메뉴 건너뛰기




Volumn 32, Issue 4, 2004, Pages 351-359

Native osteoprotegerin gene transfer inhibits the development of murine osteolytic bone disease induced by tumor xenografts

Author keywords

[No Author keywords available]

Indexed keywords

BETA GALACTOSIDASE; LENTIVIRUS VECTOR; OSTEOPROTEGERIN;

EID: 1642634597     PISSN: 0301472X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.exphem.2004.01.006     Document Type: Article
Times cited : (20)

References (60)
  • 1
    • 0030791806 scopus 로고    scopus 로고
    • Mechanisms of bone lesions in multiple myeloma and lymphoma
    • Roodman G.D. Mechanisms of bone lesions in multiple myeloma and lymphoma. Cancer. 80:1997;1557-1563.
    • (1997) Cancer , vol.80 , pp. 1557-1563
    • Roodman, G.D.1
  • 2
    • 0000285711 scopus 로고    scopus 로고
    • Multiple myeloma
    • G.R. Lee, & J. Foerster. Baltimore, MD: Williams & Wilkins
    • Foerster J., Paraskevas F. Multiple myeloma. Lee G.R., Foerster J. Wintrobe's Clinical Hematology. 1999;2631-2680 Williams & Wilkins, Baltimore, MD.
    • (1999) Wintrobe's Clinical Hematology , pp. 2631-2680
    • Foerster, J.1    Paraskevas, F.2
  • 5
    • 0026690115 scopus 로고
    • Abnormal bone remodeling in patients with myelomatosis and normal biochemical indices of bone resorption
    • Taube T., Beneton M.N., McCloskey E.V., Rogers S., Greaves M., Kanis J.A. Abnormal bone remodeling in patients with myelomatosis and normal biochemical indices of bone resorption. Eur J Haematol. 49:1992;192-198.
    • (1992) Eur J Haematol , vol.49 , pp. 192-198
    • Taube, T.1    Beneton, M.N.2    McCloskey, E.V.3    Rogers, S.4    Greaves, M.5    Kanis, J.A.6
  • 6
    • 9044219839 scopus 로고    scopus 로고
    • Efficacy of pamidronate in reducing skeletal events in patients with advanced multiple myeloma
    • Berenson J.R., Lichtenstein A., Porter L., et al., Myeloma Aredia Study Group. Efficacy of pamidronate in reducing skeletal events in patients with advanced multiple myeloma. N Engl J Med. 334:1996;529-530.
    • (1996) N Engl J Med , vol.334 , pp. 529-530
    • Berenson, J.R.1    Lichtenstein, A.2    Et Al., P.L.3    Aredia Study Group, M.4
  • 7
    • 0024379867 scopus 로고
    • Production of interleukin-1 by bone marrow myeloma cells
    • Cozzolino F., Torcia M., Aldinucci D., et al. Production of interleukin-1 by bone marrow myeloma cells. Blood. 74:1989;380-387.
    • (1989) Blood , vol.74 , pp. 380-387
    • Cozzolino, F.1    Torcia, M.2    Aldinucci, D.3
  • 8
    • 0024599280 scopus 로고
    • Interleukin-1 β rather than lymphotoxin as the major bone resorbing activity in human multiple myeloma
    • Kawano M., Yamamoto I., Iwato K., et al. Interleukin-1 β rather than lymphotoxin as the major bone resorbing activity in human multiple myeloma. Blood. 73:1989;1646-1649.
    • (1989) Blood , vol.73 , pp. 1646-1649
    • Kawano, M.1    Yamamoto, I.2    Iwato, K.3
  • 9
    • 0024419152 scopus 로고
    • Production of cytokines by bone marrow cells obtained from patients with multiple myeloma
    • Lichtenstein A., Berenson J.R., Norman D., et al. Production of cytokines by bone marrow cells obtained from patients with multiple myeloma. Blood. 74:1989;1266-1273.
    • (1989) Blood , vol.74 , pp. 1266-1273
    • Lichtenstein, A.1    Berenson, J.R.2    Norman, D.3
  • 10
    • 0025223325 scopus 로고
    • Interleukin-6 is a major myeloma cell growth factor in vitro and in vivo especially in patients with terminal disease
    • Klein B., Zhang X.G., Jourdan M., Portier M., Bataille R. Interleukin-6 is a major myeloma cell growth factor in vitro and in vivo especially in patients with terminal disease. Curr Top Microbiol Immunol. 166:1990;23-31.
