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Volumn 373, Issue 1-2, 2013, Pages 63-72

Involvement of Ext1 and heparanase in migration of mouse FBJ osteosarcoma cells

Author keywords

Cell motility; Ext1; FBJ osteosarcoma; Glycosaminoglycan; Heparan sulfate; Heparanase; Saccharide primer

Indexed keywords

EXOSTOSIN 1; GLYCOPROTEIN; HEPARAN SULFATE; HEPARANASE; SMALL INTERFERING RNA; TUMOR SUPPRESSOR PROTEIN; UNCLASSIFIED DRUG;

EID: 84871790084     PISSN: 03008177     EISSN: 15734919     Source Type: Journal    
DOI: 10.1007/s11010-012-1475-8     Document Type: Article
Times cited : (10)

References (44)
  • 1
    • 0037154175 scopus 로고    scopus 로고
    • Tumor cell surface heparan sulfate as cryptic promoters or inhibitors of tumor growth and metastasis
    • 11805315 10.1073/pnas.012578299 1:CAS:528:DC%2BD38Xht1Wjtb4%3D
    • Liu D, Shriver Z, Venkataraman G, El Shabrawi Y, Sasisekharan R (2002) Tumor cell surface heparan sulfate as cryptic promoters or inhibitors of tumor growth and metastasis. Proc Natl Acad Sci USA 99:568-573
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 568-573
    • Liu, D.1    Shriver, Z.2    Venkataraman, G.3    El Shabrawi, Y.4    Sasisekharan, R.5
  • 2
    • 0035782873 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans in invasion and metastasis
    • 11292374 10.1006/scdb.2000.0241 1:CAS:528:DC%2BD3MXis1SisLs%3D
    • Sanderson RD (2001) Heparan sulfate proteoglycans in invasion and metastasis. Semin Cell Dev Biol 12:89-98
    • (2001) Semin Cell Dev Biol , vol.12 , pp. 89-98
    • Sanderson, R.D.1
  • 3
    • 33847401445 scopus 로고    scopus 로고
    • Decreased EXT expression and intracellular accumulation of heparan sulphate proteoglycan in osteochondromas and peripheral chondrosarcomas
    • 17226760 10.1002/path.2127 1:CAS:528:DC%2BD2sXjs1yrs70%3D
    • Hameetman L, David G, Yavas A, White SJ, Taminiau AH, Cleton-Jansen AM, Hogendoorn PC, Bovee JV (2007) Decreased EXT expression and intracellular accumulation of heparan sulphate proteoglycan in osteochondromas and peripheral chondrosarcomas. J Pathol 211:399-409
    • (2007) J Pathol , vol.211 , pp. 399-409
    • Hameetman, L.1    David, G.2    Yavas, A.3    White, S.J.4    Taminiau, A.H.5    Cleton-Jansen, A.M.6    Hogendoorn, P.C.7    Bovee, J.V.8
  • 4
    • 0034681139 scopus 로고    scopus 로고
    • The putative tumor suppressors EXT1 and EXT2 form a stable complex that accumulates in the Golgi apparatus and catalyzes the synthesis of heparan sulfate
    • 10639137 10.1073/pnas.97.2.668 1:CAS:528:DC%2BD3cXot1ahsA%3D%3D
    • McCormick C, Duncan G, Goutsos KT, Tufaro F (2000) The putative tumor suppressors EXT1 and EXT2 form a stable complex that accumulates in the Golgi apparatus and catalyzes the synthesis of heparan sulfate. Proc Natl Acad Sci USA 97:668-673
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 668-673
    • McCormick, C.1    Duncan, G.2    Goutsos, K.T.3    Tufaro, F.4
  • 5
    • 36349019110 scopus 로고    scopus 로고
    • Contribution of EXT1, EXT2, and EXTL3 to heparan sulfate chain elongation
    • 17761672 10.1074/jbc.M703560200 1:CAS:528:DC%2BD2sXht1CltbbL
    • Busse M, Feta A, Presto J, Wilen M, Gronning M, Kjellen L, Kusche-Gullberg M (2007) Contribution of EXT1, EXT2, and EXTL3 to heparan sulfate chain elongation. J Biol Chem 282:32802-32810
