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Volumn 16, Issue 5, 2011, Pages 1861-1872

The roles of ADAMTS metalloproteinases in tumorigenesis and metastasis

Author keywords

ADAMTS; Angiogenesis; Metalloproteinase; Metastasis; Review; Thrombospondin type 1 repeat

Indexed keywords

ADAM PROTEIN; ANGIOGENESIS INHIBITOR; METALLOPROTEINASE; THROMBOSPONDIN;

EID: 79955027296     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/3827     Document Type: Article
Times cited : (79)

References (79)
  • 1
    • 0036516460 scopus 로고    scopus 로고
    • Matrix metalloproteinases: A tail of a frog that became a prince
    • C. E. Brinckerhoff and L. M. Matrisian: Matrix metalloproteinases: a tail of a frog that became a prince. Nat Rev Mol Cell Biol, 3(3), 207-14 (2002)
    • (2002) Nat Rev Mol Cell Biol , vol.3 , Issue.3 , pp. 207-214
    • Brinckerhoff, C.E.1    Matrisian, L.M.2
  • 2
    • 0037192458 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors and cancer: Trials and tribulations
    • DOI 10.1126/science.1067100
    • L. M. Coussens, B. Fingleton and L. M. Matrisian: Matrix Metalloproteinase Inhibitors and Cancer - Trials and Tribulations. Science, 295(5564), 2387-2392 (2002) (Pubitemid 34270240)
    • (2002) Science , vol.295 , Issue.5564 , pp. 2387-2392
    • Coussens, L.M.1    Fingleton, B.2    Matrisian, L.M.3
  • 3
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • M. Egeblad and Z. Werb: New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer, 2(3), 161-74 (2002) (Pubitemid 37328786)
    • (2002) Nature Reviews Cancer , vol.2 , Issue.3 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 4
    • 34648815810 scopus 로고    scopus 로고
    • Emerging roles of proteases in tumour suppression
    • DOI 10.1038/nrc2228, PII NRC2228
    • C. Lopez-Otin and L. M. Matrisian: Emerging roles of proteases in tumor suppression. Nat Rev Cancer, 7(10), 800-8 (2007) (Pubitemid 47463671)
    • (2007) Nature Reviews Cancer , vol.7 , Issue.10 , pp. 800-808
    • Lopez-Otin, C.1    Matrisian, L.M.2
  • 6
    • 21644449866 scopus 로고    scopus 로고
    • ADAMTS proteinases: A multi-domain, multi-functional family with roles in extracellular matrix turnover and arthritis
    • DOI 10.1186/ar1783
    • G. C. Jones and G. P. Riley: ADAMTS proteinases: a multi-domain, multi-functional family with roles in extracellular matrix turnover and arthritis. Arthritis research & therapy, 7(4), 160-9 (2005) (Pubitemid 40936607)
    • (2005) Arthritis Research and Therapy , vol.7 , Issue.4 , pp. 160-169
    • Jones, G.C.1    Riley, G.P.2
  • 7
    • 70450253102 scopus 로고    scopus 로고
    • A disintegrin-like and metalloprotease (reprolysin-type) with thrombospondin type 1 motif (ADAMTS) superfamily: Functions and mechanisms
    • S. S. Apte: A disintegrin-like and metalloprotease (reprolysin-type) with thrombospondin type 1 motif (ADAMTS) superfamily: functions and mechanisms. The Journal of Biological Chemistry, 284(46), 31493-7 (2009)
    • (2009) The Journal of Biological Chemistry , vol.284 , Issue.46 , pp. 31493-31497
    • Apte, S.S.1
  • 8
    • 34147105872 scopus 로고    scopus 로고
    • ADAMs in cancer cell proliferation and progression
