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Volumn 53, Issue , 2006, Pages 297-321

Chondroitin Sulfate Proteoglycans in Tumor Progression

Author keywords

[No Author keywords available]

Indexed keywords

PROTEOCHONDROITIN SULFATE;

EID: 33846149695     PISSN: 10543589     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1054-3589(05)53014-X     Document Type: Review
Times cited : (40)

References (196)
  • 1
    • 0036907633 scopus 로고    scopus 로고
    • Bizarre parosteal osteochondromatous proliferation (Nora's lesion): A retrospective study of 12 cases, 2 arising in long bones
    • Abramovici L., and Steiner G.C. Bizarre parosteal osteochondromatous proliferation (Nora's lesion): A retrospective study of 12 cases, 2 arising in long bones. Hum. Pathol. 33 (2002) 1205-1210
    • (2002) Hum. Pathol. , vol.33 , pp. 1205-1210
    • Abramovici, L.1    Steiner, G.C.2
  • 3
    • 0025761007 scopus 로고
    • Hypomethylation of the decorin proteoglycan gene in human colon cancer
    • Adany R., and Iozzo R.V. Hypomethylation of the decorin proteoglycan gene in human colon cancer. Biochem. J. 276 Pt 2 (1991) 301-306
    • (1991) Biochem. J. , vol.276 , Issue.PART 2 , pp. 301-306
    • Adany, R.1    Iozzo, R.V.2
  • 5
    • 0037089667 scopus 로고    scopus 로고
    • Prognostic relevance of cell biologic and biochemical features in conventional chondrosarcomas
    • Aigner T., Muller S., Neureiter D., Illstrup D.M., Kirchner T., and Bjornsson J. Prognostic relevance of cell biologic and biochemical features in conventional chondrosarcomas. Cancer 94 (2002) 2273-2281
    • (2002) Cancer , vol.94 , pp. 2273-2281
    • Aigner, T.1    Muller, S.2    Neureiter, D.3    Illstrup, D.M.4    Kirchner, T.5    Bjornsson, J.6
  • 6
    • 0036589677 scopus 로고    scopus 로고
    • Interaction of CD44 with different forms of hyaluronic acid: Its role in adhesion and migration of tumor cells
    • Alaniz L., Cabrera P.V., Blanco G., Ernst G., Rimoldi G., Alvarez E., and Hajos S.E. Interaction of CD44 with different forms of hyaluronic acid: Its role in adhesion and migration of tumor cells. Cell Commun. Adhes. 9 (2002) 117-130
    • (2002) Cell Commun. Adhes. , vol.9 , pp. 117-130
    • Alaniz, L.1    Cabrera, P.V.2    Blanco, G.3    Ernst, G.4    Rimoldi, G.5    Alvarez, E.6    Hajos, S.E.7
  • 7
    • 0034118422 scopus 로고    scopus 로고
    • Type XV collagen in human colonic adenocarcinomas has a different distribution than other basement membrane zone proteins
    • Amenta P.S., Briggs K., Xu K., Gamboa E., Jukkola A.F., Li D., and Myers J.C. Type XV collagen in human colonic adenocarcinomas has a different distribution than other basement membrane zone proteins. Hum. Pathol. 31 (2000) 359-366
    • (2000) Hum. Pathol. , vol.31 , pp. 359-366
    • Amenta, P.S.1    Briggs, K.2    Xu, K.3    Gamboa, E.4    Jukkola, A.F.5    Li, D.6    Myers, J.C.7
  • 8
    • 0037371896 scopus 로고    scopus 로고
    • Loss of types XV and XIX collagen precedes basement membrane invasion in ductal carcinoma of the female breast
    • Amenta P.S., Hadad S., Lee M.T., Barnard N., Li D., and Myers J.C. Loss of types XV and XIX collagen precedes basement membrane invasion in ductal carcinoma of the female breast. J. Pathol. 199 (2003) 298-308
    • (2003) J. Pathol. , vol.199 , pp. 298-308
    • Amenta, P.S.1    Hadad, S.2    Lee, M.T.3    Barnard, N.4    Li, D.5    Myers, J.C.6
  • 9
    • 0036744260 scopus 로고    scopus 로고
    • Mice deficient in small leucine-rich proteoglycans: Novel in vivo models for osteoporosis, osteoarthritis, Ehlers-Danlos syndrome, muscular dystrophy, and corneal diseases
    • Ameye L., and Young M.F. Mice deficient in small leucine-rich proteoglycans: Novel in vivo models for osteoporosis, osteoarthritis, Ehlers-Danlos syndrome, muscular dystrophy, and corneal diseases. Glycobiology 12 (2002) 107R-116R
    • (2002) Glycobiology , vol.12
    • Ameye, L.1    Young, M.F.2
  • 10
    • 0025368750 scopus 로고
    • Glycosaminoglycan content, oxalate self-exchange and protein phosphorylation in erythrocytes of patients with "idiopathic" calcium oxalate nephrolithiasis
    • Baggio B., Marzaro G., Gambaro G., Marchini F., Williams H.E., and Borsatti A. Glycosaminoglycan content, oxalate self-exchange and protein phosphorylation in erythrocytes of patients with "idiopathic" calcium oxalate nephrolithiasis. Clin. Sci. Lond. 79 (1990) 113-116
    • (1990) Clin. Sci. Lond. , vol.79 , pp. 113-116
    • Baggio, B.1    Marzaro, G.2    Gambaro, G.3    Marchini, F.4    Williams, H.E.5    Borsatti, A.6
  • 11
    • 0344412939 scopus 로고    scopus 로고
    • Aberrant expression and localization of decorin in human oral dysplasia and squamous cell carcinoma
    • Banerjee A.G., Bhattacharyya I., Lydiatt W.M., and Vishwanatha J.K. Aberrant expression and localization of decorin in human oral dysplasia and squamous cell carcinoma. Cancer Res. 63 (2003) 7769-7776
    • (2003) Cancer Res. , vol.63 , pp. 7769-7776
    • Banerjee, A.G.1    Bhattacharyya, I.2    Lydiatt, W.M.3    Vishwanatha, J.K.4
  • 14
    • 85047683466 scopus 로고    scopus 로고
    • Inhibin binding protein (InhBP/p120), betaglycan, and the continuing search for the inhibin receptor
    • Bernard D.J., Chapman S.C., and Woodruff T.K. Inhibin binding protein (InhBP/p120), betaglycan, and the continuing search for the inhibin receptor. Mol. Endocrinol. 16 (2002) 207-212
    • (2002) Mol. Endocrinol. , vol.16 , pp. 207-212
    • Bernard, D.J.1    Chapman, S.C.2    Woodruff, T.K.3
  • 15
    • 0037413426 scopus 로고    scopus 로고
    • A comparative analysis of structure and spatial distribution of decorin in human leiomyoma and normal myometrium
    • Berto A.G., Sampaio L.O., Franco C.R., Cesar Jr. R.M., and Michelacci Y.M. A comparative analysis of structure and spatial distribution of decorin in human leiomyoma and normal myometrium. Biochim. Biophys. Acta 1619 (2003) 98-112
    • (2003) Biochim. Biophys. Acta , vol.1619 , pp. 98-112
    • Berto, A.G.1    Sampaio, L.O.2    Franco, C.R.3    Cesar Jr., R.M.4    Michelacci, Y.M.5
  • 16
    • 10344256152 scopus 로고    scopus 로고
    • Expression of HYAL2 mRNA, hyaluronan and hyaluronidase in B-cell non-Hodgkin lymphoma: Relationship with tumor aggressiveness
    • Bertrand P., Courel M.N., Maingonnat C., Jardin F., Tilly H., and Bastard C. Expression of HYAL2 mRNA, hyaluronan and hyaluronidase in B-cell non-Hodgkin lymphoma: Relationship with tumor aggressiveness. Int. J. Cancer 113 (2005) 207-212
    • (2005) Int. J. Cancer , vol.113 , pp. 207-212
    • Bertrand, P.1    Courel, M.N.2    Maingonnat, C.3    Jardin, F.4    Tilly, H.5    Bastard, C.6
  • 17
    • 11844301388 scopus 로고    scopus 로고
    • Matrix revolutions: "Tails" of basement-membrane components with angiostatic functions
    • Bix G., and Iozzo R.V. Matrix revolutions: "Tails" of basement-membrane components with angiostatic functions. Trends Cell Biol. 15 (2005) 52-60
    • (2005) Trends Cell Biol. , vol.15 , pp. 52-60
    • Bix, G.1    Iozzo, R.V.2
  • 19
    • 0031685581 scopus 로고    scopus 로고
    • Expression of the NG2 proteoglycan enhances the growth and metastatic properties of melanoma cells
    • Burg M.A., Grako K.A., and Stallcup W.B. Expression of the NG2 proteoglycan enhances the growth and metastatic properties of melanoma cells. J. Cell. Physiol. 177 (1998) 299-312
    • (1998) J. Cell. Physiol. , vol.177 , pp. 299-312
    • Burg, M.A.1    Grako, K.A.2    Stallcup, W.B.3
  • 20
    • 11144232998 scopus 로고    scopus 로고
    • Human high molecular weight-melanoma-associated antigen (HMW-MAA): A melanoma cell surface chondroitin sulfate proteoglycan (MSCP) with biological and clinical significance
    • Campoli M.R., Chang C.C., Kageshita T., Wang X., McCarthy J.B., and Ferrone S. Human high molecular weight-melanoma-associated antigen (HMW-MAA): A melanoma cell surface chondroitin sulfate proteoglycan (MSCP) with biological and clinical significance. Crit. Rev. Immunol. 24 (2004) 267-296
    • (2004) Crit. Rev. Immunol. , vol.24 , pp. 267-296
    • Campoli, M.R.1    Chang, C.C.2    Kageshita, T.3    Wang, X.4    McCarthy, J.B.5    Ferrone, S.6
  • 21
    • 1642392311 scopus 로고    scopus 로고
    • Increased and localized accumulation of chondroitin sulphate proteoglycans in the hyperplastic human prostate
    • Cardoso L.E., Falcao P.G., and Sampaio F.J. Increased and localized accumulation of chondroitin sulphate proteoglycans in the hyperplastic human prostate. BJU Int. 93 (2004) 532-538
