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Volumn 129, Issue 1, 2010, Pages 105-114

Protective role of osteopontin in endodontic infection

Author keywords

Bone loss; Cytokine; Migration; Neutrophil; Osteopontin; Peri apical

Indexed keywords

GAMMA INTERFERON; IMMUNOGLOBULIN G1; IMMUNOGLOBULIN G2A; INTERLEUKIN 10; INTERLEUKIN 12; INTERLEUKIN 1ALPHA; LEUKOCYTE ELASTASE; OSTEOCLAST DIFFERENTIATION FACTOR; OSTEOPONTIN; SECNIDAZOLE;

EID: 71649095659     PISSN: 00192805     EISSN: 13652567     Source Type: Journal    
DOI: 10.1111/j.1365-2567.2009.03159.x     Document Type: Article
Times cited : (28)

References (58)
  • 1
    • 22544468953 scopus 로고    scopus 로고
    • Pathogenesis of apical periodontitis and the causes of endodontic failures
    • Nair PNR. Pathogenesis of apical periodontitis and the causes of endodontic failures. Crit Rev Oral Biol Med 2004 15: 348 381.
    • (2004) Crit Rev Oral Biol Med , vol.15 , pp. 348-381
    • Nair, P.N.R.1
  • 2
    • 0032321488 scopus 로고    scopus 로고
    • Periapical inflammatory responses and their modulation
    • Stashenko P, Teles R, D'Souza R. Periapical inflammatory responses and their modulation. Crit Rev Oral Biol Med 1998 9: 498 521.
    • (1998) Crit Rev Oral Biol Med , vol.9 , pp. 498-521
    • Stashenko, P.1    Teles, R.2    D'Souza, R.3
  • 3
    • 0036694807 scopus 로고    scopus 로고
    • Enhanced neutrophil emigration and Porphyromonas gingivalis reduction following PGG-glucan treatment of mice
    • Niederman R, Kelderman H, Socransky S et al. Enhanced neutrophil emigration and Porphyromonas gingivalis reduction following PGG-glucan treatment of mice. Arch Oral Biol 2002 47: 613 618.
    • (2002) Arch Oral Biol , vol.47 , pp. 613-618
    • Niederman, R.1    Kelderman, H.2    Socransky, S.3
  • 4
    • 0029179226 scopus 로고
    • Reduction of infection-stimulated periapical bone resorption by the biological response modifier PGG glucan
    • Stashenko P, Wang CY, Riley E, Wu Y, Ostroff G, Niederman R. Reduction of infection-stimulated periapical bone resorption by the biological response modifier PGG glucan. J Dent Res 1995 74: 323 330.
    • (1995) J Dent Res , vol.74 , pp. 323-330
    • Stashenko, P.1    Wang, C.Y.2    Riley, E.3    Wu, Y.4    Ostroff, G.5    Niederman, R.6
  • 5
    • 0036259824 scopus 로고    scopus 로고
    • Mice lacking monocyte chemoattractant protein 1 have enhanced susceptibility to an interstitial polymicrobial infection due to impaired monocyte recruitment
    • Chae P, Im M, Gibson F, Jiang Y, Graves DT. Mice lacking monocyte chemoattractant protein 1 have enhanced susceptibility to an interstitial polymicrobial infection due to impaired monocyte recruitment. Infect Immun 2002 70: 3164 3169.
    • (2002) Infect Immun , vol.70 , pp. 3164-3169
    • Chae, P.1    Im, M.2    Gibson, F.3    Jiang, Y.4    Graves, D.T.5
  • 6
    • 0346497862 scopus 로고    scopus 로고
    • Gamma interferon (IFN-gamma) and IFN-gamma-inducing cytokines interleukin-12 (IL-12) and IL-18 do not augment infection-stimulated bone resorption in vivo
    • Sasaki H, Balto K, Kawashima N et al. Gamma interferon (IFN-gamma) and IFN-gamma-inducing cytokines interleukin-12 (IL-12) and IL-18 do not augment infection-stimulated bone resorption in vivo. Clin Diagn Lab Immunol 2004 11: 106 110.
