메뉴 건너뛰기




Volumn 13, Issue 4, 2014, Pages 2080-2093

Deciphering the role of the ADAM17-dependent secretome in cell signaling

Author keywords

ADAM17; label free; migration; proliferation; secretome; signaling; SILAC

Indexed keywords

CADHERIN; CANSTATIN; CERULOPLASMIN; COMPLEMENT COMPONENT C1R; COMPLEMENT COMPONENT C1S; CYSTATIN C; EPHRIN RECEPTOR; FIBRILLIN 1; FIBROMODULIN; FIBULIN 5; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; HERMES ANTIGEN; LACTADHERIN; MATRILIN; MIMECAN; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; NERVE CELL ADHESION MOLECULE; OSTEONECTIN; OSTEOPROTEGERIN; PERLECAN; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; PROSAPOSIN; PROTEIN TYROSINE KINASE; SCLEROPROTEIN; SERINE PROTEINASE INHIBITOR; SYNDECAN 4; TENASCIN; TRANSCRIPTION FACTOR RUNX2; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME; ADAM PROTEIN; PROTEOME; TUMOR NECROSIS FACTOR-ALPHA CONVERTASE;

EID: 84898767133     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr401224u     Document Type: Article
Times cited : (39)

References (81)
  • 1
    • 0035500490 scopus 로고    scopus 로고
    • The many faces of metalloproteases: Cell growth, invasion, angiogenesis and metastasis
    • Chang, C.; Werb, Z. The many faces of metalloproteases: cell growth, invasion, angiogenesis and metastasis Trends Cell Biol. 2001, 11, S37-43
    • (2001) Trends Cell Biol. , vol.11 , pp. 37-43
    • Chang, C.1    Werb, Z.2
  • 2
    • 0037224740 scopus 로고    scopus 로고
    • The ADAMs family of metalloproteases: Multidomain proteins with multiple functions
    • Seals, D. F.; Courtneidge, S. A. The ADAMs family of metalloproteases: multidomain proteins with multiple functions Genes Dev. 2003, 17, 7-30
    • (2003) Genes Dev. , vol.17 , pp. 7-30
    • Seals, D.F.1    Courtneidge, S.A.2
  • 3
    • 34247341829 scopus 로고    scopus 로고
    • Proteomics discovery of metalloproteinase substrates in the cellular context by iTRAQ labeling reveals a diverse MMP-2 substrate degradome
    • Dean, R. A.; Overall, C. M. Proteomics discovery of metalloproteinase substrates in the cellular context by iTRAQ labeling reveals a diverse MMP-2 substrate degradome Mol. Cell. Proteomics. 2007, 6, 611-23
    • (2007) Mol. Cell. Proteomics. , vol.6 , pp. 611-623
    • Dean, R.A.1    Overall, C.M.2
  • 4
    • 33745477470 scopus 로고    scopus 로고
    • Proteomic identification of desmoglein 2 and activated leukocyte cell adhesion molecule as substrates of ADAM17 and ADAM10 by difference gel electrophoresis
    • Bech-Serra, J. J.; Santiago-Josefat, B.; Esselens, C.; Saftig, P.; Baselga, J.; Arribas, J.; Canals, F. Proteomic identification of desmoglein 2 and activated leukocyte cell adhesion molecule as substrates of ADAM17 and ADAM10 by difference gel electrophoresis Mol. Cell. Biol. 2006, 26, 5086-95
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 5086-5095
    • Bech-Serra, J.J.1    Santiago-Josefat, B.2    Esselens, C.3    Saftig, P.4    Baselga, J.5    Arribas, J.6    Canals, F.7
  • 5
    • 84859738660 scopus 로고    scopus 로고
    • 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
    • Starr, A. E.; Bellac, C. L.; Dufour, A.; Goebeler, V.; Overall, C. M. 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. 2012, 287, 13382-95
    • (2012) J. Biol. Chem. , vol.287 , pp. 13382-13395
    • Starr, A.E.1    Bellac, C.L.2    Dufour, A.3    Goebeler, V.4    Overall, C.M.5
  • 7
    • 77951134556 scopus 로고    scopus 로고