    • (2004) BJU Int. , vol.93 , pp. 532-538
    • Cardoso, L.E.1    Falcao, P.G.2    Sampaio, F.J.3
  • 22
    • 3042745689 scopus 로고    scopus 로고
    • The globular domains of PG-M/versican modulate the proliferation-apoptosis equilibrium and invasive capabilities of tumor cells
    • Cattaruzza S., Schiappacassi M., Kimata K., Colombatti A., and Perris R. The globular domains of PG-M/versican modulate the proliferation-apoptosis equilibrium and invasive capabilities of tumor cells. FASEB J. 18 (2004) 779-781
    • (2004) FASEB J. , vol.18 , pp. 779-781
    • Cattaruzza, S.1    Schiappacassi, M.2    Kimata, K.3    Colombatti, A.4    Perris, R.5
  • 23
    • 0346037291 scopus 로고    scopus 로고
    • Distribution of PG-M/versican variants in human tissues and de novo expression of isoform V3 upon endothelial cell activation, migration, and neoangiogenesis in vitro
    • Cattaruzza S., Schiappacassi M., Ljungberg-Rose A., Spessotto P., Perissinotto D., Morgelin M., Mucignat M.T., Colombatti A., and Perris R. Distribution of PG-M/versican variants in human tissues and de novo expression of isoform V3 upon endothelial cell activation, migration, and neoangiogenesis in vitro. J. Biol. Chem. 277 (2002) 47626-47635
    • (2002) J. Biol. Chem. , vol.277 , pp. 47626-47635
    • Cattaruzza, S.1    Schiappacassi, M.2    Ljungberg-Rose, A.3    Spessotto, P.4    Perissinotto, D.5    Morgelin, M.6    Mucignat, M.T.7    Colombatti, A.8    Perris, R.9
  • 25
    • 0036163970 scopus 로고    scopus 로고
    • Neoplastic changes in saccharide sequence of dermatan sulfate chains derived from human colon cancer
    • Daidouji K., Takagaki K., Yoshihara S., Matsuya H., Sasaki M., and Endo M. Neoplastic changes in saccharide sequence of dermatan sulfate chains derived from human colon cancer. Dig. Dis. Sci. 47 (2002) 331-337
    • (2002) Dig. Dis. Sci. , vol.47 , pp. 331-337
    • Daidouji, K.1    Takagaki, K.2    Yoshihara, S.3    Matsuya, H.4    Sasaki, M.5    Endo, M.6
  • 26
  • 27
    • 0029785662 scopus 로고    scopus 로고
    • Decorin-induced growth suppression is associated with up-regulation of p21, an inhibitor of cyclin-dependent kinases
    • De Luca A., Santra M., Baldi A., Giordano A., and Iozzo R.V. Decorin-induced growth suppression is associated with up-regulation of p21, an inhibitor of cyclin-dependent kinases. J. Biol. Chem. 271 (1996) 18961-18965
    • (1996) J. Biol. Chem. , vol.271 , pp. 18961-18965
    • De Luca, A.1    Santra, M.2    Baldi, A.3    Giordano, A.4    Iozzo, R.V.5
  • 29
    • 0035970621 scopus 로고    scopus 로고
    • Anti-tumor activities of chondroitinase AC and chondroitinase B: Inhibition of angiogenesis, proliferation and invasion
    • Denholm E.M., Lin Y.Q., and Silver P.J. Anti-tumor activities of chondroitinase AC and chondroitinase B: Inhibition of angiogenesis, proliferation and invasion. Eur. J. Pharmacol. 416 (2001) 213-221
    • (2001) Eur. J. Pharmacol. , vol.416 , pp. 213-221
    • Denholm, E.M.1    Lin, Y.Q.2    Silver, P.J.3
  • 30
    • 5444261094 scopus 로고    scopus 로고
    • The stroma reaction myofibroblast: A key player in the control of tumor cell behavior
    • Desmouliere A., Guyot C., and Gabbiani G. The stroma reaction myofibroblast: A key player in the control of tumor cell behavior. Int. J. Dev. Biol. 48 (2004) 509-517
    • (2004) Int. J. Dev. Biol. , vol.48 , pp. 509-517
    • Desmouliere, A.1    Guyot, C.2    Gabbiani, G.3
  • 31
    • 0142120297 scopus 로고    scopus 로고
    • Differential expression of versican isoforms is a component of the human melanoma cell differentiation process
    • Domenzain C., Docampo M.J., Serra M., Miquel L., and Bassols A. Differential expression of versican isoforms is a component of the human melanoma cell differentiation process. Biochim. Biophys. Acta 1642 (2003) 107-114
    • (2003) Biochim. Biophys. Acta , vol.1642 , pp. 107-114
    • Domenzain, C.1    Docampo, M.J.2    Serra, M.3    Miquel, L.4    Bassols, A.5
  • 32
    • 0031842692 scopus 로고    scopus 로고
    • Cell biology of astrocyte proteoglycans
    • Dow K.E., and Wang W. Cell biology of astrocyte proteoglycans. Cell. Mol. Life Sci. 54 (1998) 567-581
    • (1998) Cell. Mol. Life Sci. , vol.54 , pp. 567-581
    • Dow, K.E.1    Wang, W.2
  • 33
    • 3142713032 scopus 로고    scopus 로고
    • Testican-1: A differentially expressed proteoglycan with protease inhibiting activities
    • Edgell C.J., BaSalamah M.A., and Marr H.S. Testican-1: A differentially expressed proteoglycan with protease inhibiting activities. Int. Rev. Cytol. 236 (2004) 101-122
    • (2004) Int. Rev. Cytol. , vol.236 , pp. 101-122
    • Edgell, C.J.1    BaSalamah, M.A.2    Marr, H.S.3
  • 34
    • 0142103466 scopus 로고    scopus 로고
    • Cleavage of syndecan-1 by membrane type matrix metalloproteinase-1 stimulates cell migration
    • Endo K., Takino T., Miyamori H., Kinsen H., Yoshizaki T., Furukawa M., and Sato H. Cleavage of syndecan-1 by membrane type matrix metalloproteinase-1 stimulates cell migration. J. Biol. Chem. 278 (2003) 40764-40770
    • (2003) J. Biol. Chem. , vol.278 , pp. 40764-40770
    • Endo, K.1    Takino, T.2    Miyamori, H.3    Kinsen, H.4    Yoshizaki, T.5    Furukawa, M.6    Sato, H.7
  • 35
    • 0024297813 scopus 로고
    • Tumor formation dependent on proteoglycan biosynthesis
    • Esko J.D., Rostand K.S., and Weinke J.L. Tumor formation dependent on proteoglycan biosynthesis. Science 241 (1988) 1092-1096
    • (1988) Science , vol.241 , pp. 1092-1096
    • Esko, J.D.1    Rostand, K.S.2    Weinke, J.L.3
  • 36
    • 0034442863 scopus 로고    scopus 로고
    • Progress in deciphering the information content of the "glycome": A crescendo in the closing years of the millennium
    • Feizi T. Progress in deciphering the information content of the "glycome": A crescendo in the closing years of the millennium. Glycoconj. J. 17 (2000) 553-565
    • (2000) Glycoconj. J. , vol.17 , pp. 553-565
    • Feizi, T.1
  • 38
    • 0035005707 scopus 로고    scopus 로고
    • Glypicans in growth control and cancer
    • Filmus J. Glypicans in growth control and cancer. Glycobiology 11 (2001) 19R-23R
    • (2001) Glycobiology , vol.11
    • Filmus, J.1
  • 40
    • 0028057613 scopus 로고
    • Disruption of epithelial cell-matrix interactions induces apoptosis
    • Frisch S.M., and Francis H. Disruption of epithelial cell-matrix interactions induces apoptosis. J. Cell Biol. 124 (1994) 619-626
    • (1994) J. Cell Biol. , vol.124 , pp. 619-626
    • Frisch, S.M.1    Francis, H.2
  • 41
    • 0020577072 scopus 로고
    • A cell-surface molecule involved in organ-specific homing of lymphocytes
    • Gallatin W.M., Weissman I.L., and Butcher E.C. A cell-surface molecule involved in organ-specific homing of lymphocytes. Nature 304 (1983) 30-34
    • (1983) Nature , vol.304 , pp. 30-34
    • Gallatin, W.M.1    Weissman, I.L.2    Butcher, E.C.3
  • 42
    • 10744221616 scopus 로고    scopus 로고
    • Essential role of glycosaminoglycans in Fgf signaling during mouse gastrulation
    • Garcia-Garcia M.J., and Anderson K.V. Essential role of glycosaminoglycans in Fgf signaling during mouse gastrulation. Cell 114 (2003) 727-737
    • (2003) Cell , vol.114 , pp. 727-737
    • Garcia-Garcia, M.J.1    Anderson, K.V.2
  • 43
    • 0037063999 scopus 로고    scopus 로고
    • Hyaluronan oligosaccharides inhibit anchorage-independent growth of tumor cells by suppressing the phosphoinositide 3-kinase/Akt cell survival pathway
    • Ghatak S., Misra S., and Toole B.P. Hyaluronan oligosaccharides inhibit anchorage-independent growth of tumor cells by suppressing the phosphoinositide 3-kinase/Akt cell survival pathway. J. Biol. Chem. 277 (2002) 38013-38020
    • (2002) J. Biol. Chem. , vol.277 , pp. 38013-38020
    • Ghatak, S.1    Misra, S.2    Toole, B.P.3
  • 44
    • 0029913918 scopus 로고    scopus 로고
    • Expression of CD44 splice variants in normal respiratory epithelium and bronchial carcinomas: No evidence for altered CD44 splicing in metastasis
    • Givehchian M., Woerner S.M., Lacroix J., Zoller M., Drings P., Becker H., Kayser K., Ridder R., and von Knebel Doeberitz M. Expression of CD44 splice variants in normal respiratory epithelium and bronchial carcinomas: No evidence for altered CD44 splicing in metastasis. Oncogene 12 (1996) 1137-1144
    • (1996) Oncogene , vol.12 , pp. 1137-1144
    • Givehchian, M.1    Woerner, S.M.2    Lacroix, J.3    Zoller, M.4    Drings, P.5    Becker, H.6    Kayser, K.7    Ridder, R.8    von Knebel Doeberitz, M.9
  • 45
    • 0035016641 scopus 로고    scopus 로고
