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Volumn 450, Issue 1, 2014, Pages 213-218

Matrix metalloproteinase-14 is a mechanically regulated activator of secreted MMPs and invasion

Author keywords

Cleavage peptide; Contractility; Force; Function blocking antibody; MT1 MMP; Pancreatic cancer

Indexed keywords

BLOCKING ANTIBODY; GELATINASE A; GELATINASE B; MATRIX METALLOPROTEINASE 14;

EID: 84904760970     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2014.05.086     Document Type: Article
Times cited : (32)

References (35)
  • 1
    • 77950931419 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Regulators of the tumor microenvironment
    • K. Kessenbrock, V. Plaks, and Z. Werb Matrix metalloproteinases: regulators of the tumor microenvironment Cell 141 2010 52 67
    • (2010) Cell , vol.141 , pp. 52-67
    • Kessenbrock, K.1    Plaks, V.2    Werb, Z.3
  • 5
    • 84857566619 scopus 로고    scopus 로고
    • Cellular traction stresses increase with increasing metastatic potential
    • C.M. Kraning-Rush, J.P. Califano, and C.A. Reinhart-King Cellular traction stresses increase with increasing metastatic potential PLoS One 7 2012
    • (2012) PLoS One , vol.7
    • Kraning-Rush, C.M.1    Califano, J.P.2    Reinhart-King, C.A.3
  • 6
    • 66249100268 scopus 로고    scopus 로고
    • The mechanical rigidity of the extracellular matrix regulates the structure, motility, and proliferation of glioma cells
    • T.A. Ulrich, E.M.D. Pardo, and S. Kumar The mechanical rigidity of the extracellular matrix regulates the structure, motility, and proliferation of glioma cells Cancer Res. 69 2009 4167 4174
    • (2009) Cancer Res. , vol.69 , pp. 4167-4174
    • Ulrich, T.A.1    Pardo, E.M.D.2    Kumar, S.3
  • 7
    • 79959636906 scopus 로고    scopus 로고
    • The physics of cancer: The role of physical interactions and mechanical forces in metastasis
    • D. Wirtz, K. Konstantopoulos, and P.C. Searson The physics of cancer: the role of physical interactions and mechanical forces in metastasis Nat. Rev. Cancer 11 2011 512 522
    • (2011) Nat. Rev. Cancer , vol.11 , pp. 512-522
    • Wirtz, D.1    Konstantopoulos, K.2    Searson, P.C.3
  • 8
    • 79951545991 scopus 로고    scopus 로고
    • Mechanical load induces a 100-fold increase in the rate of collagen proteolysis by MMP-1
    • A.S. Adhikari, J. Chai, and A.R. Dunn Mechanical load induces a 100-fold increase in the rate of collagen proteolysis by MMP-1 J. Am. Chem. Soc. 133 2011 1686 1689
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 1686-1689
    • Adhikari, A.S.1    Chai, J.2    Dunn, A.R.3
  • 10
    • 84898059547 scopus 로고    scopus 로고
    • Cellular traction stresses mediate extracellular matrix degradation by invadopodia
    • R.J. Jerrell, and A. Parekh Cellular traction stresses mediate extracellular matrix degradation by invadopodia Acta Biomater. 10 2014 1886 1896
    • (2014) Acta Biomater. , vol.10 , pp. 1886-1896
    • Jerrell, R.J.1    Parekh, A.2
  • 13
    • 84905233374 scopus 로고    scopus 로고
    • Cellular contractility and extracellular matrix stiffness regulate matrix metalloproteinase activity in pancreatic cancer cells
    • [Epub ahead of print]
    • A. Haage, and I.C. Schneider Cellular contractility and extracellular matrix stiffness regulate matrix metalloproteinase activity in pancreatic cancer cells FASEB J. 2014 [Epub ahead of print]
    • (2014) FASEB J.
    • Haage, A.1    Schneider, I.C.2
  • 14
    • 36549085160 scopus 로고    scopus 로고
    • Control of matrix metalloproteinase catalytic activity
    • H.J. Ra, and W.C. Parks Control of matrix metalloproteinase catalytic activity Matrix Biol. 26 2007 587 596
    • (2007) Matrix Biol. , vol.26 , pp. 587-596
    • Ra, H.J.1    Parks, W.C.2
  • 15
    • 70350417461 scopus 로고    scopus 로고
