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Volumn 69, Issue 1, 2005, Pages 87-95

Inhibitory effects of mevastatin and a geranylgeranyl transferase I inhibitor (GGTI-2166) on mononuclear osteoclast formation induced by receptor activator of NFκB ligand (RANKL) or tumor necrosis factor-α (TNF-α)

Author keywords

FTI; Geranylgeranylation; GGTI; Osteoclast differentiation; Small G protein; Statin

Indexed keywords

ACID PHOSPHATASE TARTRATE RESISTANT ISOENZYME; CLOSTRIDIUM DIFFICILE TOXIN B; COLONY STIMULATING FACTOR 1; COMPACTIN; FARNESYL DIPHOSPHATE; FTI 2153; GERANYLGERANIOL; GERANYLGERANYL PYROPHOSPHATE; GERANYLTRANSFERASE; GGTI 2166; GUANINE NUCLEOTIDE BINDING PROTEIN; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE INHIBITOR; MEVALONIC ACID; MEVINOLIN; OSTEOCLAST DIFFERENTIATION FACTOR; PROTEIN FARNESYLTRANSFERASE INHIBITOR; RAC PROTEIN; RHO FACTOR; SIMVASTATIN; TRANSFERASE INHIBITOR; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 9944250487     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2004.08.036     Document Type: Article
Times cited : (37)

References (39)
  • 1
    • 85003152202 scopus 로고
    • Modulation of osteoclast differentiation
    • T. Suda, T. Takahashi, and T.J. Martin Modulation of osteoclast differentiation Endocr Rev 13 1992 66 80
    • (1992) Endocr Rev , vol.13 , pp. 66-80
    • Suda, T.1    Takahashi, T.2    Martin, T.J.3
  • 2
    • 0033828271 scopus 로고    scopus 로고
    • Regulation of the differentiation and function of osteoclasts
    • T.J. Chambers Regulation of the differentiation and function of osteoclasts J Pathology 192 2000 4 13
    • (2000) J Pathology , vol.192 , pp. 4-13
    • Chambers, T.J.1
  • 3
    • 0033304730 scopus 로고    scopus 로고
    • Modulation of osteoclast differentiation and function by the new members of the tumor necrosis factor receptor and ligand families
    • T. Suda, N. Takahashi, N. Udagawa, E. Jimi, M.T. Gillespie, and T.J. Martin Modulation of osteoclast differentiation and function by the new members of the tumor necrosis factor receptor and ligand families Endocr Rev 20 1999 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
  • 5
    • 0030267458 scopus 로고    scopus 로고
    • Rho: Theme and variations
    • A.J. Ridly Rho: theme and variations Curr Biol 6 1996 1256 1264
    • (1996) Curr Biol , vol.6 , pp. 1256-1264
    • Ridly, A.J.1
  • 6
    • 0029968827 scopus 로고    scopus 로고
    • Rho family GTPases: The cytoskeleton and beyond
    • M. Symons Rho family GTPases: the cytoskeleton and beyond Trends Biochem Sci 2 1996 178 181
    • (1996) Trends Biochem Sci , vol.2 , pp. 178-181
    • Symons, M.1
  • 7
    • 0027470176 scopus 로고
    • Different structural organization of Ras and Rho effector domains
    • A.J. Self, H.F. Paterson, and A. Hall Different structural organization of Ras and Rho effector domains Oncogene 8 1993 655 661
    • (1993) Oncogene , vol.8 , pp. 655-661
    • Self, A.J.1    Paterson, H.F.2    Hall, A.3
  • 8
    • 0031814992 scopus 로고    scopus 로고
    • Inhibiting geranylgeranylation blocks growth and promotes apoptosis in pulmonary vascular smooth muscle cells
    • W.W. Stark Jr., M.A. Blaskovich, B.A. Johnson, Y. Qian, A. Vasudevan, and B. Pitt Inhibiting geranylgeranylation blocks growth and promotes apoptosis in pulmonary vascular smooth muscle cells Am J Physiol 275 1998 55 63
    • (1998) Am J Physiol , vol.275 , pp. 55-63
    • Stark Jr., W.W.1    Blaskovich, M.A.2    Johnson, B.A.3    Qian, Y.4    Vasudevan, A.5    Pitt, B.6