    • (1990) Curr Top Microbiol Immunol , vol.166 , pp. 23-31
    • Klein, B.1    Zhang, X.G.2    Jourdan, M.3    Portier, M.4    Bataille, R.5
  • 11
    • 0025885099 scopus 로고
    • Role of bone marrow stromal cells in the growth of human multiple myeloma
    • Caligaris-Cappio F., Bergui L., Gregoretti M.G., et al. Role of bone marrow stromal cells in the growth of human multiple myeloma. Blood. 77:1991;2688-2693.
    • (1991) Blood , vol.77 , pp. 2688-2693
    • Caligaris-Cappio, F.1    Bergui, L.2    Gregoretti, M.G.3
  • 12
    • 0023227925 scopus 로고
    • Production of lymphotoxin, a bone resorbing cytokine, by cultured human myeloma cells
    • Garrett I.R., Durie B.G., Nedwin G.E. Production of lymphotoxin, a bone resorbing cytokine, by cultured human myeloma cells. N Engl J Med. 317:1987;526-532.
    • (1987) N Engl J Med , vol.317 , pp. 526-532
    • Garrett, I.R.1    Durie, B.G.2    Nedwin, G.E.3
  • 13
    • 0023739441 scopus 로고
    • Hypercalcemia of malignancy revisited
    • Mundy G.R. Hypercalcemia of malignancy revisited. J Clin Invest. 82:1988;1-6.
    • (1988) J Clin Invest , vol.82 , pp. 1-6
    • Mundy, G.R.1
  • 14
    • 0022996159 scopus 로고
    • Bone destruction and hypercalcemia in plasma cell myeloma
    • Mundy G.R., Bertolini D.R. Bone destruction and hypercalcemia in plasma cell myeloma. Semin Oncol. 13:1986;291-299.
    • (1986) Semin Oncol , vol.13 , pp. 291-299
    • Mundy, G.R.1    Bertolini, D.R.2
  • 15
    • 0025903876 scopus 로고
    • Essential role of macrophage colony-stimulating factor in the osteoclast differentiation supported by stromal cells
    • Kodama H., Nose M., Niida S., Yamasaki A. Essential role of macrophage colony-stimulating factor in the osteoclast differentiation supported by stromal cells. J Exp Med. 173:1991;1291-1294.
    • (1991) J Exp Med , vol.173 , pp. 1291-1294
    • Kodama, H.1    Nose, M.2    Niida, S.3    Yamasaki, A.4
  • 16
    • 0029825852 scopus 로고    scopus 로고
    • Hepatocyte growth factor and its receptor c-Met in multiple myeloma
    • Borset M., Hjorth-Hansen H., Seidel C., Sundan A., Waage A. Hepatocyte growth factor and its receptor c-Met in multiple myeloma. Blood. 88:1996;3998-4004.
    • (1996) Blood , vol.88 , pp. 3998-4004
    • Borset, M.1    Hjorth-Hansen, H.2    Seidel, C.3    Sundan, A.4    Waage, A.5
  • 17
    • 0029778863 scopus 로고    scopus 로고
    • Concomitant expression of hepatocyte growth factor/scatter factor and the receptor c-Met in human myeloma cell lines
    • Borset M., Lien E., Espevik T., Helseth E., Waage A., Sundan A. Concomitant expression of hepatocyte growth factor/scatter factor and the receptor c-Met in human myeloma cell lines. J Biol Chem. 271:1996;24655-24661.
    • (1996) J Biol Chem , vol.271 , pp. 24655-24661
    • Borset, M.1    Lien, E.2    Espevik, T.3    Helseth, E.4    Waage, A.5    Sundan, A.6
  • 18
    • 0342322717 scopus 로고    scopus 로고
    • Macrophage inflammatory protein 1-α is a potential osteoclast stimulatory factor in multiple myeloma
    • Choi S.J., Cruz J.C., Craig F., et al. Macrophage inflammatory protein 1-α is a potential osteoclast stimulatory factor in multiple myeloma. Blood. 96:2000;671-675.
