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Volumn 182, Issue 11, 2009, Pages 6943-6950

Osteopontin enhances phagocytosis through a novel osteopontin receptor, the αXβ2 integrin

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA X BETA 2 INTEGRIN; INTEGRIN; INTERLEUKIN 1; MANGANESE; OSTEOPONTIN; UNCLASSIFIED DRUG; GLYCOPROTEIN P 15095; SPP1 PROTEIN, MOUSE;

EID: 67449126814     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.0900065     Document Type: Article
Times cited : (87)

References (49)
  • 2
    • 0024337752 scopus 로고
    • Structural and functional studies of the early T lymphocyte activation 1 (Eta-1) gene: Definition of a novel T cell-dependent response associated with genetic resistance to bacterial infection
    • Patarca, R., G. J. Freeman, R. P. Singh, F. Y. Wei, T. Durfee, F. Blattner, D. C. Regnier, C. A. Kozak, B. A. Mock, H. C. Morse, 3rd, et al. 1989. Structural and functional studies of the early T lymphocyte activation 1 (Eta-1) gene: definition of a novel T cell-dependent response associated with genetic resistance to bacterial infection. J. Exp. Med. 170: 145-161.
    • (1989) J. Exp. Med. , vol.170 , pp. 145-161
    • Patarca, R.1    Freeman, G.J.2    Singh, R.P.3    Wei, F.Y.4    Durfee, T.5    Blattner, F.6    Regnier, D.C.7    Kozak, C.A.8    Mock, B.A.9    Morse III, H.C.10
  • 6
    • 0032770008 scopus 로고    scopus 로고
    • Attenuated host resistance against Mycobacterium bovis BCG infection in mice lacking osteopontin
    • Nau, G. J., L. Liaw, G. L. Chupp, J. S. Berman, B. L. Hogan, and R. A. Young. 1999. Attenuated host resistance against Mycobacterium bovis BCG infection in mice lacking osteopontin. Infect. Immun. 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
  • 10
    • 0033555820 scopus 로고    scopus 로고
    • Osteopontin is associated with T cells in sarcoid granulomas and has T cell adhesive and cytokine-like properties in vitro
    • O'Regan, A. W., G. L. Chupp, J. A. Lowry, M. Goetschkes, N. Mulligan, and J. S. Berman. 1999. Osteopontin is associated with T cells in sarcoid granulomas and has T cell adhesive and cytokine-like properties in vitro. J. Immunol. 162: 1024-1031.
    • (1999) J. Immunol. , vol.162 , pp. 1024-1031
    • O'Regan, A.W.1    Chupp, G.L.2    Lowry, J.A.3    Goetschkes, M.4    Mulligan, N.5    Berman, J.S.6
  • 11
    • 0028875692 scopus 로고
    • Posttranslational modifications of bovine osteopontin: Identification of twenty-eight phosphorylation and three O-glycosylation sites
    • Sørensen, E. S., P. Højrup, and T. E. Petersen. 1995. Posttranslational modifications of bovine osteopontin: identification of twenty-eight phosphorylation and three O-glycosylation sites. Protein Sci. 4: 2040-2049.
    • (1995) Protein Sci. , vol.4 , pp. 2040-2049
    • Sørensen, E.S.1    Højrup, P.2    Petersen, T.E.3
  • 12
    • 23944440915 scopus 로고    scopus 로고
    • Posttranslationally modified residues of native human osteopontin are located in clusters: Identification of thirty-six phosphorylation and five O-glycosylation sites and their biological implications
    • Christensen, B., M. S. Nielsen, K. F. Haselmann, T. E. Petersen, and E. S. Sørensen. 2005. Posttranslationally modified residues of native human osteopontin are located in clusters: identification of thirty-six phosphorylation and five O-glycosylation sites and their biological implications. Biochem. J. 390: 285-292.