    • Matrix invasion by tumour cells: A focus on MT1-MMP trafficking to invadopodia
    • R. Poincloux, F. Lizarraga, and P. Chavrier Matrix invasion by tumour cells: a focus on MT1-MMP trafficking to invadopodia J. Cell Sci. 122 2009 3015 3024
    • (2009) J. Cell Sci. , vol.122 , pp. 3015-3024
    • Poincloux, R.1    Lizarraga, F.2    Chavrier, P.3
  • 16
    • 57149087260 scopus 로고    scopus 로고
    • Secretion of active membrane type 1 matrix metalloproteinase (MMP-14) into extracellular space in microvesicular exosomes
    • J. Hakulinen, L. Sankkila, N. Sugiyama, K. Lehti, and J. Keski-Oja Secretion of active membrane type 1 matrix metalloproteinase (MMP-14) into extracellular space in microvesicular exosomes J. Cell. Biochem. 105 2008 1211 1218
    • (2008) J. Cell. Biochem. , vol.105 , pp. 1211-1218
    • Hakulinen, J.1    Sankkila, L.2    Sugiyama, N.3    Lehti, K.4    Keski-Oja, J.5
  • 17
    • 34547569807 scopus 로고    scopus 로고
    • Multi-step pericellular proteolysis controls the transition from individual to collective cancer cell invasion
    • K. Wolf, Y.I. Wu, Y. Liu, J. Geiger, E. Tam, C. Overall, M.S. Stack, and P. Friedl Multi-step pericellular proteolysis controls the transition from individual to collective cancer cell invasion Nat. Cell Biol. 9 2007 893 904
    • (2007) Nat. Cell Biol. , vol.9 , pp. 893-904
    • Wolf, K.1    Wu, Y.I.2    Liu, Y.3    Geiger, J.4    Tam, E.5    Overall, C.6    Stack, M.S.7    Friedl, P.8
  • 19
    • 84859375474 scopus 로고    scopus 로고
    • Invasive matrix degradation at focal adhesions occurs via protease recruitment by a FAK-p130Cas complex
    • Y. Wang, and M.A. McNiven Invasive matrix degradation at focal adhesions occurs via protease recruitment by a FAK-p130Cas complex J. Cell Biol. 196 2012 375 385
    • (2012) J. Cell Biol. , vol.196 , pp. 375-385
    • Wang, Y.1    McNiven, M.A.2
  • 20
    • 0032854578 scopus 로고    scopus 로고
    • Specialized surface protrusions of invasive cells, invadopodia and lamellipodia, have differential MT1-MMP, MMP-2, and TIMP-2 localization
    • R.A. Greenwald, S. Zucker, L.M. Golub, New York Acad Sciences New York
    • W.T. Chen, and J.Y. Wang Specialized surface protrusions of invasive cells, invadopodia and lamellipodia, have differential MT1-MMP, MMP-2, and TIMP-2 localization R.A. Greenwald, S. Zucker, L.M. Golub, Inhibition of Matrix Metalloproteinases: Therapeutic Applications 1999 New York Acad Sciences New York 361 371
    • (1999) Inhibition of Matrix Metalloproteinases: Therapeutic Applications , pp. 361-371
    • Chen, W.T.1    Wang, J.Y.2
  • 22
    • 84869194048 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Changing roles in tumor progression and metastasis
    • L.A. Shuman Moss, S. Jensen-Taubman, and W.G. Stetler-Stevenson Matrix metalloproteinases: changing roles in tumor progression and metastasis Am. J. Pathol. 181 2012 1895 1899
    • (2012) Am. J. Pathol. , vol.181 , pp. 1895-1899
    • Shuman Moss, L.A.1    Jensen-Taubman, S.2    Stetler-Stevenson, W.G.3
  • 23
    • 75749157368 scopus 로고    scopus 로고
    • Selective matrix metalloproteinase (MMP) inhibitors in cancer therapy: Ready for prime time?
    • S. Zucker, and J. Cao Selective matrix metalloproteinase (MMP) inhibitors in cancer therapy: ready for prime time? Cancer Biol. Ther. 8 2009 2371 2373
    • (2009) Cancer Biol. Ther. , vol.8 , pp. 2371-2373
    • Zucker, S.1    Cao, J.2
  • 25
    • 37049015152 scopus 로고    scopus 로고
    • Membrane type 1-matrix metalloproteinase: Substrate diversity in pericellular proteolysis
    • M.V. Barbolina, and M.S. Stack Membrane type 1-matrix metalloproteinase: substrate diversity in pericellular proteolysis Semin. Cell Dev. Biol. 19 2008 24 33
    • (2008) Semin. Cell Dev. Biol. , vol.19 , pp. 24-33
    • Barbolina, M.V.1    Stack, M.S.2
  • 26