    • (2004) Clin Diagn Lab Immunol , vol.11 , pp. 106-110
    • Sasaki, H.1    Balto, K.2    Kawashima, N.3
  • 7
    • 0034292422 scopus 로고    scopus 로고
    • IL-10, but not IL-4, suppresses infection-stimulated bone resorption in vivo
    • Sasaki H, Hou L, Belani A et al. IL-10, but not IL-4, suppresses infection-stimulated bone resorption in vivo. J Immunol 2000 165: 3626 3630.
    • (2000) J Immunol , vol.165 , pp. 3626-3630
    • Sasaki, H.1    Hou, L.2    Belani, A.3
  • 8
    • 42149085600 scopus 로고    scopus 로고
    • Pathophysiological role of osteopontin in hepatic inflammation, toxicity and cancer
    • Ramaiah SK, Rittling S. Pathophysiological role of osteopontin in hepatic inflammation, toxicity and cancer. Toxicol Sci 2007 103: 4 13.
    • (2007) Toxicol Sci , vol.103 , pp. 4-13
    • Ramaiah, S.K.1    Rittling, S.2
  • 9
    • 0034603119 scopus 로고    scopus 로고
    • Eta-1 (osteopontin): An early component of type-1 (cell-mediated) immunity
    • Ashkar S, Weber GF, Panoutsakopoulou V et al. Eta-1 (osteopontin): an early component of type-1 (cell-mediated) immunity. Science 2000 287: 860 864.
    • (2000) Science , vol.287 , pp. 860-864
    • Ashkar, S.1    Weber, G.F.2    Panoutsakopoulou, V.3
  • 10
    • 23044431647 scopus 로고    scopus 로고
    • Osteopontin functionally activates dendritic cells and induces their differentiation toward a Th1-polarizing phenotype
    • Renkl AC, Wussler J, Ahrens T et al. Osteopontin functionally activates dendritic cells and induces their differentiation toward a Th1-polarizing phenotype. Blood 2005 106: 946 955.
    • (2005) Blood , vol.106 , pp. 946-955
    • Renkl, A.C.1    Wussler, J.2    Ahrens, T.3
  • 11
    • 44449146212 scopus 로고    scopus 로고
    • Engagement of the Type i interferon receptor on dendritic cells inhibits T helper 17 cell development: Role of intracellular osteopontin
    • Shinohara ML, Kim JH, Garcia VA, Cantor H. Engagement of the Type I interferon receptor on dendritic cells inhibits T helper 17 cell development: role of intracellular osteopontin. Immunity 2008 29: 68 78.
    • (2008) Immunity , vol.29 , pp. 68-78
    • Shinohara, M.L.1    Kim, J.H.2    Garcia, V.A.3    Cantor, H.4
  • 12
    • 33644669749 scopus 로고    scopus 로고
    • Higher neutrophil infiltration mediated by osteopontin is a likely contributing factor to the increased susceptibility of females to alcoholic liver disease
    • Banerjee A, Apte UM, Smith R, Ramaiah SK. Higher neutrophil infiltration mediated by osteopontin is a likely contributing factor to the increased susceptibility of females to alcoholic liver disease. J Pathol 2006 208: 473 485.
    • (2006) J Pathol , vol.208 , pp. 473-485
    • Banerjee, A.1    Apte, U.M.2    Smith, R.3    Ramaiah, S.K.4
  • 13
    • 5644276291 scopus 로고    scopus 로고
    • Osteopontin as a mediator of NKT cell function in T cell-mediated liver diseases
    • Diao H, Kon S, Iwabuchi K et al. Osteopontin as a mediator of NKT cell function in T cell-mediated liver diseases. Immunity 2004 21: 539 550.
    • (2004) Immunity , vol.21 , pp. 539-550
    • Diao, H.1    Kon, S.2    Iwabuchi, K.3
  • 14
    • 0031906847 scopus 로고    scopus 로고
    • Evidence for a role of osteopontin in macrophage infiltration in response to pathological stimuli in vivo
    • Giachelli CM, Lombardi D, Johnson RJ, Murry CE, Almeida M. Evidence for a role of osteopontin in macrophage infiltration in response to pathological stimuli in vivo. Am J Pathol 1998 152: 353 358.
