메뉴 건너뛰기




Volumn 37, Issue 7, 2011, Pages 559-566

Anti-cancer role of SPARC, an inhibitor of adipogenesis

Author keywords

Adipogenesis; Cancer; SPARC

Indexed keywords

COLLAGENASE 3; GELATINASE A; MATRILYSIN; OSTEONECTIN; PLASMIN; STROMELYSIN; TRYPSIN;

EID: 79960025480     PISSN: 03057372     EISSN: 15321967     Source Type: Journal    
DOI: 10.1016/j.ctrv.2010.12.001     Document Type: Review
Times cited : (64)

References (124)
  • 1
    • 63449135077 scopus 로고    scopus 로고
    • MicroRNA-199b-5p impairs cancer stem cells through negative regulation of HES1 in medulloblastoma
    • Garzia L., Andolfo I., Cusanelli E., Marino N., Petrosino G., De Martino D., et al. MicroRNA-199b-5p impairs cancer stem cells through negative regulation of HES1 in medulloblastoma. PLoS One 2009, 4:e4998.
    • (2009) PLoS One , vol.4
    • Garzia, L.1    Andolfo, I.2    Cusanelli, E.3    Marino, N.4    Petrosino, G.5    De Martino, D.6
  • 2
    • 34248637891 scopus 로고    scopus 로고
    • Outcome of children with posterior fossa medulloblastoma: a single institution experience over the decade 1994-2003
    • Kombogiorgas D., Sgouros S., Walsh A., Hockley A., Stevens M., Grundy R., et al. Outcome of children with posterior fossa medulloblastoma: a single institution experience over the decade 1994-2003. Child's Nerv Sys 2007, 23:399-405.
    • (2007) Child's Nerv Sys , vol.23 , pp. 399-405
    • Kombogiorgas, D.1    Sgouros, S.2    Walsh, A.3    Hockley, A.4    Stevens, M.5    Grundy, R.6
  • 3
    • 20344387015 scopus 로고    scopus 로고
    • Radiation-induced cerebellar glioblastoma at the site of a treated medulloblastoma
    • Yang S., Wang K., Cho B., Kim Y., Lim S., Park S., et al. Radiation-induced cerebellar glioblastoma at the site of a treated medulloblastoma. J Neurosurg: Pediat 2005, 102:417-422.
    • (2005) J Neurosurg: Pediat , vol.102 , pp. 417-422
    • Yang, S.1    Wang, K.2    Cho, B.3    Kim, Y.4    Lim, S.5    Park, S.6
  • 4
    • 60749137517 scopus 로고    scopus 로고
    • RNAi-mediated downregulation of radiation-induced MMP-9 leads to apoptosis via activation of ERK and Akt in IOMM-Lee cells
    • Gogineni V., Kargiotis O., Klopfenstein J., Gujrati M., Dinh D., Rao J. RNAi-mediated downregulation of radiation-induced MMP-9 leads to apoptosis via activation of ERK and Akt in IOMM-Lee cells. Inte J Oncol 2009, 34:209-218.
    • (2009) Inte J Oncol , vol.34 , pp. 209-218
    • Gogineni, V.1    Kargiotis, O.2    Klopfenstein, J.3    Gujrati, M.4    Dinh, D.5    Rao, J.6
  • 6
    • 47949132157 scopus 로고    scopus 로고
    • The role of the matricellular protein SPARC in the dynamic interaction between the tumor and the host
    • Podhajcer O., Benedetti L., Girotti M., Prada F., Salvatierra E., Llera A. The role of the matricellular protein SPARC in the dynamic interaction between the tumor and the host. Cancer Metastasis Rev 2008, 27:691-705.
    • (2008) Cancer Metastasis Rev , vol.27 , pp. 691-705
    • Podhajcer, O.1    Benedetti, L.2    Girotti, M.3    Prada, F.4    Salvatierra, E.5    Llera, A.6
  • 7
    • 0025823515 scopus 로고
    • Extracellular proteins that modulate cell-matrix interactions. SPARC, tenascin, and thrombospondin
    • Sage E., Bornstein P. Extracellular proteins that modulate cell-matrix interactions. SPARC, tenascin, and thrombospondin. J Biol Chem 1991, 266:14831-14834.
    • (1991) J Biol Chem , vol.266 , pp. 14831-14834
    • Sage, E.1    Bornstein, P.2
  • 8
    • 0022542156 scopus 로고
    • Bramson R: Endothelial cell injury in vitro is associated with increased secretion of an Mr 43, 000 glycoprotein ligand
    • Sage E., Tupper J. Bramson R: Endothelial cell injury in vitro is associated with increased secretion of an Mr 43, 000 glycoprotein ligand. J Cell Physiol 1986, 127:373-387.
    • (1986) J Cell Physiol , vol.127 , pp. 373-387
    • Sage, E.1    Tupper, J.2
  • 9
    • 0021323613 scopus 로고
    • Characterization of a novel serum albumin-binding glycoprotein secreted by endothelial cells in culture
    • Sage H., Johnson C., Bornstein P. Characterization of a novel serum albumin-binding glycoprotein secreted by endothelial cells in culture. J Biol Chem 1984, 259:3993-4007.
    • (1984) J Biol Chem , vol.259 , pp. 3993-4007
    • Sage, H.1    Johnson, C.2    Bornstein, P.3
  • 11
    • 0029142749 scopus 로고
    • Distribution of SPARC in normal and neoplastic human tissue
    • Porter P., Sage E., Lane T., Funk S., Gown A. Distribution of SPARC in normal and neoplastic human tissue. J Histochem Cytochem 1995, 43:791-800.
    • (1995) J Histochem Cytochem , vol.43 , pp. 791-800
    • Porter, P.1    Sage, E.2    Lane, T.3    Funk, S.4    Gown, A.5
  • 12
    • 0032984442 scopus 로고    scopus 로고
    • Cell cycle-dependent nuclear location of the matricellular protein SPARC: association with the nuclear matrix
    • Gooden M., Vernon R., Bassuk J., Sage E. Cell cycle-dependent nuclear location of the matricellular protein SPARC: association with the nuclear matrix. J Cell Biochem 1999, 74:152-167.
    • (1999) J Cell Biochem , vol.74 , pp. 152-167
    • Gooden, M.1    Vernon, R.2    Bassuk, J.3    Sage, E.4
  • 13
    • 0027082811 scopus 로고
    • The extracellular regulation of growth factor action
    • Flaumenhaft R., Rifkin D. The extracellular regulation of growth factor action. Mol Biol Cell 1992, 3:1057-1065.
    • (1992) Mol Biol Cell , vol.3 , pp. 1057-1065
    • Flaumenhaft, R.1    Rifkin, D.2
  • 14
    • 0024439457 scopus 로고
    • How does extracellular matrix control capillary morphogenesis
    • Ingber D., Folkman J. How does extracellular matrix control capillary morphogenesis. Cell 1989, 58:803-805.
    • (1989) Cell , vol.58 , pp. 803-805
    • Ingber, D.1    Folkman, J.2
  • 15
    • 0024315634 scopus 로고
    • Mechanochemical switching between growth and differentiation during fibroblast growth factor-stimulated angiogenesis in vitro: role of extracellular matrix
    • Ingber D., Folkman J. Mechanochemical switching between growth and differentiation during fibroblast growth factor-stimulated angiogenesis in vitro: role of extracellular matrix. J Cell Biol 1989, 109:317-330.
    • (1989) J Cell Biol , vol.109 , pp. 317-330
    • Ingber, D.1    Folkman, J.2
  • 16
    • 0025372477 scopus 로고
    • Fibronectin controls capillary endothelial cell growth by modulating cell shape
    • Ingber D. Fibronectin controls capillary endothelial cell growth by modulating cell shape. Proc Nat Acad Sci USA 1990, 87:3579-3583.
    • (1990) Proc Nat Acad Sci USA , vol.87 , pp. 3579-3583
    • Ingber, D.1
  • 17
    • 0033104891 scopus 로고    scopus 로고
    • Disruption of the SparcLocus in mice alters the differentiation of lenticular epithelial cells and leads to cataract formation
    • Bassuk J.A., Birkebak T.E.D., Rothmier J.D., Clark J.M., Bradshaw A.M.Y., Muchowski P.J., et al. Disruption of the SparcLocus in mice alters the differentiation of lenticular epithelial cells and leads to cataract formation. Exp Eye Res 1999, 68:321-331.