  • 9
    • 0029012991 scopus 로고
    • The small GTP-binding protein, rho p21, is involved in bone resorption by regulating cytoskeletal organization in osteoclasts
    • D. Zhang, N. Udagawa, I. Nakamura, H. Murakami, S. Saito, and K. Yamasaki The small GTP-binding protein, rho p21, is involved in bone resorption by regulating cytoskeletal organization in osteoclasts J Cell Sci 108 1995 2285 2292
    • (1995) J Cell Sci , vol.108 , pp. 2285-2292
    • Zhang, D.1    Udagawa, N.2    Nakamura, I.3    Murakami, H.4    Saito, S.5    Yamasaki, K.6
  • 10
    • 0030797216 scopus 로고    scopus 로고
    • Endocytic pathway from the basal plasma membrane to the ruffled border membrane in bone-resorbing osteoclasts
    • H. Palokangas, M. Mulari, and H.K. Vaananen Endocytic pathway from the basal plasma membrane to the ruffled border membrane in bone-resorbing osteoclasts J Cell Sci 110 1997 1767 1780
    • (1997) J Cell Sci , vol.110 , pp. 1767-1780
    • Palokangas, H.1    Mulari, M.2    Vaananen, H.K.3
  • 11
    • 0032938495 scopus 로고    scopus 로고
    • Rac-GTPase, osteoclast cytoskeleton and bone resorption
    • S. Razzouk, M. Lieberherr, and G. Cournot Rac-GTPase, osteoclast cytoskeleton and bone resorption Eur J Cell Biol 78 1999 249 255
    • (1999) Eur J Cell Biol , vol.78 , pp. 249-255
    • Razzouk, S.1    Lieberherr, M.2    Cournot, G.3
  • 12
    • 0035914465 scopus 로고    scopus 로고
    • Down regulation of small GTPase Rab7 impairs osteoclast polarization and bone resorption
    • H. Zhao, T. Laitala-Leinonen, V. Parikka, and H.K. Vaananen Down regulation of small GTPase Rab7 impairs osteoclast polarization and bone resorption J Biol Chem 276 2001 39295 39302
    • (2001) J Biol Chem , vol.276 , pp. 39295-39302
    • Zhao, H.1    Laitala-Leinonen, T.2    Parikka, V.3    Vaananen, H.K.4
  • 13
    • 0021170342 scopus 로고
    • The p21 ras C-terminus is required for transformation and membrane association
    • B.M. Willumsen, A. Christensen, N.L. Hubbert, A.G. Papageorge, and D.R. Lowy The p21 ras C-terminus is required for transformation and membrane association Nature 310 1984 583 586
    • (1984) Nature , vol.310 , pp. 583-586
    • Willumsen, B.M.1    Christensen, A.2    Hubbert, N.L.3    Papageorge, A.G.4    Lowy, D.R.5
  • 14
    • 0024406286 scopus 로고
    • All ras proteins are polyisoprenylated but only some are palmitoylated
    • J.F. Hancock, A.I. Magee, J.E. Childs, and C.J. Marshall All ras proteins are polyisoprenylated but only some are palmitoylated Cell 57 1989 1167 1177
    • (1989) Cell , vol.57 , pp. 1167-1177
    • Hancock, J.F.1    Magee, A.I.2    Childs, J.E.3    Marshall, C.J.4
  • 15
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: Molecular mechanisms and functional consequences
    • F.L. Zyang, and P.J. Casey Protein prenylation: molecular mechanisms and functional consequences Annu Rev Bichem 65 1996 241 269
    • (1996) Annu Rev Bichem , vol.65 , pp. 241-269
    • Zyang, F.L.1    Casey, P.J.2
  • 16
    • 0033930168 scopus 로고    scopus 로고
    • Protein geranylgeranylation is required for osteoclast formation, function, and survival: Inhibition by bisphosphonates and GGTI-298
    • F.P. Coxon, M.H. Helfrich, R. Van't Hof, S. Sebti, S.H. Ralston, and A. Hamilton Protein geranylgeranylation is required for osteoclast formation, function, and survival: inhibition by bisphosphonates and GGTI-298 J Bone Miner Res 15 2000 1467 1476
    • (2000) J Bone Miner Res , vol.15 , pp. 1467-1476