    • DOI 10.1111/j.1349-7006.2007.00434.x
    • S. Mochizuki and Y. Okada: ADAMs in cancer cell proliferation and progression. Cancer Sci, 98(5), 621-8 (2007) (Pubitemid 46563436)
    • (2007) Cancer Science , vol.98 , Issue.5 , pp. 621-628
    • Mochizuki, S.1    Okada, Y.2
  • 10
    • 77953345122 scopus 로고    scopus 로고
    • Matrix metalloproteinases, a disintegrin and metalloproteinases, and a disintegrin and metalloproteinases with thrombospondin motifs in non-neoplastic diseases
    • T. Shiomi, V. Lemaitre, J. D'Armiento and Y. Okada: Matrix metalloproteinases, a disintegrin and metalloproteinases, and a disintegrin and metalloproteinases with thrombospondin motifs in non-neoplastic diseases. Pathol Int, 60(7), 477-96 (2010)
    • (2010) Pathol Int , vol.60 , Issue.7 , pp. 477-496
    • Shiomi, T.1    Lemaitre, V.2    D'Armiento, J.3    Okada, Y.4
  • 11
    • 0031036524 scopus 로고    scopus 로고
    • Molecular cloning of a gene encoding a new type of metalloproteinase- disintegrin family protein with thrombospondin motifs as an inflammation associated gene
    • DOI 10.1074/jbc.272.1.556
    • K. Kuno, N. Kanada, E. Nakashima, F. Fujiki, F. Ichimura and K. Matsushima: Molecular Cloning of a Gene Encoding a New Type of Metalloproteinase-disintegrin Family Protein with Thrombospondin Motifs as an Inflammation Associated Gene. The Journal of Biological Chemistry, 272(1), 556-562 (1997) (Pubitemid 27021194)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.1 , pp. 556-562
    • Kuno, K.1    Kanada, N.2    Nakashirma, E.3    Fujiki, F.4    Ichimura, F.5    Matsushima, K.6
  • 14
    • 40149083619 scopus 로고    scopus 로고
    • The secreted metalloprotease ADAMTS20 is required for melanoblast survival
    • D. L. Silver, L. Hou, R. Somerville, M. E. Young, S. S. Apte and W. J. Pavan: The secreted metalloprotease ADAMTS20 is required for melanoblast survival. PLoS genetics, 4(2), e1000003-e1000003 (2008)
    • (2008) PLoS Genetics , vol.4 , Issue.2
    • Silver, D.L.1    Hou, L.2    Somerville, R.3    Young, M.E.4    Apte, S.S.5    Pavan, W.6
  • 16
    • 15344342865 scopus 로고    scopus 로고
    • Functional evolution of ADAMTS genes: Evidence from analyses of phylogeny and gene organizations
    • A. C. Nicholson, S. B. Malik, J. M. Logsdon, Jr. and E. G. Van Meir: Functional evolution of ADAMTS genes: evidence from analyses of phylogeny and gene organizations. BMC Evol Biol, 5(1), 11 (2005)
    • (2005) BMC Evol Biol , vol.5 , Issue.1 , pp. 11
    • Nicholson, A.C.1    Malik, S.B.2    Logsdon Jr., J.M.3    Van Meir, E.G.4
  • 18
    • 34848826829 scopus 로고    scopus 로고
    • Crystal Structures of Human ADAMTS-1 Reveal a Conserved Catalytic Domain and a Disintegrin-like Domain with a Fold Homologous to Cysteine-Rich Domains
    • DOI 10.1016/j.jmb.2007.07.047, PII S0022283607009849
    • S. Gerhardt, G. Hassall, P. Hawtin, E. McCall, L. Flavell, C. Minshull, D. Hargreaves, A. Ting, R. A. Pauptit, A. E. Parker and W. M. Abbott: Crystal structures of human ADAMTS-1 reveal a conserved catalytic domain and a disintegrin-like domain with a fold homologous to cysteine-rich domains. Journal of molecular biology, 373(4), 891-902 (2007) (Pubitemid 47505246)