    • Multiplex N-terminome analysis of MMP-2 and MMP-9 substrate degradomes by iTRAQ-TAILS quantitative proteomics
    • Prudova, A.; auf dem Keller, U.; Butler, G. S.; Overall, C. M. Multiplex N-terminome analysis of MMP-2 and MMP-9 substrate degradomes by iTRAQ-TAILS quantitative proteomics Mol. Cell. Proteomics 2010, 9, 894-911
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 894-911
    • Prudova, A.1    Auf Dem Keller, U.2    Butler, G.S.3    Overall, C.M.4
  • 8
    • 84872593231 scopus 로고    scopus 로고
    • Systems-level analysis of proteolytic events in increased vascular permeability and complement activation in skin inflammation
    • auf dem Keller, U.; Prudova, A.; Eckhard, U.; Fingleton, B.; Overall, C. M. Systems-level analysis of proteolytic events in increased vascular permeability and complement activation in skin inflammation Sci. Signaling 2013, 6, rs2
    • (2013) Sci. Signaling , vol.6 , pp. 2
    • Auf Dem Keller, U.1    Prudova, A.2    Eckhard, U.3    Fingleton, B.4    Overall, C.M.5
  • 10
    • 69249098287 scopus 로고    scopus 로고
    • ADAM17 as a therapeutic target in multiple diseases
    • Arribas, J.; Esselens, C. ADAM17 as a therapeutic target in multiple diseases Curr. Pharm. Des. 2009, 15, 2319-35
    • (2009) Curr. Pharm. Des. , vol.15 , pp. 2319-2335
    • Arribas, J.1    Esselens, C.2
  • 11
    • 79960923986 scopus 로고    scopus 로고
    • ADAM17: A molecular switch to control inflammation and tissue regeneration
    • Scheller, J.; Chalaris, A.; Garbers, C.; Rose-John, S. ADAM17: a molecular switch to control inflammation and tissue regeneration Trends Immunol. 2011, 32, 380-7
    • (2011) Trends Immunol. , vol.32 , pp. 380-387
    • Scheller, J.1    Chalaris, A.2    Garbers, C.3    Rose-John, S.4
  • 12
    • 63649105591 scopus 로고    scopus 로고
    • The good, the bad and the ugly substrates for ADAM10 and ADAM17 in brain pathology, inflammation and cancer
    • Pruessmeyer, J.; Ludwig, A. The good, the bad and the ugly substrates for ADAM10 and ADAM17 in brain pathology, inflammation and cancer Semin. Cell Dev. Biol. 2009, 20, 164-74
    • (2009) Semin. Cell Dev. Biol. , vol.20 , pp. 164-174
    • Pruessmeyer, J.1    Ludwig, A.2
  • 13
    • 84866531672 scopus 로고    scopus 로고
    • A disintegrin and metalloproteases: Molecular scissors in angiogenesis, inflammation and atherosclerosis
    • van der Vorst, E. P.; Keijbeck, A. A.; de Winther, M. P.; Donners, M. M. A disintegrin and metalloproteases: molecular scissors in angiogenesis, inflammation and atherosclerosis Atherosclerosis 2012, 224, 302-8
    • (2012) Atherosclerosis , vol.224 , pp. 302-308
    • Van Der Vorst, E.P.1    Keijbeck, A.A.2    De Winther, M.P.3    Donners, M.M.4
  • 14
    • 11244261160 scopus 로고    scopus 로고
    • ADAMs: Key components in EGFR signalling and development
    • Blobel, C. P. ADAMs: key components in EGFR signalling and development Nat. Rev. Mol. Cell Biol. 2005, 6, 32-43
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 32-43
    • Blobel, C.P.1
  • 15
    • 33748037366 scopus 로고    scopus 로고
    • Multiple acquired renal carcinoma tumor capabilities abolished upon silencing of ADAM17
    • Franovic, A.; Robert, I.; Smith, K.; Kurban, G.; Pause, A.; Gunaratnam, L.; Lee, S. Multiple acquired renal carcinoma tumor capabilities abolished upon silencing of ADAM17 Cancer Res. 2006, 66, 8083-90
    • (2006) Cancer Res. , vol.66 , pp. 8083-8090
    • Franovic, A.1    Robert, I.2    Smith, K.3    Kurban, G.4    Pause, A.5    Gunaratnam, L.6    Lee, S.7
  • 17