    • Matrix gene expression analysis and cellular phenotyping in chordoma reveals focal differentiation pattern of neoplastic cells mimicking nucleus pulposus development
    • Gottschalk D., Fehn M., Patt S., Saeger W., Kirchner T., and Aigner T. Matrix gene expression analysis and cellular phenotyping in chordoma reveals focal differentiation pattern of neoplastic cells mimicking nucleus pulposus development. Am. J. Pathol. 158 (2001) 1571-1578
    • (2001) Am. J. Pathol. , vol.158 , pp. 1571-1578
    • Gottschalk, D.1    Fehn, M.2    Patt, S.3    Saeger, W.4    Kirchner, T.5    Aigner, T.6
  • 50
    • 0027848938 scopus 로고
    • Differential expression of CD44 splice variants in intestinal- and diffuse-type human gastric carcinomas and normal gastric mucosa
    • Heider K.H., Dammrich J., Skroch-Angel P., Muller-Hermelink H.K., Vollmers H.P., Herrlich P., and Ponta H. Differential expression of CD44 splice variants in intestinal- and diffuse-type human gastric carcinomas and normal gastric mucosa. Cancer Res. 53 (1993) 4197-4203
    • (1993) Cancer Res. , vol.53 , pp. 4197-4203
    • Heider, K.H.1    Dammrich, J.2    Skroch-Angel, P.3    Muller-Hermelink, H.K.4    Vollmers, H.P.5    Herrlich, P.6    Ponta, H.7
  • 51
    • 0030568078 scopus 로고    scopus 로고
    • The effect of TGF-beta 1 on cell proliferation and proteoglycan production in human melanoma cells depends on the degree of cell differentiation
    • Heredia A., Villena J., Romaris M., Molist A., and Bassols A. The effect of TGF-beta 1 on cell proliferation and proteoglycan production in human melanoma cells depends on the degree of cell differentiation. Cancer Lett. 109 (1996) 39-47
    • (1996) Cancer Lett. , vol.109 , pp. 39-47
    • Heredia, A.1    Villena, J.2    Romaris, M.3    Molist, A.4    Bassols, A.5
  • 53
    • 1342300719 scopus 로고    scopus 로고
    • Introduction: Stroma reaction and cancer progression
    • Hornebeck W., and Birembaut P. Introduction: Stroma reaction and cancer progression. Crit. Rev. Oncol. Hematol. 49 (2004) 177-178
    • (2004) Crit. Rev. Oncol. Hematol. , vol.49 , pp. 177-178
    • Hornebeck, W.1    Birembaut, P.2
  • 54
    • 0344443722 scopus 로고    scopus 로고
    • Thrombomodulin-mediated cell adhesion: Involvement of its lectin-like domain
    • Huang H.C., Shi G.Y., Jiang S.J., Shi C.S., Wu C.M., Yang H.Y., and Wu H.L. Thrombomodulin-mediated cell adhesion: Involvement of its lectin-like domain. J. Biol. Chem. 278 (2003) 46750-46759
    • (2003) J. Biol. Chem. , vol.278 , pp. 46750-46759
    • Huang, H.C.1    Shi, G.Y.2    Jiang, S.J.3    Shi, C.S.4    Wu, C.M.5    Yang, H.Y.6    Wu, H.L.7
  • 55
    • 0029974248 scopus 로고    scopus 로고
    • Altered expression of CD44 isoforms in squamous-cell carcinomas and cell lines derived from them
    • Hudson D.L., Speight P.M., and Watt F.M. Altered expression of CD44 isoforms in squamous-cell carcinomas and cell lines derived from them. Int. J. Cancer 66 (1996) 457-463
    • (1996) Int. J. Cancer , vol.66 , pp. 457-463
    • Hudson, D.L.1    Speight, P.M.2    Watt, F.M.3
  • 56
    • 0028929294 scopus 로고
    • Altered immunohistochemical expression of small proteoglycans in the tumor tissue and stroma of basal cell carcinoma
    • Hunzelmann N., Schonherr E., Bonnekoh B., Hartmann C., Kresse H., and Krieg T. Altered immunohistochemical expression of small proteoglycans in the tumor tissue and stroma of basal cell carcinoma. J. Invest. Dermatol. 104 (1995) 509-513
    • (1995) J. Invest. Dermatol. , vol.104 , pp. 509-513
    • Hunzelmann, N.1    Schonherr, E.2    Bonnekoh, B.3    Hartmann, C.4    Kresse, H.5    Krieg, T.6
  • 57
    • 0029940271 scopus 로고    scopus 로고
    • Cell surface chondroitin sulfate proteoglycans in tumor cell adhesion, motility and invasion
    • Iida J., Meijne A.M., Knutson J.R., Furcht L.T., and McCarthy J.B. Cell surface chondroitin sulfate proteoglycans in tumor cell adhesion, motility and invasion. Semin. Cancer Biol. 7 (1996) 155-162
    • (1996) Semin. Cancer Biol. , vol.7 , pp. 155-162
    • Iida, J.1    Meijne, A.M.2    Knutson, J.R.3    Furcht, L.T.4    McCarthy, J.B.5
  • 58
    • 0032489387 scopus 로고    scopus 로고
    • A role of chondroitin sulfate glycosaminoglycan binding site in alpha4beta1 integrin-mediated melanoma cell adhesion
    • Iida J., Meijne A.M., Oegema Jr. T.R., Yednock T.A., Kovach N.L., Furcht L.T., and McCarthy J.B. A role of chondroitin sulfate glycosaminoglycan binding site in alpha4beta1 integrin-mediated melanoma cell adhesion. J. Biol. Chem. 273 (1998) 5955-5962
    • (1998) J. Biol. Chem. , vol.273 , pp. 5955-5962
    • Iida, J.1    Meijne, A.M.2    Oegema Jr., T.R.3    Yednock, T.A.4    Kovach, N.L.5    Furcht, L.T.6    McCarthy, J.B.7
  • 59
    • 0035374347 scopus 로고    scopus 로고
    • Melanoma chondroitin sulfate proteoglycan regulates matrix metalloproteinase-dependent human melanoma invasion into type I collagen
    • Iida J., Pei D., Kang T., Simpson M.A., Herlyn M., Furcht L.T., and McCarthy J.B. Melanoma chondroitin sulfate proteoglycan regulates matrix metalloproteinase-dependent human melanoma invasion into type I collagen. J. Biol. Chem. 276 (2001) 18786-18794
    • (2001) J. Biol. Chem. , vol.276 , pp. 18786-18794
    • Iida, J.1    Pei, D.2    Kang, T.3    Simpson, M.A.4    Herlyn, M.5    Furcht, L.T.6    McCarthy, J.B.7
  • 61
    • 0017152358 scopus 로고
    • The stromal reaction of tumors: An expression of immune surveillance
    • Ioachim H.L. The stromal reaction of tumors: An expression of immune surveillance. J. Natl. Cancer Inst. 57 (1976) 465-475
    • (1976) J. Natl. Cancer Inst. , vol.57 , pp. 465-475
    • Ioachim, H.L.1
  • 62
    • 0029353166 scopus 로고
    • Tumor stroma as a regulator of neoplastic behavior: Agonistic and antagonistic elements embedded in the same connective tissue
    • Iozzo R.V. Tumor stroma as a regulator of neoplastic behavior: Agonistic and antagonistic elements embedded in the same connective tissue. Lab. Invest. 73 (1995) 157-160
    • (1995) Lab. Invest. , vol.73 , pp. 157-160
    • Iozzo, R.V.1
  • 63
    • 0031657808 scopus 로고    scopus 로고
    • Matrix proteoglycans: From molecular design to cellular function
    • Iozzo R.V. Matrix proteoglycans: From molecular design to cellular function. Annu. Rev. Biochem. 67 (1998) 609-652
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 609-652
    • Iozzo, R.V.1
  • 64
    • 0033516558 scopus 로고    scopus 로고
    • The biology of the small leucine-rich proteoglycans: Functional network of interactive proteins
    • Iozzo R.V. The biology of the small leucine-rich proteoglycans: Functional network of interactive proteins. J. Biol. Chem. 274 (1999) 18843-18846
    • (1999) J. Biol. Chem. , vol.274 , pp. 18843-18846
    • Iozzo, R.V.1
  • 65
    • 0028018781 scopus 로고
    • Altered proteoglycan gene expression and the tumor stroma
    • Iozzo R.V., and Cohen I. Altered proteoglycan gene expression and the tumor stroma. EXS 70 (1994) 199-214
    • (1994) EXS , vol.70 , pp. 199-214
    • Iozzo, R.V.1    Cohen, I.2
  • 66
    • 0033582415 scopus 로고    scopus 로고
    • Decorin is a biological ligand for the epidermal growth factor receptor
    • Iozzo R.V., Moscatello D.K., McQuillan D.J., and Eichstetter I. Decorin is a biological ligand for the epidermal growth factor receptor. J. Biol. Chem. 274 (1999) 4489-4492
    • (1999) J. Biol. Chem. , vol.274 , pp. 4489-4492
    • Iozzo, R.V.1    Moscatello, D.K.2    McQuillan, D.J.3    Eichstetter, I.4
  • 67
    • 0029833998 scopus 로고    scopus 로고
    • 2B1 antigen characteristically expressed on extracellular matrices of human malignant tumors is a large chondroitin sulfate proteoglycan, PG-M/versican
    • Isogai Z., Shinomura T., Yamakawa N., Takeuchi J., Tsuji T., Heinegard D., and Kimata K. 2B1 antigen characteristically expressed on extracellular matrices of human malignant tumors is a large chondroitin sulfate proteoglycan, PG-M/versican. Cancer Res. 56 (1996) 3902-3908
    • (1996) Cancer Res. , vol.56 , pp. 3902-3908
    • Isogai, Z.1    Shinomura, T.2    Yamakawa, N.3    Takeuchi, J.4    Tsuji, T.5    Heinegard, D.6    Kimata, K.7
  • 68
    • 0036710437 scopus 로고    scopus 로고
    • Immunohistochemical localization of large chondroitin sulfate proteoglycan in odontogenic tumor
    • Ito Y., Abiko Y., Tanaka Y., Rahemtulla F., and Kaku T. Immunohistochemical localization of large chondroitin sulfate proteoglycan in odontogenic tumor. Med. Electron Microsc. 35 (2002) 173-177