    • (2007) Journal of Molecular Biology , vol.373 , Issue.4 , pp. 891-902
    • Gerhardt, S.1    Hassall, G.2    Hawtin, P.3    McCall, E.4    Flavell, L.5    Minshull, C.6    Hargreaves, D.7    Ting, A.8    Pauptit, R.A.9    Parker, A.E.10    Abbott, W.M.11
  • 20
    • 0032577568 scopus 로고    scopus 로고
    • ADAMTS-1 protein anchors at the extracellular matrix through the thrombospondin type I motifs and its spacing region
    • DOI 10.1074/jbc.273.22.13912
    • K. Kuno and K. Matsushima: ADAMTS-1 Protein Anchors at the Extracellular Matrix through the Thrombospondin Type I Motifs and Its Spacing Region. The Journal of Biological Chemistry, 273(22), 13912-13917 (1998) (Pubitemid 28268445)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.22 , pp. 13912-13917
    • Kuno, K.1    Matsushima, K.2
  • 24
    • 2442595171 scopus 로고    scopus 로고
    • Proprotein Convertase Furin Interacts with and Cleaves Pro-ADAMTS4 (Aggrecanase-1) in the trans-Golgi Network
    • DOI 10.1074/jbc.M312797200
    • P. Wang, M. Tortorella, K. England, A. M. Malfait, G. Thomas, E. C. Arner and D. Pei: Proprotein convertase furin interacts with and cleaves pro-ADAMTS4 (Aggrecanase-1) in the trans-Golgi network. J Biol Chem, 279(15), 15434-40 (2004) (Pubitemid 38618943)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.15 , pp. 15434-15440
    • Wang, P.1    Tortorella, M.2    England, K.3    Malfait, A.-M.4    Thomas, G.5    Arner, E.C.6    Pei, D.7
  • 26
    • 0344875565 scopus 로고    scopus 로고
    • Cleavage of the ADAMTS13 propeptide is not required for protease activity
    • DOI 10.1074/jbc.M309872200
    • E. M. Majerus, X. Zheng, E. A. Tuley and J. E. Sadler: Cleavage of the ADAMTS13 propeptide is not required for protease activity. J Biol Chem, 278(47), 46643-8 (2003) (Pubitemid 37452240)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.47 , pp. 46643-46648
    • Majerus, E.M.1    Zheng, X.2    Tuley, E.A.3    Sadler, J.E.4
  • 28
    • 34547125794 scopus 로고    scopus 로고
    • TIMP-3 inhibition of ADAMTS-4 (Aggrecanase-1) is modulated by interactions between aggrecan and the C-terminal domain of ADAMTS-4
    • DOI 10.1074/jbc.M610721200
    • G. J. Wayne, S. J. Deng, A. Amour, S. Borman, R. Matico, H. L. Carter and G. Murphy: TIMP-3 inhibition of ADAMTS-4 (Aggrecanase-1) is modulated by interactions between aggrecan and the C-terminal domain of ADAMTS-4. J Biol Chem, 282(29), 20991-8 (2007) (Pubitemid 47099922)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.29 , pp. 20991-20998
    • Wayne, G.J.1    Deng, S.-J.2    Amour, A.3    Borman, S.4    Matico, R.5    Carter, H.L.6    Murphy, G.7
  • 29
    • 0036800192 scopus 로고    scopus 로고
    • Metalloproteinase inhibitors: Biological actions and therapeutic opportunities
    • DOI 10.1242/jcs.00063
    • A. H. Baker, D. R. Edwards and G. Murphy: Metalloproteinase inhibitors: biological actions and therapeutic opportunities. Journal of cell science, 115(Pt 19), 3719-27 (2002) (Pubitemid 35203598)
    • (2002) Journal of Cell Science , vol.115 , Issue.19 , pp. 3719-3727
    • Baker, A.H.1    Edwards, D.R.2    Murphy, G.3
  • 30
    • 77956644315 scopus 로고    scopus 로고
