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Volumn 420, Issue 1, 2009, Pages 105-113

Characterization of the catalytic activity of the membrane-anchored metalloproteinase ADAM15 in cell-based assays

Author keywords

ADAM (a disintegrin and metalloproteinase); ADAM15; Ectodomain shedding; Fibroblast growth factor receptor 2 (FGFR2)

Indexed keywords

ADAM (A DISINTEGRIN AND METALLOPROTEINASE); ADAM15; CALCIUM IONOPHORE; CATALYTIC ACTIVITY; CATALYTIC PROPERTIES; CELL-BASED ASSAYS; ECTODOMAIN SHEDDING; EXTRACELLULAR DOMAINS; FIBROBLAST GROWTH FACTOR RECEPTOR 2; FIBROBLAST GROWTH FACTOR RECEPTOR 2 (FGFR2); HUMAN CANCER; HYDROXAMATE; IN-CELL; INTACT CELLS; MEMBRANE PROTEINS; METALLOPROTEINASE; METALLOPROTEINASES; NEOVASCULARIZATION; OVER-EXPRESSION; PEPTIDE SUBSTRATES; PHORBOL ESTERS; PROSTATE CANCERS; TISSUE INHIBITOR;

EID: 65649119654     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20082127     Document Type: Article
Times cited : (47)

References (51)
  • 1
    • 11244261160 scopus 로고    scopus 로고
    • ADAMs: Key players in EGFR-signaling, development and disease
    • Blobel, C. P. (2005) ADAMs: key players in EGFR-signaling, development and disease. Nat. Rev. Mol. Cell Biol. 6, 32-43
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 32-43
    • Blobel, C.P.1
  • 2
    • 0032741143 scopus 로고    scopus 로고
    • Metalloprotease-disintegrins: Modular proteins capable of promoting cell-cell interactions and triggering signals by protein ectodomain shedding
    • Schlöndorff, J. and Blobel, C. P. (1999) Metalloprotease-disintegrins: modular proteins capable of promoting cell-cell interactions and triggering signals by protein ectodomain shedding. J. Cell. Sci. 112, 3603-3617
    • (1999) J. Cell. Sci , vol.112 , pp. 3603-3617
    • Schlöndorff, J.1    Blobel, C.P.2
  • 3
    • 0037224740 scopus 로고    scopus 로고
    • The ADAMs family of metalloproteases: Multidomain proteins with multiple functions
    • Seals, D. F. and Courtneidge, S. A. (2003) The ADAMs family of metalloproteases: multidomain proteins with multiple functions. Genes Dev. 17, 7-30
    • (2003) Genes Dev , vol.17 , pp. 7-30
    • Seals, D.F.1    Courtneidge, S.A.2
  • 5
    • 17244371476 scopus 로고    scopus 로고
    • Homeostatic effects of the metalloproteinase disintegrin ADAM15 in degenerative cartilage remodelling
    • Bohm, B., Aigner, T., Roy, B., Brodie, T. A., Blobel, C. and Burkhardt, H. (2005) Homeostatic effects of the metalloproteinase disintegrin ADAM15 in degenerative cartilage remodelling. Arthritis Rheum. 52, 1100-1109
    • (2005) Arthritis Rheum , vol.52 , pp. 1100-1109
    • Bohm, B.1    Aigner, T.2    Roy, B.3    Brodie, T.A.4    Blobel, C.5    Burkhardt, H.6
  • 6
    • 0035462010 scopus 로고    scopus 로고
    • Highly enhanced expression of the disintegrin metalloproteinase MDC15 (metargidin) in rheumatoid synovial tissue
    • Bohm, B. B., Aigner, T., Blobel, C. P., Kalden, J. R. and Burkhardt, H. (2001) Highly enhanced expression of the disintegrin metalloproteinase MDC15 (metargidin) in rheumatoid synovial tissue. Arthritis Rheum. 44, 2046-2054
    • (2001) Arthritis Rheum , vol.44 , pp. 2046-2054
    • Bohm, B.B.1    Aigner, T.2    Blobel, C.P.3    Kalden, J.R.4    Burkhardt, H.5
  • 7
    • 0343618582 scopus 로고    scopus 로고
    • Up-regulation of MDC15 (metargidin) messenger RNA in human osteoarthritic cartilage