    • (2002) Med. Electron Microsc. , vol.35 , pp. 173-177
    • Ito, Y.1    Abiko, Y.2    Tanaka, Y.3    Rahemtulla, F.4    Kaku, T.5
  • 69
    • 0037238131 scopus 로고    scopus 로고
    • The lymphatics revisited: New perspectives from the hyaluronan receptor LYVE-1
    • Jackson D.G. The lymphatics revisited: New perspectives from the hyaluronan receptor LYVE-1. Trends Cardiovasc. Med. 13 (2003) 1-7
    • (2003) Trends Cardiovasc. Med. , vol.13 , pp. 1-7
    • Jackson, D.G.1
  • 70
    • 0028809263 scopus 로고
    • Proteoglycan forms of the lymphocyte homing receptor CD44 are alternatively spliced variants containing the v3 exon
    • Jackson D.G., Bell J.I., Dickinson R., Timans J., Shields J., and Whittle N. Proteoglycan forms of the lymphocyte homing receptor CD44 are alternatively spliced variants containing the v3 exon. J. Cell Biol. 128 (1995) 673-685
    • (1995) J. Cell Biol. , vol.128 , pp. 673-685
    • Jackson, D.G.1    Bell, J.I.2    Dickinson, R.3    Timans, J.4    Shields, J.5    Whittle, N.6
  • 71
    • 0025835537 scopus 로고
    • Glycosaminoglycans as polyelectrolytes: Rejuvenation of original concepts
    • Jaques L.B. Glycosaminoglycans as polyelectrolytes: Rejuvenation of original concepts. Semin. Thromb. Hemost. 17 Suppl 1 (1991) 1-4
    • (1991) Semin. Thromb. Hemost. , vol.17 , Issue.SUPPL. 1 , pp. 1-4
    • Jaques, L.B.1
  • 73
    • 0037277035 scopus 로고    scopus 로고
    • CD44 and its partners in metastasis
    • Jothy S. CD44 and its partners in metastasis. Clin. Exp. Metastasis 20 (2003) 195-201
    • (2003) Clin. Exp. Metastasis , vol.20 , pp. 195-201
    • Jothy, S.1
  • 74
    • 0022390059 scopus 로고
    • Immunohistological detection of human malignant melanoma using monoclonal antibody to a melanoma-associated antigen
    • Kageshita T., Johno M., Ono T., Arao T., and Imai K. Immunohistological detection of human malignant melanoma using monoclonal antibody to a melanoma-associated antigen. Arch. Dermatol. Res. 277 (1985) 334-336
    • (1985) Arch. Dermatol. Res. , vol.277 , pp. 334-336
    • Kageshita, T.1    Johno, M.2    Ono, T.3    Arao, T.4    Imai, K.5
  • 75
    • 0037240613 scopus 로고    scopus 로고
    • Hyaluronan, CD44 and versican in epidermal keratinocyte tumours
    • Karvinen S., Kosma V.M., Tammi M.I., and Tammi R. Hyaluronan, CD44 and versican in epidermal keratinocyte tumours. Br. J. Dermatol. 148 (2003) 86-94
    • (2003) Br. J. Dermatol. , vol.148 , pp. 86-94
    • Karvinen, S.1    Kosma, V.M.2    Tammi, M.I.3    Tammi, R.4
  • 76
    • 0036653448 scopus 로고    scopus 로고
    • Angiogenesis inhibitors in lung cancer
    • Kim E.S., and Herbst R.S. Angiogenesis inhibitors in lung cancer. Curr. Oncol. Rep. 4 (2002) 325-333
    • (2002) Curr. Oncol. Rep. , vol.4 , pp. 325-333
    • Kim, E.S.1    Herbst, R.S.2
  • 79
    • 0033570019 scopus 로고    scopus 로고
    • Structural characteristics of oversulfated chondroitin/dermatan sulfates in the fibrous lesions of the liver with cirrhosis
    • Koshiishi I., Takenouchi M., and Imanari T. Structural characteristics of oversulfated chondroitin/dermatan sulfates in the fibrous lesions of the liver with cirrhosis. Arch. Biochem. Biophys. 370 (1999) 151-155
    • (1999) Arch. Biochem. Biophys. , vol.370 , pp. 151-155
    • Koshiishi, I.1    Takenouchi, M.2    Imanari, T.3
  • 81
    • 0026759822 scopus 로고
    • The core protein of epican, a heparan sulfate proteoglycan on keratinocytes, is an alternative form of CD44
    • Kugelman L.C., Ganguly S., Haggerty J.G., Weissman S.M., and Milstone L.M. The core protein of epican, a heparan sulfate proteoglycan on keratinocytes, is an alternative form of CD44. J. Invest. Dermatol. 99 (1992) 886-891
    • (1992) J. Invest. Dermatol. , vol.99 , pp. 886-891
    • Kugelman, L.C.1    Ganguly, S.2    Haggerty, J.G.3    Weissman, S.M.4    Milstone, L.M.5
  • 82
    • 4143149752 scopus 로고    scopus 로고
    • Lumican expression is associated with the formation of mesenchyme-like elements in salivary pleomorphic adenomas
    • Kusafuka K., Ishiwata T., Sugisaki Y., Takemura T., Kusafuka M., Hisha H., and Ikehara S. Lumican expression is associated with the formation of mesenchyme-like elements in salivary pleomorphic adenomas. J. Pathol. 203 (2004) 953-960
    • (2004) J. Pathol. , vol.203 , pp. 953-960
    • Kusafuka, K.1    Ishiwata, T.2    Sugisaki, Y.3    Takemura, T.4    Kusafuka, M.5    Hisha, H.6    Ikehara, S.7
  • 86
    • 0034698054 scopus 로고    scopus 로고
    • Basement membrane zone type XV collagen is a disulfide-bonded chondroitin sulfate proteoglycan in human tissues and cultured cells
    • Li D., Clark C.C., and Myers J.C. Basement membrane zone type XV collagen is a disulfide-bonded chondroitin sulfate proteoglycan in human tissues and cultured cells. J. Biol. Chem. 275 (2000) 22339-22347
    • (2000) J. Biol. Chem. , vol.275 , pp. 22339-22347
    • Li, D.1    Clark, C.C.2    Myers, J.C.3
  • 87
    • 1842367361 scopus 로고    scopus 로고
    • Glypican and biglycan in the nuclei of neurons and glioma cells: Presence of functional nuclear localization signals and dynamic changes in glypican during the cell cycle
    • Liang Y., Haring M., Roughley P.J., Margolis R.K., and Margolis R.U. Glypican and biglycan in the nuclei of neurons and glioma cells: Presence of functional nuclear localization signals and dynamic changes in glypican during the cell cycle. J. Cell Biol. 139 (1997) 851-864
    • (1997) J. Cell Biol. , vol.139 , pp. 851-864
    • Liang, Y.1    Haring, M.2    Roughley, P.J.3    Margolis, R.K.4    Margolis, R.U.5
  • 88
    • 0029112809 scopus 로고
    • Heparin proteoglycans synthesized by mouse mastocytoma contain chondroitin sulphate
    • Lidholt K., Eriksson I., and Kjellen L. Heparin proteoglycans synthesized by mouse mastocytoma contain chondroitin sulphate. Biochem. J. 311 Pt 1 (1995) 233-238
    • (1995) Biochem. J. , vol.311 , Issue.PART 1 , pp. 233-238
    • Lidholt, K.1    Eriksson, I.2    Kjellen, L.3
  • 89
    • 0030691086 scopus 로고    scopus 로고
    • Overexpression of a single helix-loop-helix-type transcription factor, scleraxis, enhances aggrecan gene expression in osteoblastic osteosarcoma ROS17/2.8 cells
    • Liu Y., Watanabe H., Nifuji A., Yamada Y., Olson E.N., and Noda M. Overexpression of a single helix-loop-helix-type transcription factor, scleraxis, enhances aggrecan gene expression in osteoblastic osteosarcoma ROS17/2.8 cells. J. Biol. Chem. 272 (1997) 29880-29885
    • (1997) J. Biol. Chem. , vol.272 , pp. 29880-29885
    • Liu, Y.1    Watanabe, H.2    Nifuji, A.3    Yamada, Y.4    Olson, E.N.5    Noda, M.6
  • 90
    • 16844364920 scopus 로고    scopus 로고
    • HYAL1 hyaluronidase: A molecular determinant of bladder tumor growth and invasion
    • Lokeshwar V.B., Cerwinka W.H., and Lokeshwar B.L. HYAL1 hyaluronidase: A molecular determinant of bladder tumor growth and invasion. Cancer Res. 65 (2005) 2243-2250
    • (2005) Cancer Res. , vol.65 , pp. 2243-2250
    • Lokeshwar, V.B.1    Cerwinka, W.H.2    Lokeshwar, B.L.3
  • 91
    • 0025987832 scopus 로고
    • Structure and expression of the membrane proteoglycan betaglycan, a component of the TGF-beta receptor system
    • Lopez-Casillas F., Cheifetz S., Doody J., Andres J.L., Lane W.S., and Massague J. Structure and expression of the membrane proteoglycan betaglycan, a component of the TGF-beta receptor system. Cell 67 (1991) 785-795
    • (1991) Cell , vol.67 , pp. 785-795
    • Lopez-Casillas, F.1    Cheifetz, S.2    Doody, J.3    Andres, J.L.4    Lane, W.S.5    Massague, J.6
  • 92
    • 17844374587 scopus 로고    scopus 로고
    • Functional comparison of long and short splice forms of RPTPbeta: Implications for glioblastoma treatment
    • Lorente G., Nelson A., Mueller S., Kuo J., Urfer R., Nikolich K., and Foehr E.D. Functional comparison of long and short splice forms of RPTPbeta: Implications for glioblastoma treatment. Neurooncology 7 (2005) 154-163
    • (2005) Neurooncology , vol.7 , pp. 154-163
    • Lorente, G.1    Nelson, A.2    Mueller, S.3    Kuo, J.4    Urfer, R.5    Nikolich, K.6    Foehr, E.D.7
  • 94
    • 11244323919 scopus 로고    scopus 로고
    • Phosphorylation of NG2 proteoglycan by protein kinase C-alpha regulates polarized membrane distribution and cell motility
    • Makagiansar I.T., Williams S., Dahlin-Huppe K., Fukushi J., Mustelin T., and Stallcup W.B. Phosphorylation of NG2 proteoglycan by protein kinase C-alpha regulates polarized membrane distribution and cell motility. J. Biol. Chem. 279 (2004) 55262-55270
