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Volumn 16, Issue 2, 2006, Pages 79-87

Osteopontin: Role in cell signaling and cancer progression

Author keywords

[No Author keywords available]

Indexed keywords

CYTOKINE; DNA FRAGMENT; EPIDERMAL GROWTH FACTOR RECEPTOR; GROWTH FACTOR; HERMES ANTIGEN; INTEGRIN; MATRIX METALLOPROTEINASE; OSTEOPONTIN; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN TYROSINE KINASE; SCLEROPROTEIN; TUMOR MARKER;

EID: 32644467590     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcb.2005.12.005     Document Type: Review
Times cited : (614)

References (80)
  • 1
    • 0033830925 scopus 로고    scopus 로고
    • FGF signals for cell proliferation and migration through different pathways
    • B. Boilly FGF signals for cell proliferation and migration through different pathways Cytokine Growth Factor Rev. 11 2000 295 302
    • (2000) Cytokine Growth Factor Rev. , vol.11 , pp. 295-302
    • Boilly, B.1
  • 2
    • 15744372725 scopus 로고    scopus 로고
    • Role of transforming growth factor beta in human cancer
    • R.L. Elliott, and G.C. Blobe Role of transforming growth factor beta in human cancer J. Clin. Oncol. 23 2005 2078 2093
    • (2005) J. Clin. Oncol. , vol.23 , pp. 2078-2093
    • Elliott, R.L.1    Blobe, G.C.2
  • 3
    • 0035966343 scopus 로고    scopus 로고
    • The metastatic gene osteopontin: A candidate target for cancer therapy
    • G.F. Weber The metastatic gene osteopontin: a candidate target for cancer therapy Biochim. Biophys. Acta 1552 2001 61 85
    • (2001) Biochim. Biophys. Acta , vol.1552 , pp. 61-85
    • Weber, G.F.1
  • 4
    • 2942511574 scopus 로고    scopus 로고
    • Role of osteopontin in tumor progression
    • S.R. Rittling, and A.F. Chambers Role of osteopontin in tumor progression Br. J. Cancer 90 2004 1877 1881
    • (2004) Br. J. Cancer , vol.90 , pp. 1877-1881
    • Rittling, S.R.1    Chambers, A.F.2
  • 5
    • 0028340397 scopus 로고
    • Specific reduction in osteopontin synthesis by antisense RNA inhibits the tumorigenicity of transformed Rat1 fibroblasts
    • H.A. Gardner Specific reduction in osteopontin synthesis by antisense RNA inhibits the tumorigenicity of transformed Rat1 fibroblasts Oncogene 9 1994 2321 2326
    • (1994) Oncogene , vol.9 , pp. 2321-2326
    • Gardner, H.A.1
  • 6
    • 0035021027 scopus 로고    scopus 로고
    • Osteopontin as a means to cope with environmental insults: Regulation of inflammation, tissue remodeling, and cell survival
    • D.T. Denhardt Osteopontin as a means to cope with environmental insults: regulation of inflammation, tissue remodeling, and cell survival J. Clin. Invest. 107 2001 1055 1061
    • (2001) J. Clin. Invest. , vol.107 , pp. 1055-1061
    • Denhardt, D.T.1
  • 7
    • 0030803397 scopus 로고    scopus 로고
    • Potential roles of osteopontin and alphaVbeta3 integrin in the development of coronary artery restenosis after angioplasty
    • D. Panda Potential roles of osteopontin and alphaVbeta3 integrin in the development of coronary artery restenosis after angioplasty Proc. Natl. Acad. Sci. U. S. A. 94 1997 9308 9313
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 9308-9313
    • Panda, D.1
  • 8
    • 1542270075 scopus 로고    scopus 로고
    • Osteopontin: Correlation with interstitial fibrosis in human diabetic kidney and PI 3-kinase-mediated enhancement of expression by glucose in human proximal tubular epithelial cells
    • A. Junaid, and F.M. Amara Osteopontin: correlation with interstitial fibrosis in human diabetic kidney and PI 3-kinase-mediated enhancement of expression by glucose in human proximal tubular epithelial cells Histopathology 44 2004 136 146
    • (2004) Histopathology , vol.44 , pp. 136-146
    • Junaid, A.1    Amara, F.M.2
  • 9
    • 18244406113 scopus 로고    scopus 로고
    • Osteopontin-deficiency suppresses growth of B16 melanoma cells implanted in bone and osteoclastogenesis in co-cultures
    • Y. Ohyama Osteopontin-deficiency suppresses growth of B16 melanoma cells implanted in bone and osteoclastogenesis in co-cultures J. Bone Miner. Res. 19 2004 1706 1711