    • (1999) Exp Eye Res , vol.68 , pp. 321-331
    • Bassuk, J.A.1    Birkebak, T.E.D.2    Rothmier, J.D.3    Clark, J.M.4    Bradshaw, A.M.Y.5    Muchowski, P.J.6
  • 18
    • 20444461133 scopus 로고    scopus 로고
    • Genome-wide expression analysis of therapy-resistant tumors reveals SPARC as a novel target for cancer therapy
    • Tai I., Dai M., Owen D., Chen L. Genome-wide expression analysis of therapy-resistant tumors reveals SPARC as a novel target for cancer therapy. J Clin Invest 2005, 115:1492-1502.
    • (2005) J Clin Invest , vol.115 , pp. 1492-1502
    • Tai, I.1    Dai, M.2    Owen, D.3    Chen, L.4
  • 19
    • 0028887451 scopus 로고    scopus 로고
    • SPARC mediates focal adhesion disassembly in endothelial cells through a follistatin-like region and the Ca2+-binding EF-hand
    • Murphy-Ullrich J., Lane T., Pallero M., Sage E. SPARC mediates focal adhesion disassembly in endothelial cells through a follistatin-like region and the Ca2+-binding EF-hand. J Cell Biochem 2004, 57:341-350.
    • (2004) J Cell Biochem , vol.57 , pp. 341-350
    • Murphy-Ullrich, J.1    Lane, T.2    Pallero, M.3    Sage, E.4
  • 20
    • 0027308138 scopus 로고
    • Modulation of SPARC expression during butyrate-induced terminal differentiation of cultured human keratinocytes: regulation via a TGF-(β)-dependent pathway
    • Ford R., Wang G., Jannati P., Adler D., Racanelli P., Higgins P., et al. Modulation of SPARC expression during butyrate-induced terminal differentiation of cultured human keratinocytes: regulation via a TGF-(β)-dependent pathway. Exp Cell Res 1993, 206:261-275.
    • (1993) Exp Cell Res , vol.206 , pp. 261-275
    • Ford, R.1    Wang, G.2    Jannati, P.3    Adler, D.4    Racanelli, P.5    Higgins, P.6
  • 21
    • 1842338681 scopus 로고    scopus 로고
    • Limited cleavage of extracellular matrix protein BM-40 by matrix metalloproteinases increases its affinity for collagens
    • Sasaki T., Göhring W., Mann K., Maurer P., Hohenester E., Knäuper V., et al. Limited cleavage of extracellular matrix protein BM-40 by matrix metalloproteinases increases its affinity for collagens. J Biol Chem 1997, 272:9237-9243.
    • (1997) J Biol Chem , vol.272 , pp. 9237-9243
    • Sasaki, T.1    Göhring, W.2    Mann, K.3    Maurer, P.4    Hohenester, E.5    Knäuper, V.6
  • 22
    • 0026500981 scopus 로고
    • The extracellular glycoprotein SPARC interacts with platelet-derived growth factor (PDGF)-AB and -BB and inhibits the binding of PDGF to its receptors
    • Raines E., Lane T., Iruela-Arispe M., Ross R., Sage E.H. The extracellular glycoprotein SPARC interacts with platelet-derived growth factor (PDGF)-AB and -BB and inhibits the binding of PDGF to its receptors. Proc Nat Acad Sci USA 1992, 89:1281-1285.
    • (1992) Proc Nat Acad Sci USA , vol.89 , pp. 1281-1285
    • Raines, E.1    Lane, T.2    Iruela-Arispe, M.3    Ross, R.4    Sage, E.H.5
  • 23
    • 0032491588 scopus 로고    scopus 로고
    • SPARC (BM-40, osteonectin) inhibits the mitogenic effect of vascular endothelial growth factor on microvascular endothelial cells
    • Kupprion C., Motamed K., Sage E. SPARC (BM-40, osteonectin) inhibits the mitogenic effect of vascular endothelial growth factor on microvascular endothelial cells. J Biol Chem 1998, 273:29635-29640.
    • (1998) J Biol Chem , vol.273 , pp. 29635-29640
    • Kupprion, C.1    Motamed, K.2    Sage, E.3
  • 24
    • 0026638285 scopus 로고    scopus 로고
    • SPARC antagonizes the effect of basic fibroblast growth factor on the migration of bovine aortic endothelial cells
    • Hasselaar P., Sage E. SPARC antagonizes the effect of basic fibroblast growth factor on the migration of bovine aortic endothelial cells. J Cell Biochem 2004, 49:272-283.
    • (2004) J Cell Biochem , vol.49 , pp. 272-283
    • Hasselaar, P.1    Sage, E.2
  • 25
    • 0033527654 scopus 로고    scopus 로고
    • SPARC regulates the expression of collagen type I and transforming growth factor-beta1 in mesangial cells
    • Francki A., Bradshaw A., Bassuk J. SPARC regulates the expression of collagen type I and transforming growth factor-beta1 in mesangial cells. J Biol Chem 1999, 274:32145-32152.
    • (1999) J Biol Chem , vol.274 , pp. 32145-32152
    • Francki, A.1    Bradshaw, A.2    Bassuk, J.3
  • 26
    • 33846813508 scopus 로고    scopus 로고
    • Synergism between vitamin D and secreted protein acidic and rich in cysteine-induced apoptosis and growth inhibition results in increased susceptibility of therapy-resistant colorectal cancer cells to chemotherapy
    • Taghizadeh F., Tang M., Tai I. Synergism between vitamin D and secreted protein acidic and rich in cysteine-induced apoptosis and growth inhibition results in increased susceptibility of therapy-resistant colorectal cancer cells to chemotherapy. Mol Cancer Ther 2007, 6:309-317.
    • (2007) Mol Cancer Ther , vol.6 , pp. 309-317
    • Taghizadeh, F.1    Tang, M.2    Tai, I.3
  • 27
    • 0032752257 scopus 로고    scopus 로고
    • SPARC (osteonectin/BM-40)
    • Motamed K. SPARC (osteonectin/BM-40). Int J Biochem Cell Biol 1999, 31:1363-1366.
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 1363-1366
    • Motamed, K.1
  • 28
    • 0033044637 scopus 로고    scopus 로고
    • Machine learning approaches for the prediction of signal peptides and other protein sorting signals
    • Nielsen H., Brunak S., Von Heijne G. Machine learning approaches for the prediction of signal peptides and other protein sorting signals. Protein Eng Design Sele 1999, 12:3-9.
    • (1999) Protein Eng Design Sele , vol.12 , pp. 3-9
    • Nielsen, H.1    Brunak, S.2    Von Heijne, G.3
  • 29
    • 0028839859 scopus 로고
    • The C-terminal portion of BM-40 (SPARC/osteonectin) is an autonomously folding and crystallizable domain that binds calcium and collagen IV
    • Maurer P., Hohenadl C., Hohenester E., Göhring W., Timpl R., Engel J. The C-terminal portion of BM-40 (SPARC/osteonectin) is an autonomously folding and crystallizable domain that binds calcium and collagen IV. J Mol Biol 1995, 253:347-357.
    • (1995) J Mol Biol , vol.253 , pp. 347-357
    • Maurer, P.1    Hohenadl, C.2    Hohenester, E.3    Göhring, W.4    Timpl, R.5    Engel, J.6
  • 30
    • 0029155744 scopus 로고
    • Role of N-linked glycosylation in human osteonectin
    • Xie R., Long G. Role of N-linked glycosylation in human osteonectin. J Biol Chem 1995, 270:23212-23217.
    • (1995) J Biol Chem , vol.270 , pp. 23212-23217
    • Xie, R.1    Long, G.2
  • 31
    • 0035022957 scopus 로고    scopus 로고
    • SPARC, a matricellular protein that functions in cellular differentiation and tissue response to injury
    • Bradshaw A., Sage E. SPARC, a matricellular protein that functions in cellular differentiation and tissue response to injury. J Clin Invest 2001, 107:1049-1054.