    • (2007) J Biol Chem , vol.282 , pp. 32802-32810
    • Busse, M.1    Feta, A.2    Presto, J.3    Wilen, M.4    Gronning, M.5    Kjellen, L.6    Kusche-Gullberg, M.7
  • 6
    • 0031594163 scopus 로고    scopus 로고
    • Evaluation of locus heterogeneity and EXT1 mutations in 34 families with hereditary multiple exostoses
    • 9521425 10.1002/(SICI)1098-1004(1998)11:3<231: AID-HUMU8>3.0.CO;2-K 1:CAS:528:DyaK1cXhvVehsrY%3D
    • Raskind WH, Conrad EU, Matsushita M, Wijsman EM, Wells DE, Chapman N, Sandell LJ, Wagner M, Houck J (1998) Evaluation of locus heterogeneity and EXT1 mutations in 34 families with hereditary multiple exostoses. Hum Mutat 11:231-239
    • (1998) Hum Mutat , vol.11 , pp. 231-239
    • Raskind, W.H.1    Conrad, E.U.2    Matsushita, M.3    Wijsman, E.M.4    Wells, D.E.5    Chapman, N.6    Sandell, L.J.7    Wagner, M.8    Houck, J.9
  • 7
    • 0028908915 scopus 로고
    • Natural-history study of hereditary multiple exostoses
    • 7702095 10.1002/ajmg.1320550113 1:STN:280:DyaK2M3hs1Kmuw%3D%3D
    • Wicklund CL, Pauli RM, Johnston D, Hecht JT (1995) Natural-history study of hereditary multiple exostoses. Am J Med Genet 55:43-46
    • (1995) Am J Med Genet , vol.55 , pp. 43-46
    • Wicklund, C.L.1    Pauli, R.M.2    Johnston, D.3    Hecht, J.T.4
  • 8
    • 0032563303 scopus 로고    scopus 로고
    • Substrate specificity of heparanases from human hepatoma and platelets
    • 9668050 10.1074/jbc.273.30.18770 1:CAS:528:DyaK1cXltFGrsLo%3D
    • Pikas DS, Li JP, Vlodavsky I, Lindahl U (1998) Substrate specificity of heparanases from human hepatoma and platelets. J Biol Chem 273:18770-18777
    • (1998) J Biol Chem , vol.273 , pp. 18770-18777
    • Pikas, D.S.1    Li, J.P.2    Vlodavsky, I.3    Lindahl, U.4
  • 9
    • 77952002191 scopus 로고    scopus 로고
    • Unraveling the specificity of heparanase utilizing synthetic substrates
    • 20181948 10.1074/jbc.M110.104166 1:CAS:528:DC%2BC3cXlsVOhs7w%3D
    • Peterson SB, Liu J (2010) Unraveling the specificity of heparanase utilizing synthetic substrates. J Biol Chem 285:14504-14513
    • (2010) J Biol Chem , vol.285 , pp. 14504-14513
    • Peterson, S.B.1    Liu, J.2
  • 10
    • 33748683743 scopus 로고    scopus 로고
    • Regulation, function and clinical significance of heparanase in cancer metastasis and angiogenesis
    • 16901744 10.1016/j.biocel.2006.06.004 1:CAS:528:DC%2BD28XpvFSjurs%3D
    • Ilan N, Elkin M, Vlodavsky I (2006) Regulation, function and clinical significance of heparanase in cancer metastasis and angiogenesis. Int J Biochem Cell Biol 38:2018-2039
    • (2006) Int J Biochem Cell Biol , vol.38 , pp. 2018-2039
    • Ilan, N.1    Elkin, M.2    Vlodavsky, I.3
  • 11
    • 61449222897 scopus 로고    scopus 로고
    • Cell surface heparan sulfate released by heparanase promotes melanoma cell migration and angiogenesis
    • 19115257 10.1002/jcb.22005 1:CAS:528:DC%2BD1MXhslehsL4%3D
    • Roy M, Marchetti D (2009) Cell surface heparan sulfate released by heparanase promotes melanoma cell migration and angiogenesis. J Cell Biochem 106:200-209
    • (2009) J Cell Biochem , vol.106 , pp. 200-209
    • Roy, M.1    Marchetti, D.2
  • 12
    • 0034904048 scopus 로고    scopus 로고
    • Molecular properties and involvement of heparanase in cancer metastasis and angiogenesis