    • (2005) Biochem. J. , vol.390 , pp. 285-292
    • Christensen, B.1    Nielsen, M.S.2    Haselmann, K.F.3    Petersen, T.E.4    Sørensen, E.S.5
  • 13
    • 34547102777 scopus 로고    scopus 로고
    • Cell type-specific post-translational modifications of mouse osteopontin are associated with different adhesive properties
    • Christensen, B., C. C. Kazanecki, T. E. Petersen, S. R. Rittling, D. T. Denhardt, and E. S. Sørensen. 2007. Cell type-specific post-translational modifications of mouse osteopontin are associated with different adhesive properties. J. Biol. Chem. 282: 19463-19472.
    • (2007) J. Biol. Chem. , vol.282 , pp. 19463-19472
    • Christensen, B.1    Kazanecki, C.C.2    Petersen, T.E.3    Rittling, S.R.4    Denhardt, D.T.5    Sørensen, E.S.6
  • 14
    • 0035167115 scopus 로고    scopus 로고
    • Osteopontin is involved in the initiation of cutaneous contact hypersensitivity by inducing Langerhans and dendritic cell migration to lymph nodes
    • Weiss, J. M., A. C. Renkl, C. S. Maier, M. Kimmig, L. Liaw, T. Ahrens, S. Kon, M. Maeda, H. Hotta, T. Uede, and J. C. Simon. 2001. Osteopontin is involved in the initiation of cutaneous contact hypersensitivity by inducing Langerhans and dendritic cell migration to lymph nodes. J. Exp. Med. 194: 1219-1229.
    • (2001) J. Exp. Med. , vol.194 , pp. 1219-1229
    • Weiss, J.M.1    Renkl, A.C.2    Maier, C.S.3    Kimmig, M.4    Liaw, L.5    Ahrens, T.6    Kon, S.7    Maeda, M.8    Hotta, H.9    Uede, T.10    Simon, J.C.11
  • 16
    • 20244386058 scopus 로고    scopus 로고
    • Phosphorylation-dependent interaction of osteopontin with its receptors regulates macrophage migration and activation
    • Weber, G. F., S. Zawaideh, S. Hikita, V. A. Kumar, H. Cantor, and S. Ashkar. 2002. Phosphorylation-dependent interaction of osteopontin with its receptors regulates macrophage migration and activation. J. Leukocyte Biol. 72: 752-761.
    • (2002) J. Leukocyte 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
  • 17
    • 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, R. P., R. Patarca, J. Schwartz, P. Singh, and H. Cantor. 1990. 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. 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
  • 18
    • 0031906847 scopus 로고    scopus 로고
    • Evidence for a role of osteopontin in macrophage infiltration in response to pathological stimuli in vivo
    • Giachelli, C. M., D. Lombardi, R. J. Johnson, C. E. Murry, and M. Almeida. 1998. Evidence for a role of osteopontin in macrophage infiltration in response to pathological stimuli in vivo. Am. J. Pathol. 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
  • 19
    • 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., K. Suzuki, H. A. Goldberg, S. R. Rittling, D. T. Denhardt, C. A. McCulloch, and J. Sodek. 2004. 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. 198: 155-167.
    • (2004) J. Cell. Physiol. , vol.198 , pp. 155-167
    • Zhu, B.1    Suzuki, K.2    Goldberg, H.A.3    Rittling, S.R.4    Denhardt, D.T.5    McCulloch, C.A.6    Sodek, J.7
  • 20
    • 33947249865 scopus 로고    scopus 로고
    • A constitutive endogenous osteopontin production is important for macrophage function and differentiation
    • Nyström, T., P. Dunér, and A. Hultgårdh-Nilsson. 2007. A constitutive endogenous osteopontin production is important for macrophage function and differentiation. Exp. Cell Res. 313: 1149-1160.
    • (2007) Exp. Cell Res. , vol.313 , pp. 1149-1160
    • Nyström, T.1    Dunér, P.2    Hultgårdh-Nilsson, A.3
  • 22
    • 0035050845 scopus 로고    scopus 로고
    • Monocyte chemoattractant protein-1 and osteopontin differentially regulate monocytes recruitment in experimental glomerulonephritis
    • Panzer, U., F. Thaiss, G. Zahner, P. Barth, M. Reszka, R. R. Reinking, G. Wolf, U. Helmchen, and R. A. Stahl. 2001. Monocyte chemoattractant protein-1 and osteopontin differentially regulate monocytes recruitment in experimental glomerulonephritis. Kidney Int. 59: 1762-1769.
