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Volumn 13, Issue 2, 2002, Pages 62-71

PDGF BB purified from osteoclasts acts as osteoblastogenesis inhibitory factor (OBIF)

Author keywords

Differentiation; Mass spectrometry; Platelet derived growth factor BB; Protein purification; Receptor activator of NF b ligand

Indexed keywords


EID: 77953662385     PISSN: 15240215     EISSN: 19434731     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (10)

References (33)
  • 1
    • 0034659815 scopus 로고    scopus 로고
    • Proteomics to study genes and genomes
    • Pandey A, Mann M. Proteomics to study genes and genomes. Nature 2000;405:837-46.
    • (2000) Nature , vol.405 , pp. 837-846
    • Pandey, A.1    Mann, M.2
  • 2
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons
    • Karas M, Hillenkamp F. Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Anal Chem 1988;60:2299-2301.
    • (1988) Anal Chem , vol.60 , pp. 2299-2301
    • Karas, M.1    Hillenkamp, F.2
  • 3
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn JB, Mann M, Meng CK, Wong SF, Whitehouse CM. Electrospray ionization for mass spectrometry of large biomolecules. Science 1989;246:64-71.
    • (1989) Science , vol.246 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 4
    • 0034284970 scopus 로고    scopus 로고
    • Bone resorption by osteoclasts
    • Teitelbaum SL. Bone resorption by osteoclasts. Science 2000;289:1504-1508.
    • (2000) Science , vol.289 , pp. 1504-1508
    • Teitelbaum, S.L.1
  • 5
    • 0034285013 scopus 로고    scopus 로고
    • The osteoblast: A sophisticated fibroblast under central surveillance
    • Ducy P, Schinke T, Karsenty G. The osteoblast: a sophisticated fibroblast under central surveillance. Science 2000;289:1501-1504.
    • (2000) Science , vol.289 , pp. 1501-1504
    • Ducy, P.1    Schinke, T.2    Karsenty, G.3
  • 6
    • 0033599563 scopus 로고    scopus 로고
    • A new member of tumor necrosis factor ligand family, ODF/OPGL/ TRANCE/RANKL, regulates osteoclast differentiation and function
    • Takahashi N, Udagawa N, Suda T. A new member of tumor necrosis factor ligand family, ODF/OPGL/ TRANCE/RANKL, regulates osteoclast differentiation and function. Biochem Biophys Res Commun 1999; 256:449-455.
    • (1999) Biochem Biophys Res Commun , vol.256 , pp. 449-455
    • Takahashi, N.1    Udagawa, N.2    Suda, T.3
  • 7
    • 0033304730 scopus 로고    scopus 로고
    • Modulation of osteoclast differentiation and function by the new members of the tumor necrosis factor receptor and ligand families
    • Suda T, Takahashi N, Udagawa N, Jimi E, Gillespie MT, Martin TJ. Modulation of osteoclast differentiation and function by the new members of the tumor necrosis factor receptor and ligand families. Endocr Rev 1999;20: 345-357.
    • (1999) Endocr Rev , vol.20 , pp. 345-357
    • Suda, T.1    Takahashi, N.2    Udagawa, N.3    Jimi, E.4    Gillespie, M.T.5    Martin, T.J.6
  • 8
    • 0030989969 scopus 로고    scopus 로고
    • Isolation of a novel cytokine from human fibroblasts that specifically inhibits osteoclastogenesis
    • Tsuda E, Goto M, Mochizuki S, et al. Isolation of a novel cytokine from human fibroblasts that specifically inhibits osteoclastogenesis. Biochem Biophys Res Commun 1997;234: 137-142.
    • (1997) Biochem Biophys Res Commun , vol.234 , pp. 137-142
    • Tsuda, E.1    Goto, M.2    Mochizuki, S.3
  • 9
    • 0031005576 scopus 로고    scopus 로고
    • Osteoprotegerin: A novel secreted protein involved in the regulation of bone density
    • Simonet WS, Lacey DL, Dunstan CR, et al. Osteoprotegerin: a novel secreted protein involved in the regulation of bone density. Cell 1997;89:309-319.
    • (1997) Cell , vol.89 , pp. 309-319
    • Simonet, W.S.1    Lacey, D.L.2    Dunstan, C.R.3
  • 10
    • 0032584208 scopus 로고    scopus 로고
    • Osteoclast differentiation factor is a ligand for osteoprotegerin/osteoclastogenesis- inhibitory factor and is identical to TRANCE/RANKL