    • 11489924 1:CAS:528:DC%2BD3MXlvVGlt7o%3D
    • Vlodavsky I, Friedmann Y (2001) Molecular properties and involvement of heparanase in cancer metastasis and angiogenesis. J Clin Invest 108:341-347
    • (2001) J Clin Invest , vol.108 , pp. 341-347
    • Vlodavsky, I.1    Friedmann, Y.2
  • 13
    • 79952728727 scopus 로고    scopus 로고
    • Heparanase plays a dual role in driving hepatocyte growth factor (HGF) signaling by enhancing HGF expression and activity
    • 21131364 10.1074/jbc.M110.183277 1:CAS:528:DC%2BC3MXitVyrsrc%3D
    • Ramani VC, Yang Y, Ren Y, Nan L, Sanderson RD (2011) Heparanase plays a dual role in driving hepatocyte growth factor (HGF) signaling by enhancing HGF expression and activity. J Biol Chem 286:6490-6499
    • (2011) J Biol Chem , vol.286 , pp. 6490-6499
    • Ramani, V.C.1    Yang, Y.2    Ren, Y.3    Nan, L.4    Sanderson, R.D.5
  • 14
    • 77950559481 scopus 로고    scopus 로고
    • Heparanase-enhanced shedding of syndecan-1 by myeloma cells promotes endothelial invasion and angiogenesis
    • 20097882 10.1182/blood-2009-07-234757 1:CAS:528:DC%2BC3cXktlOku7k%3D
    • Purushothaman A, Uyama T, Kobayashi F, Yamada S, Sugahara K, Rapraeger AC, Sanderson RD (2010) Heparanase-enhanced shedding of syndecan-1 by myeloma cells promotes endothelial invasion and angiogenesis. Blood 115:2449-2457
    • (2010) Blood , vol.115 , pp. 2449-2457
    • Purushothaman, A.1    Uyama, T.2    Kobayashi, F.3    Yamada, S.4    Sugahara, K.5    Rapraeger, A.C.6    Sanderson, R.D.7
  • 15
    • 78651273016 scopus 로고    scopus 로고
    • Glycan changes: Cancer metastasis and anti-cancer vaccines
    • 21289447 10.1007/s12038-010-0073-8 1:CAS:528:DC%2BC3cXhs1Wnt7zI
    • Li M, Song L, Qin X (2010) Glycan changes: cancer metastasis and anti-cancer vaccines. J Biosci 35:665-673
    • (2010) J Biosci , vol.35 , pp. 665-673
    • Li, M.1    Song, L.2    Qin, X.3
  • 16
    • 0031566246 scopus 로고    scopus 로고
    • Inhibition of highly metastatic FBJ-LL cell migration by ganglioside GD1a highly expressed in poorly metastatic FBJ-S1 cells
    • 9070274 10.1006/bbrc.1997.6096 1:CAS:528:DyaK2sXhsVegtrk%3D
    • Hyuga S, Yamagata S, Tai T, Yamagata T (1997) Inhibition of highly metastatic FBJ-LL cell migration by ganglioside GD1a highly expressed in poorly metastatic FBJ-S1 cells. Biochem Biophys Res Commun 231:340-343
    • (1997) Biochem Biophys Res Commun , vol.231 , pp. 340-343
    • Hyuga, S.1    Yamagata, S.2    Tai, T.3    Yamagata, T.4
  • 17
    • 79551515947 scopus 로고    scopus 로고
    • Structural analysis of glycans
    • A.C.R. Varki J.D. Esko (eds) et al. 2 Cold Spring Harbor Laboratory Press New York
    • Mulloy B, Hart GW, Stanley P (2009) Structural analysis of glycans. In: Varki ACR, Esko JD et al (eds) Essentials of glycobiology, 2nd edn. Cold Spring Harbor Laboratory Press, New York
    • (2009) Essentials of Glycobiology
    • Mulloy, B.1    Hart, G.W.2    Stanley, P.3
  • 18
    • 77954144429 scopus 로고    scopus 로고
    • Antibodies and lectins in glycan analysis
    • A.C.R. Varki J.D. Esko (eds) et al. 2 Cold Spring Harbor Laboratory Press New York
    • Cummings RD, Etzler ME (2009) Antibodies and lectins in glycan analysis. In: Varki ACR, Esko JD et al (eds) Essentials of glycobiology, 2nd edn. Cold Spring Harbor Laboratory Press, New York