    • (2001) J Clin Invest , vol.107 , pp. 1049-1054
    • Bradshaw, A.1    Sage, E.2
  • 32
    • 0032712968 scopus 로고    scopus 로고
    • SPARC, a matricellular glycoprotein with important biological functions
    • Yan Q., Sage E. SPARC, a matricellular glycoprotein with important biological functions. J Histochem Cytochem 1999, 47:1495-1506.
    • (1999) J Histochem Cytochem , vol.47 , pp. 1495-1506
    • Yan, Q.1    Sage, E.2
  • 33
    • 0028355889 scopus 로고
    • SPARC is a source of copper-binding peptides that stimulate angiogenesis
    • Lane T., Iruela-Arispe M., Johnson R., Sage E. SPARC is a source of copper-binding peptides that stimulate angiogenesis. J Cell biol 1994, 125:929-943.
    • (1994) J Cell biol , vol.125 , pp. 929-943
    • Lane, T.1    Iruela-Arispe, M.2    Johnson, R.3    Sage, E.4
  • 34
    • 0022826510 scopus 로고
    • Isolation and chemical characterization of the phosphoproteins of chicken bone matrix: heterogeneity in molecular weight and composition
    • Uchiyama A., Suzuki M., Lefteriou B., Glimcher M. Isolation and chemical characterization of the phosphoproteins of chicken bone matrix: heterogeneity in molecular weight and composition. Biochemistry 1986, 25:7572-7583.
    • (1986) Biochemistry , vol.25 , pp. 7572-7583
    • Uchiyama, A.1    Suzuki, M.2    Lefteriou, B.3    Glimcher, M.4
  • 35
    • 0023643437 scopus 로고
    • Calcium binding domains and calcium-induced conformational transition of SPARC/BM-40/osteonectin, an extracellular glycoprotein expressed in mineralized and nonmineralized tissues
    • Engel J., Taylor W., Paulsson M., Sage H., Hogan B. Calcium binding domains and calcium-induced conformational transition of SPARC/BM-40/osteonectin, an extracellular glycoprotein expressed in mineralized and nonmineralized tissues. Biochemistry 1987, 26:6958-6965.
    • (1987) Biochemistry , vol.26 , pp. 6958-6965
    • Engel, J.1    Taylor, W.2    Paulsson, M.3    Sage, H.4    Hogan, B.5
  • 36
    • 0141509866 scopus 로고    scopus 로고
    • Cleavage of the matricellular protein SPARC by matrix metalloproteinase 3 produces polypeptides that influence angiogenesis
    • Sage E., Reed M., Funk S., Truong T., Steadele M., Puolakkainen P., et al. Cleavage of the matricellular protein SPARC by matrix metalloproteinase 3 produces polypeptides that influence angiogenesis. J Biol Chem 2003, 278:37849-37857.
    • (2003) J Biol Chem , vol.278 , pp. 37849-37857
    • Sage, E.1    Reed, M.2    Funk, S.3    Truong, T.4    Steadele, M.5    Puolakkainen, P.6
  • 37
    • 33751503496 scopus 로고    scopus 로고
    • SPARC and Hevin expression correlate with tumour angiogenesis in hepatocellular carcinoma
    • Lau C., Poon R., Cheung S., Yu W., Fan S. SPARC and Hevin expression correlate with tumour angiogenesis in hepatocellular carcinoma. J Pathol 2006, 210:459-468.
    • (2006) J Pathol , vol.210 , pp. 459-468
    • Lau, C.1    Poon, R.2    Cheung, S.3    Yu, W.4    Fan, S.5
  • 38
    • 0038709289 scopus 로고    scopus 로고
    • Clinical significance of secreted protein acidic and rich in cystein in esophageal carcinoma and its relation to carcinoma progression
    • Yamashita K., Upadhay S., Mimori K., Inoue H., Mori M. Clinical significance of secreted protein acidic and rich in cystein in esophageal carcinoma and its relation to carcinoma progression. Cancer 2003, 97:2412-2419.
    • (2003) Cancer , vol.97 , pp. 2412-2419
    • Yamashita, K.1    Upadhay, S.2    Mimori, K.3    Inoue, H.4    Mori, M.5
  • 39
    • 0036435916 scopus 로고    scopus 로고
    • Localization of SPARC in developing, mature, and chronically injured human allograft kidneys
    • Alpers C., Hudkins K., Segerer S., Sage E., Pichler R., Couser W., et al. Localization of SPARC in developing, mature, and chronically injured human allograft kidneys. Kidney Int 2002, 62:2073-2086.
    • (2002) Kidney Int , vol.62 , pp. 2073-2086
    • Alpers, C.1    Hudkins, K.2    Segerer, S.3    Sage, E.4    Pichler, R.5    Couser, W.6
  • 40
    • 12344334608 scopus 로고    scopus 로고
    • Integrins in bone recognition and metastasis
    • Byzova T. Integrins in bone recognition and metastasis. J Musculosk Neuro Inter 2004, 4:374.
    • (2004) J Musculosk Neuro Inter , vol.4 , pp. 374
    • Byzova, T.1
  • 41
    • 33646484782 scopus 로고    scopus 로고
    • Novel function of alternatively activated macrophages: stabilin-1-mediated clearance of SPARC
    • Kzhyshkowska J., Workman G., Cardo-Vila M., Arap W., Pasqualini R., Gratchev A., et al. Novel function of alternatively activated macrophages: stabilin-1-mediated clearance of SPARC. J Immunol 2006, 176:5825-5832.
    • (2006) J Immunol , vol.176 , pp. 5825-5832
    • Kzhyshkowska, J.1    Workman, G.2    Cardo-Vila, M.3    Arap, W.4    Pasqualini, R.5    Gratchev, A.6
  • 42
    • 49149112969 scopus 로고    scopus 로고
    • Alternatively activated macrophages regulate extracellular levels of the hormone placental lactogen via receptor-mediated uptake and transcytosis
    • Kzhyshkowska J., Gratchev A., Schmuttermaier C., Brundiers H., Krusell L., Mamidi S., et al. Alternatively activated macrophages regulate extracellular levels of the hormone placental lactogen via receptor-mediated uptake and transcytosis. J Immunol 2008, 180:3028-3037.
    • (2008) J Immunol , vol.180 , pp. 3028-3037
    • Kzhyshkowska, J.1    Gratchev, A.2    Schmuttermaier, C.3    Brundiers, H.4    Krusell, L.5    Mamidi, S.6
  • 43
    • 40349103691 scopus 로고    scopus 로고
    • Transcription factor SOX-5 enhances nasopharyngeal carcinoma progression by down-regulating SPARC gene expression
    • Huang D., Lin Y., Jan P., Hwang Y., Liang S., Peng Y., et al. Transcription factor SOX-5 enhances nasopharyngeal carcinoma progression by down-regulating SPARC gene expression. J Pathol 2008, 214:445-455.
    • (2008) J Pathol , vol.214 , pp. 445-455
    • Huang, D.1    Lin, Y.2    Jan, P.3    Hwang, Y.4    Liang, S.5    Peng, Y.6
  • 44
    • 28644450043 scopus 로고    scopus 로고
    • An RNA polymerase II construct synthesizes short-hairpin RNA with a quantitative indicator and mediates highly efficient RNAi
    • Zhou H., Xia X., Xu Z. An RNA polymerase II construct synthesizes short-hairpin RNA with a quantitative indicator and mediates highly efficient RNAi. Nucl Acids Res 2005, 33:e62.
    • (2005) Nucl Acids Res , vol.33
    • Zhou, H.1    Xia, X.2    Xu, Z.3
  • 45
    • 0031027870 scopus 로고    scopus 로고
    • The expression of the secreted protein acidic and rich in cysteine (SPARC) is associated with the neoplastic progression of human melanoma
    • Ledda F., Bravo A.I., Adris S., Bover L., Mordoh J., Podhajcer O.L. The expression of the secreted protein acidic and rich in cysteine (SPARC) is associated with the neoplastic progression of human melanoma. J Invest Dermatol 1997, 108:210-214.