    • Coxon, F.P.1    Helfrich, M.H.2    Van'T Hof, R.3    Sebti, S.4    Ralston, S.H.5    Hamilton, A.6
  • 17
    • 13044283050 scopus 로고    scopus 로고
    • Alendronate mechanism of action: Geranylgeraniol, an intermediate in the mevalonate pathway, prevents inhibition of osteoclast formation, bone resorption, and kinase activation in vitro
    • J.E. Fisher, M.J. Rogers, J.M. Halasy, S.P. Luckman, D.E. Hughes, and P.J. Masarachia Alendronate mechanism of action: geranylgeraniol, an intermediate in the mevalonate pathway, prevents inhibition of osteoclast formation, bone resorption, and kinase activation in vitro Proc Natl Acad Sci USA 96 1999 133 138
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 133-138
    • Fisher, J.E.1    Rogers, M.J.2    Halasy, J.M.3    Luckman, S.P.4    Hughes, D.E.5    Masarachia, P.J.6
  • 18
    • 0035051719 scopus 로고    scopus 로고
    • Visualization of bisphosphonate-induced caspase-3 activity in apoptotic osteoclasts in vitro
    • H.L. Benford, N.W. McGowan, M.H. Helfrich, M.E. Nuttall, and M.J. Rogers Visualization of bisphosphonate-induced caspase-3 activity in apoptotic osteoclasts in vitro Bone 28 2001 465 473
    • (2001) Bone , vol.28 , pp. 465-473
    • Benford, H.L.1    McGowan, N.W.2    Helfrich, M.H.3    Nuttall, M.E.4    Rogers, M.J.5
  • 19
    • 0033837292 scopus 로고    scopus 로고
    • Cytochemical and ultrastructural examination of apoptotic odontoclasts induced by bisphosphonate administration
    • J. Watanabe, N. Amizuka, T. Noda, and H. Ozawa Cytochemical and ultrastructural examination of apoptotic odontoclasts induced by bisphosphonate administration Cell Tissue Res 301 2000 375 387
    • (2000) Cell Tissue Res , vol.301 , pp. 375-387
    • Watanabe, J.1    Amizuka, N.2    Noda, T.3    Ozawa, H.4
  • 20
    • 0033554651 scopus 로고    scopus 로고
    • Farnesyl pyrophosphate synthase is the molecular target of nitrogen-containing bisphosphonates
    • E. van Beek, E. Pieterman, L. Cohen, C. Lowik, and S. Papapoulos Farnesyl pyrophosphate synthase is the molecular target of nitrogen-containing bisphosphonates Biochem Biophys Res Commun 264 1999 108 111
    • (1999) Biochem Biophys Res Commun , vol.264 , pp. 108-111
    • Van Beek, E.1    Pieterman, E.2    Cohen, L.3    Lowik, C.4    Papapoulos, S.5
  • 21
    • 0345161422 scopus 로고    scopus 로고
    • The role of geranylgeranylation in bone resorption and its suppression by bisphosphonates in fetal bone explants in vitro: A clue to the mechanism of action of nitrogen-containing bisphosphonates
    • E. van Beek, C. Lowik, G. van der Pluijm, and S. Papapoulos The role of geranylgeranylation in bone resorption and its suppression by bisphosphonates in fetal bone explants in vitro: A clue to the mechanism of action of nitrogen-containing bisphosphonates J Bone Miner Res 14 1999 722 729
    • (1999) J Bone Miner Res , vol.14 , pp. 722-729
    • Van Beek, E.1    Lowik, C.2    Van Der Pluijm, G.3    Papapoulos, S.4
  • 22
    • 0031977199 scopus 로고    scopus 로고
    • Nitrogen-containing bisphosphonates inhibit the mevalonate pathway and prevent post-translational prenylation of GTP-binding proteins, including Ras
    • S.P. Luckman, D.E. Hughes, F.P. Coxon, R. Graham, G. Russell, and M.J. Rogers Nitrogen-containing bisphosphonates inhibit the mevalonate pathway and prevent post-translational prenylation of GTP-binding proteins, including Ras J Bone Miner Res 13 1998 581 589
    • (1998) J Bone Miner Res , vol.13 , pp. 581-589