    • Yasuda H, Shima N, Nakagawa N, et al. Osteoclast differentiation factor is a ligand for osteoprotegerin/osteoclastogenesis- inhibitory factor and is identical to TRANCE/RANKL. Proc Natl Acad Sci USA 1998;95: 3597-3602.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3597-3602
    • Yasuda, H.1    Shima, N.2    Nakagawa, N.3
  • 11
    • 0032540319 scopus 로고    scopus 로고
    • Osteoprotegerin ligand is a cytokine that regulates osteoclast differentiation and activation
    • Lacey DL, Timms E, Tan HL, et al. Osteoprotegerin ligand is a cytokine that regulates osteoclast differentiation and activation. Cell 1998;93:165-176.
    • (1998) Cell , vol.93 , pp. 165-176
    • Lacey, D.L.1    Timms, E.2    Tan, H.L.3
  • 12
    • 0030714605 scopus 로고    scopus 로고
    • A homologue of the TNF receptor and its ligand enhance T-cell growth and dendritic-cell function
    • Anderson DM, Maraskovsky E, Billingsley WL, et al. A homologue of the TNF receptor and its ligand enhance T-cell growth and dendritic-cell function. Nature 1997; 390:175-179.
    • (1997) Nature , vol.390 , pp. 175-179
    • Anderson, D.M.1    Maraskovsky, E.2    Billingsley, W.L.3
  • 13
    • 0028145856 scopus 로고
    • Influence of osteoclasts and osteoclast-like cells on osteoblast alkaline phosphatase activity and collagen synthesis
    • Galvin RJ, Cullison JW, Avioli LV, Osdoby PA. Influence of osteoclasts and osteoclast-like cells on osteoblast alkaline phosphatase activity and collagen synthesis. J Bone Miner Res 1994;9:1167-78.
    • (1994) J Bone Miner Res , vol.9 , pp. 1167-1178
    • Galvin, R.J.1    Cullison, J.W.2    Avioli, L.V.3    Osdoby, P.A.4
  • 14
    • 0023790708 scopus 로고
    • Osteoblastic cells are involved in osteoclast formation
    • Takahashi N, Akatsu T, Udagawa N, et al. Osteoblastic cells are involved in osteoclast formation. Endocrinology 1988;123:2600-2602.
    • (1988) Endocrinology , vol.123 , pp. 2600-2602
    • Takahashi, N.1    Akatsu, T.2    Udagawa, N.3
  • 15
    • 13044316551 scopus 로고    scopus 로고
    • Tumor necrosis factor receptor family member RANK mediates osteoclast differentiation and activation induced by osteoprotegerin ligand
    • Hsu H, Lacey DL, Dunstan CR, et al. Tumor necrosis factor receptor family member RANK mediates osteoclast differentiation and activation induced by osteoprotegerin ligand. Proc Natl Acad Sci USA 1999;96: 3540-3545.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3540-3545
    • Hsu, H.1    Lacey, D.L.2    Dunstan, C.R.3
  • 16
    • 0020678843 scopus 로고
    • In vitro differentiation and calcification in a new clonal osteogenic cell line derived from newborn mouse calvaria
    • Sudo H, Kodama HA, Amagai Y, Yamamoto S, Kasai S. In vitro differentiation and calcification in a new clonal osteogenic cell line derived from newborn mouse calvaria. J Cell Biol 1983;96:191-198.
    • (1983) J Cell Biol , vol.96 , pp. 191-198
    • Sudo, H.1    Kodama, H.A.2    Amagai, Y.3    Yamamoto, S.4    Kasai, S.5
  • 18
    • 0032538566 scopus 로고    scopus 로고
    • Transforming growth factor-beta stimulates the production of osteoprotegerin/ osteoclastogenesis inhibitory factor by bone marrow stromal cells
    • Takai H, Kanematsu M, Yano K, et al. Transforming growth factor-beta stimulates the production of osteoprotegerin/ osteoclastogenesis inhibitory factor by bone marrow stromal cells. J Biol Chem 1998;273: 27091-27096.
    • (1998) J Biol Chem , vol.273 , pp. 27091-27096
    • Takai, H.1    Kanematsu, M.2    Yano, K.3
  • 19
    • 0033547411 scopus 로고    scopus 로고
    • Serial passage of MC3T3-E1 cells alters osteoblastic function and responsiveness to transforming growth factor-beta1 and bone morphogenetic protein-2
    • Chung CY, Iida-Klein A, Wyatt LE, et al. Serial passage of MC3T3-E1 cells alters osteoblastic function and responsiveness to transforming growth factor-beta1 and bone morphogenetic protein-2. Biochem Biophys Res Commun 1999;265:246-251.
    • (1999) Biochem Biophys Res Commun , vol.265 , pp. 246-251