    • (1997) J Invest Dermatol , vol.108 , pp. 210-214
    • Ledda, F.1    Bravo, A.I.2    Adris, S.3    Bover, L.4    Mordoh, J.5    Podhajcer, O.L.6
  • 46
    • 0031797532 scopus 로고    scopus 로고
    • SPARC: a signal of astrocytic neoplastic transformation and reactive response in human primary and xenograft gliomas
    • Rempel S.A., Golembieski W.A., Ge S., Lemke N., Elisevich K., Mikkelsen T., et al. SPARC: a signal of astrocytic neoplastic transformation and reactive response in human primary and xenograft gliomas. J Neuropathol Exp Neurol 1998, 57:1112-1121.
    • (1998) J Neuropathol Exp Neurol , vol.57 , pp. 1112-1121
    • Rempel, S.A.1    Golembieski, W.A.2    Ge, S.3    Lemke, N.4    Elisevich, K.5    Mikkelsen, T.6
  • 48
    • 0034019916 scopus 로고    scopus 로고
    • Differential expression of osteonectin/SPARC during human prostate cancer progression
    • Thomas R., True L.D., Bassuk J.A., Lange P.H., Vessella R.L. Differential expression of osteonectin/SPARC during human prostate cancer progression. Clin Cancer Res 2000, 6:1140-1149.
    • (2000) Clin Cancer Res , vol.6 , pp. 1140-1149
    • Thomas, R.1    True, L.D.2    Bassuk, J.A.3    Lange, P.H.4    Vessella, R.L.5
  • 49
    • 30044445818 scopus 로고    scopus 로고
    • Survey of differentially methylated promoters in prostate cancer cell lines
    • Wang Y., Yu Q., Cho A., Rondeau G., Welsh J., Adamson E., et al. Survey of differentially methylated promoters in prostate cancer cell lines. Neoplasia (New York, NY) 2005, 7:748-760.
    • (2005) Neoplasia (New York, NY) , vol.7 , pp. 748-760
    • Wang, Y.1    Yu, Q.2    Cho, A.3    Rondeau, G.4    Welsh, J.5    Adamson, E.6
  • 50
    • 34548014545 scopus 로고    scopus 로고
    • Overexpression of SPARC protein contrasts with its transcriptional silencing by aberrant hypermethylation of SPARC CpG-rich region in endometrial carcinoma
    • Rodriguez-Jimenez F., Caldes T., Iniesta P., Vidart J., Lopez G. Overexpression of SPARC protein contrasts with its transcriptional silencing by aberrant hypermethylation of SPARC CpG-rich region in endometrial carcinoma. Oncol Rep 2007, 17:1301-1307.
    • (2007) Oncol Rep , vol.17 , pp. 1301-1307
    • Rodriguez-Jimenez, F.1    Caldes, T.2    Iniesta, P.3    Vidart, J.4    Lopez, G.5
  • 51
    • 0042284883 scopus 로고    scopus 로고
    • SPARC/osteonectin is a frequent target for aberrant methylation in pancreatic adenocarcinoma and a mediator of tumor-stromal interactions
    • Sato N., Fukushima N., Maehara N., Matsubayashi H., Koopmann J., Su G., et al. SPARC/osteonectin is a frequent target for aberrant methylation in pancreatic adenocarcinoma and a mediator of tumor-stromal interactions. Oncogene 2003, 22:5021-5030.
    • (2003) Oncogene , vol.22 , pp. 5021-5030
    • Sato, N.1    Fukushima, N.2    Maehara, N.3    Matsubayashi, H.4    Koopmann, J.5    Su, G.6
  • 52
    • 44349137412 scopus 로고    scopus 로고
    • SPARC promoter hypermethylation in colorectal cancers can be reversed by 5-Aza-2(prime)deoxycytidine to increase SPARC expression and improve therapy response
    • Cheetham S., Tang M.J., Mesak F., Kennecke H., Owen D., Tai I.T. SPARC promoter hypermethylation in colorectal cancers can be reversed by 5-Aza-2(prime)deoxycytidine to increase SPARC expression and improve therapy response. Br J Cancer 2008, 98:1810-1819.
    • (2008) Br J Cancer , vol.98 , pp. 1810-1819
    • Cheetham, S.1    Tang, M.J.2    Mesak, F.3    Kennecke, H.4    Owen, D.5    Tai, I.T.6
  • 53
    • 33644503560 scopus 로고    scopus 로고
    • Low or absent SPARC expression in acute myeloid leukemia with MLL rearrangements is associated with sensitivity to growth inhibition by exogenous SPARC protein
    • DiMartino J., Lacayo N., Varadi M., Li L., Saraiya C., Ravindranath Y., et al. Low or absent SPARC expression in acute myeloid leukemia with MLL rearrangements is associated with sensitivity to growth inhibition by exogenous SPARC protein. Leukemia 2006, 20:426-432.
    • (2006) Leukemia , vol.20 , pp. 426-432
    • DiMartino, J.1    Lacayo, N.2    Varadi, M.3    Li, L.4    Saraiya, C.5    Ravindranath, Y.6
  • 54
    • 0036274359 scopus 로고    scopus 로고
    • The fundamental role of epigenetic events in cancer
    • Jones P.A., Baylin S.B. The fundamental role of epigenetic events in cancer. Nat Rev Genet 2002, 3:415-428.
    • (2002) Nat Rev Genet , vol.3 , pp. 415-428
    • Jones, P.A.1    Baylin, S.B.2
  • 55
    • 0037068312 scopus 로고    scopus 로고
    • CpG island hypermethylation and tumor suppressor genes: a booming present, a brighter future
    • Esteller M. CpG island hypermethylation and tumor suppressor genes: a booming present, a brighter future. Oncogene 2002, 21:5427-5440.
    • (2002) Oncogene , vol.21 , pp. 5427-5440
    • Esteller, M.1
  • 56
    • 3042693554 scopus 로고    scopus 로고
    • Aberrant CpG island hypermethylation of multiple genes in colorectal neoplasia
    • Lee S., Hwang K., Lee H., Kim J., Kang G. Aberrant CpG island hypermethylation of multiple genes in colorectal neoplasia. Lab Invest 2004, 84:884-893.
    • (2004) Lab Invest , vol.84 , pp. 884-893
    • Lee, S.1    Hwang, K.2    Lee, H.3    Kim, J.4    Kang, G.5
  • 60
    • 33750617498 scopus 로고    scopus 로고
    • Meat consumption and risk of colorectal cancer: a meta-analysis of prospective studies
    • Larsson S., Wolk A. Meat consumption and risk of colorectal cancer: a meta-analysis of prospective studies. Int J Cancer 2006, 119:2657-2664.
    • (2006) Int J Cancer , vol.119 , pp. 2657-2664
    • Larsson, S.1    Wolk, A.2
  • 61
    • 18844432308 scopus 로고    scopus 로고
    • Adiponectin and adiponectin receptors
    • Kadowaki T., Yamauchi T. Adiponectin and adiponectin receptors. Endocr Rev 2005, 26:439-451.
    • (2005) Endocr Rev , vol.26 , pp. 439-451
    • Kadowaki, T.1    Yamauchi, T.2
  • 62
    • 0028787490 scopus 로고
    • A novel serum protein similar to C1q, produced exclusively in adipocytes
    • Scherer P., Williams S., Fogliano M., Baldini G., Lodish H. A novel serum protein similar to C1q, produced exclusively in adipocytes. J Biol Chem 1995, 270:26746-26749.
    • (1995) J Biol Chem , vol.270 , pp. 26746-26749
    • Scherer, P.1    Williams, S.2    Fogliano, M.3    Baldini, G.4    Lodish, H.5
  • 63
    • 0031821520 scopus 로고    scopus 로고
    • Understanding adipocyte differentiation
    • Gregoire F., Smas C., Sul H. Understanding adipocyte differentiation. Physiol Rev 1998, 78:783-809.
    • (1998) Physiol Rev , vol.78 , pp. 783-809
    • Gregoire, F.1    Smas, C.2    Sul, H.3
  • 64
    • 0034523640 scopus 로고    scopus 로고
    • Molecular regulation of adipogenesis
    • Rosen E., Spiegelman B. Molecular regulation of adipogenesis. Ann Rev Cell Dev Biol 2000, 16:145-171.