    • Luckman, S.P.1    Hughes, D.E.2    Coxon, F.P.3    Graham, R.4    Russell, G.5    Rogers, M.J.6
  • 23
    • 0034062795 scopus 로고    scopus 로고
    • Compactin suppresses bone resorption by inhibiting the fusion of prefusion osteoclasts and disrupting the actin ring in osteoclasts
    • J.T. Woo, S. Kasai, P.H. Stern, and K. Nagai Compactin suppresses bone resorption by inhibiting the fusion of prefusion osteoclasts and disrupting the actin ring in osteoclasts J Bone Miner Res 15 2000 650 662
    • (2000) J Bone Miner Res , vol.15 , pp. 650-662
    • Woo, J.T.1    Kasai, S.2    Stern, P.H.3    Nagai, K.4
  • 24
    • 0032586714 scopus 로고    scopus 로고
    • Prostaglandin E2 cooperates with TRANCE in osteoclast induction from hemopoietic precursors: Synergistic activation of differentiation, cell spreading, and fusion
    • M.R. Wani, K. Fuller, N.S. Kim, Y. Choi, and T. Chambers Prostaglandin E2 cooperates with TRANCE in osteoclast induction from hemopoietic precursors: synergistic activation of differentiation, cell spreading, and fusion Endocrinology 140 1999 1927 1935
    • (1999) Endocrinology , vol.140 , pp. 1927-1935
    • Wani, M.R.1    Fuller, K.2    Kim, N.S.3    Choi, Y.4    Chambers, T.5
  • 26
    • 0033214457 scopus 로고    scopus 로고
    • Antitumor efficacy of a novel class of non-thiol-containing peptidomimetic inhibitors of farnesyltransferase and geranylgeranyltransferase I: Combination therapy with the cytotoxic agents cisplatin, Taxol, and gemcitabine
    • J. Sun, M.A. Blaskovich, D. Knowles, Y. Qian, J. Ohkanda, and R.D. Bailey Antitumor efficacy of a novel class of non-thiol-containing peptidomimetic inhibitors of farnesyltransferase and geranylgeranyltransferase I: combination therapy with the cytotoxic agents cisplatin, Taxol, and gemcitabine Cancer Res 59 1999 4919 4949
    • (1999) Cancer Res , vol.59 , pp. 4919-4949
    • Sun, J.1    Blaskovich, M.A.2    Knowles, D.3    Qian, Y.4    Ohkanda, J.5    Bailey, R.D.6
  • 27
    • 0032515914 scopus 로고    scopus 로고
    • ADP ribosylation of rho proteins: Effects on nucleotide binding, GTPase activity, and effector coupling
    • P. Sehr, G. Joseph, H. Genth, I. Just, E. Pick, and K. Aktories ADP ribosylation of rho proteins: effects on nucleotide binding, GTPase activity, and effector coupling Biochemistry 37 1998 5296 5304
    • (1998) Biochemistry , vol.37 , pp. 5296-5304
    • Sehr, P.1    Joseph, G.2    Genth, H.3    Just, I.4    Pick, E.5    Aktories, K.6
  • 28
    • 0034677177 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha stimulates osteoclast differentiation by a mechanism independent of the ODF/RANKL-RANK interaction
    • K. Kobayashi, N. Takahashi, E. Jimi, N. Udagawa, M. Takami, and S. Kotake Tumor necrosis factor alpha stimulates osteoclast differentiation by a mechanism independent of the ODF/RANKL-RANK interaction J Exp Med 191 2000 275 286
    • (2000) J Exp Med , vol.191 , pp. 275-286
    • Kobayashi, K.1    Takahashi, N.2    Jimi, E.3    Udagawa, N.4    Takami, M.5    Kotake, S.6
  • 29
    • 0034681337 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha induces differentiation of and bone resorption
    • Y. Azuma, K. Kaji, R. Katogi, S. Takeshita, and A. Kudo Tumor necrosis factor-alpha induces differentiation of and bone resorption J Biol Chem 275 2000 4858 4864
    • (2000) J Biol Chem , vol.275 , pp. 4858-4864
    • Azuma, Y.1    Kaji, K.2    Katogi, R.3    Takeshita, S.4    Kudo, A.5
  • 30
    • 0032584208 scopus 로고    scopus 로고
