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Volumn 35, Issue 1, 2004, Pages 34-46

ADAM gene expression and regulation during human osteoclast formation

Author keywords

ADAM; Bone; Gene regulation; Human; Metalloprotease; Osteoclast fusion

Indexed keywords

ADAM 10 PROTEIN; ADAM 15 PROTEIN; ADAM 28 PROTEIN; ADAM 8 PROTEIN; ADAM 9 PROTEIN; ADAM PROTEIN; COLONY STIMULATING FACTOR; DISINTEGRIN; F ACTIN; METALLOPROTEINASE; OSTEOCLAST DIFFERENTIATION FACTOR; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME; UNCLASSIFIED DRUG;

EID: 2942707947     PISSN: 87563282     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bone.2003.12.029     Document Type: Article
Times cited : (60)

References (50)
  • 1
    • 0027530667 scopus 로고
    • 1,25-Dihydroxyvitamin D3 and phorbol myristate produce divergent phenotypes in a monomyelocytic cell line
    • Biskobing D.M., Rubin J. 1, 25-Dihydroxyvitamin D3 and phorbol myristate produce divergent phenotypes in a monomyelocytic cell line. Endocrinology. 132:1993;862-866
    • (1993) Endocrinology , vol.132 , pp. 862-866
    • Biskobing, D.M.1    Rubin, J.2
  • 2
    • 0029127505 scopus 로고
    • The osteoclast clear zone is a specialized cell-extracellular matrix adhesion structure
    • Väänänen H.K., Horton M.A. The osteoclast clear zone is a specialized cell-extracellular matrix adhesion structure. J. Cell Sci. 108:1995;2729-2732
    • (1995) J. Cell Sci. , vol.108 , pp. 2729-2732
    • Väänänen, H.K.1    Horton, M.A.2
  • 3
    • 0030020733 scopus 로고    scopus 로고
    • Protein machinery of vesicle budding and fusion
    • Rothman J.E. Protein machinery of vesicle budding and fusion. Protein Sci. 5:1996;185-194
    • (1996) Protein Sci. , vol.5 , pp. 185-194
    • Rothman, J.E.1
  • 4
    • 0026492542 scopus 로고
    • Membrane fusion
    • White J.M. Membrane fusion. Science. 258:1992;917-924
    • (1992) Science , vol.258 , pp. 917-924
    • White, J.M.1
  • 5
    • 0028820623 scopus 로고
    • ADAM, a novel family of membrane proteins containing a disintegrin and metalloprotease domain: Multipotential functions in cell-cell and cell-matrix interactions
    • Wolfsberg T.G., Primakoff P., Myles D.G., White J.M. ADAM, a novel family of membrane proteins containing a disintegrin and metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions. J. Cell Biol. 131:1995;275-278
    • (1995) J. Cell Biol. , vol.131 , pp. 275-278
    • Wolfsberg, T.G.1    Primakoff, P.2    Myles, D.G.3    White, J.M.4
  • 7
    • 0030834283 scopus 로고    scopus 로고
    • Metalloprotease-disintegrins: Links to cell adhesion and cleavage of TNFa and Notch
    • Blobel C.P. Metalloprotease-disintegrins: links to cell adhesion and cleavage of TNFa and Notch. Cell. 90:1997;589-592
    • (1997) Cell , vol.90 , pp. 589-592
    • Blobel, C.P.1
  • 8
    • 0026510747 scopus 로고
    • A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion
    • Blobel C.P., Wolfsberg T.G., Turck C.W., Myles D.G., Primakoff P., White J.M. A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature. 356:1992;248
    • (1992) Nature , vol.356 , pp. 248
    • Blobel, C.P.1    Wolfsberg, T.G.2    Turck, C.W.3    Myles, D.G.4    Primakoff, P.5    White, J.M.6
  • 9
    • 0031566190 scopus 로고    scopus 로고
    • Expression of members of a novel membrane linked metalloproteinase family (ADAM) in human articular chondrocytes
    • McKie N., Edwards T., Dallas D.J., Houghton A., Stringer B., Graham R., et al. Expression of members of a novel membrane linked metalloproteinase family (ADAM) in human articular chondrocytes. Biochem. Biophys. Res. Commun. 230:1997;335-339
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 335-339
    • McKie, N.1    Edwards, T.2    Dallas, D.J.3    Houghton, A.4    Stringer, B.5    Graham, R.6
  • 10