    • (2004) J. Bone Miner. Res. , vol.19 , pp. 1706-1711
    • Ohyama, Y.1
  • 10
    • 0023664074 scopus 로고
    • Isolation, characterization, and biosynthesis of a phosphorylated glycoprotein from rat bone
    • C.W. Prince Isolation, characterization, and biosynthesis of a phosphorylated glycoprotein from rat bone J. Biol. Chem. 262 1987 2900 2907
    • (1987) J. Biol. Chem. , vol.262 , pp. 2900-2907
    • Prince, C.W.1
  • 11
    • 0028228866 scopus 로고
    • Adhesive properties of osteopontin: Regulation by a naturally occurring thrombin-cleavage in close proximity to the GRGDS cell-binding domain
    • D.R. Senger Adhesive properties of osteopontin: regulation by a naturally occurring thrombin-cleavage in close proximity to the GRGDS cell-binding domain Mol. Biol. Cell 5 1994 565 574
    • (1994) Mol. Biol. Cell , vol.5 , pp. 565-574
    • Senger, D.R.1
  • 12
    • 0030946791 scopus 로고    scopus 로고
    • 32P-labeled osteopontin from cultured chicken osteoblasts
    • 32P-labeled osteopontin from cultured chicken osteoblasts J. Biol. Chem. 272 1997 13966 13973
    • (1997) J. Biol. Chem. , vol.272 , pp. 13966-13973
    • Salih, E.1
  • 13
    • 0025895928 scopus 로고
    • Osteopontin, a substrate for transglutaminase and factor XIII activity
    • C.W. Prince Osteopontin, a substrate for transglutaminase and factor XIII activity Biochem. Biophys. Res. Commun. 177 1991 1205 1210
    • (1991) Biochem. Biophys. Res. Commun. , vol.177 , pp. 1205-1210
    • Prince, C.W.1
  • 14
    • 0035958935 scopus 로고    scopus 로고
    • Osteopontin, a novel substrate for matrix metalloproteinase-3 (stromelysin-1) and matrix metalloproteinase-7 (matrilysin)
    • R. Agnihotri Osteopontin, a novel substrate for matrix metalloproteinase-3 (stromelysin-1) and matrix metalloproteinase-7 (matrilysin) J. Biol. Chem. 276 2001 28261 28267
    • (2001) J. Biol. Chem. , vol.276 , pp. 28261-28267
    • Agnihotri, R.1
  • 15
    • 4644360517 scopus 로고    scopus 로고
    • Identification of promoter regions involved in cell- and developmental stage-specific osteopontin expression in bone, kidney, placenta, and mammary gland: An analysis of transgenic mice
    • Y. Higashibata Identification of promoter regions involved in cell- and developmental stage-specific osteopontin expression in bone, kidney, placenta, and mammary gland: an analysis of transgenic mice J. Bone Miner. Res. 19 2004 78 88
    • (2004) J. Bone Miner. Res. , vol.19 , pp. 78-88
    • Higashibata, Y.1
  • 16
    • 3242807371 scopus 로고    scopus 로고
    • Osteopontin is strongly expressed by alveolar macrophages in the lungs of acute respiratory distress syndrome
    • F. Takahashi Osteopontin is strongly expressed by alveolar macrophages in the lungs of acute respiratory distress syndrome Lung 182 2004 173 185
    • (2004) Lung , vol.182 , pp. 173-185
    • Takahashi, F.1
  • 17
    • 0034013170 scopus 로고    scopus 로고
    • Antibodies to different peptides in osteopontin reveal complexities in the various secreted forms
    • S. Kon Antibodies to different peptides in osteopontin reveal complexities in the various secreted forms J. Cell. Biochem. 77 2000 487 498
    • (2000) J. Cell. Biochem. , vol.77 , pp. 487-498
    • Kon, S.1
  • 18
    • 0032533862 scopus 로고    scopus 로고
    • Distinct roles of osteopontin in host defense activity and tumor survival during squamous cell carcinoma progression in vivo
    • H.C. Crawford Distinct roles of osteopontin in host defense activity and tumor survival during squamous cell carcinoma progression in vivo Cancer Res. 58 1998 5206 5215
    • (1998) Cancer Res. , vol.58 , pp. 5206-5215
    • Crawford, H.C.1
  • 19
    • 0037237957 scopus 로고    scopus 로고
    • Six genes expressed in bones and teeth encode the current members of the SIBLING family of proteins
    • L.W. Fisher, and N.S. Fedarko Six genes expressed in bones and teeth encode the current members of the SIBLING family of proteins Connect. Tissue Res. 44 2003 33 40
    • (2003) Connect. Tissue Res. , vol.44 , pp. 33-40
    • Fisher, L.W.1    Fedarko, N.S.2
  • 20
    • 2942679170 scopus 로고    scopus 로고