    • Bohm, B. B., Aigner, T., Gehrsitz, A., Blobel, C. P., Kalden, J. R. and Burkhardt, H. (1999) Up-regulation of MDC15 (metargidin) messenger RNA in human osteoarthritic cartilage. Arthritis Rheum. 42, 1946-1950
    • (1999) Arthritis Rheum , vol.42 , pp. 1946-1950
    • Bohm, B.B.1    Aigner, T.2    Gehrsitz, A.3    Blobel, C.P.4    Kalden, J.R.5    Burkhardt, H.6
  • 9
    • 0029670028 scopus 로고    scopus 로고
    • Metargidin, a membrane-anchored metalloprotease-disintegrin protein with an RGD integrin binding sequence
    • Krätzschmar, J., Lum, L. and Blobel, C. P. (1996) Metargidin, a membrane-anchored metalloprotease-disintegrin protein with an RGD integrin binding sequence. J. Biol. Chem. 271, 4593-4596
    • (1996) J. Biol. Chem , vol.271 , pp. 4593-4596
    • Krätzschmar, J.1    Lum, L.2    Blobel, C.P.3
  • 10
    • 0033532191 scopus 로고    scopus 로고
    • Evidence for a role of a tumor necrosis factor-α (TNF-α)-converting enzyme-like protease in shedding of TRANCE, a TNF family member involved in osteoclastogenesis and dendritic cell survival
    • Lum, L., Wong, B. R., Josien, R., Becherer, J. D., Erdjument-Bromage, H., Schlondorff, J., Tempst, P., Choi, Y. and Blobel, C. P. (1999) Evidence for a role of a tumor necrosis factor-α (TNF-α)-converting enzyme-like protease in shedding of TRANCE, a TNF family member involved in osteoclastogenesis and dendritic cell survival. J. Biol. Chem. 274, 13613-13618
    • (1999) J. Biol. Chem , vol.274 , pp. 13613-13618
    • Lum, L.1    Wong, B.R.2    Josien, R.3    Becherer, J.D.4    Erdjument-Bromage, H.5    Schlondorff, J.6    Tempst, P.7    Choi, Y.8    Blobel, C.P.9
  • 12
    • 0037564023 scopus 로고    scopus 로고
    • Malignancy-associated regions of transcriptional activation: Gene expression profiling identifies common chromosomal regions of a recurrent transcriptional activation in human prostate, breast, ovarian, and colon cancers
    • Glinsky, G. V., Krones-Herzig, A. and Glinskii, A. B. (2003) Malignancy-associated regions of transcriptional activation: gene expression profiling identifies common chromosomal regions of a recurrent transcriptional activation in human prostate, breast, ovarian, and colon cancers. Neoplasia 5, 218-228
    • (2003) Neoplasia , vol.5 , pp. 218-228
    • Glinsky, G.V.1    Krones-Herzig, A.2    Glinskii, A.B.3
  • 13
    • 0036145144 scopus 로고    scopus 로고
    • Chromosomal imbalances of primary and metastatic lung adenocarcinomas
    • Goeze, A., Schluns, K., Wolf, G., Thasler, Z., Petersen, S. and Petersen, I. (2002) Chromosomal imbalances of primary and metastatic lung adenocarcinomas. J. Pathol. 196, 8-16
    • (2002) J. Pathol , vol.196 , pp. 8-16
    • Goeze, A.1    Schluns, K.2    Wolf, G.3    Thasler, Z.4    Petersen, S.5    Petersen, I.6
  • 14
    • 0036791587 scopus 로고    scopus 로고
    • Chromosomal aberrations related to metastasis of human solid tumors
    • Qin, L. X. (2002) Chromosomal aberrations related to metastasis of human solid tumors. World J. Gastroenterol. 8, 769-776
    • (2002) World J. Gastroenterol , vol.8 , pp. 769-776
    • Qin, L.X.1
  • 17
    • 39449130768 scopus 로고    scopus 로고
    • ADAM15 supports prostate cancer metastasis by modulating tumor cell-endothelial cell interaction