    • (1998) Am J Pathol , vol.152 , pp. 353-358
    • Giachelli, C.M.1    Lombardi, D.2    Johnson, R.J.3    Murry, C.E.4    Almeida, M.5
  • 16
    • 0037251307 scopus 로고    scopus 로고
    • Novel murine mammary epithelial cell lines that form osteolytic bone metastases: Effect of strain background on tumor homing
    • Chen Y, Rittling SR. Novel murine mammary epithelial cell lines that form osteolytic bone metastases: effect of strain background on tumor homing. Clin Exp Metastasis 2003 20: 111 120.
    • (2003) Clin Exp Metastasis , vol.20 , pp. 111-120
    • Chen, Y.1    Rittling, S.R.2
  • 17
    • 44449113589 scopus 로고    scopus 로고
    • Th1 biased response to a novel Porphyromonas gingivalis protein aggravates bone resorption caused by this oral pathogen
    • Leshem O, Kashino SS, Goncalves RB et al. Th1 biased response to a novel Porphyromonas gingivalis protein aggravates bone resorption caused by this oral pathogen. Microbes Infect 2008 10: 664 672.
    • (2008) Microbes Infect , vol.10 , pp. 664-672
    • Leshem, O.1    Kashino, S.S.2    Goncalves, R.B.3
  • 18
    • 0020513594 scopus 로고
    • Polymorphic expression of a neutrophil differentiation antigen revealed by monoclonal antibody 74
    • Hirsch S, Gordon S. Polymorphic expression of a neutrophil differentiation antigen revealed by monoclonal antibody 74. Immunogenetics 1983 18: 229 239.
    • (1983) Immunogenetics , vol.18 , pp. 229-239
    • Hirsch, S.1    Gordon, S.2
  • 20
    • 33144458447 scopus 로고    scopus 로고
    • Override of the osteoclast defect in osteopontin-deficient mice by metastatic tumor growth in the bone
    • Natasha T, Kuhn M, Kelly O, Rittling SR. Override of the osteoclast defect in osteopontin-deficient mice by metastatic tumor growth in the bone. Am J Pathol 2006 168: 551 561.
    • (2006) Am J Pathol , vol.168 , pp. 551-561
    • Natasha, T.1    Kuhn, M.2    Kelly, O.3    Rittling, S.R.4
  • 21
    • 33644698789 scopus 로고    scopus 로고
    • Lab assembly of a low-cost, robust SYBR green buffer system for quantitative real-time polymerase chain reaction
    • Pellissier F, Glogowski CM, Heinemann SF, Ballivet M, Ossipow V. Lab assembly of a low-cost, robust SYBR green buffer system for quantitative real-time polymerase chain reaction. Anal Biochem 2006 350: 310 312.
    • (2006) Anal Biochem , vol.350 , pp. 310-312
    • Pellissier, F.1    Glogowski, C.M.2    Heinemann, S.F.3    Ballivet, M.4    Ossipow, V.5
  • 22
    • 0037129827 scopus 로고    scopus 로고
    • Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes
    • RESEARCH0034
    • Vandesompele J, De PK, Pattyn F, et al. Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes. Genome Biol 2002 3: RESEARCH0034.
    • (2002) Genome Biol , vol.3
    • Vandesompele, J.1    De, P.K.2    Pattyn, F.3
  • 23
    • 0038824761 scopus 로고    scopus 로고
    • Customized molecular phenotyping by quantitative gene expression and pattern recognition analysis
    • Akilesh S, Shaffer DJ, Roopenian D. Customized molecular phenotyping by quantitative gene expression and pattern recognition analysis. Genome Res 2003 13: 1719 1727.
    • (2003) Genome Res , vol.13 , pp. 1719-1727
    • Akilesh, S.1    Shaffer, D.J.2    Roopenian, D.3
  • 24
    • 33745598573 scopus 로고    scopus 로고
    • T-cell expression cloning of Porphyromonas gingivalis genes coding for T helper-biased immune responses during infection
    • Goncalves RB, Leshem O, Bernards K, Webb JR, Stashenko PP, Campos-Neto A. T-cell expression cloning of Porphyromonas gingivalis genes coding for T helper-biased immune responses during infection. Infect Immun 2006 74: 3958 3966.