    • 84866546263 scopus 로고    scopus 로고
    • A disintegrin and metalloproteinase 17 (ADAM17) and epidermal growth factor receptor (EGFR) signaling drive the epithelial response to Staphylococcus aureus toxic shock syndrome toxin-1 (TSST-1)
    • Breshears, L. M.; Schlievert, P. M.; Peterson, M. L. A disintegrin and metalloproteinase 17 (ADAM17) and epidermal growth factor receptor (EGFR) signaling drive the epithelial response to Staphylococcus aureus toxic shock syndrome toxin-1 (TSST-1) J. Biol. Chem. 2012, 287, 32578-87
    • (2012) J. Biol. Chem. , vol.287 , pp. 32578-32587
    • Breshears, L.M.1    Schlievert, P.M.2    Peterson, M.L.3
  • 18
    • 0033573049 scopus 로고    scopus 로고
    • Ectodomain shedding of TGF-alpha and other transmembrane proteins is induced by receptor tyrosine kinase activation and MAP kinase signaling cascades
    • Fan, H.; Derynck, R. Ectodomain shedding of TGF-alpha and other transmembrane proteins is induced by receptor tyrosine kinase activation and MAP kinase signaling cascades EMBO J. 1999, 18, 6962-72
    • (1999) EMBO J. , vol.18 , pp. 6962-6972
    • Fan, H.1    Derynck, R.2
  • 19
    • 79955456934 scopus 로고    scopus 로고
    • Species specificity of ADAM10 and ADAM17 proteins in interleukin-6 (IL-6) trans-signaling and novel role of ADAM10 in inducible IL-6 receptor shedding
    • Garbers, C.; Janner, N.; Chalaris, A.; Moss, M. L.; Floss, D. M.; Meyer, D.; Koch-Nolte, F.; Rose-John, S.; Scheller, J. Species specificity of ADAM10 and ADAM17 proteins in interleukin-6 (IL-6) trans-signaling and novel role of ADAM10 in inducible IL-6 receptor shedding J. Biol. Chem. 2011, 286, 14804-11
    • (2011) J. Biol. Chem. , vol.286 , pp. 14804-14811
    • Garbers, C.1    Janner, N.2    Chalaris, A.3    Moss, M.L.4    Floss, D.M.5    Meyer, D.6    Koch-Nolte, F.7    Rose-John, S.8    Scheller, J.9
  • 20
    • 0034026325 scopus 로고    scopus 로고
    • Shedding of interleukin-6 receptor and tumor necrosis factor alpha. Contribution of the stalk sequence to the cleavage pattern of transmembrane proteins
    • Althoff, K.; Reddy, P.; Voltz, N.; Rose-John, S.; Mullberg, J. Shedding of interleukin-6 receptor and tumor necrosis factor alpha. Contribution of the stalk sequence to the cleavage pattern of transmembrane proteins Eur. J. Biochem. 2000, 267, 2624-31
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2624-2631
    • Althoff, K.1    Reddy, P.2    Voltz, N.3    Rose-John, S.4    Mullberg, J.5
  • 21
    • 79955479177 scopus 로고    scopus 로고
    • ADAM17 (TACE) regulates TGFbeta signaling through the cleavage of vasorin
    • Malapeira, J.; Esselens, C.; Bech-Serra, J. J.; Canals, F.; Arribas, J. ADAM17 (TACE) regulates TGFbeta signaling through the cleavage of vasorin Oncogene 2011, 30, 1912-22
    • (2011) Oncogene , vol.30 , pp. 1912-1922
    • Malapeira, J.1    Esselens, C.2    Bech-Serra, J.J.3    Canals, F.4    Arribas, J.5
  • 22
    • 59649123850 scopus 로고    scopus 로고
    • ADAM-17 regulates endothelial cell morphology, proliferation, and in vitro angiogenesis
    • Gooz, P.; Gooz, M.; Baldys, A.; Hoffman, S. ADAM-17 regulates endothelial cell morphology, proliferation, and in vitro angiogenesis Biochem. Biophys. Res. Commun. 2009, 380, 33-8
    • (2009) Biochem. Biophys. Res. Commun. , vol.380 , pp. 33-38
    • Gooz, P.1    Gooz, M.2    Baldys, A.3    Hoffman, S.4
  • 24
    • 79955470772 scopus 로고    scopus 로고
    • The "a Disintegrin and Metalloproteases" ADAM10 and ADAM17: Novel drug targets with therapeutic potential?