    • (2004) J. Biol. Chem. , vol.279 , pp. 55262-55270
    • Makagiansar, I.T.1    Williams, S.2    Dahlin-Huppe, K.3    Fukushi, J.4    Mustelin, T.5    Stallcup, W.B.6
  • 95
    • 1342279516 scopus 로고    scopus 로고
    • An introduction to matrikines: Extracellular matrix-derived peptides which regulate cell activity. Implication in tumor invasion
    • Maquart F.X., Pasco S., Ramont L., Hornebeck W., and Monboisse J.C. An introduction to matrikines: Extracellular matrix-derived peptides which regulate cell activity. Implication in tumor invasion. Crit. Rev. Oncol. Hematol. 49 (2004) 199-202
    • (2004) Crit. Rev. Oncol. Hematol. , vol.49 , pp. 199-202
    • Maquart, F.X.1    Pasco, S.2    Ramont, L.3    Hornebeck, W.4    Monboisse, J.C.5
  • 96
    • 16544366235 scopus 로고    scopus 로고
    • CD44 in cancer progression: Adhesion, migration and growth regulation
    • Marhaba R., and Zoller M. CD44 in cancer progression: Adhesion, migration and growth regulation. J. Mol. Histol. 35 (2004) 211-231
    • (2004) J. Mol. Histol. , vol.35 , pp. 211-231
    • Marhaba, R.1    Zoller, M.2
  • 97
    • 21644438258 scopus 로고    scopus 로고
    • Proteoglycans and injury of the central nervous system
    • Matsui F., and Oohira A. Proteoglycans and injury of the central nervous system. Congenit. Anom. Kyoto 44 (2004) 181-188
    • (2004) Congenit. Anom. Kyoto , vol.44 , pp. 181-188
    • Matsui, F.1    Oohira, A.2
  • 98
    • 13544251390 scopus 로고    scopus 로고
    • Fibromodulin as a novel tumor-associated antigen (TAA) in chronic lymphocytic leukemia (CLL), which allows expansion of specific CD8+ autologous T lymphocytes
    • Mayr C., Bund D., Schlee M., Moosmann A., Kofler D.M., Hallek M., and Wendtner C.M. Fibromodulin as a novel tumor-associated antigen (TAA) in chronic lymphocytic leukemia (CLL), which allows expansion of specific CD8+ autologous T lymphocytes. Blood 105 (2005) 1566-1573
    • (2005) Blood , vol.105 , pp. 1566-1573
    • Mayr, C.1    Bund, D.2    Schlee, M.3    Moosmann, A.4    Kofler, D.M.5    Hallek, M.6    Wendtner, C.M.7
  • 99
    • 0036554867 scopus 로고    scopus 로고
    • Differential gene expression in human lung adenocarcinomas and squamous cell carcinomas
    • McDoniels-Silvers A.L., Nimri C.F., Stoner G.D., Lubet R.A., and You M. Differential gene expression in human lung adenocarcinomas and squamous cell carcinomas. Clin. Cancer Res. 8 (2002) 1127-1138
    • (2002) Clin. Cancer Res. , vol.8 , pp. 1127-1138
    • McDoniels-Silvers, A.L.1    Nimri, C.F.2    Stoner, G.D.3    Lubet, R.A.4    You, M.5
  • 100
    • 0034934322 scopus 로고    scopus 로고
    • Analysis of differentially expressed genes in human hepatocellular carcinoma using suppression subtractive hybridization
    • Miyasaka Y., Enomoto N., Nagayama K., Izumi N., Marumo F., Watanabe M., and Sato C. Analysis of differentially expressed genes in human hepatocellular carcinoma using suppression subtractive hybridization. Br. J. Cancer 85 (2001) 228-234
    • (2001) Br. J. Cancer , vol.85 , pp. 228-234
    • Miyasaka, Y.1    Enomoto, N.2    Nagayama, K.3    Izumi, N.4    Marumo, F.5    Watanabe, M.6    Sato, C.7
  • 101
    • 0036456428 scopus 로고    scopus 로고
    • Chondroitin sulphate proteoglycans in the CNS injury response
    • Morgenstern D.A., Asher R.A., and Fawcett J.W. Chondroitin sulphate proteoglycans in the CNS injury response. Prog. Brain Res. 137 (2002) 313-332
    • (2002) Prog. Brain Res. , vol.137 , pp. 313-332
    • Morgenstern, D.A.1    Asher, R.A.2    Fawcett, J.W.3
  • 102
    • 0036683241 scopus 로고    scopus 로고
    • CD44 directs membrane-type 1 matrix metalloproteinase to lamellipodia by associating with its hemopexin-like domain
    • Mori H., Tomari T., Koshikawa N., Kajita M., Itoh Y., Sato H., Tojo H., Yana I., and Seiki M. CD44 directs membrane-type 1 matrix metalloproteinase to lamellipodia by associating with its hemopexin-like domain. EMBO J. 21 (2002) 3949-3959
    • (2002) EMBO J. , vol.21 , pp. 3949-3959
    • Mori, H.1    Tomari, T.2    Koshikawa, N.3    Kajita, M.4    Itoh, Y.5    Sato, H.6    Tojo, H.7    Yana, I.8    Seiki, M.9
  • 103
    • 0032955842 scopus 로고    scopus 로고
    • Cooperative role for activated alpha4 beta1 integrin and chondroitin sulfate proteoglycans in cell adhesion to the heparin III domain of fibronectin: Identification of a novel heparin and cell binding sequence in repeat III5
    • Moyano J.V., Carnemolla B., Albar J.P., Leprini A., Gaggero B., Zardi L., and Garcia-Pardo A. Cooperative role for activated alpha4 beta1 integrin and chondroitin sulfate proteoglycans in cell adhesion to the heparin III domain of fibronectin: Identification of a novel heparin and cell binding sequence in repeat III5. J. Biol. Chem. 274 (1999) 135-142
    • (1999) J. Biol. Chem. , vol.274 , pp. 135-142
    • Moyano, J.V.1    Carnemolla, B.2    Albar, J.P.3    Leprini, A.4    Gaggero, B.5    Zardi, L.6    Garcia-Pardo, A.7
  • 105
    • 2442637440 scopus 로고    scopus 로고
    • CD44-chondroitin sulfate interactions mediate leukocyte rolling under physiological flow conditions
    • Murai T., Sougawa N., Kawashima H., Yamaguchi K., and Miyasaka M. CD44-chondroitin sulfate interactions mediate leukocyte rolling under physiological flow conditions. Immunol. Lett. 93 (2004) 163-170
    • (2004) Immunol. Lett. , vol.93 , pp. 163-170
    • Murai, T.1    Sougawa, N.2    Kawashima, H.3    Yamaguchi, K.4    Miyasaka, M.5
  • 106
    • 2442483899 scopus 로고    scopus 로고
    • Increased invasion and expression of MMP-9 in human colorectal cell lines by a CD44-dependent mechanism
    • Murray D., Morrin M., and McDonnell S. Increased invasion and expression of MMP-9 in human colorectal cell lines by a CD44-dependent mechanism. Anticancer Res. 24 (2004) 489-494
    • (2004) Anticancer Res. , vol.24 , pp. 489-494
    • Murray, D.1    Morrin, M.2    McDonnell, S.3
  • 107
    • 3242788189 scopus 로고    scopus 로고
    • Role of the extracellular matrix in prostate carcinogenesis
    • Nagle R.B. Role of the extracellular matrix in prostate carcinogenesis. J. Cell. Biochem. 91 (2004) 36-40
    • (2004) J. Cell. Biochem. , vol.91 , pp. 36-40
    • Nagle, R.B.1
  • 108
    • 0037731301 scopus 로고    scopus 로고
    • Testican 2 abrogates inhibition of membrane-type matrix metalloproteinases by other testican family proteins
    • Nakada M., Miyamori H., Yamashita J., and Sato H. Testican 2 abrogates inhibition of membrane-type matrix metalloproteinases by other testican family proteins. Cancer Res. 63 (2003) 3364-3369
    • (2003) Cancer Res. , vol.63 , pp. 3364-3369
    • Nakada, M.1    Miyamori, H.2    Yamashita, J.3    Sato, H.4
  • 109
    • 0035893764 scopus 로고    scopus 로고
    • Suppression of membrane-type 1 matrix metalloproteinase (MMP)-mediated MMP-2 activation and tumor invasion by testican 3 and its splicing variant gene product, N-Tes
    • Nakada M., Yamada A., Takino T., Miyamori H., Takahashi T., Yamashita J., and Sato H. Suppression of membrane-type 1 matrix metalloproteinase (MMP)-mediated MMP-2 activation and tumor invasion by testican 3 and its splicing variant gene product, N-Tes. Cancer Res. 61 (2001) 8896-8902
    • (2001) Cancer Res. , vol.61 , pp. 8896-8902
    • Nakada, M.1    Yamada, A.2    Takino, T.3    Miyamori, H.4    Takahashi, T.5    Yamashita, J.6    Sato, H.7
  • 111
    • 0030985660 scopus 로고    scopus 로고
    • Immunohistochemical localization of extracellular matrix components in human breast tumours with special reference to PG-M/versican
    • Nara Y., Kato Y., Torii Y., Tsuji Y., Nakagaki S., Goto S., Isobe H., Nakashima N., and Takeuchi J. Immunohistochemical localization of extracellular matrix components in human breast tumours with special reference to PG-M/versican. Histochem. J. 29 (1997) 21-30
    • (1997) Histochem. J. , vol.29 , pp. 21-30
    • Nara, Y.1    Kato, Y.2    Torii, Y.3    Tsuji, Y.4    Nakagaki, S.5    Goto, S.6    Isobe, H.7    Nakashima, N.8    Takeuchi, J.9
  • 112
    • 0036278883 scopus 로고    scopus 로고
    • The expression of decorin in human ovarian tumors
    • Nash M.A., Deavers M.T., and Freedman R.S. The expression of decorin in human ovarian tumors. Clin. Cancer Res. 8 (2002) 1754-1760
    • (2002) Clin. Cancer Res. , vol.8 , pp. 1754-1760
    • Nash, M.A.1    Deavers, M.T.2    Freedman, R.S.3
  • 115
    • 0028882499 scopus 로고
    • Generation of truncated forms of the NG2 proteoglycan by cell surface proteolysis
    • Nishiyama A., Lin X.H., and Stallcup W.B. Generation of truncated forms of the NG2 proteoglycan by cell surface proteolysis. Mol. Biol. Cell 6 (1995) 1819-1832