    • 0031577162 scopus 로고    scopus 로고
    • Expression of members of the novel membrane linked metalloproteinase family ADAM in cells derived from a range of haematological malignancies
    • Wu E., Croucher P.I., McKie N. Expression of members of the novel membrane linked metalloproteinase family ADAM in cells derived from a range of haematological malignancies. Biochem. Biophys. Res. Commun. 235:1997;437-442
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 437-442
    • Wu, E.1    Croucher, P.I.2    McKie, N.3
  • 11
    • 0035059212 scopus 로고    scopus 로고
    • ADAM 8: A novel osteoclast stimulating factor
    • Choi S.J., Han J., Roodman G.D. ADAM 8: a novel osteoclast stimulating factor. J. Bone Miner. Res. 16:2001;814-822
    • (2001) J. Bone Miner. Res. , vol.16 , pp. 814-822
    • Choi, S.J.1    Han, J.2    Roodman, G.D.3
  • 13
    • 0038374867 scopus 로고    scopus 로고
    • ADAM 12 in human liver cancers: TGF-β-regulated expression in stellate cells is associated with matrix remodelling
    • Le Pabic H., Bonnier D., Wewer U.M., Coutand A., Musso O., Baffet G., et al. ADAM 12 in human liver cancers: TGF-β-regulated expression in stellate cells is associated with matrix remodelling. Hepatology. 37(15):2003;1056-1066
    • (2003) Hepatology , vol.37 , Issue.15 , pp. 1056-1066
    • Le Pabic, H.1    Bonnier, D.2    Wewer, U.M.3    Coutand, A.4    Musso, O.5    Baffet, G.6
  • 14
    • 0031470904 scopus 로고    scopus 로고
    • SUP-17, a Caenorhabditis elegans ADAM protein related to Drosophila KUZBANIAN, and its role in LIN-12/NOTCH signalling
    • Wen C., Metzstein M.M., Greenwald L. SUP-17, a Caenorhabditis elegans ADAM protein related to Drosophila KUZBANIAN, and its role in LIN-12/NOTCH signalling. Development. 124:1997;4759-4767
    • (1997) Development , vol.124 , pp. 4759-4767
    • Wen, C.1    Metzstein, M.M.2    Greenwald, L.3
  • 15
    • 0031568847 scopus 로고    scopus 로고
    • ADAM 13: A novel ADAM expressed in somitic mesoderm and neural crest cells during Xenopus laevis development
    • Alfandari D., Wolfsberg T.G., White J.M., DeSimone D.W. ADAM 13: a novel ADAM expressed in somitic mesoderm and neural crest cells during Xenopus laevis development. Dev. Biol. 182:1997;314-330
    • (1997) Dev. Biol. , vol.182 , pp. 314-330
    • Alfandari, D.1    Wolfsberg, T.G.2    White, J.M.3    Desimone, D.W.4
  • 16
    • 0037080699 scopus 로고    scopus 로고
    • Kuzbanian-mediated cleavage of Drosophila Notch
    • Lieber T., Kidd S., Young M.W. Kuzbanian-mediated cleavage of Drosophila Notch. Genes Dev. 16:2002;209-221
    • (2002) Genes Dev. , vol.16 , pp. 209-221
    • Lieber, T.1    Kidd, S.2    Young, M.W.3
  • 17
    • 8044257704 scopus 로고    scopus 로고
    • A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells
    • Black R.A., Rauch C.T., Kozlosky C.J., Peschon J.J., Slack J.L., Wolfson M.F., et al. A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells. Nature. 385:1997;729-733
    • (1997) Nature , vol.385 , pp. 729-733
    • Black, R.A.1    Rauch, C.T.2    Kozlosky, C.J.3    Peschon, J.J.4    Slack, J.L.5    Wolfson, M.F.6
  • 19
    • 17444373968 scopus 로고    scopus 로고
    • A metalloprotease-disintegrin, MDC9/meltrin-gamma/ADAM9 and PKCdelta are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor
    • Izumi Y., Hirata M., Hasuwa H., Iwamoto R., Umata T., Miyado K., et al. A metalloprotease-disintegrin, MDC9/meltrin-gamma/ADAM9 and PKCdelta are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor. EMBO J. 17:1998;7260-7272
    • (1998) EMBO J. , vol.17 , pp. 7260-7272
    • Izumi, Y.1    Hirata, M.2    Hasuwa, H.3    Iwamoto, R.4    Umata, T.5    Miyado, K.6
  • 21
    • 0026471735 scopus 로고
    • Structure, function and evolutionary relationship of proteins containing a disintegrin domain
