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Volumn 287, Issue 6, 2012, Pages 3788-3797

C-terminal modification of osteopontin inhibits interaction with the α Vβ 3-integrin

Author keywords

[No Author keywords available]

Indexed keywords

ARG GLY ASPS; C TERMINUS; C-TERMINAL REGIONS; CELL ATTACHMENTS; DEPHOSPHORYLATIONS; INTEGRIN BINDING; INTEGRIN RECEPTORS; INTEGRINS; ISOFORMS; MAMMALIAN SPECIES; OSTEOPONTIN; PHOSPHORYLATED PROTEINS;

EID: 84856699976     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.277996     Document Type: Article
Times cited : (47)

References (35)
  • 2
    • 78650555935 scopus 로고    scopus 로고
    • Osteopontin and allergic disease: Pathophysiology and implications for diagnostics and therapy
    • Frenzel, D. F., and Weiss, J. M. (2011) Osteopontin and allergic disease: pathophysiology and implications for diagnostics and therapy. Expert Rev. Clin. Immunol. 7, 93-109
    • (2011) Expert Rev. Clin. Immunol. , vol.7 , pp. 93-109
    • Frenzel, D.F.1    Weiss, J.M.2
  • 4
    • 0023695494 scopus 로고
    • Secreted phosphoproteins associated with neoplastic transformation: Close homology with plasma proteins cleaved during blood coagulation
    • Senger, D. R., Perruzzi, C. A., Gracey, C. F., Papadopoulos, A., and Tenen, D. G. (1988) Secreted phosphoproteins associated with neoplastic transformation: close homology with plasma proteins cleaved during blood coagulation. Cancer Res. 48, 5770-5774
    • (1988) Cancer Res. , vol.48 , pp. 5770-5774
    • Senger, D.R.1    Perruzzi, C.A.2    Gracey, C.F.3    Papadopoulos, A.4    Tenen, D.G.5
  • 6
    • 41649098345 scopus 로고    scopus 로고
    • Post-translational modification and proteolytic processing of urinary osteopontin
    • DOI 10.1042/BJ20071021
    • Christensen, B., Petersen, T. E., and Sørensen, E. S. (2008) Post-translational modification and proteolytic processing of urinary osteopontin. Biochem. J. 411, 53-61 (Pubitemid 351482346)
    • (2008) Biochemical Journal , vol.411 , Issue.1 , pp. 53-61
    • Christensen, B.1    Petersen, T.E.2    Sorensen, E.S.3
  • 7
    • 70350315761 scopus 로고    scopus 로고
    • Considerable variation in the concentration of osteopontin in human milk, bovine milk, and infant formulas
    • Schack, L., Lange, A., Kelsen, J., Agnholt, J., Christensen, B., Petersen, T. E., and Sørensen, E. S. (2009) Considerable variation in the concentration of osteopontin in human milk, bovine milk, and infant formulas. J. Dairy Sci. 92, 5378-5385
    • (2009) J. Dairy Sci. , vol.92 , pp. 5378-5385
    • Schack, L.1    Lange, A.2    Kelsen, J.3    Agnholt, J.4    Christensen, B.5    Petersen, T.E.6    Sørensen, E.S.7
  • 13
    • 35648934023 scopus 로고    scopus 로고
    • Control of osteopontin signaling and function by post-translational phosphorylation and protein folding
    • DOI 10.1002/jcb.21558
    • Kazanecki, C. C., Uzwiak, D. J., and Denhardt, D. T. (2007) Control of osteopontin signaling and function by post-translational phosphorylation and protein folding. J. Cell. Biochem. 102, 912-924 (Pubitemid 350036931)
    • (2007) Journal of Cellular Biochemistry , vol.102 , Issue.4 , pp. 912-924
    • Kazanecki, C.C.1    Uzwiak, D.J.2    Denhardt, D.T.3
  • 14
    • 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
  • 17
    • 3042701269 scopus 로고    scopus 로고
    • Post-translational modifications of sibling proteins and their roles in osteogenesis and dentinogenesis
    • Qin, C., Baba, O., and Butler, W. T. (2004) Post-translational modifications of sibling proteins and their roles in osteogenesis and dentinogenesis. Crit. Rev. Oral Biol. Med. 15, 126-136
    • (2004) Crit. Rev. Oral Biol. Med. , vol.15 , pp. 126-136
    • Qin, C.1    Baba, O.2    Butler, W.T.3
  • 18
    • 0035958935 scopus 로고    scopus 로고
    • Osteopontin, a novel substrate for matrix metalloproteinase-3 (stromelysin-1) and matrix metalloproteinase-7 (matrilysin)