    • (2000) Ann Rev Cell Dev Biol , vol.16 , pp. 145-171
    • Rosen, E.1    Spiegelman, B.2
  • 65
    • 27744464555 scopus 로고    scopus 로고
    • Changes in integrin expression during adipocyte differentiation
    • Liu J., DeYoung S., Zhang M., Cheng A., Saltiel A. Changes in integrin expression during adipocyte differentiation. Cell Metabol 2005, 2:165-177.
    • (2005) Cell Metabol , vol.2 , pp. 165-177
    • Liu, J.1    DeYoung, S.2    Zhang, M.3    Cheng, A.4    Saltiel, A.5
  • 66
    • 59449099155 scopus 로고    scopus 로고
    • SPARC inhibits adipogenesis by its enhancement of -catenin signaling
    • Nie J., Sage E. SPARC inhibits adipogenesis by its enhancement of -catenin signaling. J Biol Chem 2009, 284:1279-1290.
    • (2009) J Biol Chem , vol.284 , pp. 1279-1290
    • Nie, J.1    Sage, E.2
  • 67
    • 33748979745 scopus 로고    scopus 로고
    • Invadopodia: specialized cell structures for cancer invasion
    • Weaver A. Invadopodia: specialized cell structures for cancer invasion. Clin Exp Metastasis 2006, 23:97-105.
    • (2006) Clin Exp Metastasis , vol.23 , pp. 97-105
    • Weaver, A.1
  • 68
    • 0345526459 scopus 로고    scopus 로고
    • Extracellular matrix substrata alter adipocyte yield and lipogenesis in primary cultures of stromal-vascular cells from human adipose
    • O'Connor K., Song H., Rosenzweig N., Jansen D. Extracellular matrix substrata alter adipocyte yield and lipogenesis in primary cultures of stromal-vascular cells from human adipose. Biotechnol Lett 2003, 25:1967-1972.
    • (2003) Biotechnol Lett , vol.25 , pp. 1967-1972
    • O'Connor, K.1    Song, H.2    Rosenzweig, N.3    Jansen, D.4
  • 70
    • 0035403704 scopus 로고    scopus 로고
    • The expression of SPARC in adipose tissue and its increased plasma concentration in patients with coronary artery disease
    • Takahashi M., Nagaretani H., Funahashi T., Nishizawa H., Maeda N., Kishida K., et al. The expression of SPARC in adipose tissue and its increased plasma concentration in patients with coronary artery disease. Obesity 2001, 9:388-393.
    • (2001) Obesity , vol.9 , pp. 388-393
    • Takahashi, M.1    Nagaretani, H.2    Funahashi, T.3    Nishizawa, H.4    Maeda, N.5    Kishida, K.6
  • 72
    • 0036144741 scopus 로고    scopus 로고
    • SPARC-null mice exhibit accelerated cutaneous wound closure
    • Bradshaw A., Reed M., Sage E. SPARC-null mice exhibit accelerated cutaneous wound closure. J Histochem Cytochem 2002, 50:1-10.
    • (2002) J Histochem Cytochem , vol.50 , pp. 1-10
    • Bradshaw, A.1    Reed, M.2    Sage, E.3
  • 73
    • 34250340913 scopus 로고    scopus 로고
    • Targeting SPARC expression decreases glioma cellular survival and invasion associated with reduced activities of FAK and ILK kinases
    • Shi Q., Bao S., Song L., Wu Q., Bigner D., Hjelmeland A., et al. Targeting SPARC expression decreases glioma cellular survival and invasion associated with reduced activities of FAK and ILK kinases. Oncogene 2007, 26:4084-4094.
    • (2007) Oncogene , vol.26 , pp. 4084-4094
    • Shi, Q.1    Bao, S.2    Song, L.3    Wu, Q.4    Bigner, D.5    Hjelmeland, A.6
  • 74
    • 0037736569 scopus 로고    scopus 로고
    • Osteonectin-null mutation compromises osteoblast formation, maturation, and survival
    • Delany A., Kalajzic I., Bradshaw A., Sage E., Canalis E. Osteonectin-null mutation compromises osteoblast formation, maturation, and survival. Endocrinology 2003, 144:2588-2596.
    • (2003) Endocrinology , vol.144 , pp. 2588-2596
    • Delany, A.1    Kalajzic, I.2    Bradshaw, A.3    Sage, E.4    Canalis, E.5
  • 75
    • 34347235843 scopus 로고    scopus 로고
    • Wnt signaling stimulates osteoblastogenesis of mesenchymal precursors by suppressing CCAAT/enhancer-binding protein and peroxisome proliferator-activated receptor
    • Kang S., Bennett C., Gerin I., Rapp L., Hankenson K., MacDougald O. Wnt signaling stimulates osteoblastogenesis of mesenchymal precursors by suppressing CCAAT/enhancer-binding protein and peroxisome proliferator-activated receptor. J Biol Chem 2007, 282:14515-14524.
    • (2007) J Biol Chem , vol.282 , pp. 14515-14524
    • Kang, S.1    Bennett, C.2    Gerin, I.3    Rapp, L.4    Hankenson, K.5    MacDougald, O.6
  • 76
    • 0034604110 scopus 로고    scopus 로고
    • Role of transforming growth factor beta in human disease
    • Blobe G., Schiemann W., Lodish H. Role of transforming growth factor beta in human disease. The New Eng J Med 2000, 342:1350-1358.
    • (2000) The New Eng J Med , vol.342 , pp. 1350-1358
    • Blobe, G.1    Schiemann, W.2    Lodish, H.3
  • 77
    • 0036151842 scopus 로고    scopus 로고
    • Inhibition of PDGF-stimulated and matrix-mediated proliferation of human vascular smooth muscle cells by SPARC is independent of changes in cell shape or cyclin-dependent kinase inhibitors
    • Motamed K., Funk S., Koyama H., Ross R., Raines E., Sage E. Inhibition of PDGF-stimulated and matrix-mediated proliferation of human vascular smooth muscle cells by SPARC is independent of changes in cell shape or cyclin-dependent kinase inhibitors. J Cell Biochem 2002, 84:759-771.
    • (2002) J Cell Biochem , vol.84 , pp. 759-771
    • Motamed, K.1    Funk, S.2    Koyama, H.3    Ross, R.4    Raines, E.5    Sage, E.6
  • 78
    • 0033621614 scopus 로고    scopus 로고
    • Induction of TGF-beta1 by the matricellular protein SPARC in a rat model of glomerulonephritis
    • Bassuk J., Pichler R., Rothmier J., Pippen J., Gordon K., Meek R., et al. Induction of TGF-beta1 by the matricellular protein SPARC in a rat model of glomerulonephritis. Kidney Int 2000, 57:117-128.
    • (2000) Kidney Int , vol.57 , pp. 117-128
    • Bassuk, J.1    Pichler, R.2    Rothmier, J.3    Pippen, J.4    Gordon, K.5    Meek, R.6
  • 79
    • 0028175379 scopus 로고
    • TGF-beta 1 induces the expression of type I collagen and SPARC, and enhances contraction of collagen gels, by fibroblasts from young and aged donors
    • Reed M., Vernon R., Abrass I., Sage E. TGF-beta 1 induces the expression of type I collagen and SPARC, and enhances contraction of collagen gels, by fibroblasts from young and aged donors. J Cell Physiol 1994, 158:169-179.
    • (1994) J Cell Physiol , vol.158 , pp. 169-179
    • Reed, M.1    Vernon, R.2    Abrass, I.3    Sage, E.4
  • 80
    • 7344226188 scopus 로고    scopus 로고
    • Regulation of low density lipoprotein receptor mRNA levels by estradiol 17 beta and chorionic gonadotropin in human placenta
    • Shanker Y., Shetty U., Rao A. Regulation of low density lipoprotein receptor mRNA levels by estradiol 17 beta and chorionic gonadotropin in human placenta. Mol Cell Biochem 1998, 187:133-139.