    • Blobel C.P., White J.M. Structure, function and evolutionary relationship of proteins containing a disintegrin domain. Curr. Opin. Cell Biol. 4:1992;760-765
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 760-765
    • Blobel, C.P.1    White, J.M.2
  • 22
    • 0030940446 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of bovine fertilin alpha and beta (ADAM 1 and ADAM 2): A candidate sperm-egg binding/fusion complex
    • Waters S.I., White J.M. Biochemical and molecular characterization of bovine fertilin alpha and beta (ADAM 1 and ADAM 2): a candidate sperm-egg binding/fusion complex. Biol. Reprod. 56:1997;1245-1254
    • (1997) Biol. Reprod. , vol.56 , pp. 1245-1254
    • Waters, S.I.1    White, J.M.2
  • 23
    • 0034608081 scopus 로고    scopus 로고
    • Binding of ADAM12, a marker of skeletal muscle regeneration, to the muscle-specific actin-binding protein, alpha-actinin-2, is required for myoblast fusion
    • Galliano M.F., Huet C., Frygelius J., Polgren A., Wewer U.M., Engvall E. Binding of ADAM12, a marker of skeletal muscle regeneration, to the muscle-specific actin-binding protein, alpha-actinin-2, is required for myoblast fusion. J. Biol. Chem. 275:2000;13933-13939
    • (2000) J. Biol. Chem. , vol.275 , pp. 13933-13939
    • Galliano, M.F.1    Huet, C.2    Frygelius, J.3    Polgren, A.4    Wewer, U.M.5    Engvall, E.6
  • 24
    • 0024454316 scopus 로고
    • The osteoclast functional antigen, implicated in the regulation of bone resorption, is biochemically related to the vitronectin receptor
    • Davies J., Warwick J., Totty N., Philp R., Helfrich M., Horton M.A. The osteoclast functional antigen, implicated in the regulation of bone resorption, is biochemically related to the vitronectin receptor. J. Cell Biol. 109:1989;1817-1826
    • (1989) J. Cell Biol. , vol.109 , pp. 1817-1826
    • Davies, J.1    Warwick, J.2    Totty, N.3    Philp, R.4    Helfrich, M.5    Horton, M.A.6
  • 26
    • 0001408581 scopus 로고    scopus 로고
    • Generation of human osteoclasts in stromal cell-free and stromal cell-rich cultures: Differences in osteoclast CD11c/CD18 integrin expression
    • Lader C.S., Scopes J., Horton M.A., Flanagan A.M. Generation of human osteoclasts in stromal cell-free and stromal cell-rich cultures: differences in osteoclast CD11c/CD18 integrin expression. Br. J. Haematol. 111:2000;1210-1217
    • (2000) Br. J. Haematol. , vol.111 , pp. 1210-1217
    • Lader, C.S.1    Scopes, J.2    Horton, M.A.3    Flanagan, A.M.4
  • 27
    • 0028077307 scopus 로고
    • The effect of biphosphonates on the resorption cycle of isolated osteoclasts
    • Selander K., Lehenkari P., Väänänen H.K. The effect of biphosphonates on the resorption cycle of isolated osteoclasts. Calcif. Tissue Int. 55:1994;368-375
    • (1994) Calcif. Tissue Int. , vol.55 , pp. 368-375
    • Selander, K.1    Lehenkari, P.2    Väänänen, H.K.3
  • 29
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:1987;156-159
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 30
    • 0030895688 scopus 로고    scopus 로고
    • Trafficking of matrix collagens through bone-resorbing osteoclasts
    • Nesbitt S.A., Horton M.A. Trafficking of matrix collagens through bone-resorbing osteoclasts. Science. 76:1997;266-269
    • (1997) Science , vol.76 , pp. 266-269
    • Nesbitt, S.A.1    Horton, M.A.2
  • 31
    • 0022338260 scopus 로고
    • Monoclonal antibodies to osteoclastomas (giant cell bone tumours): Definition of osteoclast-specific cellular antigens
    • Horton M.A., Lewis D., McNulty K., Pringle J.A.S., Chambers T.J. Monoclonal antibodies to osteoclastomas (giant cell bone tumours): definition of osteoclast-specific cellular antigens. Cancer Res. 45:1985;5663-5669
    • (1985) Cancer Res. , vol.45 , pp. 5663-5669
    • Horton, M.A.1    Lewis, D.2    McNulty, K.3    Pringle, J.A.S.4    Chambers, T.J.5