    • Reactive site mutants of N-TIMP-3that selectively inhibit ADAMTS-4 and ADAMTS-5: Biological and structural implications
    • N. H. Lim, M. Kashiwagi, R. Visse, J. Jones, J. J. Enghild, K. Brew and H. Nagase: Reactive site mutants of N-TIMP-3that selectively inhibit ADAMTS-4 and ADAMTS-5: Biological and structural implications. Biochem J (2010)
    • (2010) Biochem J
    • Lim, N.H.1    Kashiwagi, M.2    Visse, R.3    Jones, J.4    Enghild, J.J.5    Brew, K.6    Nagase, H.7
  • 35
    • 27944478173 scopus 로고    scopus 로고
    • Matrix-degrading proteases ADAMTS4 and ADAMTS5 (disintegrins and metalloproteinases with thrombospondin motifs 4 and 5) are expressed in human glioblastomas
    • DOI 10.1002/ijc.21258
    • J. Held-Feindt, E. B. Paredes, U. Blomer, C. Seidenbecher, A. M. Stark, H. M. Mehdorn and R. Mentlein: Matrix-degrading proteases ADAMTS4 and ADAMTS5 (disintegrins and metalloproteinases with thrombospondin motifs 4 and 5) are expressed in human glioblastomas. Int J Cancer, 118(1), 55-61 (2006) (Pubitemid 41681580)
    • (2006) International Journal of Cancer , vol.118 , Issue.1 , pp. 55-61
    • Held-Feindt, J.1    Paredes, E.B.2    Blomer, U.3    Seidenbecher, C.4    Stark, A.M.5    Mehdorn, H.M.6    Mentlein, R.7
  • 36
    • 0038757017 scopus 로고    scopus 로고
    • METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity
    • F. Vazquez, G. Hastings, M. A. Ortega, T. F. Lane, S. Oikemus, M. Lombardo and M. L. Iruela-Arispe: METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity. J Biol Chem, 274(33), 23349-57 (1999)
    • (1999) J Biol Chem , vol.274 , Issue.33 , pp. 23349-23357
    • Vazquez, F.1    Hastings, G.2    Ortega, M.A.3    Lane, T.F.4    Oikemus, S.5    Lombardo, M.6    Iruela-Arispe, M.L.7
  • 39
    • 33646144000 scopus 로고    scopus 로고
    • Full-length ADAMTS-1 and the ADAMTS-1 fragments display pro- and antimetastatic activity, respectively
    • Y. J. Liu, Y. Xu and Q. Yu: Full-length ADAMTS-1 and the ADAMTS-1 fragments display pro- and antimetastatic activity, respectively. Oncogene, 25(17), 2452-67 (2006)
    • (2006) Oncogene , vol.25 , Issue.17 , pp. 2452-2467
    • Liu, Y.J.1    Xu, Y.2    Yu, Q.3
  • 40
    • 2942541805 scopus 로고    scopus 로고
    • The carboxyl-terminal half region of ADAMTS-1 suppresses both tumorigenicity and experimental tumor metastatic potential
    • DOI 10.1016/j.bbrc.2004.05.105, PII S0006291X04010964
    • K. Kuno, K. Bannai, M. Hakozaki, K. Matsushima and K. Hirose: The carboxyl-terminal half region of ADAMTS-1 suppresses both tumorigenicity and experimental tumor metastatic potential. Biochem Biophys Res Commun, 319(4), 1327-33 (2004) (Pubitemid 38759556)
    • (2004) Biochemical and Biophysical Research Communications , vol.319 , Issue.4 , pp. 1327-1333
    • Kuno, K.1    Bannai, K.2    Hakozaki, M.3    Matsushima, K.4    Hirose, K.5
  • 41
    • 33845679095 scopus 로고    scopus 로고
    • ADAMTS1, CRABP1, and NR3C1 identified as epigenetically deregulated genes in colorectal tumorigenesis
    • G. E. Lind, K. Kleivi, G. I. Meling, M. R. Teixeira, E. Thiis-Evensen, T. O. Rognum and R. A. Lothe: ADAMTS1, CRABP1, and NR3C1 identified as epigenetically deregulated genes in colorectal tumorigenesis. Cell Oncol, 28(5-6), 259-72 (2006) (Pubitemid 44950097)