    • Saftig, P.; Reiss, K. The "A Disintegrin And Metalloproteases" ADAM10 and ADAM17: novel drug targets with therapeutic potential? Eur. J. Cell Biol. 2011, 90, 527-35
    • (2011) Eur. J. Cell Biol. , vol.90 , pp. 527-535
    • Saftig, P.1    Reiss, K.2
  • 25
    • 77957755656 scopus 로고    scopus 로고
    • Secretome proteomics for discovery of cancer biomarkers
    • Makridakis, M.; Vlahou, A. Secretome proteomics for discovery of cancer biomarkers J. Proteomics 2010, 73, 2291-305
    • (2010) J. Proteomics , vol.73 , pp. 2291-2305
    • Makridakis, M.1    Vlahou, A.2
  • 27
    • 78349311747 scopus 로고    scopus 로고
    • Cancer secretomics reveal pathophysiological pathways in cancer molecular oncology
    • Karagiannis, G. S.; Pavlou, M. P.; Diamandis, E. P. Cancer secretomics reveal pathophysiological pathways in cancer molecular oncology Mol. Oncol. 2010, 4, 496-510
    • (2010) Mol. Oncol. , vol.4 , pp. 496-510
    • Karagiannis, G.S.1    Pavlou, M.P.2    Diamandis, E.P.3
  • 29
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox, J.; Mann, M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification Nat. Biotechnol. 2008, 26, 1367-72
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 31
    • 84855171722 scopus 로고    scopus 로고
    • Expression2Kinases: MRNA profiling linked to multiple upstream regulatory layers
    • Chen, E. Y.; Xu, H.; Gordonov, S.; Lim, M. P.; Perkins, M. H.; Ma'ayan, A. Expression2Kinases: mRNA profiling linked to multiple upstream regulatory layers Bioinformatics 2012, 28, 105-11
    • (2012) Bioinformatics , vol.28 , pp. 105-111
    • Chen, E.Y.1    Xu, H.2    Gordonov, S.3    Lim, M.P.4    Perkins, M.H.5    Ma'Ayan, A.6
  • 34
    • 79952242675 scopus 로고    scopus 로고
    • High resolution analysis of snake venom metalloproteinase (SVMP) peptide bond cleavage specificity using proteome based peptide libraries and mass spectrometry
    • Paes Leme, A. F.; Escalante, T.; Pereira, J. G.; Oliveira, A. K.; Sanchez, E. F.; Gutierrez, J. M.; Serrano, S. M.; Fox, J. W. High resolution analysis of snake venom metalloproteinase (SVMP) peptide bond cleavage specificity using proteome based peptide libraries and mass spectrometry J. Proteomics 2011, 74, 401-10
    • (2011) J. Proteomics , vol.74 , pp. 401-410
    • Paes Leme, A.F.1    Escalante, T.2    Pereira, J.G.3    Oliveira, A.K.4    Sanchez, E.F.5    Gutierrez, J.M.6    Serrano, S.M.7    Fox, J.W.8
  • 36
    • 43849099076 scopus 로고    scopus 로고
    • Relative protein quantification by isobaric SILAC with immonium ion splitting (ISIS)
    • Colzani, M.; Schutz, F.; Potts, A.; Waridel, P.; Quadroni, M. Relative protein quantification by isobaric SILAC with immonium ion splitting (ISIS) Mol. Cell. Proteomics 2008, 7, 927-37
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 927-937
    • Colzani, M.1    Schutz, F.2    Potts, A.3    Waridel, P.4    Quadroni, M.5
  • 37
    • 82755163975 scopus 로고    scopus 로고
    • Comparison of three quantitative phosphoproteomic strategies to study receptor tyrosine kinase signaling
    • Zhang, G.; Neubert, T. A. Comparison of three quantitative phosphoproteomic strategies to study receptor tyrosine kinase signaling J. Proteome Res. 2011, 10, 5454-62