    • (1998) Mol Cell Biochem , vol.187 , pp. 133-139
    • Shanker, Y.1    Shetty, U.2    Rao, A.3
  • 81
    • 15444345967 scopus 로고    scopus 로고
    • Differential effects of various growth factors and cytokines on the syntheses of DNA, type I collagen, laminin, fibronectin, osteonectin/secreted protein, acidic and rich in cysteine (SPARC), and alkaline phosphatase by human pulp cells in culture
    • Shiba H., Fujita T., Doi N., Nakamura S., Nakanishi K., Takemoto T., et al. Differential effects of various growth factors and cytokines on the syntheses of DNA, type I collagen, laminin, fibronectin, osteonectin/secreted protein, acidic and rich in cysteine (SPARC), and alkaline phosphatase by human pulp cells in culture. J Cell Physiol 1998, 174:194-205.
    • (1998) J Cell Physiol , vol.174 , pp. 194-205
    • Shiba, H.1    Fujita, T.2    Doi, N.3    Nakamura, S.4    Nakanishi, K.5    Takemoto, T.6
  • 82
    • 0141541761 scopus 로고    scopus 로고
    • SPARC inhibits epithelial cell proliferation in part through stimulation of the transforming growth factor-beta-signaling system
    • Schiemann B., Neil J., Schiemann W. SPARC inhibits epithelial cell proliferation in part through stimulation of the transforming growth factor-beta-signaling system. Mol Biol Cell 2003, 14:3977-3988.
    • (2003) Mol Biol Cell , vol.14 , pp. 3977-3988
    • Schiemann, B.1    Neil, J.2    Schiemann, W.3
  • 83
    • 0036707707 scopus 로고    scopus 로고
    • Doxycycline-inducible expression of SPARC/Osteonectin/BM40 in MDA-MB-231 human breast cancer cells results in growth inhibition
    • Dhanesuan N., Sharp J., Blick T., Price J., Thompson E. Doxycycline-inducible expression of SPARC/Osteonectin/BM40 in MDA-MB-231 human breast cancer cells results in growth inhibition. Breast Cancer Res Treat 2002, 75:73-85.
    • (2002) Breast Cancer Res Treat , vol.75 , pp. 73-85
    • Dhanesuan, N.1    Sharp, J.2    Blick, T.3    Price, J.4    Thompson, E.5
  • 84
    • 43049121355 scopus 로고    scopus 로고
    • SPARC-induced increase in glioma matrix and decrease in vascularity are associated with reduced VEGF expression and secretion
    • Yunker C., Golembieski W., Lemke N., Schultz C., Cazacu S., Brodie C., et al. SPARC-induced increase in glioma matrix and decrease in vascularity are associated with reduced VEGF expression and secretion. Int J Cancer 2008, 122:2735-2743.
    • (2008) Int J Cancer , vol.122 , pp. 2735-2743
    • Yunker, C.1    Golembieski, W.2    Lemke, N.3    Schultz, C.4    Cazacu, S.5    Brodie, C.6
  • 85
    • 39649116456 scopus 로고    scopus 로고
    • SPARC modulates the proliferation of stromal but not melanoma cells unless endogenous SPARC expression is downregulated
    • Haber C., Gottifredi V., Llera A., Salvatierra E., Prada F., Alonso L., et al. SPARC modulates the proliferation of stromal but not melanoma cells unless endogenous SPARC expression is downregulated. Int J Cancer 2007, 122:1465-1475.
    • (2007) Int J Cancer , vol.122 , pp. 1465-1475
    • Haber, C.1    Gottifredi, V.2    Llera, A.3    Salvatierra, E.4    Prada, F.5    Alonso, L.6
  • 87
    • 0037115291 scopus 로고    scopus 로고
    • SPARC is a key Schwannian-derived inhibitor controlling neuroblastoma tumor angiogenesis
    • Chlenski A., Liu S., Crawford S., Volpert O., DeVries G., Evangelista A., et al. SPARC is a key Schwannian-derived inhibitor controlling neuroblastoma tumor angiogenesis. Cancer Res 2002, 62:7357-7363.
    • (2002) Cancer Res , vol.62 , pp. 7357-7363
    • Chlenski, A.1    Liu, S.2    Crawford, S.3    Volpert, O.4    DeVries, G.5    Evangelista, A.6
  • 88
    • 0023374396 scopus 로고
    • In vivo expression of mRNA for the Ca2+-binding protein SPARC (osteonectin) revealed by in situ hybridization
    • Holland P., Harper S., McVey J., Hogan B. In vivo expression of mRNA for the Ca2+-binding protein SPARC (osteonectin) revealed by in situ hybridization. J Cell Biol 1987, 105:473-482.
    • (1987) J Cell Biol , vol.105 , pp. 473-482
    • Holland, P.1    Harper, S.2    McVey, J.3    Hogan, B.4
  • 89
    • 0024395113 scopus 로고
    • SPARC, a secreted protein associated with cellular proliferation, inhibits cell spreading in vitro and exhibits Ca+ 2-dependent binding to the extracellular matrix
    • Sage H., Vernon R., Funk S., Everitt E., Angello J. SPARC, a secreted protein associated with cellular proliferation, inhibits cell spreading in vitro and exhibits Ca+ 2-dependent binding to the extracellular matrix. J Cell Biol 1989, 109:341-356.
    • (1989) J Cell Biol , vol.109 , pp. 341-356
    • Sage, H.1    Vernon, R.2    Funk, S.3    Everitt, E.4    Angello, J.5
  • 90
    • 0025921473 scopus 로고
    • The Ca2 (+)-binding glycoprotein SPARC modulates cell cycle progression in bovine aortic endothelial cells
    • Funk S., Sage E. The Ca2 (+)-binding glycoprotein SPARC modulates cell cycle progression in bovine aortic endothelial cells. Proc Nat Acad Sci USA 1991, 88:2648-2652.
    • (1991) Proc Nat Acad Sci USA , vol.88 , pp. 2648-2652
    • Funk, S.1    Sage, E.2
  • 91
    • 10644236100 scopus 로고    scopus 로고
    • Secreted protein acidic, rich in cysteine (SPARC), mediates cellular survival of gliomas through AKT activation
    • Shi Q., Bao S., Maxwell J., Reese E., Friedman H., Bigner D., et al. Secreted protein acidic, rich in cysteine (SPARC), mediates cellular survival of gliomas through AKT activation. J Biol Chem 2004, 279:52200-52209.
    • (2004) J Biol Chem , vol.279 , pp. 52200-52209
    • Shi, Q.1    Bao, S.2    Maxwell, J.3    Reese, E.4    Friedman, H.5    Bigner, D.6
  • 92
    • 47749119594 scopus 로고    scopus 로고
    • Forced expression of MMP9 rescues the loss of angiogenesis and abrogates metastasis of pancreatic tumors triggered by the absence of host SPARC
    • Arnold S., Mira E., Muneer S., Korpanty G., Beck A., Holloway S., et al. Forced expression of MMP9 rescues the loss of angiogenesis and abrogates metastasis of pancreatic tumors triggered by the absence of host SPARC. Exp Biol Med 2008, 233:860-873.
    • (2008) Exp Biol Med , vol.233 , pp. 860-873
    • Arnold, S.1    Mira, E.2    Muneer, S.3    Korpanty, G.4    Beck, A.5    Holloway, S.6
  • 93
    • 0028947280 scopus 로고
    • Expression of SPARC during development of the chicken chorioallantoic membrane: evidence for regulated proteolysis in vivo
    • Iruela-Arispe M., Lane T., Redmond D., Reilly M., Bolender R., Kavanagh T., et al. Expression of SPARC during development of the chicken chorioallantoic membrane: evidence for regulated proteolysis in vivo. Mol Biol Cell 1995, 6:327-343.
    • (1995) Mol Biol Cell , vol.6 , pp. 327-343
    • Iruela-Arispe, M.1    Lane, T.2    Redmond, D.3    Reilly, M.4    Bolender, R.5    Kavanagh, T.6
  • 94
    • 0025609345 scopus 로고
    • Sage E: Functional mapping of SPARC. Peptides from two distinct Ca+ (+)-binding sites modulate cell shape
    • Lane T. Sage E: Functional mapping of SPARC. Peptides from two distinct Ca+ (+)-binding sites modulate cell shape. J Cell Biol 1990, 111:3065-3076.