    • (2006) Cellular Oncology , vol.28 , Issue.5-6 , pp. 259-272
    • Lind, G.E.1    Kleivi, K.2    Meling, G.I.3    Teixeira, M.R.4    Thiis-Evensen, E.5    Rognum, T.O.6    Lothe, R.A.7
  • 42
    • 0038109791 scopus 로고    scopus 로고
    • 165
    • DOI 10.1074/jbc.M212964200
    • A. Luque, D. R. Carpizo and M. L. Iruela-Arispe: ADAMTS1/METH1 inhibits endothelial cell proliferation by direct binding and sequestration of VEGF165. J Biol Chem, 278(26), 23656-65 (2003) (Pubitemid 36830188)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.26 , pp. 23656-23665
    • Luque, A.1    Carpizo, D.R.2    Iruela-Arispe, M.L.3
  • 43
    • 21244501417 scopus 로고    scopus 로고
    • ADAMTS1 proteinase is up-regulated in wounded skin and regulates migration of fibroblasts and endothelial cells
    • DOI 10.1074/jbc.M412212200
    • M. Krampert, S. Kuenzle, S. N. M. Thai, N. Lee, M. L. Iruela-Arispe and S. Werner: ADAMTS1 proteinase is upregulated in wounded skin and regulates migration of fibroblasts and endothelial cells. The Journal of Biological Chemistry, 280(25), 23844-52 (2005) (Pubitemid 40884871)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.25 , pp. 23844-23852
    • Krampert, M.1    Kuenzle, S.2    Thai, S.N.-M.3    Lee, N.4    Iruela-Arispe, M.L.5    Werner, S.6
  • 44
    • 33751073396 scopus 로고    scopus 로고
    • ADAMTS1 mediates the release of antiangiogenic polypeptides from TSP1 and 2
    • DOI 10.1038/sj.emboj.7601400, PII 7601400
    • N. V. Lee, M. Sato, D. S. Annis, J. a. Loo, L. Wu, D. F. Mosher and M. L. Iruela-Arispe: ADAMTS1 mediates the release of antiangiogenic polypeptides from TSP1 and 2. The EMBO journal, 25(22), 5270-83 (2006) (Pubitemid 44764137)
    • (2006) EMBO Journal , vol.25 , Issue.22 , pp. 5270-5283
    • Lee, N.V.1    Sato, M.2    Annis, D.S.3    Loo, J.A.4    Wu, L.5    Mosher, D.F.6    Iruela-Arispe, M.L.7
  • 47
    • 69249228553 scopus 로고    scopus 로고
    • ADAMTS1 and MMP1 proteolytically engage EGF-like ligands in an osteolytic signaling cascade for bone metastasis
    • X. Lu, Q. Wang, G. Hu, C. Van Poznak, M. Fleisher, M. Reiss, J. Massague and Y. Kang: ADAMTS1 and MMP1 proteolytically engage EGF-like ligands in an osteolytic signaling cascade for bone metastasis. Genes Dev, 23(16), 1882-94 (2009)
    • (2009) Genes Dev , vol.23 , Issue.16 , pp. 1882-1894
    • Lu, X.1    Wang, Q.2    Hu, G.3    Van Poznak, C.4    Fleisher, M.5    Reiss, M.6    Massague, J.7    Kang, Y.8
  • 50
    • 33751087882 scopus 로고    scopus 로고
    • Identification of substrates of the extracellular protease ADAMTS1 by DIGE proteomic analysis
    • F. Canals, N. Colome, C. Ferrer, C. Plaza-Calonge Mdel and J. C. Rodriguez-Manzaneque: Identification of substrates of the extracellular protease ADAMTS1 by DIGE proteomic analysis. Proteomics, 6 Suppl 1, S28-35 (2006)
    • (2006) Proteomics , vol.6 , Issue.SUPPL. 1
    • Canals, F.1    Colome, N.2    Ferrer, C.3    Plaza-Calonge Mdel, C.4    Rodriguez-Manzaneque, J.C.5
  • 51
    • 33745812768 scopus 로고    scopus 로고
    • ADAMTS1 interacts with, cleaves, and modifies the extracellular location of the matrix inhibitor tissue factor pathway inhibitor-2