    • (2011) J. Proteome Res. , vol.10 , pp. 5454-5462
    • Zhang, G.1    Neubert, T.A.2
  • 39
    • 34147105872 scopus 로고    scopus 로고
    • ADAMs in cancer cell proliferation and progression
    • Mochizuki, S.; Okada, Y. ADAMs in cancer cell proliferation and progression Cancer Sci. 2007, 98, 621-8
    • (2007) Cancer Sci. , vol.98 , pp. 621-628
    • Mochizuki, S.1    Okada, Y.2
  • 40
    • 0036302814 scopus 로고    scopus 로고
    • Protease degradomics: A new challenge for proteomics
    • Lopez-Otin, C.; Overall, C. M. Protease degradomics: a new challenge for proteomics Nat. Rev. Mol. Cell Biol. 2002, 3, 509-19
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 509-519
    • Lopez-Otin, C.1    Overall, C.M.2
  • 41
  • 43
    • 53549102755 scopus 로고    scopus 로고
    • The tumor microenvironment and its role in promoting tumor growth
    • Whiteside, T. L. The tumor microenvironment and its role in promoting tumor growth Oncogene 2008, 27, 5904-12
    • (2008) Oncogene , vol.27 , pp. 5904-5912
    • Whiteside, T.L.1
  • 44
    • 84872685152 scopus 로고    scopus 로고
    • Differential secretome analysis of cancer-associated fibroblasts and bone marrow-derived precursors to identify microenvironmental regulators of colon cancer progression
    • De Boeck, A.; Hendrix, A.; Maynard, D.; Van Bockstal, M.; Daniels, A.; Pauwels, P.; Gespach, C.; Bracke, M.; De Wever, O. Differential secretome analysis of cancer-associated fibroblasts and bone marrow-derived precursors to identify microenvironmental regulators of colon cancer progression Proteomics 2013, 13, 379-88
    • (2013) Proteomics , vol.13 , pp. 379-388
    • De Boeck, A.1    Hendrix, A.2    Maynard, D.3    Van Bockstal, M.4    Daniels, A.5    Pauwels, P.6    Gespach, C.7    Bracke, M.8    De Wever, O.9
  • 45
    • 45549103524 scopus 로고    scopus 로고
    • Breast tumor microenvironment: Proteomics highlights the treatments targeting secretome
    • Chen, S. T.; Pan, T. L.; Juan, H. F.; Chen, T. Y.; Lin, Y. S.; Huang, C. M. Breast tumor microenvironment: proteomics highlights the treatments targeting secretome J. Proteome Res. 2008, 7, 1379-87
    • (2008) J. Proteome Res. , vol.7 , pp. 1379-1387
    • Chen, S.T.1    Pan, T.L.2    Juan, H.F.3    Chen, T.Y.4    Lin, Y.S.5    Huang, C.M.6
  • 46
    • 77950931419 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Regulators of the tumor microenvironment
    • Kessenbrock, K.; Plaks, V.; Werb, Z. Matrix metalloproteinases: regulators of the tumor microenvironment Cell 2010, 141, 52-67
    • (2010) Cell , vol.141 , pp. 52-67
    • Kessenbrock, K.1    Plaks, V.2    Werb, Z.3
  • 47
    • 20144368873 scopus 로고    scopus 로고
    • Gene expression profiling reveals cross-talk between melanoma and fibroblasts: Implications for host-tumor interactions in metastasis
    • Gallagher, P. G.; Bao, Y.; Prorock, A.; Zigrino, P.; Nischt, R.; Politi, V.; Mauch, C.; Dragulev, B.; Fox, J. W. Gene expression profiling reveals cross-talk between melanoma and fibroblasts: implications for host-tumor interactions in metastasis Cancer Res. 2005, 65, 4134-46
    • (2005) Cancer Res. , vol.65 , pp. 4134-4146
    • Gallagher, P.G.1    Bao, Y.2    Prorock, A.3    Zigrino, P.4    Nischt, R.5    Politi, V.6    Mauch, C.7    Dragulev, B.8    Fox, J.W.9