    • (2000) Blood , vol.96 , pp. 671-675
    • Choi, S.J.1    Cruz, J.C.2    Craig, F.3
  • 19
    • 0003285768 scopus 로고    scopus 로고
    • Multiple myeloma disrupts the TRANCE/OPG cytokine axis
    • [abstract]
    • Sordillo E.M., Wong B.R., Deng F.L., et al. Multiple myeloma disrupts the TRANCE/OPG cytokine axis. [abstract] Blood. 96:2000;549a.
    • (2000) Blood , vol.96
    • Sordillo, E.M.1    Wong, B.R.2    Deng, F.L.3
  • 20
    • 0032540319 scopus 로고    scopus 로고
    • Osteoprotegerin ligand is a cytokine that regulates osteoclast differentiation and activation
    • Lacey D.L., Timms E., Tan H.L., et al. Osteoprotegerin ligand is a cytokine that regulates osteoclast differentiation and activation. Cell. 93:1998;165-176.
    • (1998) Cell , vol.93 , pp. 165-176
    • Lacey, D.L.1    Timms, E.2    Tan, H.L.3
  • 21
    • 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. 95:1998;3597-3602.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3597-3602
    • Yasuda, H.1    Shima, N.2    Nakagawa, N.3
  • 22
    • 0031765480 scopus 로고    scopus 로고
    • A combination of osteoclast differentiation factor and macrophage colony-stimulating factor is sufficient for both human and mouse osteoclast formation in vitro
    • Quinn J.M.W., Elliott J., Gillespie M.T., Martin T.J. A combination of osteoclast differentiation factor and macrophage colony-stimulating factor is sufficient for both human and mouse osteoclast formation in vitro. Endocrinology. 139:1998;4424-4427.
    • (1998) Endocrinology , vol.139 , pp. 4424-4427
    • Quinn, J.M.W.1    Elliott, J.2    Gillespie, M.T.3    Martin, T.J.4
  • 23
    • 0032495975 scopus 로고    scopus 로고
    • Osteoclast differentiation factor (ODF) induces osteoclast-like cell formation in human peripheral blood mononuclear cell cultures
    • Matsuzaki K., Udagawa N., Takahashi N., et al. Osteoclast differentiation factor (ODF) induces osteoclast-like cell formation in human peripheral blood mononuclear cell cultures. Biochem Biophys Res Commun. 246:1998;199-204.
    • (1998) Biochem Biophys Res Commun , vol.246 , pp. 199-204
    • Matsuzaki, K.1    Udagawa, N.2    Takahashi, N.3
  • 24
    • 0032494113 scopus 로고    scopus 로고
    • Trance is necessary and sufficient for osteoblast-mediated activation of bone resorption in osteoclasts
    • Fuller K., Wong B., Fox S., Choi Y., Chambers T.J. Trance is necessary and sufficient for osteoblast-mediated activation of bone resorption in osteoclasts. J Exp Med. 188:1998;997-1001.
    • (1998) J Exp Med , vol.188 , pp. 997-1001
    • Fuller, K.1    Wong, B.2    Fox, S.3    Choi, Y.4    Chambers, T.J.5
  • 25
    • 0033519221 scopus 로고    scopus 로고
    • The ligand for osteoprotegerin (OPGL) directly activates mature osteoclasts
    • Burgess T.L., Qian Y., Kaufman S., et al. The ligand for osteoprotegerin (OPGL) directly activates mature osteoclasts. J Cell Biol. 145:1999;527-538.
    • (1999) J Cell Biol , vol.145 , pp. 527-538
    • Burgess, T.L.1    Qian, Y.2    Kaufman, S.3
  • 26
    • 0033611467 scopus 로고    scopus 로고
    • OPGL is a key regulator of osteoclastogenesis, lymphocyte development and lymph-node organogenesis
    • Kong Y.-Y., Yoshida H., Sarosi I., et al. OPGL is a key regulator of osteoclastogenesis, lymphocyte development and lymph-node organogenesis. Nature. 397:1999;315-323.
    • (1999) Nature , vol.397 , pp. 315-323
    • Kong, Y.-Y.1    Yoshida, H.2    Sarosi, I.3
  • 27
    • 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. 324:1997;137-142.
    • (1997) Biochem Biophys Res Commun , vol.324 , pp. 137-142
    • Tsuda, E.1    Goto, M.2    Mochizuki, S.3
  • 28
    • 0031005576 scopus 로고    scopus 로고
    • Osteoprotegerin: A novel secreted protein involved in the regulation of bone density
    • Simonet W.S., Lacey D.L., Dunstan C.R., et al. Osteoprotegerin: a novel secreted protein involved in the regulation of bone density. Cell. 89:1997;309-319.