    • (2009) Essentials of Glycobiology
    • Cummings, R.D.1    Etzler, M.E.2
  • 20
    • 79952284868 scopus 로고    scopus 로고
    • Accelerated biosynthesis of neolacto-series glycosphingolipids in differentiated mouse embryonal carcinoma F9 cells detected by using dodecyl N-acetylglucosaminide as a saccharide primer
    • 21148159 10.1093/jb/mvq142 1:CAS:528:DC%2BC3MXis1elurs%3D
    • Ogasawara N, Katagiri YU, Kiyokawa N, Kaneko T, Sato B, Nakajima H, Miyagawa Y, Kushi Y, Ishida H, Kiso M, Okita H, Sato T, Fujimoto J (2011) Accelerated biosynthesis of neolacto-series glycosphingolipids in differentiated mouse embryonal carcinoma F9 cells detected by using dodecyl N-acetylglucosaminide as a saccharide primer. J Biochem 149:321-330
    • (2011) J Biochem , vol.149 , pp. 321-330
    • Ogasawara, N.1    Katagiri, Y.U.2    Kiyokawa, N.3    Kaneko, T.4    Sato, B.5    Nakajima, H.6    Miyagawa, Y.7    Kushi, Y.8    Ishida, H.9    Kiso, M.10    Okita, H.11    Sato, T.12    Fujimoto, J.13
  • 21
    • 0031590791 scopus 로고    scopus 로고
    • Glycosylation of lactosylceramide analogs in animal cells: Amphipathic disaccharide primers for glycosphingolipid synthesis
    • 9434771 10.1006/bbrc.1997.7876 1:CAS:528:DyaK1cXivFygsQ%3D%3D
    • Miura Y, Yamagata T (1997) Glycosylation of lactosylceramide analogs in animal cells: amphipathic disaccharide primers for glycosphingolipid synthesis. Biochem Biophys Res Commun 241:698-703
    • (1997) Biochem Biophys Res Commun , vol.241 , pp. 698-703
    • Miura, Y.1    Yamagata, T.2
  • 22
    • 0031871002 scopus 로고    scopus 로고
    • Glycosylation of amphipathic lactoside primers with consequent inhibition of endogenous glycosphingolipid synthesis
    • 9644257 10.1093/oxfordjournals.jbchem.a022073 1:CAS:528: DyaK1cXmslyku74%3D
    • Nakajima H, Miura Y, Yamagata T (1998) Glycosylation of amphipathic lactoside primers with consequent inhibition of endogenous glycosphingolipid synthesis. J Biochem 124:148-156
    • (1998) J Biochem , vol.124 , pp. 148-156
    • Nakajima, H.1    Miura, Y.2    Yamagata, T.3
  • 23
    • 70649100501 scopus 로고    scopus 로고
    • Structural analysis of glycosphingolipid analogues obtained by the saccharide primer method using CE-ESI-MS
    • 19813238 10.1002/elps.200800719 1:CAS:528:DC%2BD1MXhtleqtbzM
    • Zhu X, Hatanaka K, Yamagata T, Sato T (2009) Structural analysis of glycosphingolipid analogues obtained by the saccharide primer method using CE-ESI-MS. Electrophoresis 30:3519-3526
    • (2009) Electrophoresis , vol.30 , pp. 3519-3526
    • Zhu, X.1    Hatanaka, K.2    Yamagata, T.3    Sato, T.4
  • 24
    • 0034527689 scopus 로고    scopus 로고
    • Azido glycoside primer: A versatile building block for the biocombinatorial synthesis of glycosphingolipid analogues
    • 11125817 10.1016/S0008-6215(00)00238-X 1:CAS:528:DC%2BD3cXptVWks7c%3D
    • Kasuya MCZ, Wang LX, Lee YC, Mitsuki M, Nakajima H, Miura Y, Sato T, Hatanaka K, Yamagata S, Yamagata T (2000) Azido glycoside primer: a versatile building block for the biocombinatorial synthesis of glycosphingolipid analogues. Carbohydr Res 329:755-763
    • (2000) Carbohydr Res , vol.329 , pp. 755-763
    • Kasuya, M.C.Z.1    Wang, L.X.2    Lee, Y.C.3    Mitsuki, M.4    Nakajima, H.5    Miura, Y.6    Sato, T.7    Hatanaka, K.8    Yamagata, S.9    Yamagata, T.10