    • (1990) J Cell Biol , vol.111 , pp. 3065-3076
    • Lane, T.1
  • 95
    • 51349153865 scopus 로고    scopus 로고
    • HSP27 mediates SPARC-induced changes in glioma morphology, migration, and invasion
    • Golembieski W., Thomas S., Schultz C., Yunker C., McClung H., Lemke N., et al. HSP27 mediates SPARC-induced changes in glioma morphology, migration, and invasion. Glia 2008, 56:1061-1075.
    • (2008) Glia , vol.56 , pp. 1061-1075
    • Golembieski, W.1    Thomas, S.2    Schultz, C.3    Yunker, C.4    McClung, H.5    Lemke, N.6
  • 96
    • 64549154509 scopus 로고    scopus 로고
    • Downregulation of SPARC expression inhibits cell migration and invasion in malignant gliomas
    • Seno T., Harada H., Kohno S., Teraoka M., Inoue A., Ohnishi T. Downregulation of SPARC expression inhibits cell migration and invasion in malignant gliomas. Int J Oncol 2009, 34:707-715.
    • (2009) Int J Oncol , vol.34 , pp. 707-715
    • Seno, T.1    Harada, H.2    Kohno, S.3    Teraoka, M.4    Inoue, A.5    Ohnishi, T.6
  • 97
    • 0026533415 scopus 로고
    • Expression of SPARC is correlated with altered morphologies in transfected F9 embryonal carcinoma cells
    • Everitt E., Sage E. Expression of SPARC is correlated with altered morphologies in transfected F9 embryonal carcinoma cells. Exp Cell Res 1992, 199:134-146.
    • (1992) Exp Cell Res , vol.199 , pp. 134-146
    • Everitt, E.1    Sage, E.2
  • 98
    • 0031056656 scopus 로고    scopus 로고
    • Suppression of SPARC expression by antisense RNA abrogates the tumorigenicity of human melanoma cells
    • Ledda M., Adris S., Bravo A., Kairiyama C., Bover L., Chernajovsky Y., et al. Suppression of SPARC expression by antisense RNA abrogates the tumorigenicity of human melanoma cells. Nature Med 1997, 3:171-176.
    • (1997) Nature Med , vol.3 , pp. 171-176
    • Ledda, M.1    Adris, S.2    Bravo, A.3    Kairiyama, C.4    Bover, L.5    Chernajovsky, Y.6
  • 99
    • 20444493997 scopus 로고    scopus 로고
    • Secreted protein acidic and rich in cysteine produced by human melanoma cells modulates polymorphonuclear leukocyte recruitment and antitumor cytotoxic capacity
    • Alvarez M., Prada F., Salvatierra E., Bravo A., Lutzky V., Carbone C., et al. Secreted protein acidic and rich in cysteine produced by human melanoma cells modulates polymorphonuclear leukocyte recruitment and antitumor cytotoxic capacity. Cancer Res 2005, 65:5123-5132.
    • (2005) Cancer Res , vol.65 , pp. 5123-5132
    • Alvarez, M.1    Prada, F.2    Salvatierra, E.3    Bravo, A.4    Lutzky, V.5    Carbone, C.6
  • 100
    • 33747894237 scopus 로고    scopus 로고
    • SPARC represses E-cadherin and induces mesenchymal transition during melanoma development
    • Robert G., Gaggioli C., Bailet O., Chavey C., Abbe P., Aberdam E., et al. SPARC represses E-cadherin and induces mesenchymal transition during melanoma development. Cancer Res 2006, 66:7516-7523.
    • (2006) Cancer Res , vol.66 , pp. 7516-7523
    • Robert, G.1    Gaggioli, C.2    Bailet, O.3    Chavey, C.4    Abbe, P.5    Aberdam, E.6
  • 101
    • 0034648765 scopus 로고    scopus 로고
    • Angiogenesis in cancer and other diseases
    • Carmeliet P., Jain R. Angiogenesis in cancer and other diseases. Nature 2000, 407:249-257.
    • (2000) Nature , vol.407 , pp. 249-257
    • Carmeliet, P.1    Jain, R.2
  • 104
    • 0030853194 scopus 로고    scopus 로고
    • Regulation of human monocyte matrix metalloproteinases by SPARC
    • Shankavaram U., DeWitt D., Funk S., Sage E., Wahl L. Regulation of human monocyte matrix metalloproteinases by SPARC. J Cell Physiol 1998, 173:327-334.
    • (1998) J Cell Physiol , vol.173 , pp. 327-334
    • Shankavaram, U.1    DeWitt, D.2    Funk, S.3    Sage, E.4    Wahl, L.5
  • 105
    • 0032935664 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases. Specific messages from ubiquitous messengers
    • Schaeffer H., Weber M. Mitogen-activated protein kinases. Specific messages from ubiquitous messengers. Mol Cell Biol 1999, 19:2435-2444.
    • (1999) Mol Cell Biol , vol.19 , pp. 2435-2444
    • Schaeffer, H.1    Weber, M.2
  • 106
    • 28844466823 scopus 로고    scopus 로고
    • SPARC expression is associated with impaired tumor growth, inhibited angiogenesis and changes in the extracellular matrix
    • Chlenski A., Liu S., Guerrero L., Yang Q., Tian Y., Salwen H., et al. SPARC expression is associated with impaired tumor growth, inhibited angiogenesis and changes in the extracellular matrix. Int J Cancer 2005, 118:310-316.
    • (2005) Int J Cancer , vol.118 , pp. 310-316
    • Chlenski, A.1    Liu, S.2    Guerrero, L.3    Yang, Q.4    Tian, Y.5    Salwen, H.6
  • 107
    • 23444459571 scopus 로고
    • The biology of SPARC, a protein that modulates cell-matrix interactions
    • Lane T., Sage E. The biology of SPARC, a protein that modulates cell-matrix interactions. FASEB J 1994, 8:163-173.
    • (1994) FASEB J , vol.8 , pp. 163-173
    • Lane, T.1    Sage, E.2
  • 108
    • 28244480457 scopus 로고    scopus 로고
    • Absence of host-secreted protein acidic and rich in cysteine (SPARC) augments peritoneal ovarian carcinomatosis
    • Said N., Motamed K. Absence of host-secreted protein acidic and rich in cysteine (SPARC) augments peritoneal ovarian carcinomatosis. Amer J Pathol 2005, 167:1739-1752.
    • (2005) Amer J Pathol , vol.167 , pp. 1739-1752
    • Said, N.1    Motamed, K.2
  • 109
    • 0031681296 scopus 로고    scopus 로고
    • CD 95 (APO-1/Fas)-mediated apoptosis in normal and malignant liver, colon, and hematopoietic cells
    • Krammer P., Galle P., Moller P., Debatin K. CD 95 (APO-1/Fas)-mediated apoptosis in normal and malignant liver, colon, and hematopoietic cells. Adv Cancer Res 1998, 75:251-273.
    • (1998) Adv Cancer Res , vol.75 , pp. 251-273
    • Krammer, P.1    Galle, P.2    Moller, P.3    Debatin, K.4
  • 110
    • 0034536743 scopus 로고    scopus 로고
    • Regulation of death receptor-mediated apoptosis pathways
    • Schmitz I., Kirchhoff S., Krammer P. Regulation of death receptor-mediated apoptosis pathways. Int J Biochem Cell Biol 2000, 32:1123-1136.
    • (2000) Int J Biochem Cell Biol , vol.32 , pp. 1123-1136
    • Schmitz, I.1    Kirchhoff, S.2    Krammer, P.3
  • 111
    • 0034879902 scopus 로고    scopus 로고
    • SPARC (secreted protein acidic and rich in cysteine) induces apoptosis in ovarian cancer cells
    • Yiu G., Chan W., Ng S., Chan P., Cheung K., Berkowitz R., et al. SPARC (secreted protein acidic and rich in cysteine) induces apoptosis in ovarian cancer cells. Amer J Pathol 2001, 159:609-622.