    • (2006) Infect Immun , vol.74 , pp. 3958-3966
    • Goncalves, R.B.1    Leshem, O.2    Bernards, K.3    Webb, J.R.4    Stashenko, P.P.5    Campos-Neto, A.6
  • 25
    • 0038505147 scopus 로고    scopus 로고
    • The contribution of interleukin-1 and tumor necrosis factor to periodontal tissue destruction
    • Graves DT, Cochran D. The contribution of interleukin-1 and tumor necrosis factor to periodontal tissue destruction. J Periodontol 2003 74: 391 401.
    • (2003) J Periodontol , vol.74 , pp. 391-401
    • Graves, D.T.1    Cochran, D.2
  • 28
    • 44449157284 scopus 로고    scopus 로고
    • T cell response mediated by myeloid cell-derived IL-12 is responsible for Porphyromonas gingivalis-induced periodontitis in IL-10-deficient mice
    • Sasaki H, Suzuki N, Kent R Jr., Kawashima N, Takeda J, Stashenko P. T cell response mediated by myeloid cell-derived IL-12 is responsible for Porphyromonas gingivalis-induced periodontitis in IL-10-deficient mice. J Immunol 2008 180: 6193 6198.
    • (2008) J Immunol , vol.180 , pp. 6193-6198
    • Sasaki, H.1    Suzuki, N.2    Kent Jr., R.3    Kawashima, N.4    Takeda, J.5    Stashenko, P.6
  • 29
    • 0033215121 scopus 로고    scopus 로고
    • Cutting edge: Mouse IgG1 antibodies comprise two functionally distinct types that are differentially regulated by IL-4 and IL-12
    • Faquim-Mauro EL, Coffman RL, Abrahamsohn IA, Macedo MS. Cutting edge: mouse IgG1 antibodies comprise two functionally distinct types that are differentially regulated by IL-4 and IL-12. J Immunol 1999 163: 3572 3576.
    • (1999) J Immunol , vol.163 , pp. 3572-3576
    • Faquim-Mauro, E.L.1    Coffman, R.L.2    Abrahamsohn, I.A.3    MacEdo, M.S.4
  • 30
    • 33645529154 scopus 로고    scopus 로고
    • Osteopontin participates in Th1-mediated host resistance against nonlethal malaria parasite Plasmodium chabaudi chabaudi infection in mice
    • Maeno Y, Nakazawa S, Yamamoto N et al. Osteopontin participates in Th1-mediated host resistance against nonlethal malaria parasite Plasmodium chabaudi chabaudi infection in mice. Infect Immun 2006 74: 2423 2427.
    • (2006) Infect Immun , vol.74 , pp. 2423-2427
    • Maeno, Y.1    Nakazawa, S.2    Yamamoto, N.3
  • 31
    • 0032770008 scopus 로고    scopus 로고
    • Attenuated host resistance against Mycobacterium bovis BCG infection in mice lacking osteopontin
    • Nau GJ, Liaw L, Chupp GL, Berman JS, Hogan BL, Young RA. Attenuated host resistance against Mycobacterium bovis BCG infection in mice lacking osteopontin. Infect Immun 1999 67: 4223 4230.
    • (1999) Infect Immun , vol.67 , pp. 4223-4230
    • Nau, G.J.1    Liaw, L.2    Chupp, G.L.3    Berman, J.S.4    Hogan, B.L.5    Young, R.A.6
  • 32
    • 58849083626 scopus 로고    scopus 로고
    • Regulation of T-helper-cell lineage development by osteopontin: The inside story
    • Cantor H, Shinohara ML. Regulation of T-helper-cell lineage development by osteopontin: the inside story. Nat Rev Immunol 2009 9: 137 141.
    • (2009) Nat Rev Immunol , vol.9 , pp. 137-141
    • Cantor, H.1    Shinohara, M.L.2
  • 33
    • 35948959449 scopus 로고    scopus 로고
    • Role of osteopontin in neutrophil function
    • Koh A, da Silva AP, Bansal AK et al. Role of osteopontin in neutrophil function. Immunology 2007 122: 466 475.