    • Najy, A. J., Day, K. C. and Day, M. L. (2008) ADAM15 supports prostate cancer metastasis by modulating tumor cell-endothelial cell interaction. Cancer Res. 68, 1092-1099
    • (2008) Cancer Res , vol.68 , pp. 1092-1099
    • Najy, A.J.1    Day, K.C.2    Day, M.L.3
  • 19
    • 49649103585 scopus 로고    scopus 로고
    • The ectodomain shedding of E-cadherin by ADAM15 supports ErbB receptor activation
    • Najy, A. J., Day, K. C. and Day, M. L. (2008) The ectodomain shedding of E-cadherin by ADAM15 supports ErbB receptor activation. J. Biol. Chem. 283, 18393-18401
    • (2008) J. Biol. Chem , vol.283 , pp. 18393-18401
    • Najy, A.J.1    Day, K.C.2    Day, M.L.3
  • 22
    • 22144454605 scopus 로고    scopus 로고
    • Evaluation of the contributions of ADAMs 9, 12, 15, 17, and 19 to heart development and ectodomain shedding of neuregulins β1 and β2
    • Horiuchi, K., Zhou, H. M., Kelly, K., Manova, K. and Blobel, C. P. (2005) Evaluation of the contributions of ADAMs 9, 12, 15, 17, and 19 to heart development and ectodomain shedding of neuregulins β1 and β2. Dev. Biol. 283, 459-471
    • (2005) Dev. Biol , vol.283 , pp. 459-471
    • Horiuchi, K.1    Zhou, H.M.2    Kelly, K.3    Manova, K.4    Blobel, C.P.5
  • 24
    • 1042278167 scopus 로고    scopus 로고
    • Evidence for a critical role of the TNFα convertase (TACE) in ectodomain shedding of the p75 neurotrophin receptor (p75NTR)
    • Weskamp, G., Schlöndorff, J., Lum, L., Saftig, P., Hartmann, D., Becherer, D., Murphy, G. and Blobel, C. P. (2004) Evidence for a critical role of the TNFα convertase (TACE) in ectodomain shedding of the p75 neurotrophin receptor (p75NTR). J. Biol. Chem. 279, 4241-4249
    • (2004) J. Biol. Chem , vol.279 , pp. 4241-4249
    • Weskamp, G.1    Schlöndorff, J.2    Lum, L.3    Saftig, P.4    Hartmann, D.5    Becherer, D.6    Murphy, G.7    Blobel, C.P.8
  • 25
    • 5644290647 scopus 로고    scopus 로고
    • Evaluation of the contribution of different ADAMs to TNFα shedding and of the function of the TNFα ectodomain in ensuring selective stimulated shedding by the TNFα convertase (TACE/ADAM17)
    • Zheng, Y., Saftig, P., Hartmann, D. and Blobel, C. (2004) Evaluation of the contribution of different ADAMs to TNFα shedding and of the function of the TNFα ectodomain in ensuring selective stimulated shedding by the TNFα convertase (TACE/ADAM17). J. Biol. Chem. 279, 42898-42906
    • (2004) J. Biol. Chem , vol.279 , pp. 42898-42906
    • Zheng, Y.1    Saftig, P.2    Hartmann, D.3    Blobel, C.4
  • 26
    • 26444448409 scopus 로고    scopus 로고
    • L1 is sequentially processed by two differently activated metalloproteases and presenilin/γ-secretase and regulates neural cell adhesion, cell migration, and neurite outgrowth
    • Maretzky, T., Schulte, M., Ludwig, A., Rose-John, S., Blobel, C., Hartmann, D., Altevogt, P., Saftig, P. and Reiss, K. (2005) L1 is sequentially processed by two differently activated metalloproteases and presenilin/γ-secretase and regulates neural cell adhesion, cell migration, and neurite outgrowth. Mol. Cell. Biol. 25, 9040-9053
    • (2005) Mol. Cell. Biol , vol.25 , pp. 9040-9053
    • Maretzky, T.1    Schulte, M.2    Ludwig, A.3    Rose-John, S.4    Blobel, C.5    Hartmann, D.6    Altevogt, P.7    Saftig, P.8    Reiss, K.9
  • 28
    • 33847276695 scopus 로고    scopus 로고
    • In search of partners: Linking extracellular proteases to substrates