    • DOI 10.1074/jbc.M513465200
    • A. X. Torres-Collado, W. Kisiel, M. L. Iruela-Arispe and J. C. Rodriguez-Manzaneque: ADAMTS1 interacts with, cleaves, and modifies the extracellular location of the matrix inhibitor tissue factor pathway inhibitor-2. J Biol Chem, 281(26), 17827-37 (2006) (Pubitemid 44035581)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.26 , pp. 17827-17837
    • Torres-Collado, A.X.1    Kisiel, W.2    Iruela-Arispe, M.L.3    Rodriguez-Manzaneque, J.C.4
  • 55
    • 33646137579 scopus 로고    scopus 로고
    • Expression of ADAMTS-8, a secreted protease with antiangiogenic properties, is downregulated in brain tumors
    • J. R. Dunn, J. E. Reed, D. G. du Plessis, E. J. Shaw, P. Reeves, A. L. Gee, P. Warnke and C. Walker: Expression of ADAMTS-8, a secreted protease with antiangiogenic properties, is downregulated in brain tumors. Br J Cancer, 94(8), 1186-93 (2006)
    • (2006) Br J Cancer , vol.94 , Issue.8 , pp. 1186-1193
    • Dunn, J.R.1    Reed, J.E.2    Du Plessis, D.G.3    Shaw, E.J.4    Reeves, P.5    Gee, A.L.6    Warnke, P.7    Walker, C.8
  • 58
    • 77749304050 scopus 로고    scopus 로고
    • ADAMTS9 is a cell-autonomously acting, antiangiogenic metalloprotease expressed by microvascular endothelial cells
    • B. H. Koo, D. M. Coe, L. J. Dixon, R. P. Somerville, C. M. Nelson, L. W. Wang, M. E. Young, D. J. Lindner and S. S. Apte: ADAMTS9 is a cell-autonomously acting, antiangiogenic metalloprotease expressed by microvascular endothelial cells. Am J Pathol, 176(3), 1494-504 (2010)
    • (2010) Am J Pathol , vol.176 , Issue.3 , pp. 1494-1504
    • Koo, B.H.1    Coe, D.M.2    Dixon, L.J.3    Somerville, R.P.4    Nelson, C.M.5    Wang, L.W.6    Young, M.E.7    Lindner, D.J.8    Apte, S.S.9
  • 59
    • 0034253787 scopus 로고    scopus 로고
    • ADAMTS9, a novel member of the ADAM-TS/metallospondin gene family
    • DOI 10.1006/geno.2000.6246
    • M. E. Clark, G. S. Kelner, L. A. Turbeville, A. Boyer, K. C. Arden and R. A. Maki: ADAMTS9, a novel member of the ADAM-TS/ metallospondin gene family. Genomics, 67(3), 343-50 (2000) (Pubitemid 30651033)
    • (2000) Genomics , vol.67 , Issue.3 , pp. 343-350
    • Clark, M.E.1    Kelner, G.S.2    Turbeville, L.A.3    Boyer, A.4    Arden, K.C.5    Maki, R.A.6
  • 60
    • 33846046177 scopus 로고    scopus 로고
    • Identification of a tumor suppressive critical region mapping to 3p14.2 in esophageal squamous cell carcinoma and studies of a candidate tumor suppressor gene, ADAMTS9
    • DOI 10.1038/sj.onc.1209767, PII 1209767
    • P. H. Lo, A. C. Leung, C. Y. Kwok, W. S. Cheung, J. M. Ko, L. C. Yang, S. Law, L. D. Wang, J. Li, E. J. Stanbridge, G. Srivastava, J. C. Tang, S. W. Tsao and M. L. Lung: Identification of a tumor suppressive critical region mapping to 3p14.2 in esophageal squamous cell carcinoma and studies of a candidate tumor suppressor gene, ADAMTS9. Oncogene, 26(1), 148-57 (2007) (Pubitemid 46067340)
    • (2007) Oncogene , vol.26 , Issue.1 , pp. 148-157
    • Lo, P.H.Y.1    Leung, A.C.C.2    Kwok, C.Y.C.3    Cheung, W.S.Y.4    Ko, J.M.Y.5    Yang, L.C.6    Law, S.7    Wang, L.D.8    Li, J.9    Stanbridge, E.J.10    Srivastava, G.11    Tang, J.C.O.12    Tsao, S.W.13    Lung, M.L.14