    • (1997) Cell , vol.89 , pp. 309-319
    • Simonet, W.S.1    Lacey, D.L.2    Dunstan, C.R.3
  • 29
    • 0033984313 scopus 로고    scopus 로고
    • The roles of osteoprotegerin and osteoprotegerin ligand in the paracrine regulation of bone resorption
    • Hofbauer L.C., Khosla S., Dunstan C.R., Lacey D.L., Boyle W.J., Riggs B.L. The roles of osteoprotegerin and osteoprotegerin ligand in the paracrine regulation of bone resorption. J Bone Miner Res. 15:2000;2-12.
    • (2000) J Bone Miner Res , vol.15 , pp. 2-12
    • Hofbauer, L.C.1    Khosla, S.2    Dunstan, C.R.3    Lacey, D.L.4    Boyle, W.J.5    Riggs, B.L.6
  • 30
    • 0009660825 scopus 로고    scopus 로고
    • Identity of osteoclastogenesis inhibitory factor (OCIF) and osteoprotegerin (OPG): A mechanism by which OPG/OCIF inhibits osteoclastogenesis in vitro
    • Yasuda H., Shima N., Nakagawa N., et al. Identity of osteoclastogenesis inhibitory factor (OCIF) and osteoprotegerin (OPG): a mechanism by which OPG/OCIF inhibits osteoclastogenesis in vitro. Endocrinology. 39:1998;1329-1337.
    • (1998) Endocrinology , vol.39 , pp. 1329-1337
    • Yasuda, H.1    Shima, N.2    Nakagawa, N.3
  • 31
    • 0032581538 scopus 로고    scopus 로고
    • Structure of the mouse osteoclastogenesis inhibitory factor/ osteoprotegerin gene and its expression in embryogenesis
    • Mizuno A., Murakami A., Nakagawa N., et al. Structure of the mouse osteoclastogenesis inhibitory factor/osteoprotegerin gene and its expression in embryogenesis. Gene. 215:1998;339-343.
    • (1998) Gene , vol.215 , pp. 339-343
    • Mizuno, A.1    Murakami, A.2    Nakagawa, N.3
  • 32
    • 0032567676 scopus 로고    scopus 로고
    • Establishment and characterization of an immortal macrophage-like cell line inducible to differentiate to osteoclasts
    • Miyamoto A., Kunisada T., Hemmi H., et al. Establishment and characterization of an immortal macrophage-like cell line inducible to differentiate to osteoclasts. Biochem Biophys Res Commun. 242:1998;703-709.
    • (1998) Biochem Biophys Res Commun , vol.242 , pp. 703-709
    • Miyamoto, A.1    Kunisada, T.2    Hemmi, H.3
  • 33
    • 7344233085 scopus 로고    scopus 로고
    • Osteoprotegerin is a receptor for the cytotoxic ligand TRAIL
    • Emery J.G., McDonnell P., Brigham Burke M., et al. Osteoprotegerin is a receptor for the cytotoxic ligand TRAIL. J Biol Chem. 273:1998;14363-14367.
    • (1998) J Biol Chem , vol.273 , pp. 14363-14367
    • Emery, J.G.1    McDonnell, P.2    Brigham Burke, M.3
  • 34
    • 0033532191 scopus 로고    scopus 로고
    • Evidence for a role of a tumor necrosis factor-α (TNF-α)-converting enzyme-like protease in shedding TRANCE, a TNF family member involved in osteoclastogenesis and dendritic cell survival
    • Lum L., Wong B.R., Josien R., et al. Evidence for a role of a tumor necrosis factor-α (TNF-α)-converting enzyme-like protease in shedding TRANCE, a TNF family member involved in osteoclastogenesis and dendritic cell survival. J Biol Chem. 274:1999;13613-13618.
    • (1999) J Biol Chem , vol.274 , pp. 13613-13618
    • Lum, L.1    Wong, B.R.2    Josien, R.3
  • 35
    • 17344381882 scopus 로고    scopus 로고
    • TR1, a new member of the tumor necrosis receptor family, induces fibroblast proliferation and inhibits osteoclastogenesis and bone resorption
    • Kwon B.S., Wang S., Udagawa N., et al. TR1, a new member of the tumor necrosis receptor family, induces fibroblast proliferation and inhibits osteoclastogenesis and bone resorption. FASEB J. 12:1998;845-854.