    • Overall, C. M. and Blobel, C. P. (2007) In search of partners: linking extracellular proteases to substrates. Nat. Rev. Mol. Cell Biol. 8, 245-257
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 245-257
    • Overall, C.M.1    Blobel, C.P.2
  • 29
    • 2442659417 scopus 로고    scopus 로고
    • Synthesis of marimastat and a marimastat conjugate for affinity chromatography and surface plasmon resonance studies
    • Jenssen, K., Sewald, K. and Sewald, N. (2004) Synthesis of marimastat and a marimastat conjugate for affinity chromatography and surface plasmon resonance studies. Bioconjug. Chem. 15, 594-600
    • (2004) Bioconjug. Chem , vol.15 , pp. 594-600
    • Jenssen, K.1    Sewald, K.2    Sewald, N.3
  • 30
    • 0034619158 scopus 로고    scopus 로고
    • An improved synthesis of the broad spectrum matrix metalloprotease inhibitor marimastat
    • Davenport, R. and Watson, R. (2000) An improved synthesis of the broad spectrum matrix metalloprotease inhibitor marimastat. Tetrahedron Lett. 41, 7983-7986
    • (2000) Tetrahedron Lett , vol.41 , pp. 7983-7986
    • Davenport, R.1    Watson, R.2
  • 31
    • 0032475960 scopus 로고    scopus 로고
    • Intracellular maturation of the mouse metalloprotease disintegrin MDC15
    • Lum, L., Reid, M. S. and Blobel, C. P. (1998) Intracellular maturation of the mouse metalloprotease disintegrin MDC15. J. Biol. Chem. 273, 26236-26247
    • (1998) J. Biol. Chem , vol.273 , pp. 26236-26247
    • Lum, L.1    Reid, M.S.2    Blobel, C.P.3
  • 32
    • 0037044786 scopus 로고    scopus 로고
    • Evidence for regulation of the tumor necrosis factor α-convertase (TACE) by protein-tyrosine phosphatase PTPH1
    • Zheng, Y., Schlondorff, J. and Blobel, C. P. (2002) Evidence for regulation of the tumor necrosis factor α-convertase (TACE) by protein-tyrosine phosphatase PTPH1. J. Biol. Chem. 277, 42463-42470
    • (2002) J. Biol. Chem , vol.277 , pp. 42463-42470
    • Zheng, Y.1    Schlondorff, J.2    Blobel, C.P.3
  • 33
    • 34247363315 scopus 로고    scopus 로고
    • Different ADAMs have distinct influences on Kit ligand processing: Phorbol-ester-stimulated ectodomain shedding of Kitl1 by ADAM17 is reduced by ADAM19
    • Kawaguchi, N., Horiuchi, K., Becherer, J. D., Toyama, Y., Besmer, P. and Blobel, C. P. (2007) Different ADAMs have distinct influences on Kit ligand processing: phorbol-ester-stimulated ectodomain shedding of Kitl1 by ADAM17 is reduced by ADAM19. J. Cell Sci. 120, 943-952
    • (2007) J. Cell Sci , vol.120 , pp. 943-952
    • Kawaguchi, N.1    Horiuchi, K.2    Becherer, J.D.3    Toyama, Y.4    Besmer, P.5    Blobel, C.P.6
  • 34
    • 33746013495 scopus 로고    scopus 로고
    • A sensitive method to monitor ectodomain shedding of ligands of the epidermal growth factor receptor
    • T. B. Patel, P. J. Bertics, ed, pp, Humana Press Inc, Totowa, NJ
    • Sahin, U., Weskamp, G., Zheng, Y., Chesneau, V., Horiuchi, K. and Blobel, C. P. (2006) A sensitive method to monitor ectodomain shedding of ligands of the epidermal growth factor receptor. In Epidermal Growth Factor: Methods and Protocols (T. B. Patel, P. J. Bertics, ed.), pp. 99-113, Humana Press Inc., Totowa, NJ
    • (2006) Epidermal Growth Factor: Methods and Protocols , pp. 99-113
    • Sahin, U.1    Weskamp, G.2    Zheng, Y.3    Chesneau, V.4    Horiuchi, K.5    Blobel, C.P.6
  • 37
    • 9844253890 scopus 로고    scopus 로고