    • (2001) Kidney Int. , vol.59 , pp. 1762-1769
    • Panzer, U.1    Thaiss, F.2    Zahner, G.3    Barth, P.4    Reszka, M.5    Reinking, R.R.6    Wolf, G.7    Helmchen, U.8    Stahl, R.A.9
  • 24
    • 34249684280 scopus 로고    scopus 로고
    • Osteopontin prevents monocyte recirculation and apoptosis
    • Burdo, T. H., M. R. Wood, and H. S. Fox. 2007. Osteopontin prevents monocyte recirculation and apoptosis. J. Leukocyte Biol. 81: 1504-1511.
    • (2007) J. Leukocyte Biol. , vol.81 , pp. 1504-1511
    • Burdo, T.H.1    Wood, M.R.2    Fox, H.S.3
  • 26
    • 50949117719 scopus 로고    scopus 로고
    • Osteopontin functions as an opsonin and facilitates phagocytosis by macrophages of hydroxyapatite-coated microspheres: Implications for bone wound healing
    • Pedraza, C. E., L. G. Nikolcheva, M. T. Kaartinen, J. E. Barralet, and M. D. McKee. 2008. Osteopontin functions as an opsonin and facilitates phagocytosis by macrophages of hydroxyapatite-coated microspheres: implications for bone wound healing. Bone 43: 708-716.
    • (2008) Bone , vol.43 , pp. 708-716
    • Pedraza, C.E.1    Nikolcheva, L.G.2    Kaartinen, M.T.3    Barralet, J.E.4    McKee, M.D.5
  • 28
    • 0031813775 scopus 로고    scopus 로고
    • 1 and potential roles for this integrin-ligand interaction in kidney morphogenesis
    • 1 and potential roles for this integrin-ligand interaction in kidney morphogenesis. Mol. Biol. Cell. 9: 1425-1435.
    • (1998) Mol. Biol. Cell. , vol.9 , pp. 1425-1435
    • Denda, S.1    Reichardt, L.F.2    Muller, U.3
  • 31
    • 0035918153 scopus 로고    scopus 로고
    • 1 integrin binding sites within a 38 amino acid domain in the N-terminal thrombin fragment of human osteopontin
    • 1 integrin binding sites within a 38 amino acid domain in the N-terminal thrombin fragment of human osteopontin. J. Biol. Chem. 276: 13483-13489.
    • (2001) J. Biol. Chem. , vol.276 , pp. 13483-13489
    • Bayless, K.J.1    Davis, G.E.2
  • 35
    • 0030064334 scopus 로고    scopus 로고
    • Receptor-ligand interaction between CD44 and osteopontin (Eta-1)
    • Weber, G. F., S. Ashkar, M. J. Glimcher, and H. Cantor. 1996. Receptor-ligand interaction between CD44 and osteopontin (Eta-1). Science 271: 509-512.
    • (1996) Science , vol.271 , pp. 509-512
    • Weber, G.F.1    Ashkar, S.2    Glimcher, M.J.3    Cantor, H.4
  • 36
    • 34249337400 scopus 로고    scopus 로고
    • - terminal osteopontin peptide binds with cyclophilin C to CD147 in murine breast cancer cells
    • - terminal osteopontin peptide binds with cyclophilin C to CD147 in murine breast cancer cells. Cancer Res. 67: 4088-4097.
    • (2007) Cancer Res. , vol.67 , pp. 4088-4097
    • Mi, Z.1    Oliver, T.2    Guo, H.3    Gao, C.4    Kuo, P.C.5
  • 37
    • 20644444103 scopus 로고    scopus 로고
    • 2 integrins: Moderators of life or death decisions
    • 2 integrins: moderators of life or death decisions. Trends Immunol. 26: 388-395.