    • (1998) FASEB J , vol.12 , pp. 845-854
    • Kwon, B.S.1    Wang, S.2    Udagawa, N.3
  • 36
    • 0032578781 scopus 로고    scopus 로고
    • Osteoclastogenesis inhibitory factor (OCIF) directly inhibits bone-resorbing activity of isolated mature osteoclasts
    • Hakeda Y., Kobayashi Y., Yamaguchi K., et al. Osteoclastogenesis inhibitory factor (OCIF) directly inhibits bone-resorbing activity of isolated mature osteoclasts. Biochem Biophys Res Commun. 251:1998;796-801.
    • (1998) Biochem Biophys Res Commun , vol.251 , pp. 796-801
    • Hakeda, Y.1    Kobayashi, Y.2    Yamaguchi, K.3
  • 37
    • 0032544518 scopus 로고    scopus 로고
    • Osteoclastogenesis inhibitory factor suppresses osteoclast survival by interfering in the interaction of stromal cells with osteoclasts
    • Akatsu T., Murakami T., Nishikawa M., et al. Osteoclastogenesis inhibitory factor suppresses osteoclast survival by interfering in the interaction of stromal cells with osteoclasts. Biochem Biophys Res Commun. 250:1998;229-234.
    • (1998) Biochem Biophys Res Commun , vol.250 , pp. 229-234
    • Akatsu, T.1    Murakami, T.2    Nishikawa, M.3
  • 38
    • 0035895083 scopus 로고    scopus 로고
    • Myeloma cells induce imbalance in the osteoprotegerin/osteoprotegerin ligand system in the human bone marrow environment
    • Giuliani N., Bataille R., Mancini C., Lazzaretti M., Barille S. Myeloma cells induce imbalance in the osteoprotegerin/osteoprotegerin ligand system in the human bone marrow environment. Blood. 98:2001;3527-3533.
    • (2001) Blood , vol.98 , pp. 3527-3533
    • Giuliani, N.1    Bataille, R.2    Mancini, C.3    Lazzaretti, M.4    Barille, S.5
  • 39
    • 0003267689 scopus 로고    scopus 로고
    • RANKL is expressed in malignant multiple myeloma (MM) cell lines
    • [abstract]
    • Altamirano C.V., Ma H.J., Parker K.M., et al. RANKL is expressed in malignant multiple myeloma (MM) cell lines. [abstract] Blood. 96:2000;365a.
    • (2000) Blood , vol.96
    • Altamirano, C.V.1    Ma, H.J.2    Parker, K.M.3
  • 40
    • 0000236587 scopus 로고    scopus 로고
    • Tumour cells isolated from patients with multiple myeloma express the critical osteoclastogenic factor, RANKL
    • [abstract]. Abstract 1552
    • Shipman C.M., Holen I., Lippitt J.M., Vandenberghe E., Croucher P.I. Tumour cells isolated from patients with multiple myeloma express the critical osteoclastogenic factor, RANKL. [abstract] Blood. 96:2000;360a. Abstract 1552.
    • (2000) Blood , vol.96
    • Shipman, C.M.1    Holen, I.2    Lippitt, J.M.3    Vandenberghe, E.4    Croucher, P.I.5
  • 41
    • 0035496947 scopus 로고    scopus 로고
    • Serum osteoprotegerin levels are reduced in patients with multiple myeloma with lytic bone disease
    • Seidel C., Hjertner O., Abildgaard N., et al. Serum osteoprotegerin levels are reduced in patients with multiple myeloma with lytic bone disease. Blood. 98:2001;2269-2271.
    • (2001) Blood , vol.98 , pp. 2269-2271
    • Seidel, C.1    Hjertner, O.2    Abildgaard, N.3
  • 42
    • 0034307372 scopus 로고    scopus 로고
    • Sundecan-1 is targeted to the uropods of polarized myeloma cells where it promotes adhesion and sequesters heparin-binding proteins
    • Borset M., Hjertner O., Yaccoby S., Epstein J., Sanderson R.D. Sundecan-1 is targeted to the uropods of polarized myeloma cells where it promotes adhesion and sequesters heparin-binding proteins. Blood. 96:2000;2528-2536.