    • Chung, C.Y.1    Iida-Klein, A.2    Wyatt, L.E.3
  • 20
    • 0036208433 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis in proteomics: Old, old fashioned, but it still climbs up the mountains
    • Rabilloud T. Two-dimensional gel electrophoresis in proteomics: Old, old fashioned, but it still climbs up the mountains. Proteomics 2002;2:3-10
    • (2002) Proteomics , vol.2 , pp. 3-10
    • Rabilloud, T.1
  • 22
    • 0030026070 scopus 로고    scopus 로고
    • Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry
    • Wilm M, Shevchenko A, Houthaeve T, et al. Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry. Nature 1996;379: 466-469.
    • (1996) Nature , vol.379 , pp. 466-469
    • Wilm, M.1    Shevchenko, A.2    Houthaeve, T.3
  • 23
    • 0019957222 scopus 로고
    • Platelet-derived growth factor. I. High yield purification and evidence for multiple forms
    • Raines EW, Ross R. Platelet-derived growth factor. I. High yield purification and evidence for multiple forms. J Biol Chem 1982;257:5154-5160.
    • (1982) J Biol Chem , vol.257 , pp. 5154-5160
    • Raines, E.W.1    Ross, R.2
  • 24
    • 0022404365 scopus 로고
    • A significant part of macrophagederived growth factor consists of at least two forms of PDGF
    • Shimokado K, Raines EW, Madtes DK, Barrett TB, Benditt EP, Ross R. A significant part of macrophagederived growth factor consists of at least two forms of PDGF. Cell 1985;43:277-286.
    • (1985) Cell , vol.43 , pp. 277-286
    • Shimokado, K.1    Raines, E.W.2    Madtes, D.K.3    Barrett, T.B.4    Benditt, E.P.5    Ross, R.6
  • 26
    • 0033535961 scopus 로고    scopus 로고
    • Accurate quantitation of protein expression and site-specific phosphorylation
    • Oda Y, Huang K, Cross FR, Cowburn D, Chait BT. Accurate quantitation of protein expression and site-specific phosphorylation. Proc Natl Acad Sci U S A 1999;96: 6591-6596.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 6591-6596
    • Oda, Y.1    Huang, K.2    Cross, F.R.3    Cowburn, D.4    Chait, B.T.5
  • 27
    • 0034789979 scopus 로고    scopus 로고
    • Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry
    • Han DK, Eng J, Zhou H, Aebersold R. Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry. Nat Biotechnol 2001;19:946-951.
    • (2001) Nat Biotechnol , vol.19 , pp. 946-951
    • Han, D.K.1    Eng, J.2    Zhou, H.3    Aebersold, R.4
  • 28
    • 0033051101 scopus 로고    scopus 로고
    • Direct analysis of protein complexes using mass spectrometry
    • Link AJ, Eng J, Schieltz DM, et al. Direct analysis of protein complexes using mass spectrometry. Nat Biotechnol 1999;17:676-82.
    • (1999) Nat Biotechnol , vol.17 , pp. 676-682
    • Link, A.J.1    Eng, J.2    Schieltz, D.M.3
  • 29
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn MP, Wolters D, Yates JR 3rd. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat Biotechnol 2001; 19:242-247.
    • (2001) Nat Biotechnol , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 30
    • 0034628508 scopus 로고    scopus 로고
    • A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae
    • Uetz P, Giot L, Cagney G, et al. A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature 2000;403:623-627.
    • (2000) Nature , vol.403 , pp. 623-627
    • Uetz, P.1    Giot, L.2    Cagney, G.3
  • 32
    • 0037050026 scopus 로고    scopus 로고
    • Functional organization of the yeast proteome by systematic analysis of protein complexes
    • Gavin AC, Bosche M, Krause R, et al. Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 2002;415:141-147.
    • (2002) Nature , vol.415 , pp. 141-147
    • Gavin, A.C.1    Bosche, M.2    Krause, R.3
  • 33
    • 0037050004 scopus 로고    scopus 로고
    • Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
    • Ho Y, Gruhler A, Heilbut A, et al. Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 2002;415: 180-1833.
    • (2002) Nature , vol.415 , pp. 180-1833
    • Ho, Y.1    Gruhler, A.2    Heilbut, A.3


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