  • 49
    • 67649095267 scopus 로고    scopus 로고
    • ADAM17 promotes breast cancer cell malignant phenotype through EGFR-PI3K-AKT activation
    • Zheng, X.; Jiang, F.; Katakowski, M.; Zhang, Z. G.; Lu, Q. E.; Chopp, M. ADAM17 promotes breast cancer cell malignant phenotype through EGFR-PI3K-AKT activation Cancer Biol. Ther. 2009, 8, 1045-54
    • (2009) Cancer Biol. Ther. , vol.8 , pp. 1045-1054
    • Zheng, X.1    Jiang, F.2    Katakowski, M.3    Zhang, Z.G.4    Lu, Q.E.5    Chopp, M.6
  • 52
    • 66149126456 scopus 로고    scopus 로고
    • Shedding light on proteolytic cleavage of CD44: The responsible sheddase and functional significance of shedding
    • Stamenkovic, I.; Yu, Q. Shedding light on proteolytic cleavage of CD44: the responsible sheddase and functional significance of shedding J. Invest. Dermatol. 2009, 129, 1321-4
    • (2009) J. Invest. Dermatol. , vol.129 , pp. 1321-1324
    • Stamenkovic, I.1    Yu, Q.2
  • 53
    • 79952480540 scopus 로고    scopus 로고
    • Migration of growth factor-stimulated epithelial and endothelial cells depends on EGFR transactivation by ADAM17
    • Maretzky, T.; Evers, A.; Zhou, W.; Swendeman, S. L.; Wong, P. M.; Rafii, S.; Reiss, K.; Blobel, C. P. Migration of growth factor-stimulated epithelial and endothelial cells depends on EGFR transactivation by ADAM17 Nat. Commun. 2011, 2, 229
    • (2011) Nat. Commun. , vol.2 , pp. 229
    • Maretzky, T.1    Evers, A.2    Zhou, W.3    Swendeman, S.L.4    Wong, P.M.5    Rafii, S.6    Reiss, K.7    Blobel, C.P.8
  • 54
    • 76849107016 scopus 로고    scopus 로고
    • Direct activation of TACE-mediated ectodomain shedding by p38 MAP kinase regulates EGF receptor-dependent cell proliferation
    • Xu, P.; Derynck, R. Direct activation of TACE-mediated ectodomain shedding by p38 MAP kinase regulates EGF receptor-dependent cell proliferation Mol. Cell 2010, 37, 551-66
    • (2010) Mol. Cell , vol.37 , pp. 551-566
    • Xu, P.1    Derynck, R.2
  • 57
    • 70349254243 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha-converting enzyme is a key regulator of agonist-induced cardiac hypertrophy and fibrosis
    • Wang, X.; Oka, T.; Chow, F. L.; Cooper, S. B.; Odenbach, J.; Lopaschuk, G. D.; Kassiri, Z.; Fernandez-Patron, C. Tumor necrosis factor-alpha-converting enzyme is a key regulator of agonist-induced cardiac hypertrophy and fibrosis Hypertension 2009, 54, 575-82
    • (2009) Hypertension , vol.54 , pp. 575-582
    • Wang, X.1    Oka, T.2    Chow, F.L.3    Cooper, S.B.4    Odenbach, J.5    Lopaschuk, G.D.6    Kassiri, Z.7    Fernandez-Patron, C.8
  • 59
    • 84860289206 scopus 로고    scopus 로고
    • ADAM17 targets MMP-2 and MMP-9 via EGFR-MEK-ERK pathway activation to promote prostate cancer cell invasion
    • Xiao, L. J.; Lin, P.; Lin, F.; Liu, X.; Qin, W.; Zou, H. F.; Guo, L.; Liu, W.; Wang, S. J.; Yu, X. G. ADAM17 targets MMP-2 and MMP-9 via EGFR-MEK-ERK pathway activation to promote prostate cancer cell invasion Int. J. Oncol. 2012, 40, 1714-24
    • (2012) Int. J. Oncol. , vol.40 , pp. 1714-1724
    • Xiao, L.J.1    Lin, P.2    Lin, F.3    Liu, X.4    Qin, W.5    Zou, H.F.6    Guo, L.7    Liu, W.8    Wang, S.J.9    Yu, X.G.10
  • 60
    • 2442678866 scopus 로고    scopus 로고