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1819-1832
    • Nishiyama, A.1    Lin, X.H.2    Stallcup, W.B.3
  • 116
    • 0035076818 scopus 로고    scopus 로고
    • Glial tumor invasion: A role for the upregulation and cleavage of BEHAB/brevican
    • Nutt C.L., Matthews R.T., and Hockfield S. Glial tumor invasion: A role for the upregulation and cleavage of BEHAB/brevican. Neuroscientist 7 (2001) 113-122
    • (2001) Neuroscientist , vol.7 , pp. 113-122
    • Nutt, C.L.1    Matthews, R.T.2    Hockfield, S.3
  • 117
    • 20344381822 scopus 로고    scopus 로고
    • Glycoconjugate glycans as viral receptors
    • Olofsson S., and Bergstrom T. Glycoconjugate glycans as viral receptors. Ann. Med. 37 (2005) 154-172
    • (2005) Ann. Med. , vol.37 , pp. 154-172
    • Olofsson, S.1    Bergstrom, T.2
  • 118
    • 0034796499 scopus 로고    scopus 로고
    • NG2 proteoglycan is expressed exclusively by mural cells during vascular morphogenesis
    • Ozerdem U., Grako K.A., Dahlin-Huppe K., Monosov E., and Stallcup W.B. NG2 proteoglycan is expressed exclusively by mural cells during vascular morphogenesis. Dev. Dyn. 222 (2001) 218-227
    • (2001) Dev. Dyn. , vol.222 , pp. 218-227
    • Ozerdem, U.1    Grako, K.A.2    Dahlin-Huppe, K.3    Monosov, E.4    Stallcup, W.B.5
  • 119
    • 1942504107 scopus 로고    scopus 로고
    • Early contribution of pericytes to angiogenic sprouting and tube formation
    • Ozerdem U., and Stallcup W.B. Early contribution of pericytes to angiogenic sprouting and tube formation. Angiogenesis 6 (2003) 241-249
    • (2003) Angiogenesis , vol.6 , pp. 241-249
    • Ozerdem, U.1    Stallcup, W.B.2
  • 120
    • 12444253931 scopus 로고    scopus 로고
    • Pathological angiogenesis is reduced by targeting pericytes via the NG2 proteoglycan
    • Ozerdem U., and Stallcup W.B. Pathological angiogenesis is reduced by targeting pericytes via the NG2 proteoglycan. Angiogenesis 7 (2004) 269-276
    • (2004) Angiogenesis , vol.7 , pp. 269-276
    • Ozerdem, U.1    Stallcup, W.B.2
  • 122
    • 0026665972 scopus 로고
    • Thrombomodulin: An anticoagulant cell surface proteoglycan with physiologically relevant glycosaminoglycan moiety
    • Parkinson J.F., Koyama T., Bang N.U., and Preissner K.T. Thrombomodulin: An anticoagulant cell surface proteoglycan with physiologically relevant glycosaminoglycan moiety. Adv. Exp. Med. Biol. 313 (1992) 177-188
    • (1992) Adv. Exp. Med. Biol. , vol.313 , pp. 177-188
    • Parkinson, J.F.1    Koyama, T.2    Bang, N.U.3    Preissner, K.T.4
  • 124
    • 0027753101 scopus 로고
    • Characterization of integrin receptors in normal and neoplastic human brain
    • Paulus W., Baur I., Schuppan D., and Roggendorf W. Characterization of integrin receptors in normal and neoplastic human brain. Am. J. Pathol. 143 (1993) 154-163
    • (1993) Am. J. Pathol. , vol.143 , pp. 154-163
    • Paulus, W.1    Baur, I.2    Schuppan, D.3    Roggendorf, W.4
  • 125
    • 0035157538 scopus 로고    scopus 로고
    • CD44s expression mitigates the phenotype of human colorectal cancer hepatic metastases
    • Pereira P.A., Rubenthiran U., Kaneko M., Jothy S., and Smith A.J. CD44s expression mitigates the phenotype of human colorectal cancer hepatic metastases. Anticancer Res. 21 (2001) 2713-2717
    • (2001) Anticancer Res. , vol.21 , pp. 2713-2717
    • Pereira, P.A.1    Rubenthiran, U.2    Kaneko, M.3    Jothy, S.4    Smith, A.J.5
  • 126
    • 0038383042 scopus 로고    scopus 로고
    • Human melanoma/NG2 chondroitin sulfate proteoglycan is expressed in the sarcolemma of postnatal human skeletal myofibers: Abnormal expression in merosin-negative and Duchenne muscular dystrophies
    • Petrini S., Tessa A., Carrozzo R., Verardo M., Pierini R., Rizza T., and Bertini E. Human melanoma/NG2 chondroitin sulfate proteoglycan is expressed in the sarcolemma of postnatal human skeletal myofibers: Abnormal expression in merosin-negative and Duchenne muscular dystrophies. Mol. Cell. Neurosci. 23 (2003) 219-231
    • (2003) Mol. Cell. Neurosci. , vol.23 , pp. 219-231
    • Petrini, S.1    Tessa, A.2    Carrozzo, R.3    Verardo, M.4    Pierini, R.5    Rizza, T.6    Bertini, E.7
  • 127
    • 0036187663 scopus 로고    scopus 로고
    • Lumican expression in alpha cells of islets in pancreas and pancreatic cancer cells
    • Ping Lu Y., Ishiwata T., and Asano G. Lumican expression in alpha cells of islets in pancreas and pancreatic cancer cells. J. Pathol. 196 (2002) 324-330
    • (2002) J. Pathol. , vol.196 , pp. 324-330
    • Ping Lu, Y.1    Ishiwata, T.2    Asano, G.3
  • 128
    • 13544269617 scopus 로고    scopus 로고
    • Versican in nonsmall cell lung cancer: Relation to hyaluronan, clinicopathologic factors, and prognosis
    • Pirinen R., Leinonen T., Bohm J., Johansson R., Ropponen K., Kumpulainen E., and Kosma V.M. Versican in nonsmall cell lung cancer: Relation to hyaluronan, clinicopathologic factors, and prognosis. Hum. Pathol. 36 (2005) 44-50
    • (2005) Hum. Pathol. , vol.36 , pp. 44-50
    • Pirinen, R.1    Leinonen, T.2    Bohm, J.3    Johansson, R.4    Ropponen, K.5    Kumpulainen, E.6    Kosma, V.M.7
  • 131
    • 4344702478 scopus 로고    scopus 로고
    • Extracellular matrix components associated with remodeling processes in brain
    • Rauch U. Extracellular matrix components associated with remodeling processes in brain. Cell Mol. Life Sci. 61 (2004) 2031-2045
    • (2004) Cell Mol. Life Sci. , vol.61 , pp. 2031-2045
    • Rauch, U.1
  • 134
    • 4944234660 scopus 로고    scopus 로고
    • A disaccharide derived from chondroitin sulphate proteoglycan promotes central nervous system repair in rats and mice
    • Rolls A., Avidan H., Cahalon L., Schori H., Bakalash S., Litvak V., Lev S., Lider O., and Schwartz M. A disaccharide derived from chondroitin sulphate proteoglycan promotes central nervous system repair in rats and mice. Eur. J. Neurosci. 20 (2004) 1973-1983
    • (2004) Eur. J. Neurosci. , vol.20 , pp. 1973-1983
    • Rolls, A.1    Avidan, H.2    Cahalon, L.3    Schori, H.4    Bakalash, S.5    Litvak, V.6    Lev, S.7    Lider, O.8    Schwartz, M.9
  • 137
    • 7944230119 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans and heparanase-partners in osteolytic tumor growth and metastasis
    • Sanderson R.D., Yang Y., Suva L.J., and Kelly T. Heparan sulfate proteoglycans and heparanase-partners in osteolytic tumor growth and metastasis. Matrix Biol. 23 (2004) 341-352
    • (2004) Matrix Biol. , vol.23 , pp. 341-352
    • Sanderson, R.D.1    Yang, Y.2    Suva, L.J.3    Kelly, T.4
  • 138
    • 0034634669 scopus 로고    scopus 로고
    • An anti-oncogenic role for decorin. Down-regulation of ErbB2 leads to growth suppression and cytodifferentiation of mammary carcinoma cells
    • Santra M., Eichstetter I., and Iozzo R.V. An anti-oncogenic role for decorin. Down-regulation of ErbB2 leads to growth suppression and cytodifferentiation of mammary carcinoma cells. J. Biol. Chem. 275 (2000) 35153-35161
    • (2000) J. Biol. Chem. , vol.275 , pp. 35153-35161
    • Santra, M.1    Eichstetter, I.2    Iozzo, R.V.3
  • 139
    • 0030798869 scopus 로고    scopus 로고
    • Ectopic expression of decorin protein core causes a generalized growth suppression in neoplastic cells of various histogenetic origin and requires endogenous p21, an inhibitor of cyclin-dependent kinases
    • Santra M., Mann D.M., Mercer E.W., Skorski T., Calabretta B., and Iozzo R.V. Ectopic expression of decorin protein core causes a generalized growth suppression in neoplastic cells of various histogenetic origin and requires endogenous p21, an inhibitor of cyclin-dependent kinases. J. Clin. Invest. 100 (1997) 149-157
    • (1997) J. Clin. Invest. , vol.100 , pp. 149-157
    • Santra, M.1    Mann, D.M.2    Mercer, E.W.3    Skorski, T.4    Calabretta, B.5    Iozzo, R.V.6
  • 140
    • 0029088680 scopus 로고
    • De novo decorin gene expression suppresses the malignant phenotype in human colon cancer cells
    • Santra M., Skorski T., Calabretta B., Lattime E.C., and Iozzo R.V. De novo decorin gene expression suppresses the malignant phenotype in human colon cancer cells. Proc. Natl. Acad. Sci. USA 92 (1995) 7016-7020
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7016-7020
    • Santra, M.1    Skorski, T.2    Calabretta, B.3    Lattime, E.C.4    Iozzo, R.V.5
  • 142
    • 0028825543 scopus 로고
    • Regulation of growth factor activation by proteoglycans: What is the role of the low affinity receptors?