    • (2007) Immunology , vol.122 , pp. 466-475
    • Koh, A.1    Da Silva, A.P.2    Bansal, A.K.3
  • 35
    • 33947249865 scopus 로고    scopus 로고
    • A constitutive endogenous osteopontin production is important for macrophage function and differentiation
    • Nystrom T, Duner P, Hultgardh-Nilsson A. A constitutive endogenous osteopontin production is important for macrophage function and differentiation. Exp Cell Res 2007 313: 1149 1160.
    • (2007) Exp Cell Res , vol.313 , pp. 1149-1160
    • Nystrom, T.1    Duner, P.2    Hultgardh-Nilsson, A.3
  • 36
    • 1642316557 scopus 로고    scopus 로고
    • Osteopontin modulates CD44-dependent chemotaxis of peritoneal macrophages through G-protein-coupled receptors: Evidence of a role for an intracellular form of osteopontin
    • Zhu B, Suzuki K, Goldberg HA et al. Osteopontin modulates CD44-dependent chemotaxis of peritoneal macrophages through G-protein-coupled receptors: evidence of a role for an intracellular form of osteopontin. J Cell Physiol 2004 198: 155 167.
    • (2004) J Cell Physiol , vol.198 , pp. 155-167
    • Zhu, B.1    Suzuki, K.2    Goldberg, H.A.3
  • 37
    • 0025311346 scopus 로고
    • Definition of a specific interaction between the early T lymphocyte activation 1 (Eta-1) protein and murine macrophages in vitro and its effect upon macrophages in vivo
    • Singh RP, Patarca R, Schwartz J, Singh P, Cantor H. Definition of a specific interaction between the early T lymphocyte activation 1 (Eta-1) protein and murine macrophages in vitro and its effect upon macrophages in vivo. J Exp Med 1990 171: 1931 1942.
    • (1990) J Exp Med , vol.171 , pp. 1931-1942
    • Singh, R.P.1    Patarca, R.2    Schwartz, J.3    Singh, P.4    Cantor, H.5
  • 38
    • 55049109753 scopus 로고    scopus 로고
    • In vivo osteopontin-induced macrophage accumulation is dependent on CD44 expression
    • Marcondes MC, Poling M, Watry DD, Hall D, Fox HS. In vivo osteopontin-induced macrophage accumulation is dependent on CD44 expression. Cell Immunol 2008 254: 56 62.
    • (2008) Cell Immunol , vol.254 , pp. 56-62
    • Marcondes, M.C.1    Poling, M.2    Watry, D.D.3    Hall, D.4    Fox, H.S.5
  • 39
    • 1642340048 scopus 로고    scopus 로고
    • Impaired anti-tumor cytotoxicity of macrophages from osteopontin- deficient mice
    • Bourassa B, Monaghan S, Rittling SR. Impaired anti-tumor cytotoxicity of macrophages from osteopontin-deficient mice. Cell Immunol 2004 227: 1 11.
    • (2004) Cell Immunol , vol.227 , pp. 1-11
    • Bourassa, B.1    Monaghan, S.2    Rittling, S.R.3
  • 40
    • 71649087063 scopus 로고    scopus 로고
    • Osteopontin as two-sided mediator of intestinal inflammation
    • Epub ahead of print
    • Heilmann K, Hoffmann U, Witte E et al. Osteopontin as two-sided mediator of intestinal inflammation. J Cell Mol Med 2008 Epub ahead of print.
    • (2008) J Cell Mol Med
    • Heilmann, K.1    Hoffmann, U.2    Witte, E.3
  • 41
    • 0033583322 scopus 로고    scopus 로고
    • 1 mediates adhesion to activated endothelial cells and transendothelial neutrophil migration through interaction with vascular cell adhesion molecule-1
    • 1 mediates adhesion to activated endothelial cells and transendothelial neutrophil migration through interaction with vascular cell adhesion molecule-1. J Cell Biol 1999 145: 413 420.
    • (1999) J Cell Biol , vol.145 , pp. 413-420
    • Taooka, Y.1    Chen, J.2    Yednock, T.3    Sheppard, D.4
  • 42
    • 0033579511 scopus 로고    scopus 로고
    • 1 binds to a novel recognition sequence (SVVYGLR) in the thrombin-cleaved amino-terminal fragment of osteopontin
    • 1 binds to a novel recognition sequence (SVVYGLR) in the thrombin-cleaved amino-terminal fragment of osteopontin. J Biol Chem 1999 274: 36328 36334.