  • 25
    • 39849084206 scopus 로고    scopus 로고
    • Glycosylation of dodecyl 2-acetamido-2-deoxy-beta-d-glucopyranoside and dodecyl beta-d-galactopyranosyl-(1-4)-2-acetamido-2-deoxy-beta-d-glucopyranoside as saccharide primers in cells
    • 18262174 10.1016/j.carres.2008.01.022 1:CAS:528:DC%2BD1cXjt1Gmur8%3D
    • Sato T, Takashiba M, Hayashi R, Zhu X, Yamagata T (2008) Glycosylation of dodecyl 2-acetamido-2-deoxy-beta-d-glucopyranoside and dodecyl beta-d-galactopyranosyl-(1-4)-2-acetamido-2-deoxy-beta-d-glucopyranoside as saccharide primers in cells. Carbohydr Res 343:831-838
    • (2008) Carbohydr Res , vol.343 , pp. 831-838
    • Sato, T.1    Takashiba, M.2    Hayashi, R.3    Zhu, X.4    Yamagata, T.5
  • 26
    • 0033975514 scopus 로고    scopus 로고
    • Synthesis and sorting of proteoglycans
    • 10633071 1:CAS:528:DC%2BD3cXht1ynt7k%3D
    • Prydz K, Dalen KT (2000) Synthesis and sorting of proteoglycans. J Cell Sci 113(Pt 2):193-205
    • (2000) J Cell Sci , vol.113 , Issue.PART 2 , pp. 193-205
    • Prydz, K.1    Dalen, K.T.2
  • 27
    • 84865825591 scopus 로고    scopus 로고
    • Glycosylation of Nα-lauryl-O-(β-d-xylopyranosyl)-l-serinamide as a Saccharide Primer in Cells
    • doi: 10.1016/j.carres.2012.08.003
    • Wang Y, Kumazawa T, Shiba K, Osumi K, Mizuno M, Sato T (2012) Glycosylation of Nα-lauryl-O-(β-d-xylopyranosyl)-l-serinamide as a Saccharide Primer in Cells. Carbohydr Res. doi: 10.1016/j.carres.2012.08.003
    • (2012) Carbohydr Res.
    • Wang, Y.1    Kumazawa, T.2    Shiba, K.3    Osumi, K.4    Mizuno, M.5    Sato, T.6
  • 28
    • 0020371140 scopus 로고
    • FBJ virus-induced osteosarcoma has type v collagen consisting of A, B and C-like chains in addition to type i collagen
    • 6284167 10.1016/0006-291X(82)91097-X 1:CAS:528:DyaL38XhslyqsL8%3D
    • Yamagata S, Miwa M, Tanaka K, Yamagata T (1982) FBJ virus-induced osteosarcoma has type V collagen consisting of A, B and C-like chains in addition to type I collagen. Biochem Biophys Res Commun 105:1208-1214
    • (1982) Biochem Biophys Res Commun , vol.105 , pp. 1208-1214
    • Yamagata, S.1    Miwa, M.2    Tanaka, K.3    Yamagata, T.4
  • 29
    • 0035501652 scopus 로고    scopus 로고
    • Ganglioside GD1a inhibits HGF-induced motility and scattering of cancer cells through suppression of tyrosine phosphorylation of c-Met
    • 11745410 10.1002/ijc.1481 1:CAS:528:DC%2BD3MXnsVers7o%3D
    • Hyuga S, Kawasaki N, Hyuga M, Ohta M, Shibayama R, Kawanishi T, Yamagata S, Yamagata T, Hayakawa T (2001) Ganglioside GD1a inhibits HGF-induced motility and scattering of cancer cells through suppression of tyrosine phosphorylation of c-Met. Int J Cancer 94:328-334
    • (2001) Int J Cancer , vol.94 , pp. 328-334
    • Hyuga, S.1    Kawasaki, N.2    Hyuga, M.3    Ohta, M.4    Shibayama, R.5    Kawanishi, T.6    Yamagata, S.7    Yamagata, T.8    Hayakawa, T.9
  • 30
    • 0032735239 scopus 로고    scopus 로고
    • Suppression by ganglioside GD1A of migration capability, adhesion to vitronectin and metastatic potential of highly metastatic FBJ-LL cells
    • 10521808 10.1002/(SICI)1097-0215(19991126)83:5<685: AID-IJC20>3.0.CO;2-4 1:CAS:528:DyaK1MXns1alsLo%3D
    • Hyuga S, Yamagata S, Takatsu Y, Hyuga M, Nakanishi H, Furukawa K, Yamagata T (1999) Suppression by ganglioside GD1A of migration capability, adhesion to vitronectin and metastatic potential of highly metastatic FBJ-LL cells. Int J Cancer 83:685-691