    • Differential effects of peroxisome proliferator activated receptor-gamma (PPAR gamma) ligands in proximal tubular cells: Thiazolidinediones are partial PPAR gamma agonists
    • Chana, R. S.; Lewington, A. J.; Brunskill, N. J. Differential effects of peroxisome proliferator activated receptor-gamma (PPAR gamma) ligands in proximal tubular cells: thiazolidinediones are partial PPAR gamma agonists Kidney Int. 2004, 65, 2081-90
    • (2004) Kidney Int. , vol.65 , pp. 2081-2090
    • Chana, R.S.1    Lewington, A.J.2    Brunskill, N.J.3
  • 61
    • 33747682898 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor gamma promotes epithelial to mesenchymal transformation by Rho GTPase-dependent activation of ERK1/2
    • Chen, L.; Necela, B. M.; Su, W.; Yanagisawa, M.; Anastasiadis, P. Z.; Fields, A. P.; Thompson, E. A. Peroxisome proliferator-activated receptor gamma promotes epithelial to mesenchymal transformation by Rho GTPase-dependent activation of ERK1/2 J. Biol. Chem. 2006, 281, 24575-87
    • (2006) J. Biol. Chem. , vol.281 , pp. 24575-24587
    • Chen, L.1    Necela, B.M.2    Su, W.3    Yanagisawa, M.4    Anastasiadis, P.Z.5    Fields, A.P.6    Thompson, E.A.7
  • 63
    • 0030986608 scopus 로고    scopus 로고
    • The family of the small leucine-rich proteoglycans: Key regulators of matrix assembly and cellular growth
    • Iozzo, R. V. The family of the small leucine-rich proteoglycans: key regulators of matrix assembly and cellular growth Crit. Rev. Biochem. Mol. Biol. 1997, 32, 141-74
    • (1997) Crit. Rev. Biochem. Mol. Biol. , vol.32 , pp. 141-174
    • Iozzo, R.V.1
  • 64
    • 79959237627 scopus 로고    scopus 로고
    • Mimecan is involved in aortic hypertrophy induced by sinoaortic denervation in rats
    • Gu, X. S.; Lei, J. P.; Shi, J. B.; Lian, W. L.; Yang, X.; Zheng, X.; Qin, Y. W. Mimecan is involved in aortic hypertrophy induced by sinoaortic denervation in rats Mol. Cell. Biochem. 2011, 352, 309-16
    • (2011) Mol. Cell. Biochem. , vol.352 , pp. 309-316
    • Gu, X.S.1    Lei, J.P.2    Shi, J.B.3    Lian, W.L.4    Yang, X.5    Zheng, X.6    Qin, Y.W.7
  • 66
    • 67649367545 scopus 로고    scopus 로고
    • Perlecan regulates developmental angiogenesis by modulating the VEGF-VEGFR2 axis
    • Zoeller, J. J.; Whitelock, J. M.; Iozzo, R. V. Perlecan regulates developmental angiogenesis by modulating the VEGF-VEGFR2 axis Matrix Biol. 2009, 28, 284-91
    • (2009) Matrix Biol. , vol.28 , pp. 284-291
    • Zoeller, J.J.1    Whitelock, J.M.2    Iozzo, R.V.3
  • 70
    • 80053617871 scopus 로고    scopus 로고
    • Levels of circulating MMCN-151, a degradation product of mimecan, reflect pathological extracellular matrix remodeling in apolipoprotein e knockout mice
    • Barascuk, N.; Vassiliadis, E.; Zheng, Q.; Wang, Y.; Wang, W.; Larsen, L.; Rasmussen, L. M.; Karsdal, M. A. Levels of circulating MMCN-151, a degradation product of mimecan, reflect pathological extracellular matrix remodeling in apolipoprotein E knockout mice Biomarker Insights 2011, 6, 97-106
    • (2011) Biomarker Insights , vol.6 , pp. 97-106
    • Barascuk, N.1    Vassiliadis, E.2    Zheng, Q.3    Wang, Y.4    Wang, W.5    Larsen, L.6    Rasmussen, L.M.7    Karsdal, M.A.8
  • 71