    • Bone sialoprotein, matrix metalloproteinase 2, and alpha(v) beta3 integrin in osteotropic cancer cell invasion
    • A. Karadag Bone sialoprotein, matrix metalloproteinase 2, and alpha(v) beta3 integrin in osteotropic cancer cell invasion J. Natl. Cancer Inst. 96 2004 956 965
    • (2004) J. Natl. Cancer Inst. , vol.96 , pp. 956-965
    • Karadag, A.1
  • 21
    • 3042703295 scopus 로고    scopus 로고
    • Three small integrin binding ligand N-linked glycoproteins (SIBLINGS) bind and activate specific matrix metalloproteinases
    • N.S. Fedarko Three small integrin binding ligand N-linked glycoproteins (SIBLINGS) bind and activate specific matrix metalloproteinases FASEB J. 18 2004 734 736
    • (2004) FASEB J. , vol.18 , pp. 734-736
    • Fedarko, N.S.1
  • 22
    • 0035671826 scopus 로고    scopus 로고
    • Elevated serum bone sialoprotein and osteopontin in colon, breast, prostate, and lung cancer
    • N.S. Fedarko Elevated serum bone sialoprotein and osteopontin in colon, breast, prostate, and lung cancer Clin. Cancer Res. 7 2001 4060 4066
    • (2001) Clin. Cancer Res. , vol.7 , pp. 4060-4066
    • Fedarko, N.S.1
  • 23
    • 0035808779 scopus 로고    scopus 로고
    • Enhancement of osteoclastic bone resorption and suppression of osteoblastic bone formation in response to reduced mechanical stress do not occur in the absence of osteopontin
    • M. Ishijima Enhancement of osteoclastic bone resorption and suppression of osteoblastic bone formation in response to reduced mechanical stress do not occur in the absence of osteopontin J. Exp. Med. 193 2001 399 404
    • (2001) J. Exp. Med. , vol.193 , pp. 399-404
    • Ishijima, M.1
  • 24
    • 12244312775 scopus 로고    scopus 로고
    • Osteopontin deficiency produces osteoclast dysfunction due to reduced CD44 surface expression
    • M.A. Chellaiah Osteopontin deficiency produces osteoclast dysfunction due to reduced CD44 surface expression Mol. Biol. Cell 14 2003 173 189
    • (2003) Mol. Biol. Cell , vol.14 , pp. 173-189
    • Chellaiah, M.A.1
  • 25
    • 0042388491 scopus 로고    scopus 로고
    • Osteopontin facilitates bone resorption, decreasing bone mineral crystallinity and content during calcium deficiency
    • S.A. Shapses Osteopontin facilitates bone resorption, decreasing bone mineral crystallinity and content during calcium deficiency Calcif. Tissue Int. 73 2003 86 92
    • (2003) Calcif. Tissue Int. , vol.73 , pp. 86-92
    • Shapses, S.A.1
  • 26
    • 5644241735 scopus 로고    scopus 로고
    • Altered vascular remodeling in osteopontin-deficient atherosclerotic mice
    • A. Strom Altered vascular remodeling in osteopontin-deficient atherosclerotic mice J. Vasc. Res. 41 2004 314 322
    • (2004) J. Vasc. Res. , vol.41 , pp. 314-322
    • Strom, A.1
  • 27
    • 0037072456 scopus 로고    scopus 로고
    • Fibroblast growth factor receptor-1 signaling induces osteopontin expression and vascular smooth muscle cell-dependent adventitial fibroblast migration in vitro
    • G. Li Fibroblast growth factor receptor-1 signaling induces osteopontin expression and vascular smooth muscle cell-dependent adventitial fibroblast migration in vitro Circulation 106 2002 854 859
    • (2002) Circulation , vol.106 , pp. 854-859
    • Li, G.1
  • 28
    • 22344448703 scopus 로고    scopus 로고
    • Mitigation of ectopic calcification in osteopontin-deficient mice by exogenous osteopontin
    • R. Ohri Mitigation of ectopic calcification in osteopontin-deficient mice by exogenous osteopontin Calcif. Tissue Int. 76 2005 307 315
    • (2005) Calcif. Tissue Int. , vol.76 , pp. 307-315
    • Ohri, R.1
  • 29
    • 17644398457 scopus 로고    scopus 로고
    • Regulation of vascular calcification: Roles of phosphate and osteopontin
    • C.M. Giachelli Regulation of vascular calcification: roles of phosphate and osteopontin Circ. Res. 96 2005 717 722
    • (2005) Circ. Res. , vol.96 , pp. 717-722
    • Giachelli, C.M.1
  • 30
    • 5644276291 scopus 로고    scopus 로고
    • Osteopontin as a mediator of NKT cell function in T cell-mediated liver diseases