    • Agnihotri, R., Crawford, H. C., Haro, H., Matrisian, L. M., Havrda, M. C., and Liaw, L. (2001) Osteopontin, a novel substrate for matrix metalloproteinase-3 (stromelysin-1) and matrix metalloproteinase-7 (matrilysin). J. Biol. Chem. 276, 28261-28267
    • (2001) J. Biol. Chem. , vol.276 , pp. 28261-28267
    • Agnihotri, R.1    Crawford, H.C.2    Haro, H.3    Matrisian, L.M.4    Havrda, M.C.5    Liaw, L.6
  • 19
    • 77950884807 scopus 로고    scopus 로고
    • Osteopontin is cleaved at multiple sites close to its integrin-binding motifs in milk and is a novel substrate for plasmin and cathepsin D
    • Christensen, B., Schack, L., Kläning, E., and Sørensen, E. S. (2010) Osteopontin is cleaved at multiple sites close to its integrin-binding motifs in milk and is a novel substrate for plasmin and cathepsin D. J. Biol. Chem. 285, 7929-7937
    • (2010) J. Biol. Chem. , vol.285 , pp. 7929-7937
    • Christensen, B.1    Schack, L.2    Kläning, E.3    Sørensen, E.S.4
  • 20
    • 0028228866 scopus 로고
    • Adhesive properties of osteopontin: Regulation by a naturally occurring thrombin-cleavage in close proximity to the GRGDS cell-binding domain
    • Senger, D. R., Perruzzi, C. A., Papadopoulos-Sergiou, A., and Van de Water, L. (1994) Adhesive properties of osteopontin: regulation by a naturally occurring thrombin cleavage in close proximity to the GRGDS cell-binding domain. Mol. Biol. Cell 5, 565-574 (Pubitemid 24183445)
    • (1994) Molecular Biology of the Cell , vol.5 , Issue.5 , pp. 565-574
    • Senger, D.R.1    Perruzzi, C.A.2    Papadopoulos-Sergiou, A.3    Van De, W.L.4
  • 21
    • 0028875692 scopus 로고
    • Posttranslational modifications of bovine osteopontin: Identification of 28 phosphorylation and 3 O-glycosylation sites
    • Sørensen, E. S., Højrup, P., and Petersen, T. E. (1995) Posttranslational modifications of bovine osteopontin: identification of 28 phosphorylation and 3 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
  • 22
    • 23944440915 scopus 로고    scopus 로고
    • Post-translationally modified residues of native human osteopontin are located in clusters: Identification of 36 phosphorylation and five O-glycosylation sites and their biological implications
    • DOI 10.1042/BJ20050341
    • Christensen, B., Nielsen, M. S., Haselmann, K. F., Petersen, T. E., and Sørensen, E. S. (2005) Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and 5 O-glycosylation sites and their biological implications. Biochem. J. 390, 285-292 (Pubitemid 41192254)
    • (2005) Biochemical Journal , vol.390 , Issue.1 , pp. 285-292
    • Christensen, B.1    Nielsen, M.S.2    Haselmann, K.F.3    Petersen, T.E.4    Sorensen, E.S.5
  • 23
    • 18244376132 scopus 로고    scopus 로고
    • Comprehensive identification of post-translational modifications of rat bone osteopontin by mass spectrometry
    • DOI 10.1021/bi050109p
    • Keykhosravani, M., Doherty-Kirby, A., Zhang, C., Brewer, D., Goldberg, H. A., Hunter, G. K., and Lajoie, G. (2005) Comprehensive identification of post-translational modifications of rat bone osteopontin by mass spectrometry. Biochemistry 44, 6990-7003 (Pubitemid 40632417)
    • (2005) Biochemistry , vol.44 , Issue.18 , pp. 6990-7003
    • Keykhosravani, M.1    Doherty-Kirby, A.2    Zhang, C.3    Brewer, D.4    Goldberg, H.A.5    Hunter, G.K.6    Lajoie, G.7
  • 24
    • 34547102777 scopus 로고    scopus 로고
    • Cell type-specific post-translational modifications of mouse osteopontin are associated with different adhesive properties
    • DOI 10.1074/jbc.M703055200
    • Christensen, B., Kazanecki, C. C., Petersen, T. E., Rittling, S. R., Denhardt, D. T., and Sørensen, E. S. (2007) Cell type-specific post-translational modifications of mouse osteopontin are associated with different adhesive properties. J. Biol. Chem. 282, 19463-19472 (Pubitemid 47100061)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.27 , pp. 19463-19472