  • 32
    • 0036405405 scopus 로고    scopus 로고
    • ADAM15 is an adherens junction molecule whose surface expression can be driven by VE-cadherin
    • Ham C., Levkau B., Raines E.W., Herren B. ADAM15 is an adherens junction molecule whose surface expression can be driven by VE-cadherin. Exp. Cell Res. 279:2002;239-247
    • (2002) Exp. Cell Res. , vol.279 , pp. 239-247
    • Ham, C.1    Levkau, B.2    Raines, E.W.3    Herren, B.4
  • 34
    • 0031059822 scopus 로고    scopus 로고
    • The human fertilin alpha gene is non-functional: Implications for its proposed role in fertilization
    • Jury J.A., Frayne J., Hall L. The human fertilin alpha gene is non-functional: implications for its proposed role in fertilization. Biochem. J. 321:1997;577-581
    • (1997) Biochem. J. , vol.321 , pp. 577-581
    • Jury, J.A.1    Frayne, J.2    Hall, L.3
  • 35
    • 0035521152 scopus 로고    scopus 로고
    • Involment of ADAM 9 in mutinucleated giant cell formation of blood monocytes
    • Namba K., Nishio M., Mori K., Miyamoto N., Tsurudome M., Ito M., et al. Involment of ADAM 9 in mutinucleated giant cell formation of blood monocytes. Cell. Immunol. 213:2001;104-113
    • (2001) Cell. Immunol. , vol.213 , pp. 104-113
    • Namba, K.1    Nishio, M.2    Mori, K.3    Miyamoto, N.4    Tsurudome, M.5    Ito, M.6
  • 36
    • 0032512831 scopus 로고    scopus 로고
    • Cloning and initial characterization of mouse meltrin β and analysis of the expression of four metalloprotease-disintegrin in bone cells
    • Inoue D., Reid M., Lum L., Krätzschmar J., Weskamp G., Myung M.M., et al. Cloning and initial characterization of mouse meltrin β and analysis of the expression of four metalloprotease-disintegrin in bone cells. J. Biol. Chem. 273:1998;4180-4187
    • (1998) J. Biol. Chem. , vol.273 , pp. 4180-4187
    • Inoue, D.1    Reid, M.2    Lum, L.3    Krätzschmar, J.4    Weskamp, G.5    Myung, M.M.6
  • 37
    • 0034674543 scopus 로고    scopus 로고
    • ADAM 12, a disintegrin metalloprotease, interacts with insulin-like growth factor-binding protein-3
    • Shi Z., Xu W., Loeche F., Wewer U.M., Murphy L.J. ADAM 12, a disintegrin metalloprotease, interacts with insulin-like growth factor-binding protein-3. J. Biol. Chem. 275:2000;18574-18580
    • (2000) J. Biol. Chem. , vol.275 , pp. 18574-18580
    • Shi, Z.1    Xu, W.2    Loeche, F.3    Wewer, U.M.4    Murphy, L.J.5
  • 38
    • 0033017290 scopus 로고    scopus 로고
    • Meltrin-α, a fusion protein involved in multinucleated giant cell and osteoclast formation
    • Abe E., Mocharla H., Yamate T., Tagushi Y., Manolagas S.C. Meltrin-α, a fusion protein involved in multinucleated giant cell and osteoclast formation. Calcif. Tissue Int. 64:1999;508-515
    • (1999) Calcif. Tissue Int. , vol.64 , pp. 508-515
    • Abe, E.1    Mocharla, H.2    Yamate, T.3    Tagushi, Y.4    Manolagas, S.C.5
  • 40
    • 0034672264 scopus 로고    scopus 로고
    • Metalloprotease-disintegrin ADAM 12 binds to the SH3 domain of Src and activates Src tyrosine kinase in C2C12 cells
    • Kang Q., Cao Y., Zolkievska A. Metalloprotease-disintegrin ADAM 12 binds to the SH3 domain of Src and activates Src tyrosine kinase in C2C12 cells. Biochem. J. 352:2000;883-892
    • (2000) Biochem. J. , vol.352 , pp. 883-892
    • Kang, Q.1    Cao, Y.2    Zolkievska, A.3
  • 42
    • 0036152858 scopus 로고    scopus 로고
    • Cardiac hypertrophy is inhibited by antagonism of ADAM 12 processing of HB-EGF: Metalloproteinase inhibitors as a new therapy
    • Asakura M., Kitakaze M., Takashima S., Liao Y., Ishikura F., Yoshinaka T., et al. Cardiac hypertrophy is inhibited by antagonism of ADAM 12 processing of HB-EGF: metalloproteinase inhibitors as a new therapy. Nat. Med. 8:2002;35-40
    • (2002) Nat. Med. , vol.8 , pp. 35-40