    • H. Diao Osteopontin as a mediator of NKT cell function in T cell-mediated liver diseases Immunity 21 2004 539 550
    • (2004) Immunity , vol.21 , pp. 539-550
    • Diao, H.1
  • 31
    • 23044431647 scopus 로고    scopus 로고
    • Osteopontin functionally activates dendritic cells and induces their differentiation toward a Th1-polarizing phenotype
    • A.C. Renkl Osteopontin functionally activates dendritic cells and induces their differentiation toward a Th1-polarizing phenotype Blood 106 2005 946 955
    • (2005) Blood , vol.106 , pp. 946-955
    • Renkl, A.C.1
  • 32
    • 0034603119 scopus 로고    scopus 로고
    • Eta-1 (osteopontin): An early component of type-1 (cell-mediated) immunity
    • S. Ashkar Eta-1 (osteopontin): an early component of type-1 (cell-mediated) immunity Science 287 2000 860 864
    • (2000) Science , vol.287 , pp. 860-864
    • Ashkar, S.1
  • 33
    • 0032407735 scopus 로고    scopus 로고
    • Introduction of an osteopontin gene confers the increase in B1 cell population and the production of anti-DNA autoantibodies
    • J. Iizuka Introduction of an osteopontin gene confers the increase in B1 cell population and the production of anti-DNA autoantibodies Lab. Invest. 78 1998 1523 1533
    • (1998) Lab. Invest. , vol.78 , pp. 1523-1533
    • Iizuka, J.1
  • 34
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • E.A. Clark, and J.S. Brugge Integrins and signal transduction pathways: the road taken Science 268 1995 233 239
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 35
    • 0036488589 scopus 로고    scopus 로고
    • Role of integrins in cell invasion and migration
    • J.D. Hood, and D. Cheresh Role of integrins in cell invasion and migration Nat. Rev. Cancer 2 2002 91 100
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 91-100
    • Hood, J.D.1    Cheresh, D.2
  • 36
    • 0141542626 scopus 로고    scopus 로고
    • Beta(3) integrin expression increases breast carcinoma cell responsiveness to the malignancy-enhancing effects of osteopontin
    • K.A. Furger Beta(3) integrin expression increases breast carcinoma cell responsiveness to the malignancy-enhancing effects of osteopontin Mol. Cancer Res. 1 2003 810 819
    • (2003) Mol. Cancer Res. , vol.1 , pp. 810-819
    • Furger, K.A.1
  • 37
    • 0033579511 scopus 로고    scopus 로고
    • The integrin alpha 9 beta 1 binds to a novel recognition sequence SVVYGLR in the thrombin cleaved amino terminal fragment of osteopontin
    • Y. Yokosaki The integrin alpha 9 beta 1 binds to a novel recognition sequence SVVYGLR in the thrombin cleaved amino terminal fragment of osteopontin J. Biol. Chem. 274 1999 36328 36334
    • (1999) J. Biol. Chem. , vol.274 , pp. 36328-36334
    • Yokosaki, Y.1
  • 38
    • 0034238108 scopus 로고    scopus 로고
    • Analysis of the alpha 4 beta 1 integrin-osteopontin interaction
    • S. Barry Analysis of the alpha 4 beta 1 integrin-osteopontin interaction Exp. Cell Res. 258 2000 342 351
    • (2000) Exp. Cell Res. , vol.258 , pp. 342-351
    • Barry, S.1
  • 39
    • 0032926684 scopus 로고    scopus 로고
    • CD44 variants but not CD44s cooperate with beta 1-containing integrins to permit cells to bind to osteopontin independently of arginine-glycine- aspartic acid, thereby stimulating cell motility and chemotaxis
    • Y.U. Katagiri CD44 variants but not CD44s cooperate with beta 1-containing integrins to permit cells to bind to osteopontin independently of arginine-glycine- aspartic acid, thereby stimulating cell motility and chemotaxis Cancer Res. 59 1999 219 226
    • (1999) Cancer Res. , vol.59 , pp. 219-226
    • Katagiri, Y.U.1
  • 40
    • 3042738008 scopus 로고    scopus 로고
    • Hyaluronan facilitates invasion of colon carcinoma cells in vitro via interaction with CD44
    • H.R. Kim Hyaluronan facilitates invasion of colon carcinoma cells in vitro via interaction with CD44 Cancer Res. 64 2004 4569 4576
    • (2004) Cancer Res. , vol.64 , pp. 4569-4576
    • Kim, H.R.1
  • 41
    • 13244284603 scopus 로고    scopus 로고
    • Autocrine activation of an osteopontin-CD44-Rac pathway enhances invasion and transformation by H-RasV12