    • (1999) Int J Cancer , vol.83 , pp. 685-691
    • Hyuga, S.1    Yamagata, S.2    Takatsu, Y.3    Hyuga, M.4    Nakanishi, H.5    Furukawa, K.6    Yamagata, T.7
  • 31
    • 0024491207 scopus 로고
    • Gelatinases of murine metastatic tumor cells
    • 2536277 10.1016/S0006-291X(89)80202-5 1:CAS:528:DyaL1MXpt1ylsQ%3D%3D
    • Yamagata S, Tanaka R, Ito Y, Shimizu S (1989) Gelatinases of murine metastatic tumor cells. Biochem Biophys Res Commun 158:228-234
    • (1989) Biochem Biophys Res Commun , vol.158 , pp. 228-234
    • Yamagata, S.1    Tanaka, R.2    Ito, Y.3    Shimizu, S.4
  • 32
    • 79959905761 scopus 로고    scopus 로고
    • Ganglioside GD1a negatively regulates hepatocyte growth factor expression through caveolin-1 at the transcriptional level in murine osteosarcoma cells
    • 21554929 10.1016/j.bbagen.2011.04.006 1:CAS:528:DC%2BC3MXosVCkur4%3D
    • Zhang L, Wang Y, Wang L, Cao T, Hyuga S, Sato T, Wu Y, Yamagata S, Yamagata T (2011) Ganglioside GD1a negatively regulates hepatocyte growth factor expression through caveolin-1 at the transcriptional level in murine osteosarcoma cells. Biochim Biophys Acta 1810:759-768
    • (2011) Biochim Biophys Acta , vol.1810 , pp. 759-768
    • Zhang, L.1    Wang, Y.2    Wang, L.3    Cao, T.4    Hyuga, S.5    Sato, T.6    Wu, Y.7    Yamagata, S.8    Yamagata, T.9
  • 33
    • 84863698357 scopus 로고    scopus 로고
    • Ganglioside GD1a regulation of caveolin-1 and Stim1 expression in mouse FBJ cells: Augmented expression of caveolin-1 and Stim1 in cells with increased GD1a content
    • 16897174 10.1007/s10719-006-5742-3 1:CAS:528:DC%2BD28Xnsl2itr8%3D
    • Wang L, Takaku S, Wang P, Hu D, Hyuga S, Sato T, Yamagata S, Yamagata T (2006) Ganglioside GD1a regulation of caveolin-1 and Stim1 expression in mouse FBJ cells: augmented expression of caveolin-1 and Stim1 in cells with increased GD1a content. Glycoconj J 23:303-315
    • (2006) Glycoconj J , vol.23 , pp. 303-315
    • Wang, L.1    Takaku, S.2    Wang, P.3    Hu, D.4    Hyuga, S.5    Sato, T.6    Yamagata, S.7    Yamagata, T.8
  • 34
    • 44949231424 scopus 로고    scopus 로고
    • Analyzing real-time PCR data by the comparative C(T) method
    • 18546601 10.1038/nprot.2008.73 1:CAS:528:DC%2BD1cXmvVemt7c%3D
    • Schmittgen TD, Livak KJ (2008) Analyzing real-time PCR data by the comparative C(T) method. Nat Protoc 3:1101-1108
    • (2008) Nat Protoc , vol.3 , pp. 1101-1108
    • Schmittgen, T.D.1    Livak, K.J.2
  • 35
    • 45549097559 scopus 로고    scopus 로고
    • Identification of chondroitin sulfate glucuronyltransferase as chondroitin synthase-3 involved in chondroitin polymerization: Chondroitin polymerization is achieved by multiple enzyme complexes consisting of chondroitin synthase family members
    • 18316376 10.1074/jbc.M707549200 1:CAS:528:DC%2BD1cXkvVSgtrk%3D
    • Izumikawa T, Koike T, Shiozawa S, Sugahara K, Tamura J, Kitagawa H (2008) Identification of chondroitin sulfate glucuronyltransferase as chondroitin synthase-3 involved in chondroitin polymerization: chondroitin polymerization is achieved by multiple enzyme complexes consisting of chondroitin synthase family members. J Biol Chem 283:11396-11406
    • (2008) J Biol Chem , vol.283 , pp. 11396-11406