    • Identification and characterization of a pro-tumor necrosis factor-α-processing enzyme from the ADAM family of zinc metalloproteases
    • Rosendahl, M. S., Ko, S. C., Long, D. L., Brewer, M. T., Rosenzweig, B., Hedl, E., Anderson, L., Pyle, S. M., Moreland, J., Meyers, M. A. et al. (1997) Identification and characterization of a pro-tumor necrosis factor-α-processing enzyme from the ADAM family of zinc metalloproteases. J. Biol. Chem. 272, 24588-24593
    • (1997) J. Biol. Chem , vol.272 , pp. 24588-24593
    • Rosendahl, M.S.1    Ko, S.C.2    Long, D.L.3    Brewer, M.T.4    Rosenzweig, B.5    Hedl, E.6    Anderson, L.7    Pyle, S.M.8    Moreland, J.9    Meyers, M.A.10
  • 43
    • 0034657228 scopus 로고    scopus 로고
    • Cloning and characterization of ADAM28: Evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28
    • Howard, L., Maciewicz, R. A. and Blobel, C. P. (2000) Cloning and characterization of ADAM28: evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28. Biochem. J. 348, 21-27
    • (2000) Biochem. J , vol.348 , pp. 21-27
    • Howard, L.1    Maciewicz, R.A.2    Blobel, C.P.3
  • 45
    • 0034615550 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases: Evolution, structure and function
    • Brew, K., Dinakarpandian, D. and Nagase, H. (2000) Tissue inhibitors of metalloproteinases: evolution, structure and function. Biochim. Biophys. Acta 1477, 267-283
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 267-283
    • Brew, K.1    Dinakarpandian, D.2    Nagase, H.3
  • 48
    • 65249090883 scopus 로고    scopus 로고
    • ADAMs 10 and 17 represent differentially regulated components of a general shedding machinery for membrane proteins such as transforming growth factor α, L-selectin and tumor necrosis factor α
    • Le Gall, S., Bobe, P., Reiss, K., Horiuchi, K., Niu, X.-D., Lundell, D., Gibb, D., Conrad, D., Saftig, P. and Blobel, C. (2009) ADAMs 10 and 17 represent differentially regulated components of a general shedding machinery for membrane proteins such as transforming growth factor α, L-selectin and tumor necrosis factor α. Mol. Biol. Cell. 20, 1785-1794
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1785-1794
    • Le Gall, S.1    Bobe, P.2    Reiss, K.3    Horiuchi, K.4    Niu, X.-D.5    Lundell, D.6    Gibb, D.7    Conrad, D.8    Saftig, P.9    Blobel, C.10
  • 50
    • 33845729910 scopus 로고    scopus 로고
    • Ectodomain shedding of the EGF-receptor ligand epigen is mediated by ADAM17
    • Sahin, U. and Blobel, C. P. (2007) Ectodomain shedding of the EGF-receptor ligand epigen is mediated by ADAM17. FEBS Lett. 581, 41-44
    • (2007) FEBS Lett , vol.581 , pp. 41-44
    • Sahin, U.1    Blobel, C.P.2
  • 51
    • 0029057781 scopus 로고
    • Membrane-associated metalloproteinase recognized by characteristic cleavage of myelin basic protein: Assay and isolation
    • Barrett, A. J, ed, pp, Academic Press, San Diego, CA
    • Howard, L. and Glynn, P. (1995) Membrane-associated metalloproteinase recognized by characteristic cleavage of myelin basic protein: assay and isolation. In Proteolytic Enzymes: Aspartic and Metalloproteases (Barrett, A. J., ed.), pp. 388-395, Academic Press, San Diego, CA
    • (1995) Proteolytic Enzymes: Aspartic and Metalloproteases , pp. 388-395
    • Howard, L.1    Glynn, P.2


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