    • T. Hidemi Autocrine activation of an osteopontin-CD44-Rac pathway enhances invasion and transformation by H-RasV12 Oncogene 24 2005 489 501
    • (2005) Oncogene , vol.24 , pp. 489-501
    • Hidemi, T.1
  • 42
    • 7244248554 scopus 로고    scopus 로고
    • Enhanced expression of CD44 variants in human atheroma and abdominal aortic aneurysm: Possible role for a feedback loop in endothelial cells
    • A. Krettek Enhanced expression of CD44 variants in human atheroma and abdominal aortic aneurysm: possible role for a feedback loop in endothelial cells Am. J. Pathol. 165 2004 1571 1581
    • (2004) Am. J. Pathol. , vol.165 , pp. 1571-1581
    • Krettek, A.1
  • 43
    • 0035824560 scopus 로고    scopus 로고
    • The osteopontin-CD44 survival signal involves activation of the phosphatidylinositol 3-kinase/Akt signaling pathway
    • Y.H. Lin, and H.F. Yang-Yen The osteopontin-CD44 survival signal involves activation of the phosphatidylinositol 3-kinase/Akt signaling pathway J. Biol. Chem. 276 2001 46024 46030
    • (2001) J. Biol. Chem. , vol.276 , pp. 46024-46030
    • Lin, Y.H.1    Yang-Yen, H.F.2
  • 44
    • 13544263379 scopus 로고    scopus 로고
    • CD44 cross-linking induces integrin-mediated adhesion and transendothelial migration in breast cancer cell line by up-regulation of LFA-1 (alpha L beta2) and VLA-4 (alpha4 beta1)
    • H.S. Wang CD44 cross-linking induces integrin-mediated adhesion and transendothelial migration in breast cancer cell line by up-regulation of LFA-1 (alpha L beta2) and VLA-4 (alpha4 beta1) Exp. Cell Res. 304 2005 116 126
    • (2005) Exp. Cell Res. , vol.304 , pp. 116-126
    • Wang, H.S.1
  • 45
    • 15544389207 scopus 로고    scopus 로고
    • Novel insights into c-Src
    • O. Alper, and E.T. Bowden Novel insights into c-Src Curr. Pharm. Des. 11 2005 1119 1130
    • (2005) Curr. Pharm. Des. , vol.11 , pp. 1119-1130
    • Alper, O.1    Bowden, E.T.2
  • 46
    • 0034941053 scopus 로고    scopus 로고
    • Pp60 (c-Src) and related tyrosine kinases: A role in the assembly and reorganization of matrix adhesion
    • T. Volberg pp60 (c-Src) and related tyrosine kinases: a role in the assembly and reorganization of matrix adhesion J. Cell Sci. 114 2001 2279 2289
    • (2001) J. Cell Sci. , vol.114 , pp. 2279-2289
    • Volberg, T.1
  • 47
    • 0037088647 scopus 로고    scopus 로고
    • Integrin-induced epidermal growth factor (EGF) receptor activation requires c-Src and p130 Cas and leads to phosphorylation of specific EGF receptor tyrosines
    • L. Moro Integrin-induced epidermal growth factor (EGF) receptor activation requires c-Src and p130 Cas and leads to phosphorylation of specific EGF receptor tyrosines J. Biol. Chem. 277 2002 9405 9414
    • (2002) J. Biol. Chem. , vol.277 , pp. 9405-9414
    • Moro, L.1
  • 48
    • 1642565264 scopus 로고    scopus 로고
    • Osteopontin induces AP-1 mediated secretion of urokinase type plasminogen activator through c-Src dependent epidermal growth factor receptor transactivation in breast cancer cells
    • R. Das Osteopontin induces AP-1 mediated secretion of urokinase type plasminogen activator through c-Src dependent epidermal growth factor receptor transactivation in breast cancer cells J. Biol. Chem. 279 2004 11051 11064
    • (2004) J. Biol. Chem. , vol.279 , pp. 11051-11064
    • Das, R.1
  • 49
    • 0037468265 scopus 로고    scopus 로고
    • Osteopontin-induced migration of human mammary epithelial cells involves activation of EGF receptor and multiple signal transduction pathways
    • A.B. Tuck Osteopontin-induced migration of human mammary epithelial cells involves activation of EGF receptor and multiple signal transduction pathways Oncogene 22 2003 1198 1205
    • (2003) Oncogene , vol.22 , pp. 1198-1205
    • Tuck, A.B.1
  • 50
    • 0034773992 scopus 로고    scopus 로고
    • The EGFR family and its ligands in human cancer. Signalling mechanisms and therapeutic opportunities
    • Y. Yarden The EGFR family and its ligands in human cancer. Signalling mechanisms and therapeutic opportunities Eur. J. Cancer 37 Suppl. 4 2001 S3 S8
    • (2001) Eur. J. Cancer , vol.37 , Issue.SUPPL. 4