    • (2000) Blood , vol.96 , pp. 2528-2536
    • Borset, M.1    Hjertner, O.2    Yaccoby, S.3    Epstein, J.4    Sanderson, R.D.5
  • 43
    • 0034700846 scopus 로고    scopus 로고
    • New insights into the role of microenvironment in multiple myeloma
    • Tricot G. New insights into the role of microenvironment in multiple myeloma. Lancet. 355:2000;248-250.
    • (2000) Lancet , vol.355 , pp. 248-250
    • Tricot, G.1
  • 44
    • 0033304809 scopus 로고    scopus 로고
    • Stimulation of osteoprotegerin ligand and inhibition of osteoprotegerin production by glucocorticoids in human lineage cells: Potential paracrine mechanisms of glucocorticoid-induced osteoporosis
    • Hofbauer L.C., Gori F., Riggs B.L., et al. Stimulation of osteoprotegerin ligand and inhibition of osteoprotegerin production by glucocorticoids in human lineage cells: potential paracrine mechanisms of glucocorticoid-induced osteoporosis. Endocrinology. 140:1999;4382-4389.
    • (1999) Endocrinology , vol.140 , pp. 4382-4389
    • Hofbauer, L.C.1    Gori, F.2    Riggs, B.L.3
  • 45
    • 0031721590 scopus 로고    scopus 로고
    • Osteoprotegerin mRNA is expressed in primary human osteoblast-like cells: Downregulation by glucocorticoids
    • Vidal N.O.A., Brändtröm H., Jonsson K.B., Ohlsson C. Osteoprotegerin mRNA is expressed in primary human osteoblast-like cells: downregulation by glucocorticoids. J Endcorinol. 159:1998;191-195.
    • (1998) J Endcorinol , vol.159 , pp. 191-195
    • Vidal, N.O.A.1    Brändtröm, H.2    Jonsson, K.B.3    Ohlsson, C.4
  • 46
    • 0032540137 scopus 로고    scopus 로고
    • Characterization of monomeric and homodimeric forms of osteoclastogenesis inhibitory factor
    • Tomoyasu A., Goto M., Fujise N., et al. Characterization of monomeric and homodimeric forms of osteoclastogenesis inhibitory factor. Biochem Biophys Res Commun. 245:1998;382-387.
    • (1998) Biochem Biophys Res Commun , vol.245 , pp. 382-387
    • Tomoyasu, A.1    Goto, M.2    Fujise, N.3
  • 48
    • 0021129808 scopus 로고
    • Arh-77, an established human IgG-producing myeloma cell line: I. Morphology, B-cell phenotypic marker profile, and expression of Epstein-Barr virus
    • Drewinko B., Mars W., Minowada J., Burk K.H., Trujillo J.M. Arh-77, an established human IgG-producing myeloma cell line I. Morphology, B-cell phenotypic marker profile, and expression of Epstein-Barr virus. Cancer. 54:1984;1883-1892.
    • (1984) Cancer , vol.54 , pp. 1883-1892
    • Drewinko, B.1    Mars, W.2    Minowada, J.3    Burk, K.H.4    Trujillo, J.M.5
  • 49
    • 0021228273 scopus 로고
    • ARH-77, an established human IgG-producing myeloma cell line: II. Growth kinetics, clonogenic capacity, chalone production, xenogeneic transplantations, and response to melphalan
    • Drewinko B., Mars W., Stragand J.J., et al. ARH-77, an established human IgG-producing myeloma cell line II. Growth kinetics, clonogenic capacity, chalone production, xenogeneic transplantations, and response to melphalan. Cancer. 54:1984;1893-1903.
    • (1984) Cancer , vol.54 , pp. 1893-1903
    • Drewinko, B.1    Mars, W.2    Stragand, J.J.3
  • 50
    • 0027279967 scopus 로고
    • Heterotransplantation of human multiple myeloma cell lines in severe combined immunodeficiency (SCID) mice
    • Tong A.W., Huang Y.-W., Zhang B.-Q., Netto G., Vitetta E.S., Stone M.J. Heterotransplantation of human multiple myeloma cell lines in severe combined immunodeficiency (SCID) mice. Anticancer Res. 13:1993;593-598.