  • 65
    • 60149098168 scopus 로고    scopus 로고
    • Regulation of chondrocyte differentiation by ADAMTS-12 metalloproteinase depends on its enzymatic activity
    • X. H. Bai, D. W. Wang, Y. Luan, X. P. Yu and C. J. Liu: Regulation of chondrocyte differentiation by ADAMTS-12 metalloproteinase depends on its enzymatic activity. Cell Mol Life Sci, 66(4), 667-80 (2009)
    • (2009) Cell Mol Life Sci , vol.66 , Issue.4 , pp. 667-680
    • Bai, X.H.1    Wang, D.W.2    Luan, Y.3    Yu, X.P.4    Liu, C.J.5
  • 66
    • 36249015281 scopus 로고    scopus 로고
    • The ADAMTS12 metalloproteinase exhibits anti-tumorigenic properties through modulation of the Ras-dependent ERK signalling pathway
    • DOI 10.1242/jcs.005751
    • M. Llamazares, A. J. Obaya, A. Moncada-Pazos, R. Heljasvaara, J. Espada, C. Lopez-Otin and S. Cal: The ADAMTS12 metalloproteinase exhibits anti-tumorigenic properties through modulation of the Ras-dependent ERK signalling pathway. J Cell Sci, 120(Pt 20), 3544-3552 (2007) (Pubitemid 350120947)
    • (2007) Journal of Cell Science , vol.120 , Issue.20 , pp. 3544-3552
    • Llamazares, M.1    Obaya, A.J.2    Moncada-Pazos, A.3    Heljasvaara, R.4    Espada, J.5    Lopez-Otin, C.6    Cal, S.7
  • 67
    • 70350036203 scopus 로고    scopus 로고
    • The ADAMTS12 metalloprotease gene is epigenetically silenced in tumor cells and transcriptionally activated in the stroma during progression of colon cancer
    • A. Moncada-Pazos, A. J. Obaya, M. F. Fraga, C. G. Viloria, G. Capella, M. Gausachs, M. Esteller, C. Lopez-Otin and S. Cal: The ADAMTS12 metalloprotease gene is epigenetically silenced in tumor cells and transcriptionally activated in the stroma during progression of colon cancer. J Cell Sci, 122(Pt 16), 2906-13 (2009)
    • (2009) J Cell Sci , vol.122 , Issue.PART 16 , pp. 2906-2913
    • Moncada-Pazos, A.1    Obaya, A.J.2    Fraga, M.F.3    Viloria, C.G.4    Capella, G.5    Gausachs, M.6    Esteller, M.7    Lopez-Otin, C.8    Cal, S.9
  • 69
    • 0033135056 scopus 로고    scopus 로고
    • Deficient activity of von Willebrand's factor-cleaving protease in patients with disseminated malignancies
    • L. Oleksowicz, N. Bhagwati and M. DeLeon- Fernandez: Deficient activity of von Willebrand's factorcleaving protease in patients with disseminated malignancies. Cancer Res, 59(9), 2244-50 (1999) (Pubitemid 29217692)
    • (1999) Cancer Research , vol.59 , Issue.9 , pp. 2244-2250
    • Oleksowicz, L.1    Bhagwati, N.2    DeLeon-Fernandez, M.3
  • 70
    • 0037085694 scopus 로고    scopus 로고
    • Deficiency of von Willebrand factor-cleaving protease activity in the plasma of malignant patients
    • DOI 10.1016/S0049-3848(02)00053-1, PII S0049384802000531
    • B. H. Koo, D. Oh, S. Y. Chung, N. K. Kim, S. Park, Y. Jang and K. H. Chung: Deficiency of von Willebrand factor-cleaving protease activity in the plasma of malignant patients. Thromb Res, 105(6), 471-6 (2002) (Pubitemid 34686905)
    • (2002) Thrombosis Research , vol.105 , Issue.6 , pp. 471-476
    • Koo, B.-H.1    Oh, D.2    Chung, S.Y.3    Kim, N.K.4    Park, S.5    Jang, Y.6    Chung, K.-H.7
  • 71
    • 0141649437 scopus 로고    scopus 로고