    • Yarden, Y.1
  • 51
    • 18344390418 scopus 로고    scopus 로고
    • ERB B receptors and cancer: The complexity of targeted inhibitors
    • N.E. Hynes, and H.A. Lane ERB B receptors and cancer: the complexity of targeted inhibitors Nat. Rev. Cancer 5 2005 341 354
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 341-354
    • Hynes, N.E.1    Lane, H.A.2
  • 52
    • 0042709227 scopus 로고    scopus 로고
    • Osteopontin stimulates cell motility and nuclear factor-κB mediated secretion of urokinase type plasminogen activator through phosphotidylinositol 3-kinase/Akt signaling pathways in breast cancer cells
    • R. Das Osteopontin stimulates cell motility and nuclear factor-κB mediated secretion of urokinase type plasminogen activator through phosphotidylinositol 3-kinase/Akt signaling pathways in breast cancer cells J. Biol. Chem. 278 2003 28593 28606
    • (2003) J. Biol. Chem. , vol.278 , pp. 28593-28606
    • Das, R.1
  • 53
    • 0036185848 scopus 로고    scopus 로고
    • The protein kinase B/Akt signaling pathway in human malignancy
    • K.M. Nicholson, and N.G. Anderson The protein kinase B/Akt signaling pathway in human malignancy Cell. Signal. 14 2002 381 395
    • (2002) Cell. Signal. , vol.14 , pp. 381-395
    • Nicholson, K.M.1    Anderson, N.G.2
  • 54
    • 1642617693 scopus 로고    scopus 로고
    • PI 3K/Akt signaling pathway and cancer
    • J.A. Fresno Vara PI 3K/Akt signaling pathway and cancer Cancer Treat. Rev. 30 2004 193 204
    • (2004) Cancer Treat. Rev. , vol.30 , pp. 193-204
    • Fresno Vara, J.A.1
  • 55
    • 0037799253 scopus 로고    scopus 로고
    • PTEN regulates RANKL- and OPN-stimulated signal transduction during osteoclast differentiation and cell motility
    • T. Sugatani PTEN regulates RANKL- and OPN-stimulated signal transduction during osteoclast differentiation and cell motility J. Biol. Chem. 278 2003 5001 5008
    • (2003) J. Biol. Chem. , vol.278 , pp. 5001-5008
    • Sugatani, T.1
  • 56
    • 0031017618 scopus 로고    scopus 로고
    • MAP3K-related kinase involved in NF kappa B induction by TNF, CD95 and IL-1
    • N.L. Malinin MAP3K-related kinase involved in NF kappa B induction by TNF, CD95 and IL-1 Nature 385 1997 540 544
    • (1997) Nature , vol.385 , pp. 540-544
    • Malinin, N.L.1
  • 57
    • 0036098552 scopus 로고    scopus 로고
    • AP-1 as a regulator of cell life and death
    • E. Shaulian, and M. Karin AP-1 as a regulator of cell life and death Nat. Cell Biol. 4 2002 E131 E136
    • (2002) Nat. Cell Biol. , vol.4
    • Shaulian, E.1    Karin, M.2
  • 58
    • 4644231399 scopus 로고    scopus 로고
    • Nuclear factor inducing kinase plays a crucial role in osteopontin induced MAPK/IκBα kinase dependent nuclear factor- κb mediated promatrix metalloproteinase-9 activation
    • H. Rangaswami Nuclear factor inducing kinase plays a crucial role in osteopontin induced MAPK/IκBα kinase dependent nuclear factor- κB mediated promatrix metalloproteinase-9 activation J. Biol. Chem. 279 2004 38921 38935
    • (2004) J. Biol. Chem. , vol.279 , pp. 38921-38935
    • Rangaswami, H.1
  • 59
    • 21444454134 scopus 로고    scopus 로고
    • JNK1 differentially regulates osteopontin induced nuclear factor inducing kinase/MEKK1 dependent activating protein-1-mediated promatrix metalloproteinase-9 activation
    • H. Rangaswami JNK1 differentially regulates osteopontin induced nuclear factor inducing kinase/MEKK1 dependent activating protein-1-mediated promatrix metalloproteinase-9 activation J. Biol. Chem. 280 2005 19381 19392
    • (2005) J. Biol. Chem. , vol.280 , pp. 19381-19392
    • Rangaswami, H.1
  • 60
    • 0038575443 scopus 로고    scopus 로고
    • Extracellular matrix remodelling: The role of matrix metalloproteinases
    • I. Stamenkovic Extracellular matrix remodelling: the role of matrix metalloproteinases J. Pathol. 200 2003 448 464
    • (2003) J. Pathol. , vol.200 , pp. 448-464
    • Stamenkovic, I.1
  • 61
    • 3042743709 scopus 로고    scopus 로고
    • The urokinase receptor as a potential target in cancer therapy
    • J. Romer The urokinase receptor as a potential target in cancer therapy Curr. Pharm. Des. 10 2004 2359 2376