    • Asakura, M.1    Kitakaze, M.2    Takashima, S.3    Liao, Y.4    Ishikura, F.5    Yoshinaka, T.6
  • 43
    • 0029057781 scopus 로고
    • Membrane-associated metalloproteinase recognized by characteristic cleavage of myelin basic protein: Assay and isolation
    • Howard L., Glynn P. Membrane-associated metalloproteinase recognized by characteristic cleavage of myelin basic protein: assay and isolation. Methods Enzymol. 248:1995;388-395
    • (1995) Methods Enzymol. , vol.248 , pp. 388-395
    • Howard, L.1    Glynn, P.2
  • 44
    • 0032540170 scopus 로고    scopus 로고
    • The metallo-disintegrin ADAM 10 (MADM) from bovine kidney has type IV collagenase activity in vitro
    • Millichip M.I., Dallas D.J., Wu E., Dale S., McKie N. The metallo-disintegrin ADAM 10 (MADM) from bovine kidney has type IV collagenase activity in vitro. Biochem. Biophys. Res. Commun. 245:1998;594-598
    • (1998) Biochem. Biophys. Res. Commun. , vol.245 , pp. 594-598
    • Millichip, M.I.1    Dallas, D.J.2    Wu, E.3    Dale, S.4    McKie, N.5
  • 45
    • 14444272986 scopus 로고    scopus 로고
    • Evidence that tumor necrosis factor alpha converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid protein precursor
    • Buxbaum J.D., Liu K.N., Luo Y., Slack L.J., Stocking K.L., Peschon J.J., et al. Evidence that tumor necrosis factor alpha converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid protein precursor. J. Biol. Chem. 273:1998;27765-27767
    • (1998) J. Biol. Chem. , vol.273 , pp. 27765-27767
    • Buxbaum, J.D.1    Liu, K.N.2    Luo, Y.3    Slack, L.J.4    Stocking, K.L.5    Peschon, J.J.6
  • 46
    • 0032923759 scopus 로고    scopus 로고
    • Processing of notch ligand delta by the metalloprotease Kusbanian
    • Qi H., Rand M.D., Wu X., Sestan N., Wang W., Rakic P., et al. Processing of notch ligand delta by the metalloprotease Kusbanian. Science. 283:1999;91-94
    • (1999) Science , vol.283 , pp. 91-94
    • Qi, H.1    Rand, M.D.2    Wu, X.3    Sestan, N.4    Wang, W.5    Rakic, P.6
  • 48
    • 0034874416 scopus 로고    scopus 로고
    • ADAM-10 protein is present in human articular cartilage primarily in the membrane-bound form and is upregulated in osteoarthritis and in response to IL-1α in bovine nasal cartilage
    • Chubinskaya S., Mikhail R., Deutsch A., Tindal M.H. ADAM-10 protein is present in human articular cartilage primarily in the membrane-bound form and is upregulated in osteoarthritis and in response to IL-1α in bovine nasal cartilage. J. Histochem. Cytochem. 49:2001;1165-1176
    • (2001) J. Histochem. Cytochem. , vol.49 , pp. 1165-1176
    • Chubinskaya, S.1    Mikhail, R.2    Deutsch, A.3    Tindal, M.H.4
  • 49
    • 9844253890 scopus 로고    scopus 로고
    • Identification and characterization of a pro-tumor necrosis factor-alpha-processing enzyme from the ADAM family of zinc metalloproteases
    • Rosendahl M.S., Ko S.C., Long I.D., Brewer M.T., Rosenzweig B., Held E., et al. Identification and characterization of a pro-tumor necrosis factor-alpha-processing enzyme from the ADAM family of zinc metalloproteases. J. Biol. Chem. 272:1997;24588-24593
    • (1997) J. Biol. Chem. , vol.272 , pp. 24588-24593
    • Rosendahl, M.S.1    Ko, S.C.2    Long, I.D.3    Brewer, M.T.4    Rosenzweig, B.5    Held, E.6
  • 50
    • 0029995478 scopus 로고    scopus 로고
    • Molecular cloning of MADM: A catalytically active mammalian disintergin-metalloproteinase expressed in various cell types
    • Howard L., Lu X., Griffith S., Glynn P. Molecular cloning of MADM: a catalytically active mammalian disintergin-metalloproteinase expressed in various cell types. Biochem. J. 317:1996;45-50
    • (1996) Biochem. J. , vol.317 , pp. 45-50
    • Howard, L.1    Lu, X.2    Griffith, S.3    Glynn, P.4


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