    • (1999) J Biol Chem , vol.274 , pp. 36328-36334
    • Yokosaki, Y.1    Matsuura, N.2    Sasaki, T.3
  • 43
    • 0032781554 scopus 로고    scopus 로고
    • Integrin signalling in neutrophils and macrophages
    • Berton G, Lowell CA. Integrin signalling in neutrophils and macrophages. Cell Signal 1999 11: 621 635.
    • (1999) Cell Signal , vol.11 , pp. 621-635
    • Berton, G.1    Lowell, C.A.2
  • 44
    • 51649127081 scopus 로고    scopus 로고
    • The phagocytes: Neutrophils and monocytes
    • Dale DC, Boxer L, Liles WC. The phagocytes: neutrophils and monocytes. Blood 2008 112: 935 945.
    • (2008) Blood , vol.112 , pp. 935-945
    • Dale, D.C.1    Boxer, L.2    Liles, W.C.3
  • 45
    • 50849132538 scopus 로고    scopus 로고
    • Cells on the run: Shear-regulated integrin activation in leukocyte rolling and arrest on endothelial cells
    • Alon R, Ley K. Cells on the run: shear-regulated integrin activation in leukocyte rolling and arrest on endothelial cells. Curr Opin Cell Biol 2008 20: 525 532.
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 525-532
    • Alon, R.1    Ley, K.2
  • 46
    • 34447649346 scopus 로고    scopus 로고
    • 2 integrins in kinetics of recruitment of lymphoid vs myeloid cell subsets to the inflamed peritoneum revealed by studies of genetically deficient mice
    • 2 integrins in kinetics of recruitment of lymphoid vs myeloid cell subsets to the inflamed peritoneum revealed by studies of genetically deficient mice. Exp Hematol 2007 35: 1256 1265.
    • (2007) Exp Hematol , vol.35 , pp. 1256-1265
    • Ulyanova, T.1    Priestley, G.V.2    Banerjee, E.R.3    Papayannopoulou, T.4
  • 47
    • 0032525350 scopus 로고    scopus 로고
    • 1 integrins are critically involved in neutrophil locomotion in extravascular tissue in vivo
    • 1 integrins are critically involved in neutrophil locomotion in extravascular tissue in vivo. J Exp Med 1998 187: 2091 2096.
    • (1998) J Exp Med , vol.187 , pp. 2091-2096
    • Werr, J.1    Xie, X.2    Hedqvist, P.3    Ruoslahti, E.4    Lindbom, L.5
  • 48
    • 0032936191 scopus 로고    scopus 로고
    • Infection-stimulated infraosseus inflammation and bone destruction is increased in P-E-selectin knockout mice
    • Kawashima N, Niederman R, Hynes RO, Ullmann-Cullere M, Stashenko P. Infection-stimulated infraosseus inflammation and bone destruction is increased in P-E-selectin knockout mice. Immunology 1999 97: 117 123.
    • (1999) Immunology , vol.97 , pp. 117-123
    • Kawashima, N.1    Niederman, R.2    Hynes, R.O.3    Ullmann-Cullere, M.4    Stashenko, P.5
  • 49
    • 0034637509 scopus 로고    scopus 로고
    • 3 integrin-mediated cell migration and phosphatidylinositol 3-kinaseAKT pathway activation
    • 3 integrin-mediated cell migration and phosphatidylinositol 3-kinaseAKT pathway activation. J Biol Chem 2000 275: 24565 24574.
    • (2000) J Biol Chem , vol.275 , pp. 24565-24574
    • Zheng, D.Q.1    Woodard, A.S.2    Tallini, G.3    Languino, L.R.4
  • 51
    • 20244386058 scopus 로고    scopus 로고
    • Phosphorylation-dependent interaction of osteopontin with its receptors regulates macrophage migration and activation
    • Weber GF, Zawaideh S, Hikita S, Kumar VA, Cantor H, Ashkar S. Phosphorylation-dependent interaction of osteopontin with its receptors regulates macrophage migration and activation. J Leukoc Biol 2002 72: 752 761.