    • (2004) Curr. Pharm. Des. , vol.10 , pp. 2359-2376
    • Romer, J.1
  • 62
    • 0032479268 scopus 로고    scopus 로고
    • Activation of MMP-2 by human GCT23 giant cell tumour cells induced by osteopontin, bone sialoprotein and GRGDSP peptides is RGD and cell shape change dependent
    • A. Teti Activation of MMP-2 by human GCT23 giant cell tumour cells induced by osteopontin, bone sialoprotein and GRGDSP peptides is RGD and cell shape change dependent Int. J. Cancer 77 1998 82 93
    • (1998) Int. J. Cancer , vol.77 , pp. 82-93
    • Teti, A.1
  • 63
    • 0037105704 scopus 로고    scopus 로고
    • Promotion of malignant astrocytoma cell migration by osteopontin expressed in the normal brain: Differences in integrin signaling during cell adhesion to osteopontin versus vitronectin
    • Q. Ding Promotion of malignant astrocytoma cell migration by osteopontin expressed in the normal brain: differences in integrin signaling during cell adhesion to osteopontin versus vitronectin Cancer Res. 62 2002 5336 5343
    • (2002) Cancer Res. , vol.62 , pp. 5336-5343
    • Ding, Q.1
  • 64
    • 0038191064 scopus 로고    scopus 로고
    • Osteopontin induces nuclear factor-κB mediated promatrix metalloproteinase-2 activation through I kappa B alpha/IKK signaling pathways and curcumin (diferulolylmethane) downregulates these pathways
    • S. Philip, and G.C. Kundu Osteopontin induces nuclear factor-κB mediated promatrix metalloproteinase-2 activation through I kappa B alpha/IKK signaling pathways and curcumin (diferulolylmethane) downregulates these pathways J. Biol. Chem. 278 2003 14487 14497
    • (2003) J. Biol. Chem. , vol.278 , pp. 14487-14497
    • Philip, S.1    Kundu, G.C.2
  • 65
    • 20944437231 scopus 로고    scopus 로고
    • The gene expression signatures of melanoma progression
    • C. Haqq The gene expression signatures of melanoma progression Proc. Natl. Acad. Sci. U. S. A. 102 2005 6092 6097
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 6092-6097
    • Haqq, C.1
  • 66
    • 6344258588 scopus 로고    scopus 로고
    • The role of osteopontin in tumor metastasis
    • P.Y. Wai, and P.C. Kuo The role of osteopontin in tumor metastasis J. Surg. Res. 121 2004 228 241
    • (2004) J. Surg. Res. , vol.121 , pp. 228-241
    • Wai, P.Y.1    Kuo, P.C.2
  • 67
    • 0034085531 scopus 로고    scopus 로고
    • Osteopontin is required for full expression of the transformed phenotype by the ras oncogene
    • Y. Wu Osteopontin is required for full expression of the transformed phenotype by the ras oncogene Br. J. Cancer 83 2000 156 163
    • (2000) Br. J. Cancer , vol.83 , pp. 156-163
    • Wu, Y.1
  • 68
    • 17844388876 scopus 로고    scopus 로고
    • Osteopontin silencing by small interfering RNA suppresses in vitro and in vivo CT26 murine colon adenocarcinoma metastasis
    • P.Y. Wai Osteopontin silencing by small interfering RNA suppresses in vitro and in vivo CT26 murine colon adenocarcinoma metastasis Carcinogenesis 26 2005 741 751
    • (2005) Carcinogenesis , vol.26 , pp. 741-751
    • Wai, P.Y.1
  • 69
    • 18244383027 scopus 로고    scopus 로고
    • Osteopontin expression correlates with melanoma invasion
    • D. Denhardt Osteopontin expression correlates with melanoma invasion J. Invest. Dermatol. 124 2005 16 18
    • (2005) J. Invest. Dermatol. , vol.124 , pp. 16-18
    • Denhardt, D.1
  • 70
    • 0037102376 scopus 로고    scopus 로고
    • Autocrine stimulation of osteopontin contributes to antiapoptotic signalling of melanocytes in dermal collagen
    • E. Geissinger Autocrine stimulation of osteopontin contributes to antiapoptotic signalling of melanocytes in dermal collagen Cancer Res. 62 2002 4820 4828
    • (2002) Cancer Res. , vol.62 , pp. 4820-4828
    • Geissinger, E.1
  • 71
    • 0034596062 scopus 로고    scopus 로고
    • Factor H binding to bone sialoprotein and osteopontin enables tumor cell evasion of complement-mediated attack
    • N.S. Fedarko Factor H binding to bone sialoprotein and osteopontin enables tumor cell evasion of complement-mediated attack J. Biol. Chem. 275 2000 16666 16672