    • (1993) Anticancer Res , vol.13 , pp. 593-598
    • Tong, A.W.1    Huang, Y.-W.2    Zhang, B.-Q.3    Netto, G.4    Vitetta, E.S.5    Stone, M.J.6
  • 51
    • 0027534880 scopus 로고
    • Disseminated growth of a human multiple myeloma cell line in mice with severe combined immunodeficiency disease
    • Huang Y.-W., Richardson J.A., Tong A.W., Zhang B.-Q., Stone M.J., Vitetta E.S. Disseminated growth of a human multiple myeloma cell line in mice with severe combined immunodeficiency disease. Cancer Res. 53:1993;1392-1396.
    • (1993) Cancer Res , vol.53 , pp. 1392-1396
    • Huang, Y.-W.1    Richardson, J.A.2    Tong, A.W.3    Zhang, B.-Q.4    Stone, M.J.5    Vitetta, E.S.6
  • 52
    • 0030019981 scopus 로고    scopus 로고
    • Development of an in vivo model of human multiple myeloma bone disease
    • Alsina M., Boyce B., Devlin R.D., et al. Development of an in vivo model of human multiple myeloma bone disease. Blood. 87:1996;1495-1501.
    • (1996) Blood , vol.87 , pp. 1495-1501
    • Alsina, M.1    Boyce, B.2    Devlin, R.D.3
  • 53
    • 0029993858 scopus 로고    scopus 로고
    • Efficient transfer, integration, and sustained long-term expression of the transgene in adult rat brains injected with a lentiviral vector
    • Naldini L., Blomer U., Gage F.H., Trono D., Verma I. Efficient transfer, integration, and sustained long-term expression of the transgene in adult rat brains injected with a lentiviral vector. Proc Natl Acad Sci USA. 93:1996;11382-11388.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 11382-11388
    • Naldini, L.1    Blomer, U.2    Gage, F.H.3    Trono, D.4    Verma, I.5
  • 54
    • 0030819379 scopus 로고    scopus 로고
    • Multiply attenuated lentiviral vector achieves efficient gene delivery in vivo
    • Zufferey R., Nagy D., Mandel R.J., Naldini L., Trono D. Multiply attenuated lentiviral vector achieves efficient gene delivery in vivo. Nat Biotechnol. 15:1997;871-875.
    • (1997) Nat Biotechnol , vol.15 , pp. 871-875
    • Zufferey, R.1    Nagy, D.2    Mandel, R.J.3    Naldini, L.4    Trono, D.5
  • 56
    • 0012720006 scopus 로고    scopus 로고
    • OPG gene transfer to control myelomatous skeletal disease in the ARH-77 SCID mouse model
    • [abstract]
    • Doran P.M., Chen D., Khosla S., Riggs B.L., Russell S.J. OPG gene transfer to control myelomatous skeletal disease in the ARH-77 SCID mouse model. [abstract] Blood. 96:2000;362a.
    • (2000) Blood , vol.96
    • Doran, P.M.1    Chen, D.2    Khosla, S.3    Riggs, B.L.4    Russell, S.J.5
  • 58
    • 0034677177 scopus 로고    scopus 로고
    • Tumor necrosis factor α stimulates osteoclast differentiation by a mechanism independent of the ODF/RANKL-RANK interaction
    • Kobayashi K., Takahashi N., Jimi E., et al. Tumor necrosis factor α stimulates osteoclast differentiation by a mechanism independent of the ODF/RANKL-RANK interaction. J Exp Med. 191:2000;275-285.
    • (2000) J Exp Med , vol.191 , pp. 275-285
    • Kobayashi, K.1    Takahashi, N.2    Jimi, E.3
  • 59
    • 0032878374 scopus 로고    scopus 로고
    • Phenotypic and molecular analysis of six human cell lines derived from patients with plasma cell dyscrasia
    • Gooding R.P., Bybee A., Cooke F., et al. Phenotypic and molecular analysis of six human cell lines derived from patients with plasma cell dyscrasia. Br J Haematol. 106:1999;669-681.
    • (1999) Br J Haematol , vol.106 , pp. 669-681
    • Gooding, R.P.1    Bybee, A.2    Cooke, F.3
  • 60
    • 0035895055 scopus 로고    scopus 로고
    • Osteoprotegerin inhibits the development of osteolytic bone disease in multiple myeloma
    • Croucher P.I., Shipman C.M., Lippitt J., et al. Osteoprotegerin inhibits the development of osteolytic bone disease in multiple myeloma. Blood. 98:2001;3534-3540.
    • (2001) Blood , vol.98 , pp. 3534-3540
    • Croucher, P.I.1    Shipman, C.M.2    Lippitt, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.