    • Osteoclast differentiation factor is a ligand for osteoprotegerin/ osteoclastogenesis-inhibitory factor and is identical to TRANCE/RANKL
    • H. Ysuda, N. Shima, N. Nakagawa, K. Yamaguchi, M. Kinosaki, and S. Mochizuki 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
    • Ysuda, H.1    Shima, N.2    Nakagawa, N.3    Yamaguchi, K.4    Kinosaki, M.5    Mochizuki, S.6
  • 31
    • 0032540319 scopus 로고    scopus 로고
    • Osteoprotegerin ligand is a cytokine that regulates osteoclast differentiation and activation
    • D.L. Lncey, E. Timms, H.L. Tan, M.J. Kelley, C.R. Dunstan, and T. Burgess Osteoprotegerin ligand is a cytokine that regulates osteoclast differentiation and activation Cell 93 1998 165 176
    • (1998) Cell , vol.93 , pp. 165-176
    • Lncey, D.L.1    Timms, E.2    Tan, H.L.3    Kelley, M.J.4    Dunstan, C.R.5    Burgess, T.6
  • 32
    • 13044316551 scopus 로고    scopus 로고
    • Tumor necrosis factor receptor family member RANK mediates osteoclast differentiation and activation induced by osteoprotegerin ligand
    • H. Hsu, D.L. Lacey, C.R. Dunstan, I. Solovyev, A. Colombero, and E. Timms Tumor necrosis factor receptor family member RANK mediates osteoclast differentiation and activation induced by osteoprotegerin ligand Proc Natl Acad Sci USA 96 1999 3540 3545
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3540-3545
    • Hsu, H.1    Lacey, D.L.2    Dunstan, C.R.3    Solovyev, I.4    Colombero, A.5    Timms, E.6
  • 33
    • 0035930612 scopus 로고    scopus 로고
    • Identification of a novel phosphonocarboxylate inhibitor of Rab geranylgeranyl transferase that specifically prevents Rab prenylation in osteoclasts and macrophages
    • F.P. Coxon, M.H. Helfrich, B. Larijani, M. Muzylak, J.E. Dunford, and D. Marshall Identification of a novel phosphonocarboxylate inhibitor of Rab geranylgeranyl transferase that specifically prevents Rab prenylation in osteoclasts and macrophages J Biol Chem 276 2001 48213 48222
    • (2001) J Biol Chem , vol.276 , pp. 48213-48222
    • Coxon, F.P.1    Helfrich, M.H.2    Larijani, B.3    Muzylak, M.4    Dunford, J.E.5    Marshall, D.6
  • 34
    • 0033521078 scopus 로고    scopus 로고
    • Stimulation of bone formation in vitro and in rodents by statins
    • G. Mundy, R. Garrett, S. Harris, J. Chan, D. Chen, and G. Rossini Stimulation of bone formation in vitro and in rodents by statins Science 286 1999 1946 1949
    • (1999) Science , vol.286 , pp. 1946-1949
    • Mundy, G.1    Garrett, R.2    Harris, S.3    Chan, J.4    Chen, D.5    Rossini, G.6
  • 35
    • 0034709764 scopus 로고    scopus 로고
    • Oral statins and increased bone mineral density in postmenopausal women
    • C.J. Edwards, D.J. Hart, and T.D. Spector Oral statins and increased bone mineral density in postmenopausal women Lancet 355 2000 2218 2219
    • (2000) Lancet , vol.355 , pp. 2218-2219
    • Edwards, C.J.1    Hart, D.J.2    Spector, T.D.3
  • 36
  • 38
    • 18544410718 scopus 로고    scopus 로고
    • Inhibitors of hydroxyl-methylglutaryl-coenzyme a reductase and risk of fracture along older women
    • K.A. Chan, S.E. Andrade, M. Boles, D.S.M. Buist, G.A. Chase, and J.G. Donahue Inhibitors of hydroxyl-methylglutaryl-coenzyme A reductase and risk of fracture along older women Lancet 355 2000 2185 2188
    • (2000) Lancet , vol.355 , pp. 2185-2188
    • Chan, K.A.1    Andrade, S.E.2    Boles, M.3    Buist, D.S.M.4    Chase, G.A.5    Donahue, J.G.6


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