    • (2001) Amer J Pathol , vol.159 , pp. 609-622
    • Yiu, G.1    Chan, W.2    Ng, S.3    Chan, P.4    Cheung, K.5    Berkowitz, R.6
  • 112
    • 36348978859 scopus 로고    scopus 로고
    • A novel interaction between procaspase 8 and SPARC enhances apoptosis and potentiates chemotherapy sensitivity in colorectal cancers
    • Tang M., Tai I. A novel interaction between procaspase 8 and SPARC enhances apoptosis and potentiates chemotherapy sensitivity in colorectal cancers. J Biol Chem 2007, 282:34457.
    • (2007) J Biol Chem , vol.282 , pp. 34457
    • Tang, M.1    Tai, I.2
  • 113
    • 55949136282 scopus 로고    scopus 로고
    • SPARC in cancer biology. Its role in cancer progression and potential for therapy
    • Tai I.T., Tang M.J. SPARC in cancer biology. Its role in cancer progression and potential for therapy. Drug Resist Updat 2008, 11:231-246.
    • (2008) Drug Resist Updat , vol.11 , pp. 231-246
    • Tai, I.T.1    Tang, M.J.2
  • 114
    • 41149093139 scopus 로고    scopus 로고
    • Analyses of the role of endogenous SPARC in mouse models of prostate and breast cancer
    • Wong S., Crowley D., Bronson R., Hynes R. Analyses of the role of endogenous SPARC in mouse models of prostate and breast cancer. Clin Exp Metast 2008, 25:109-118.
    • (2008) Clin Exp Metast , vol.25 , pp. 109-118
    • Wong, S.1    Crowley, D.2    Bronson, R.3    Hynes, R.4
  • 115
    • 77956668302 scopus 로고    scopus 로고
    • Cathepsin B facilitates autophagy-mediated apoptosis in SPARC overexpressed primitive neuroectodermal tumor cells
    • Bhoopathi P., Chetty C., Gujrati M., Dinh D., Rao J., Lakka S. Cathepsin B facilitates autophagy-mediated apoptosis in SPARC overexpressed primitive neuroectodermal tumor cells. Cell Death Differ 2010, 1-10.
    • (2010) Cell Death Differ , pp. 1-10
    • Bhoopathi, P.1    Chetty, C.2    Gujrati, M.3    Dinh, D.4    Rao, J.5    Lakka, S.6
  • 116
    • 23844504520 scopus 로고    scopus 로고
    • Endogenous osteonectin/SPARC/BM-40 expression inhibits MDA-MB-231 breast cancer cell metastasis
    • Koblinski J., Kaplan-Singer B., VanOsdol S., Wu M., Engbring J., Wang S., et al. Endogenous osteonectin/SPARC/BM-40 expression inhibits MDA-MB-231 breast cancer cell metastasis. Cancer Res 2005, 65:7370-7377.
    • (2005) Cancer Res , vol.65 , pp. 7370-7377
    • Koblinski, J.1    Kaplan-Singer, B.2    VanOsdol, S.3    Wu, M.4    Engbring, J.5    Wang, S.6
  • 117
    • 0037057334 scopus 로고    scopus 로고
    • Transcriptional upregulation of SPARC, in response to c-Jun overexpression, contributes to increased motility and invasion of MCF7 breast cancer cells
    • Briggs J., Chamboredon S., Castellazzi M., Kerry J., Bos T. Transcriptional upregulation of SPARC, in response to c-Jun overexpression, contributes to increased motility and invasion of MCF7 breast cancer cells. Oncogene 2002, 21:7077-7091.
    • (2002) Oncogene , vol.21 , pp. 7077-7091
    • Briggs, J.1    Chamboredon, S.2    Castellazzi, M.3    Kerry, J.4    Bos, T.5
  • 118
    • 37149040456 scopus 로고    scopus 로고
    • Molecular signatures of metaplastic carcinoma of the breast by large-scale transcriptional profiling: identification of genes potentially related to epithelial-mesenchymal transition
    • Lien H., Hsiao Y., Lin Y., Yao Y., Juan H., Kuo W., et al. Molecular signatures of metaplastic carcinoma of the breast by large-scale transcriptional profiling: identification of genes potentially related to epithelial-mesenchymal transition. Oncogene 2007, 26:7859-7871.
    • (2007) Oncogene , vol.26 , pp. 7859-7871
    • Lien, H.1    Hsiao, Y.2    Lin, Y.3    Yao, Y.4    Juan, H.5    Kuo, W.6
  • 119
    • 35348880889 scopus 로고    scopus 로고
    • SPARC endogenous level, rather than fibroblast-produced SPARC or stroma reorganization induced by SPARC, is responsible for melanoma cell growth
    • Prada F., Benedetti L., Bravo A., Alvarez M., Carbone C., Podhajcer O. SPARC endogenous level, rather than fibroblast-produced SPARC or stroma reorganization induced by SPARC, is responsible for melanoma cell growth. J Invest Dermatol 2007, 127:2618-2628.
    • (2007) J Invest Dermatol , vol.127 , pp. 2618-2628
    • Prada, F.1    Benedetti, L.2    Bravo, A.3    Alvarez, M.4    Carbone, C.5    Podhajcer, O.6
  • 120
    • 41549166455 scopus 로고    scopus 로고
    • Meta-analysis of colorectal cancer gene expression profiling studies identifies consistently reported candidate biomarkers
    • Chan S., Griffith O., Tai I., Jones S. Meta-analysis of colorectal cancer gene expression profiling studies identifies consistently reported candidate biomarkers. Cancer Epidemiol Biomark Prevent 2008, 17:543-552.
    • (2008) Cancer Epidemiol Biomark Prevent , vol.17 , pp. 543-552
    • Chan, S.1    Griffith, O.2    Tai, I.3    Jones, S.4
  • 121
    • 77953511554 scopus 로고    scopus 로고
    • Relationship and prognostic significance of SPARC and VEGF protein expression in colon cancer
    • Liang J., Wang H., Xiao H., Li N., Cheng C., Zhao Y., et al. Relationship and prognostic significance of SPARC and VEGF protein expression in colon cancer. J Exp Clin Cancer Res 2010, 29:71-75.
    • (2010) J Exp Clin Cancer Res , vol.29 , pp. 71-75
    • Liang, J.1    Wang, H.2    Xiao, H.3    Li, N.4    Cheng, C.5    Zhao, Y.6
  • 122
    • 0034757822 scopus 로고    scopus 로고
    • SPARC modulates cell growth, attachment and migration of U87 glioma cells on brain extracellular matrix proteins
    • Rempel S., Golembieski W., Fisher J., Maile M., Nakeff A. SPARC modulates cell growth, attachment and migration of U87 glioma cells on brain extracellular matrix proteins. J Neuro-Oncol 2001, 53:149-160.
    • (2001) J Neuro-Oncol , vol.53 , pp. 149-160
    • Rempel, S.1    Golembieski, W.2    Fisher, J.3    Maile, M.4    Nakeff, A.5
  • 123
    • 0036829855 scopus 로고    scopus 로고
    • Secreted protein acidic and rich in cysteine promotes glioma invasion and delays tumor growth in vivo
    • Schultz C., Lemke N., Ge S., Golembieski W., Rempel S. Secreted protein acidic and rich in cysteine promotes glioma invasion and delays tumor growth in vivo. Cancer Res 2002, 62:6270-6277.
    • (2002) Cancer Res , vol.62 , pp. 6270-6277
    • Schultz, C.1    Lemke, N.2    Ge, S.3    Golembieski, W.4    Rempel, S.5
  • 124
    • 0034306969 scopus 로고    scopus 로고
    • Blockade of nuclear factor-{kappa} B signaling inhibits angiogenesis and tumorigenicity of human ovarian cancer cells by suppressing expression of vascular endothelial growth factor and interleukin 8
    • Huang S., Robinson J., DeGuzman A., Bucana C., Fidler I. Blockade of nuclear factor-{kappa} B signaling inhibits angiogenesis and tumorigenicity of human ovarian cancer cells by suppressing expression of vascular endothelial growth factor and interleukin 8. Cancer Res 2000, 60:5334-5339.
    • (2000) Cancer Res , vol.60 , pp. 5334-5339
    • Huang, S.1    Robinson, J.2    DeGuzman, A.3    Bucana, C.4    Fidler, I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.