    • Schlessinger J., Lax I., and Lemmon M. Regulation of growth factor activation by proteoglycans: What is the role of the low affinity receptors?. Cell 83 (1995) 357-360
    • (1995) Cell , vol.83 , pp. 357-360
    • Schlessinger, J.1    Lax, I.2    Lemmon, M.3
  • 143
    • 0035798706 scopus 로고    scopus 로고
    • Decorin-mediated signal transduction in endothelial cells: Involvement of Akt/protein kinase B in up-regulation of p21(WAF1/CIP1) but not p27(KIP1)
    • Schonherr E., Levkau B., Schaefer L., Kresse H., and Walsh K. Decorin-mediated signal transduction in endothelial cells: Involvement of Akt/protein kinase B in up-regulation of p21(WAF1/CIP1) but not p27(KIP1). J. Biol. Chem. 276 (2001) 40687-40692
    • (2001) J. Biol. Chem. , vol.276 , pp. 40687-40692
    • Schonherr, E.1    Levkau, B.2    Schaefer, L.3    Kresse, H.4    Walsh, K.5
  • 145
    • 7244256103 scopus 로고    scopus 로고
    • Proteoglycans in brain development
    • Schwartz N.B., and Domowicz M. Proteoglycans in brain development. Glycoconj. J. 21 (2004) 329-341
    • (2004) Glycoconj. J. , vol.21 , pp. 329-341
    • Schwartz, N.B.1    Domowicz, M.2
  • 146
    • 0037426578 scopus 로고    scopus 로고
    • Membrane-type 1 matrix metalloproteinase: A key enzyme for tumor invasion
    • Seiki M. Membrane-type 1 matrix metalloproteinase: A key enzyme for tumor invasion. Cancer Lett. 194 (2003) 1-11
    • (2003) Cancer Lett. , vol.194 , pp. 1-11
    • Seiki, M.1
  • 147
    • 17044403883 scopus 로고    scopus 로고
    • V3 versican isoform expression alters the phenotype of melanoma cells and their tumorigenic potential
    • Serra M., Miquel L., Domenzain C., Docampo M.J., Fabra A., Wight T.N., and Bassols A. V3 versican isoform expression alters the phenotype of melanoma cells and their tumorigenic potential. Int. J. Cancer 114 (2005) 879-886
    • (2005) Int. J. Cancer , vol.114 , pp. 879-886
    • Serra, M.1    Miquel, L.2    Domenzain, C.3    Docampo, M.J.4    Fabra, A.5    Wight, T.N.6    Bassols, A.7
  • 148
    • 22844431508 scopus 로고    scopus 로고
    • Different expression levels of lumican in human carcinoid tumor and neuroendocrine cell carcinoma
    • Shinji S., Tajiri T., Ishiwata T., Seya T., Tanaka N., and Naito Z. Different expression levels of lumican in human carcinoid tumor and neuroendocrine cell carcinoma. Int. J. Oncol. 26 (2005) 873-880
    • (2005) Int. J. Oncol. , vol.26 , pp. 873-880
    • Shinji, S.1    Tajiri, T.2    Ishiwata, T.3    Seya, T.4    Tanaka, N.5    Naito, Z.6
  • 149
    • 0029058742 scopus 로고
    • The Alzheimer amyloid precursor proteoglycan (appican) is present in brain and is produced by astrocytes but not by neurons in primary neural cultures
    • Shioi J., Pangalos M.N., Ripellino J.A., Vassilacopoulou D., Mytilineou C., Margolis R.U., and Robakis N.K. The Alzheimer amyloid precursor proteoglycan (appican) is present in brain and is produced by astrocytes but not by neurons in primary neural cultures. J. Biol. Chem. 270 (1995) 11839-11844
    • (1995) J. Biol. Chem. , vol.270 , pp. 11839-11844
    • Shioi, J.1    Pangalos, M.N.2    Ripellino, J.A.3    Vassilacopoulou, D.4    Mytilineou, C.5    Margolis, R.U.6    Robakis, N.K.7
  • 150
    • 0036171691 scopus 로고    scopus 로고
    • Emerging views of heparan sulfate glycosaminoglycan structure/activity relationships modulating dynamic biological functions
    • Shriver Z., Liu D., and Sasisekharan R. Emerging views of heparan sulfate glycosaminoglycan structure/activity relationships modulating dynamic biological functions. Trends Cardiovasc. Med. 12 (2002) 71-77
    • (2002) Trends Cardiovasc. Med. , vol.12 , pp. 71-77
    • Shriver, Z.1    Liu, D.2    Sasisekharan, R.3
  • 152
    • 0030020460 scopus 로고    scopus 로고
    • The human homologue of rat NG2, a chondroitin sulfate proteoglycan, is not expressed on the cell surface of normal hematopoietic cells but is expressed by acute myeloid leukemia blasts from poor-prognosis patients with abnormalities of chromosome band 11q23
    • Smith F.O., Rauch C., Williams D.E., March C.J., Arthur D., Hilden J., Lampkin B.C., Buckley J.D., Buckley C.V., Woods W.G., Dinndorf P.A., Sorensen P., et al. The human homologue of rat NG2, a chondroitin sulfate proteoglycan, is not expressed on the cell surface of normal hematopoietic cells but is expressed by acute myeloid leukemia blasts from poor-prognosis patients with abnormalities of chromosome band 11q23. Blood 87 (1996) 1123-1133
    • (1996) Blood , vol.87 , pp. 1123-1133
    • Smith, F.O.1    Rauch, C.2    Williams, D.E.3    March, C.J.4    Arthur, D.5    Hilden, J.6    Lampkin, B.C.7    Buckley, J.D.8    Buckley, C.V.9    Woods, W.G.10    Dinndorf, P.A.11    Sorensen, P.12
  • 153
    • 0031874645 scopus 로고    scopus 로고
    • The normal structure and function of CD44 and its role in neoplasia
    • Sneath R.J., and Mangham D.C. The normal structure and function of CD44 and its role in neoplasia. Mol. Pathol. 51 (1998) 191-200
    • (1998) Mol. Pathol. , vol.51 , pp. 191-200
    • Sneath, R.J.1    Mangham, D.C.2
  • 154
    • 0037054935 scopus 로고    scopus 로고
    • Molecular profiling of human chondrosarcomas for matrix production and cancer markers
    • Soderstrom M., Bohling T., Ekfors T., Nelimarkka L., Aro H.T., and Vuorio E. Molecular profiling of human chondrosarcomas for matrix production and cancer markers. Int. J. Cancer 100 (2002) 144-151
    • (2002) Int. J. Cancer , vol.100 , pp. 144-151
    • Soderstrom, M.1    Bohling, T.2    Ekfors, T.3    Nelimarkka, L.4    Aro, H.T.5    Vuorio, E.6
  • 155
    • 0242552255 scopus 로고    scopus 로고
    • The NG2 proteoglycan: Past insights and future prospects
    • Stallcup W.B. The NG2 proteoglycan: Past insights and future prospects. J. Neurocytol. 31 (2002) 423-435
    • (2002) J. Neurocytol. , vol.31 , pp. 423-435
    • Stallcup, W.B.1
  • 156
    • 13444273084 scopus 로고    scopus 로고
    • CD44 binding through the hemopexin-like domain is critical for its shedding by membrane-type 1 matrix metalloproteinase
    • Suenaga N., Mori H., Itoh Y., and Seiki M. CD44 binding through the hemopexin-like domain is critical for its shedding by membrane-type 1 matrix metalloproteinase. Oncogene 24 (2005) 859-868
    • (2005) Oncogene , vol.24 , pp. 859-868
    • Suenaga, N.1    Mori, H.2    Itoh, Y.3    Seiki, M.4
  • 158
    • 11144355816 scopus 로고    scopus 로고
    • Expression of extracellular matrix components versican, chondroitin sulfate, tenascin, and hyaluronan, and their association with disease outcome in node-negative breast cancer
    • Suwiwat S., Ricciardelli C., Tammi R., Tammi M., Auvinen P., Kosma V.M., LeBaron R.G., Raymond W.A., Tilley W.D., and Horsfall D.J. Expression of extracellular matrix components versican, chondroitin sulfate, tenascin, and hyaluronan, and their association with disease outcome in node-negative breast cancer. Clin. Cancer Res. 10 (2004) 2491-2498
    • (2004) Clin. Cancer Res. , vol.10 , pp. 2491-2498
    • Suwiwat, S.1    Ricciardelli, C.2    Tammi, R.3    Tammi, M.4    Auvinen, P.5    Kosma, V.M.6    LeBaron, R.G.7    Raymond, W.A.8    Tilley, W.D.9    Horsfall, D.J.10
  • 159
    • 0036875374 scopus 로고    scopus 로고
    • Synthesis and expression of mRNA encoding for different versican splice variants is related to the aggregation of human epithelial mesothelioma cells
    • Syrokou A., Dobra K., Tzanakakis G.N., Hjerpe A., and Karamanos N.K. Synthesis and expression of mRNA encoding for different versican splice variants is related to the aggregation of human epithelial mesothelioma cells. Anticancer Res. 22 (2002) 4157-4162
    • (2002) Anticancer Res. , vol.22 , pp. 4157-4162
    • Syrokou, A.1    Dobra, K.2    Tzanakakis, G.N.3    Hjerpe, A.4    Karamanos, N.K.5
  • 160
    • 0037101954 scopus 로고    scopus 로고
    • Annexin 6 is a putative cell surface receptor for chondroitin sulfate chains
    • Takagi H., Asano Y., Yamakawa N., Matsumoto I., and Kimata K. Annexin 6 is a putative cell surface receptor for chondroitin sulfate chains. J. Cell Sci. 115 (2002) 3309-3318
    • (2002) J. Cell Sci. , vol.115 , pp. 3309-3318
    • Takagi, H.1    Asano, Y.2    Yamakawa, N.3    Matsumoto, I.4    Kimata, K.5
  • 163
    • 0037145715 scopus 로고    scopus 로고
    • Human colon adenocarcinoma is associated with specific post-translational modifications of versican and decorin
    • Theocharis A.D. Human colon adenocarcinoma is associated with specific post-translational modifications of versican and decorin. Biochim. Biophys. Acta 1588 (2002) 165-172
    • (2002) Biochim. Biophys. Acta , vol.1588 , pp. 165-172
    • Theocharis, A.D.1
  • 164
    • 0036194421 scopus 로고    scopus 로고
    • High-performance capillary electrophoretic analysis of hyaluronan and galactosaminoglycan-disaccharides in gastrointestinal carcinomas. Differential disaccharide composition as a possible tool-indicator for malignancies
    • Theocharis A.D., and Theocharis D.A. High-performance capillary electrophoretic analysis of hyaluronan and galactosaminoglycan-disaccharides in gastrointestinal carcinomas. Differential disaccharide composition as a possible tool-indicator for malignancies. Biomed. Chromatogr. 16 (2002) 157-161
    • (2002) Biomed. Chromatogr. , vol.16 , pp. 157-161
    • Theocharis, A.D.1    Theocharis, D.A.2
  • 165
    • 0036022140 scopus 로고    scopus 로고
    • NG2 proteoglycan mediates beta1 integrin-independent cell adhesion and spreading on collagen VI
    • Tillet E., Gential B., Garrone R., and Stallcup W.B. NG2 proteoglycan mediates beta1 integrin-independent cell adhesion and spreading on collagen VI. J. Cell. Biochem. 86 (2002) 726-736