    • 84555178641 scopus 로고    scopus 로고
    • Biochemical role of the collagen-rich tumour microenvironment in pancreatic cancer progression
    • M.A. Shields, S. Dangi-Garimella, A.J. Redig, and H.G. Munshi Biochemical role of the collagen-rich tumour microenvironment in pancreatic cancer progression Biochem. J. 441 2012 541 552
    • (2012) Biochem. J. , vol.441 , pp. 541-552
    • Shields, M.A.1    Dangi-Garimella, S.2    Redig, A.J.3    Munshi, H.G.4
  • 27
    • 84884532094 scopus 로고    scopus 로고
    • Development of a periplasmic FRET screening method for protease inhibitory antibodies
    • D.H. Nam, and X. Ge Development of a periplasmic FRET screening method for protease inhibitory antibodies Biotechnol. Bioeng. 110 2013 2856 2864
    • (2013) Biotechnol. Bioeng. , vol.110 , pp. 2856-2864
    • Nam, D.H.1    Ge, X.2
  • 30
    • 2142828483 scopus 로고    scopus 로고
    • Characterization of Mca-Lys-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2, a fluorogenic substrate with increased specificity constants for collagenases and tumor necrosis factor converting enzyme
    • U. Neumann, H. Kubota, K. Frei, V. Ganu, and D. Leppert Characterization of Mca-Lys-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2, a fluorogenic substrate with increased specificity constants for collagenases and tumor necrosis factor converting enzyme Anal. Biochem. 328 2004 166 173
    • (2004) Anal. Biochem. , vol.328 , pp. 166-173
    • Neumann, U.1    Kubota, H.2    Frei, K.3    Ganu, V.4    Leppert, D.5
  • 31
    • 0032579501 scopus 로고    scopus 로고
    • Membrane type-1 matrix metalloprotease and stromelysin-3 cleave more efficiently synthetic substrates containing unusual amino acids in their P1' positions
    • A. Mucha, P. Cuniasse, R. Kannan, F. Beau, A. Yiotakis, P. Basset, and V. Dive Membrane type-1 matrix metalloprotease and stromelysin-3 cleave more efficiently synthetic substrates containing unusual amino acids in their P1' positions J. Biol. Chem. 273 1998 2763 2768
    • (1998) J. Biol. Chem. , vol.273 , pp. 2763-2768
    • Mucha, A.1    Cuniasse, P.2    Kannan, R.3    Beau, F.4    Yiotakis, A.5    Basset, P.6    Dive, V.7
  • 33
    • 82755167748 scopus 로고    scopus 로고
    • Fluid shear stress and sphingosine 1-phosphate activate calpain to promote membrane type 1 matrix metalloproteinase (MT1-MMP) membrane translocation and endothelial invasion into three-dimensional collagen matrices
    • H. Kang, H.I. Kwak, R. Kaunas, and K.J. Bayless Fluid shear stress and sphingosine 1-phosphate activate calpain to promote membrane type 1 matrix metalloproteinase (MT1-MMP) membrane translocation and endothelial invasion into three-dimensional collagen matrices J. Biol. Chem. 286 2011 42017 42026
    • (2011) J. Biol. Chem. , vol.286 , pp. 42017-42026
    • Kang, H.1    Kwak, H.I.2    Kaunas, R.3    Bayless, K.J.4
  • 34
    • 0035801473 scopus 로고    scopus 로고
    • Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion
    • Y. Itoh, A. Takamura, N. Ito, Y. Maru, H. Sato, N. Suenaga, T. Aoki, and M. Seiki Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion EMBO J. 20 2001 4782 4793
    • (2001) EMBO J. , vol.20 , pp. 4782-4793
    • Itoh, Y.1    Takamura, A.2    Ito, N.3    Maru, Y.4    Sato, H.5    Suenaga, N.6    Aoki, T.7    Seiki, M.8
  • 35
    • 65249155429 scopus 로고    scopus 로고
    • Protease-dependent versus -independent cancer cell invasion programs: Three-dimensional amoeboid movement revisited
    • F. Sabeh, R. Shimizu-Hirota, and S.J. Weiss Protease-dependent versus -independent cancer cell invasion programs: three-dimensional amoeboid movement revisited J. Cell Biol. 185 2009 11 19
    • (2009) J. Cell Biol. , vol.185 , pp. 11-19
    • Sabeh, F.1    Shimizu-Hirota, R.2    Weiss, S.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.