    • (2005) Trends Immunol. , vol.26 , pp. 388-395
    • Mayadas, T.N.1    Cullere, X.2
  • 38
    • 0042565844 scopus 로고    scopus 로고
    • "Eat me" and "don't eat me" signals govern the innate immune response and tissue repair in the CNS: Emphasis on the critical role of the complement system
    • Elward, K., and P. Gasque. 2003. "Eat me" and "don't eat me" signals govern the innate immune response and tissue repair in the CNS: emphasis on the critical role of the complement system. Mol. Immunol. 40: 85-94.
    • (2003) Mol. Immunol. , vol.40 , pp. 85-94
    • Elward, K.1    Gasque, P.2
  • 41
    • 35648934023 scopus 로고    scopus 로고
    • Control of osteopontin signaling and function by post-translational phosphorylation and protein folding
    • Kazanecki, C. C., D. J. Uzwiak, and D. T. Denhardt. 2007. Control of osteopontin signaling and function by post-translational phosphorylation and protein folding. J. Cell. Biochem. 102: 912-924.
    • (2007) J. Cell. Biochem. , vol.102 , pp. 912-924
    • Kazanecki, C.C.1    Uzwiak, D.J.2    Denhardt, D.T.3
  • 42
    • 0011175654 scopus 로고
    • Purification and characterization of three proteins isolated from the proteose peptone fraction of bovine milk
    • Sørensen, E. S., and T. E. Petersen. 1993. Purification and characterization of three proteins isolated from the proteose peptone fraction of bovine milk. J. Dairy Res. 60: 189-197.
    • (1993) J. Dairy Res. , vol.60 , pp. 189-197
    • Sørensen, E.S.1    Petersen, T.E.2
  • 43
    • 0035341132 scopus 로고    scopus 로고
    • 2 subunit reveals regions that become exposed upon receptor activation
    • 2 subunit reveals regions that become exposed upon receptor activation. J. Immunol. 166: 5629-5637.
    • (2001) J. Immunol. , vol.166 , pp. 5629-5637
    • Lu, C.1    Ferzly, M.2    Takagi, J.3    Springer, T.A.4
  • 44
    • 0001894373 scopus 로고
    • Adhesion structure subpanel 5, leukocyte integrins: CD11a, CD11b, CD11c, CD18
    • S. F. Schlossman, L. Boumsell, W. Gilks, J. Harlan, T. Kishimoto, T. Morimoto, J. Ritz, S. Shaw, R. Silverstein, T. Springer, et al., eds. Oxford Univ. Press, New York
    • Petruzzelli, L., J. Luk, and T.A. Springer. 1995. Adhesion structure subpanel 5, leukocyte integrins: CD11a, CD11b, CD11c, CD18. In Leucocyte Typing V: White Cell Differentiation Antigens. S. F. Schlossman, L. Boumsell, W. Gilks, J. Harlan, T. Kishimoto, T. Morimoto, J. Ritz, S. Shaw, R. Silverstein, T. Springer, et al., eds. Oxford Univ. Press, New York, pp. 1581-1585.
    • (1995) Leucocyte Typing V: White Cell Differentiation Antigens , pp. 1581-1585
    • Petruzzelli, L.1    Luk, J.2    Springer, T.A.3
  • 46
    • 0026557165 scopus 로고
    • Antibody against the Leu-CAM β-chain (CD18) promotes both LFA-1- And CR3-dependent adhesion events
    • Robinson, M. K., D. Andrew, H. Rosen, D. Brown, S. Ortlepp, P. Stephens, and E. C. Butcher. 1992. Antibody against the Leu-CAM β-chain (CD18) promotes both LFA-1- and CR3-dependent adhesion events. J. Immunol. 148: 1080-1085.
    • (1992) J. Immunol. , vol.148 , pp. 1080-1085
    • Robinson, M.K.1    Andrew, D.2    Rosen, H.3    Brown, D.4    Ortlepp, S.5    Stephens, P.6    Butcher, E.C.7
  • 49
    • 55049109753 scopus 로고    scopus 로고
    • In vivo osteopontin-induced macrophage accumulation is dependent on CD44 expression
    • Marcondes, M. C., M. Poling, D. D. Watry, D. Hall, and H. S. Fox. 2008. In vivo osteopontin-induced macrophage accumulation is dependent on CD44 expression. Cell. Immunol. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.