    • Christensen, B.1    Kazanecki, C.C.2    Petersen, T.E.3    Rittling, S.R.4    Denhardt, D.T.5    Sorensen, E.S.6
  • 25
    • 72149088225 scopus 로고    scopus 로고
    • Osteoclast migration on phosphorylated osteopontin is regulated by endogenous tartrate-resistant acid phosphatase
    • Ek-Rylander, B., and Andersson, G. (2010) Osteoclast migration on phosphorylated osteopontin is regulated by endogenous tartrate-resistant acid phosphatase. Exp. Cell Res. 316, 443-451
    • (2010) Exp. Cell Res. , vol.316 , pp. 443-451
    • Ek-Rylander, B.1    Andersson, G.2
  • 27
    • 35649014332 scopus 로고    scopus 로고
    • Characterization of anti-osteopontin monoclonal antibodies: Binding sensitivity to post-translational modifications
    • DOI 10.1002/jcb.21487
    • Kazanecki, C. C., Kowalski, A. J., Ding, T., Rittling, S. R., and Denhardt, D. T. (2007) Characterization of anti-osteopontin monoclonal antibodies: binding sensitivity to post-translational modifications. J. Cell. Biochem. 102, 925-935 (Pubitemid 350036932)
    • (2007) Journal of Cellular Biochemistry , vol.102 , Issue.4 , pp. 925-935
    • Kazanecki, C.C.1    Kowalski, A.J.2    Ding, T.3    Rittling, S.R.4    Denhardt, D.T.5
  • 31
    • 0028237439 scopus 로고
    • Dephosphorylation of osteopontin and bone sialoprotein by osteoclastic tartrate-resistant acid phosphatase: Modulation of osteoclast adhesion in vitro
    • Ek-Rylander, B., Flores, M., Wendel, M., Heinegård, D., and Andersson, G. (1994) Dephosphorylation of osteopontin and bone sialoprotein by osteoclastic tartrate-resistant acid phosphatase: modulation of osteoclast adhesion in vitro. J. Biol. Chem. 269, 14853-14856
    • (1994) J. Biol. Chem. , vol.269 , pp. 14853-14856
    • Ek-Rylander, B.1    Flores, M.2    Wendel, M.3    Heinegård, D.4    Andersson, G.5
  • 32
    • 0031832984 scopus 로고    scopus 로고
    • Casein kinase 2 phosphorylation of recombinant rat osteopontin enhances adhesion of osteodasts but not osteoblasts
    • DOI 10.1002/(SICI)1097-4652(199807)176:1<179::AID-JCP19>3.0.CO;2-2
    • Katayama, Y., House, C. M., Udagawa, N., Kazama, J. J., McFarland, R. J., Martin, T. J., and Findlay, D. M. (1998) Casein kinase 2 phosphorylation of recombinant rat osteopontin enhances adhesion of osteoclasts but not osteoblasts. J. Cell. Physiol. 176, 179-187 (Pubitemid 28277207)
    • (1998) Journal of Cellular Physiology , vol.176 , Issue.1 , pp. 179-187
    • Katayama, Y.1    House, C.M.2    Udagawa, N.3    Kazama, J.J.4    Mcfarland, R.J.5    Martin, T.J.6    Findlay, D.M.7
  • 33
    • 33947254565 scopus 로고    scopus 로고
    • Osteopontin promotes integrin activation through outside-in and inside-out mechanisms: OPN-CD44V interaction enhances survival in gastrointestinal cancer cells
    • Lee, J. L., Wang, M. J., Sudhir, P. R., Chen, G. D., Chi, C. W., and Chen, J. Y. (2007) Osteopontin promotes integrin activation through outside-in and inside-out mechanisms: OPN-CD44V interaction enhances survival in gastrointestinal cancer cells. Cancer Res. 67, 2089-2097
    • (2007) Cancer Res. , vol.67 , pp. 2089-2097
    • Lee, J.L.1    Wang, M.J.2    Sudhir, P.R.3    Chen, G.D.4    Chi, C.W.5    Chen, J.Y.6
  • 34
    • 20244386058 scopus 로고    scopus 로고
    • Phosphorylation-dependent interaction of osteopontin with its receptors regulates macrophage migration and activation
    • Weber, G. F., Zawaideh, S., Hikita, S., Kumar, V. A., Cantor, H., and Ashkar, S. (2002) Phosphorylation-dependent interaction of osteopontin with its receptors regulates macrophage migration and activation. J. Leukocyte Biol. 72, 752-761 (Pubitemid 36277847)
    • (2002) Journal of Leukocyte Biology , vol.72 , Issue.4 , pp. 752-761
    • Weber, G.F.1    Zawaideh, S.2    Hikita, S.3    Kumar, V.A.4    Cantor, H.5    Ashkar, S.6


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