-3p inhibits gastric cancer progression through repressing myeloid zinc finger 1-facilitated expression of matrix metalloproteinase 14, Oncotarget, 7, 40314, 10.18632/oncotarget.9739 · DOI
  128. Zhou, 2000, Impaired endochondral ossification and angiogenesis in mice deficient in membrane-type matrix metalloproteinase I, Proc. Natl Acad. Sci. USA, 97, 4052, 10.1073/pnas.060037197 · DOI · Paper page
  129. Zigrino, 2012, Loss of epidermal MMP-14 expression interferes with angiogenesis but not with re-epithelialization, Eur. J. Cell Biol., 91, 748, 10.1016/j.ejcb.2012.05.003 · DOI · Paper page

Cited by

Sorted by citations

Metadata

Authors
Xia, X.-D., Alabi, A., Wang, M., Gu, H.-M., Yang, R. Z., Wang, G.-Q., & Zhang, D.-W.
Affiliations
  • Department of Orthopedics, The Sixth Affiliated Hospital (Qingyuan People’s Hospital), Guangzhou Medical University, Qingyuan 511500, China
  • Department of Pediatrics and Group on the Molecular and Cell Biology of Lipids, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, AB T6R 2G3, Canada
ORCID
Venue
Journal of Molecular Cell Biology
Publisher
Oxford University Press (OUP)
Published
2021-07-01
Volume
13
Issue
7
Pages
513-526
ISSN
1759-4685
DOI
10.1093/jmcb/mjab048
PMC
PMC8530520
Cited by
29
References
5
Language
en
Licence
creativecommons.org/licenses/by/4.0/ (vor, 22 d)
Funders
  • Canadian Institutes of Health Research (PS 155994)
  • Natural Sciences and Engineering Research Council of Canada (RGPIN-2016-06479)
  • National Natural Science Foundation of China (Joint Research Fund for Overseas Chinese Scholars and Scholars in Hong Kong and Macao (NSFC 81929002)

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