    • Von Willebrand factor cleaving protease (ADAMTS-13) in 123 patients with connective tissue diseases (systemic lupus erythematosus and systemic sclerosis)
    • P. M. Mannucci, M. Vanoli, I. Forza, M. T. Canciani and R. Scorza: Von Willebrand factor cleaving protease (ADAMTS-13) in 123 patients with connective tissue diseases (systemic lupus erythematosus and systemic sclerosis). Haematologica, 88(8), 914-8 (2003) (Pubitemid 37128091)
    • (2003) Haematologica , vol.88 , Issue.8 , pp. 914-918
    • Mannucci, P.M.1    Vanoli, M.2    Forza, I.3    Canciani, M.T.4    Scorza, R.5
  • 72
    • 0345303929 scopus 로고    scopus 로고
    • ADAMTS-13 activity in patients with brain and prostate tumors is mildly reduced, but not correlated to stage of malignancy and metastasis
    • DOI 10.1016/j.thromres.2003.08.018
    • M. Bohm, R. Gerlach, W. D. Beecken, T. Scheuer, I. Stier-Bruck and I. Scharrer: ADAMTS-13 activity in patients with brain and prostate tumors is mildly reduced, but not correlated to stage of malignancy and metastasis. Thromb Res, 111(1-2), 33-7 (2003) (Pubitemid 37485923)
    • (2003) Thrombosis Research , vol.111 , Issue.1-2 , pp. 33-37
    • Bohm, M.1    Gerlach, R.2    Beecken, W.-D.3    Scheuer, T.4    Stier-Bruck, I.5    Scharrer, I.6
  • 73
    • 33644912845 scopus 로고    scopus 로고
    • Expression profiling of metalloproteinases and tissue inhibitors of metalloproteinases in normal and degenerate human achilles tendon
    • G. C. Jones, A. N. Corps, C. J. Pennington, I. M. Clark, D. R. Edwards, M. M. Bradley, B. L. Hazleman and G. P. Riley: Expression profiling of metalloproteinases and tissue inhibitors of metalloproteinases in normal and degenerate human achilles tendon. Arthritis and rheumatism, 54(3), 832-42 (2006)
    • (2006) Arthritis and Rheumatism , vol.54 , Issue.3 , pp. 832-842
    • Jones, G.C.1    Corps, A.N.2    Pennington, C.J.3    Clark, I.M.4    Edwards, D.R.5    Bradley, M.M.6    Hazleman, B.L.7    Riley, G.P.8
  • 77
    • 67650386153 scopus 로고    scopus 로고
    • Cterminal ADAMTS-18 fragment induces oxidative platelet fragmentation, dissolves platelet aggregates, and protects against carotid artery occlusion and cerebral stroke
    • Z. Li, M. A. Nardi, Y. S. Li, W. Zhang, R. Pan, S. Dang, H. Yee, D. Quartermain, S. Jonas and S. Karpatkin: Cterminal ADAMTS-18 fragment induces oxidative platelet fragmentation, dissolves platelet aggregates, and protects against carotid artery occlusion and cerebral stroke. Blood, 113(24), 6051-60 (2009)
    • (2009) Blood , vol.113 , Issue.24 , pp. 6051-6060
    • Li, Z.1    Nardi, M.A.2    Li, Y.S.3    Zhang, W.4    Pan, R.5    Dang, S.6    Yee, H.7    Quartermain, D.8    Jonas, S.9    Karpatkin, S.10
  • 79
    • 33847276695 scopus 로고    scopus 로고
    • In search of partners: Linking extracellular proteases to substrates
    • C. M. Overall and C. P. Blobel: In search of partners: linking extracellular proteases to substrates. Nature reviews. Molecular cell biology, 8(3), 245-57 (2007)
    • (2007) Nature Reviews. Molecular Cell Biology , vol.8 , Issue.3 , pp. 245-257
    • Overall, C.M.1    Blobel, C.P.2


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