    • (2000) J. Biol. Chem. , vol.275 , pp. 16666-16672
    • Fedarko, N.S.1
  • 72
    • 0036243138 scopus 로고    scopus 로고
    • Soluble osteopontin inhibits apoptosis of adherent endothelial cells deprived of growth factors
    • S.A. Khan Soluble osteopontin inhibits apoptosis of adherent endothelial cells deprived of growth factors J. Cell. Biochem. 85 2002 728 736
    • (2002) J. Cell. Biochem. , vol.85 , pp. 728-736
    • Khan, S.A.1
  • 73
    • 4744354624 scopus 로고    scopus 로고
    • Increased cell death in osteopontin-deficient cardiac fibroblasts occurs by a caspase-3-independent pathway
    • R. Zohar Increased cell death in osteopontin-deficient cardiac fibroblasts occurs by a caspase-3-independent pathway Am. J. Physiol. Heart Circ. Physiol. 287 2004 H1730 H1739
    • (2004) Am. J. Physiol. Heart Circ. Physiol. , vol.287
    • Zohar, R.1
  • 74
    • 1542467581 scopus 로고    scopus 로고
    • Osteopontin inhibits interleukin-1 beta-stimulated increases in matrix metalloproteinase activity in adult rat cardiac fibroblasts: Role of protein kinase C-zeta
    • Z. Xie Osteopontin inhibits interleukin-1 beta-stimulated increases in matrix metalloproteinase activity in adult rat cardiac fibroblasts: role of protein kinase C-zeta J. Biol. Chem. 278 2003 48546 48552
    • (2003) J. Biol. Chem. , vol.278 , pp. 48546-48552
    • Xie, Z.1
  • 75
    • 0027932153 scopus 로고
    • Inhibition of Arg-Gly-Asp (RGD)-mediated cell adhesion to osteopontin by a monoclonal antibody against osteopontin
    • D.S. Bautista Inhibition of Arg-Gly-Asp (RGD)-mediated cell adhesion to osteopontin by a monoclonal antibody against osteopontin J. Biol. Chem. 269 1994 23280 23285
    • (1994) J. Biol. Chem. , vol.269 , pp. 23280-23285
    • Bautista, D.S.1
  • 76
    • 0034637509 scopus 로고    scopus 로고
    • Substrate specificity of alpha(v)beta(3) integrin-mediated cell migration and phosphatidylinositol 3-kinase/AKT pathway activation
    • D.Q. Zheng Substrate specificity of alpha(v)beta(3) integrin-mediated cell migration and phosphatidylinositol 3-kinase/AKT pathway activation J. Biol. Chem. 275 2000 24565 24574
    • (2000) J. Biol. Chem. , vol.275 , pp. 24565-24574
    • Zheng, D.Q.1
  • 77
    • 0031983123 scopus 로고    scopus 로고
    • Intact vitronectin induces matrix metalloproteinase-2 and tissue inhibitor of metalloproteinases-2 expression and enhanced cellular invasion by melanoma cells
    • L.M. Bafetti Intact vitronectin induces matrix metalloproteinase-2 and tissue inhibitor of metalloproteinases-2 expression and enhanced cellular invasion by melanoma cells J. Biol. Chem. 273 1998 143 149
    • (1998) J. Biol. Chem. , vol.273 , pp. 143-149
    • Bafetti, L.M.1
  • 78
    • 0031127344 scopus 로고    scopus 로고
    • Isolation and biological properties of osteopontin from bovine milk
    • K.J. Bayless Isolation and biological properties of osteopontin from bovine milk Protein Expr. Purif. 9 1997 309 314
    • (1997) Protein Expr. Purif. , vol.9 , pp. 309-314
    • Bayless, K.J.1
  • 79
    • 0035976914 scopus 로고    scopus 로고
    • Osteopontin stimulates tumor growth and activation of promatrix metalloproteinase-2 through nuclear factor-κB-mediated induction of membrane type-1 matrix metalloproteinase in murine melanoma cells
    • S. Philip Osteopontin stimulates tumor growth and activation of promatrix metalloproteinase-2 through nuclear factor-κB-mediated induction of membrane type-1 matrix metalloproteinase in murine melanoma cells J. Biol. Chem. 276 2001 44926 44935
    • (2001) J. Biol. Chem. , vol.276 , pp. 44926-44935
    • Philip, S.1
  • 80
    • 21344474104 scopus 로고    scopus 로고
    • Osteopontin, a key component of the hematopoietic stem cell niche and regulator of primitive hematopoietic progenitor cells
    • S.K. Nilsson Osteopontin, a key component of the hematopoietic stem cell niche and regulator of primitive hematopoietic progenitor cells Blood 106 2005 1232 1239
    • (2005) Blood , vol.106 , pp. 1232-1239
    • Nilsson, S.K.1


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