    • (2002) J Leukoc Biol , vol.72 , pp. 752-761
    • Weber, G.F.1    Zawaideh, S.2    Hikita, S.3    Kumar, V.A.4    Cantor, H.5    Ashkar, S.6
  • 52
    • 44449131554 scopus 로고    scopus 로고
    • Alternative translation of osteopontin generates intracellular and secreted isoforms that mediate distinct biological activities in dendritic cells
    • Shinohara ML, Kim HJ, Kim JH, Garcia VA, Cantor H. Alternative translation of osteopontin generates intracellular and secreted isoforms that mediate distinct biological activities in dendritic cells. Proc Natl Acad Sci USA 2008 105: 7235 7239.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 7235-7239
    • Shinohara, M.L.1    Kim, H.J.2    Kim, J.H.3    Garcia, V.A.4    Cantor, H.5
  • 53
    • 28544433422 scopus 로고    scopus 로고
    • Osteoclast precursors, RANKLRANK, and immunology
    • Xing L, Schwarz EM, Boyce BF. Osteoclast precursors, RANKLRANK, and immunology. Immunol Rev 2005 208: 19 29.
    • (2005) Immunol Rev , vol.208 , pp. 19-29
    • Xing, L.1    Schwarz, E.M.2    Boyce, B.F.3
  • 54
    • 0036126916 scopus 로고    scopus 로고
    • Resistance to unloading-induced three-dimensional bone loss in osteopontin-deficient mice
    • Ishijima M, Tsuji K, Rittling SR et al. Resistance to unloading-induced three-dimensional bone loss in osteopontin-deficient mice. J Bone Miner Res 2002 17: 661 667.
    • (2002) J Bone Miner Res , vol.17 , pp. 661-667
    • Ishijima, M.1    Tsuji, K.2    Rittling, S.R.3
  • 55
    • 0033529194 scopus 로고    scopus 로고
    • Osteopontin-deficient mice are resistant to ovariectomy-induced bone resorption [published erratum appears in Proc Natl Acad Sci U S A 1999 Sep 14;96(19):10944]
    • Yoshitake H, Rittling SR, Denhardt DT, Noda M. Osteopontin-deficient mice are resistant to ovariectomy-induced bone resorption [published erratum appears in Proc Natl Acad Sci U S A 1999 Sep 14;96(19):10944]. Proc Natl Acad Sci USA 1999 96: 8156 8160.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8156-8160
    • Yoshitake, H.1    Rittling, S.R.2    Denhardt, D.T.3    Noda, M.4
  • 56
    • 12244312775 scopus 로고    scopus 로고
    • Osteopontin deficiency produces osteoclast dysfunction due to reduced CD44 surface expression
    • Chellaiah MA, Kizer N, Biswas R et al. Osteopontin deficiency produces osteoclast dysfunction due to reduced CD44 surface expression. Mol Biol Cell 2003 14: 173 189.
    • (2003) Mol Biol Cell , vol.14 , pp. 173-189
    • Chellaiah, M.A.1    Kizer, N.2    Biswas, R.3
  • 57
    • 0031284863 scopus 로고    scopus 로고
    • Osteopontin antisense deoxyoligonucleotides inhibit bone resorption by mouse osteoclasts in vitro
    • Tani-Ishii N, Tsunoda A, Umemoto T. Osteopontin antisense deoxyoligonucleotides inhibit bone resorption by mouse osteoclasts in vitro. J Periodontal Res 1997 32: 480 486.
    • (1997) J Periodontal Res , vol.32 , pp. 480-486
    • Tani-Ishii, N.1    Tsunoda, A.2    Umemoto, T.3
  • 58
    • 67649236132 scopus 로고    scopus 로고
    • Both cell-surface and secreted CSF-1 expressed by tumor cells metastatic to bone can contribute to osteoclast activation
    • Yagiz K, Rittling SR. Both cell-surface and secreted CSF-1 expressed by tumor cells metastatic to bone can contribute to osteoclast activation. Exp Cell Res 2009 315: 2442 2452.
    • (2009) Exp Cell Res , vol.315 , pp. 2442-2452
    • Yagiz, K.1    Rittling, S.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.