    • 0029876376 scopus 로고    scopus 로고
    • The degradation of human endothelial cell-derived perlecan and release of bound basic fibroblast growth factor by stromelysin, collagenase, plasmin, and heparanases
    • Whitelock, J. M.; Murdoch, A. D.; Iozzo, R. V.; Underwood, P. A. The degradation of human endothelial cell-derived perlecan and release of bound basic fibroblast growth factor by stromelysin, collagenase, plasmin, and heparanases J. Biol. Chem. 1996, 271, 10079-86
    • (1996) J. Biol. Chem. , vol.271 , pp. 10079-10086
    • Whitelock, J.M.1    Murdoch, A.D.2    Iozzo, R.V.3    Underwood, P.A.4
  • 72
    • 70350668613 scopus 로고    scopus 로고
    • Active-site determinants of substrate recognition by the metalloproteinases TACE and ADAM10
    • Caescu, C. I.; Jeschke, G. R.; Turk, B. E. Active-site determinants of substrate recognition by the metalloproteinases TACE and ADAM10 Biochem. J. 2009, 424, 79-88
    • (2009) Biochem. J. , vol.424 , pp. 79-88
    • Caescu, C.I.1    Jeschke, G.R.2    Turk, B.E.3
  • 75
    • 33745086859 scopus 로고    scopus 로고
    • Proteolytic cleavage of the neural cell adhesion molecule by ADAM17/TACE is involved in neurite outgrowth
    • Kalus, I.; Bormann, U.; Mzoughi, M.; Schachner, M.; Kleene, R. Proteolytic cleavage of the neural cell adhesion molecule by ADAM17/TACE is involved in neurite outgrowth J. Neurochem. 2006, 98, 78-88
    • (2006) J. Neurochem. , vol.98 , pp. 78-88
    • Kalus, I.1    Bormann, U.2    Mzoughi, M.3    Schachner, M.4    Kleene, R.5
  • 76
    • 33744813041 scopus 로고    scopus 로고
    • EGFR signaling leads to downregulation of PTP-LAR via TACE-mediated proteolytic processing
    • Ruhe, J. E.; Streit, S.; Hart, S.; Ullrich, A. EGFR signaling leads to downregulation of PTP-LAR via TACE-mediated proteolytic processing Cell. Signalling 2006, 18, 1515-27
    • (2006) Cell. Signalling , vol.18 , pp. 1515-1527
    • Ruhe, J.E.1    Streit, S.2    Hart, S.3    Ullrich, A.4
  • 77
    • 0035253355 scopus 로고    scopus 로고
    • TNF-alpha-converting enzyme cleaves the macrophage colony-stimulating factor receptor in macrophages undergoing activation
    • Rovida, E.; Paccagnini, A.; Del Rosso, M.; Peschon, J.; Dello Sbarba, P. TNF-alpha-converting enzyme cleaves the macrophage colony-stimulating factor receptor in macrophages undergoing activation J. Immunol. 2001, 166, 1583-9
    • (2001) J. Immunol. , vol.166 , pp. 1583-1589
    • Rovida, E.1    Paccagnini, A.2    Del Rosso, M.3    Peschon, J.4    Dello Sbarba, P.5
  • 80
    • 0141509970 scopus 로고    scopus 로고
    • Stimulated shedding of vascular cell adhesion molecule 1 (VCAM-1) is mediated by tumor necrosis factor-alpha-converting enzyme (ADAM 17)
    • Garton, K. J.; Gough, P. J.; Philalay, J.; Wille, P. T.; Blobel, C. P.; Whitehead, R. H.; Dempsey, P. J.; Raines, E. W. Stimulated shedding of vascular cell adhesion molecule 1 (VCAM-1) is mediated by tumor necrosis factor-alpha-converting enzyme (ADAM 17) J. Biol. Chem. 2003, 278, 37459-64
    • (2003) J. Biol. Chem. , vol.278 , pp. 37459-37464
    • Garton, K.J.1    Gough, P.J.2    Philalay, J.3    Wille, P.T.4    Blobel, C.P.5    Whitehead, R.H.6    Dempsey, P.J.7    Raines, E.W.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.