    • Izumikawa, T.1    Koike, T.2    Shiozawa, S.3    Sugahara, K.4    Tamura, J.5    Kitagawa, H.6
  • 37
    • 0036637267 scopus 로고    scopus 로고
    • Roles of heparan-sulphate glycosaminoglycans in cancer
    • 12094238 10.1038/nrc842 1:CAS:528:DC%2BD38XkvFKltLY%3D
    • Sasisekharan R, Shriver Z, Venkataraman G, Narayanasami U (2002) Roles of heparan-sulphate glycosaminoglycans in cancer. Nat Rev Cancer 2:521-528
    • (2002) Nat Rev Cancer , vol.2 , pp. 521-528
    • Sasisekharan, R.1    Shriver, Z.2    Venkataraman, G.3    Narayanasami, U.4
  • 38
    • 79953720259 scopus 로고    scopus 로고
    • Gene expression pattern in canine mammary osteosarcoma
    • 21528706 10.2478/v10181-011-0002-2 1:CAS:528:DC%2BC3MXnt1eksrw%3D
    • Pawlowski KM, Majewska A, Szyszko K, Dolka I, Motyl T, Krol M (2011) Gene expression pattern in canine mammary osteosarcoma. Pol J Vet Sci 14:11-20
    • (2011) Pol J Vet Sci , vol.14 , pp. 11-20
    • Pawlowski, K.M.1    Majewska, A.2    Szyszko, K.3    Dolka, I.4    Motyl, T.5    Krol, M.6
  • 39
    • 0036191984 scopus 로고    scopus 로고
    • Dynamic regulation of tumor growth and metastasis by heparan sulfate glycosaminoglycans
    • 11885027 10.1055/s-2002-20565 1:CAS:528:DC%2BD38XitlWlt7k%3D
    • Liu D, Shriver Z, Qi Y, Venkataraman G, Sasisekharan R (2002) Dynamic regulation of tumor growth and metastasis by heparan sulfate glycosaminoglycans. Semin Thromb Hemost 28:67-78
    • (2002) Semin Thromb Hemost , vol.28 , pp. 67-78
    • Liu, D.1    Shriver, Z.2    Qi, Y.3    Venkataraman, G.4    Sasisekharan, R.5
  • 42
    • 78449263436 scopus 로고    scopus 로고
    • Induction of heparanase-1 expression by mutant B-Raf kinase: Role of GA binding protein in heparanase-1 promoter activation
    • 21076620 1:CAS:528:DC%2BC3cXhsVGjtL3F
    • Rao G, Liu D, Xing M, Tauler J, Prinz RA, Xu X (2010) Induction of heparanase-1 expression by mutant B-Raf kinase: role of GA binding protein in heparanase-1 promoter activation. Neoplasia 12:946-956
    • (2010) Neoplasia , vol.12 , pp. 946-956
    • Rao, G.1    Liu, D.2    Xing, M.3    Tauler, J.4    Prinz, R.A.5    Xu, X.6
  • 43
    • 33745606964 scopus 로고    scopus 로고
    • Tumor suppressor p53 regulates heparanase gene expression
    • 16474844 10.1038/sj.onc.1209425 1:CAS:528:DC%2BD28XmtlahsL0%3D
    • Baraz L, Haupt Y, Elkin M, Peretz T, Vlodavsky I (2006) Tumor suppressor p53 regulates heparanase gene expression. Oncogene 25:3939-3947
    • (2006) Oncogene , vol.25 , pp. 3939-3947
    • Baraz, L.1    Haupt, Y.2    Elkin, M.3    Peretz, T.4    Vlodavsky, I.5
  • 44
    • 49649094763 scopus 로고    scopus 로고
    • Cathepsin L is responsible for processing and activation of proheparanase through multiple cleavages of a linker segment
    • 18450756 10.1074/jbc.M801327200 1:CAS:528:DC%2BD1cXnsVCgu7c%3D
    • Abboud-Jarrous G, Atzmon R, Peretz T, Palermo C, Gadea BB, Joyce JA, Vlodavsky I (2008) Cathepsin L is responsible for processing and activation of proheparanase through multiple cleavages of a linker segment. J Biol Chem 283:18167-18176
    • (2008) J Biol Chem , vol.283 , pp. 18167-18176
    • Abboud-Jarrous, G.1    Atzmon, R.2    Peretz, T.3    Palermo, C.4    Gadea, B.B.5    Joyce, J.A.6    Vlodavsky, I.7


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