    • (2002) J. Cell. Biochem. , vol.86 , pp. 726-736
    • Tillet, E.1    Gential, B.2    Garrone, R.3    Stallcup, W.B.4
  • 166
    • 0035988837 scopus 로고    scopus 로고
    • Proteoglycans and tumor progression: Janus-faced molecules with contradictory functions in cancer
    • Timar J., Lapis K., Dudas J., Sebestyen A., Kopper L., and Kovalszky I. Proteoglycans and tumor progression: Janus-faced molecules with contradictory functions in cancer. Semin. Cancer Biol. 12 (2002) 173-186
    • (2002) Semin. Cancer Biol. , vol.12 , pp. 173-186
    • Timar, J.1    Lapis, K.2    Dudas, J.3    Sebestyen, A.4    Kopper, L.5    Kovalszky, I.6
  • 167
    • 17944402390 scopus 로고    scopus 로고
    • Identification of haemopoietic biglycan in hyperplastic thymus associated with myasthenia gravis
    • Tomoyasu H., Kikuchi A., and Kamo I. Identification of haemopoietic biglycan in hyperplastic thymus associated with myasthenia gravis. J. Neuroimmunol. 89 (1998) 59-63
    • (1998) J. Neuroimmunol. , vol.89 , pp. 59-63
    • Tomoyasu, H.1    Kikuchi, A.2    Kamo, I.3
  • 168
    • 85047688838 scopus 로고    scopus 로고
    • Expression of the proteoglycans versican and mel-CSPG in dysplastic nevi
    • Touab M., Arumi-Uria M., Barranco C., and Bassols A. Expression of the proteoglycans versican and mel-CSPG in dysplastic nevi. Am. J. Clin. Pathol. 119 (2003) 587-593
    • (2003) Am. J. Clin. Pathol. , vol.119 , pp. 587-593
    • Touab, M.1    Arumi-Uria, M.2    Barranco, C.3    Bassols, A.4
  • 171
    • 12244311868 scopus 로고    scopus 로고
    • Reduced expression of the small leucine-rich proteoglycans, lumican, and decorin is associated with poor outcome in node-negative invasive breast cancer
    • Troup S., Njue C., Kliewer E.V., Parisien M., Roskelley C., Chakravarti S., Roughley P.J., Murphy L.C., and Watson P.H. Reduced expression of the small leucine-rich proteoglycans, lumican, and decorin is associated with poor outcome in node-negative invasive breast cancer. Clin. Cancer Res. 9 (2003) 207-214
    • (2003) Clin. Cancer Res. , vol.9 , pp. 207-214
    • Troup, S.1    Njue, C.2    Kliewer, E.V.3    Parisien, M.4    Roskelley, C.5    Chakravarti, S.6    Roughley, P.J.7    Murphy, L.C.8    Watson, P.H.9
  • 172
    • 0036744549 scopus 로고    scopus 로고
    • Dermatan sulfate: New functions from an old glycosaminoglycan
    • Trowbridge J.M., and Gallo R.L. Dermatan sulfate: New functions from an old glycosaminoglycan. Glycobiology 12 (2002) 117R-125R
    • (2002) Glycobiology , vol.12
    • Trowbridge, J.M.1    Gallo, R.L.2
  • 173
    • 0036765657 scopus 로고    scopus 로고
    • Compositional and structural alterations of proteoglycans in human rectum carcinoma with special reference to versican and decorin
    • Tsara M.E., Theocharis A.D., and Theocharis D.A. Compositional and structural alterations of proteoglycans in human rectum carcinoma with special reference to versican and decorin. Anticancer Res. 22 (2002) 2893-2898
    • (2002) Anticancer Res. , vol.22 , pp. 2893-2898
    • Tsara, M.E.1    Theocharis, A.D.2    Theocharis, D.A.3
  • 174
    • 0032741674 scopus 로고    scopus 로고
    • Immunohistochemical study of chondroitin-6-sulphate and tenascin in the larynx: A loss of chondroitin-6-sulphate expression accompanies squamous cell carcinoma invasion
    • Uhlman D.L., and Niehans G.A. Immunohistochemical study of chondroitin-6-sulphate and tenascin in the larynx: A loss of chondroitin-6-sulphate expression accompanies squamous cell carcinoma invasion. J. Pathol. 189 (1999) 470-474
    • (1999) J. Pathol. , vol.189 , pp. 470-474
    • Uhlman, D.L.1    Niehans, G.A.2
  • 175
    • 0027385081 scopus 로고
    • A PCR based method for the analysis of human CD44 splice products
    • van Weering D.H.J., Bass P.D., and Bos J.L. A PCR based method for the analysis of human CD44 splice products. PCR Methods Appl. 3 (1994) 100-1006
    • (1994) PCR Methods Appl. , vol.3 , pp. 100-1006
    • van Weering, D.H.J.1    Bass, P.D.2    Bos, J.L.3
  • 176
    • 1542289879 scopus 로고    scopus 로고
    • The shedding of betaglycan is regulated by pervanadate and mediated by membrane type matrix metalloprotease-1
    • Velasco-Loyden G., Arribas J., and Lopez-Casillas F. The shedding of betaglycan is regulated by pervanadate and mediated by membrane type matrix metalloprotease-1. J. Biol. Chem. 279 (2004) 7721-7733
    • (2004) J. Biol. Chem. , vol.279 , pp. 7721-7733
    • Velasco-Loyden, G.1    Arribas, J.2    Lopez-Casillas, F.3
  • 177
  • 181
    • 0032901679 scopus 로고    scopus 로고
    • Biochemical alterations of uterine leiomyoma extracellular matrix in type IV Ehlers-Danlos syndrome
    • Wegrowski Y., Bellon G., Quereux C., and Maquart F.X. Biochemical alterations of uterine leiomyoma extracellular matrix in type IV Ehlers-Danlos syndrome. Am. J. Obstet. Gynecol. 180 (1999) 1032-1034
    • (1999) Am. J. Obstet. Gynecol. , vol.180 , pp. 1032-1034
    • Wegrowski, Y.1    Bellon, G.2    Quereux, C.3    Maquart, F.X.4
  • 182
    • 1342343091 scopus 로고    scopus 로고
    • Involvement of stromal proteoglycans in tumour progression
    • Wegrowski Y., and Maquart F.X. Involvement of stromal proteoglycans in tumour progression. Crit. Rev. Oncol. Hematol. 49 (2004) 259-268
    • (2004) Crit. Rev. Oncol. Hematol. , vol.49 , pp. 259-268
    • Wegrowski, Y.1    Maquart, F.X.2
  • 183
    • 0032544683 scopus 로고    scopus 로고
    • Uridine diphosphoglucose dehydrogenase regulates proteoglycan expression: cDNA cloning and antisense study
    • Wegrowski Y., Perreau C., Bontemps Y., and Maquart F.X. Uridine diphosphoglucose dehydrogenase regulates proteoglycan expression: cDNA cloning and antisense study. Biochem. Biophys. Res. Commun. 250 (1998) 206-211
    • (1998) Biochem. Biophys. Res. Commun. , vol.250 , pp. 206-211
    • Wegrowski, Y.1    Perreau, C.2    Bontemps, Y.3    Maquart, F.X.4
  • 185
    • 0035451542 scopus 로고    scopus 로고
    • Protein-carbohydrate interactions: Learning lessons from nature
    • Williams S.J., and Davies G.J. Protein-carbohydrate interactions: Learning lessons from nature. Trends Biotechnol. 19 (2001) 356-362
    • (2001) Trends Biotechnol. , vol.19 , pp. 356-362
    • Williams, S.J.1    Davies, G.J.2
  • 186
    • 0020532690 scopus 로고
    • Immunochemical characterization of a human high molecular weight-melanoma associated antigen identified with monoclonal antibodies
    • Wilson B.S., Ruberto G., and Ferrone S. Immunochemical characterization of a human high molecular weight-melanoma associated antigen identified with monoclonal antibodies. Cancer Immunol. Immunother. 14 (1983) 196-201
    • (1983) Cancer Immunol. Immunother. , vol.14 , pp. 196-201
    • Wilson, B.S.1    Ruberto, G.2    Ferrone, S.3
  • 187
    • 0034477147 scopus 로고    scopus 로고
    • CD44 expression and MMP-2 secretion by mouse glioma cells: Effect of interferon and anti-CD44 antibody
    • Wiranowska M., Rojiani A.M., Gottschall P.E., Moscinski L.C., Johnson J., and Saporta S. CD44 expression and MMP-2 secretion by mouse glioma cells: Effect of interferon and anti-CD44 antibody. Anticancer Res. 20 (2000) 4301-4306
    • (2000) Anticancer Res. , vol.20 , pp. 4301-4306
    • Wiranowska, M.1    Rojiani, A.M.2    Gottschall, P.E.3    Moscinski, L.C.4    Johnson, J.5    Saporta, S.6
  • 188
    • 0035958047 scopus 로고    scopus 로고
    • Identification of the motif in versican G3 domain that plays a dominant-negative effect on astrocytoma cell proliferation through inhibiting versican secretion and binding
    • Wu Y., Zhang Y., Cao L., Chen L., Lee V., Zheng P.S., Kiani C., Adams M.E., Ang L.C., Paiwand F., and Yang B.B. Identification of the motif in versican G3 domain that plays a dominant-negative effect on astrocytoma cell proliferation through inhibiting versican secretion and binding. J. Biol. Chem. 276 (2001) 14178-14186
    • (2001) J. Biol. Chem. , vol.276 , pp. 14178-14186
    • Wu, Y.1    Zhang, Y.2    Cao, L.3    Chen, L.4    Lee, V.5    Zheng, P.S.6    Kiani, C.7    Adams, M.E.8    Ang, L.C.9    Paiwand, F.10    Yang, B.B.11
  • 189
    • 0037424511 scopus 로고    scopus 로고
    • E-cadherin negatively regulates CD44-hyaluronan interaction and CD44-mediated tumor invasion and branching morphogenesis
    • Xu Y., and Yu Q. E-cadherin negatively regulates CD44-hyaluronan interaction and CD44-mediated tumor invasion and branching morphogenesis. J. Biol. Chem. 278 (2003) 8661-8668
    • (2003) J. Biol. Chem. , vol.278 , pp. 8661-8668
    • Xu, Y.1    Yu, Q.2
  • 190
    • 0028233391 scopus 로고
    • Molecular cloning of brevican, a novel brain proteoglycan of the aggrecan/versican family
    • Yamada H., Watanabe K., Shimonaka M., and Yamaguchi Y. Molecular cloning of brevican, a novel brain proteoglycan of the aggrecan/versican family. J. Biol. Chem. 269 (1994) 10119-10126
    • (1994) J. Biol. Chem. , vol.269 , pp. 10119-10126
    • Yamada, H.1    Watanabe, K.2    Shimonaka, M.3    Yamaguchi, Y.4
  • 191
    • 0032414048 scopus 로고    scopus 로고
    • Cloning and chromosomal mapping of the human gene of neuroglycan C (NGC), a neural transmembrane chondroitin sulfate proteoglycan with an EGF module
    • Yasuda Y., Tokita Y., Aono S., Matsui F., Ono T., Sonta S., Watanabe E., Nakanishi Y., and Oohira A. Cloning and chromosomal mapping of the human gene of neuroglycan C (NGC), a neural transmembrane chondroitin sulfate proteoglycan with an EGF module. Neurosci. Res. 32 (1998) 313-322
    • (1998) Neurosci. Res. , vol.32 , pp. 313-322
    • Yasuda, Y.1    Tokita, Y.2    Aono, S.3    Matsui, F.4    Ono, T.5    Sonta, S.6    Watanabe, E.7    Nakanishi, Y.8    Oohira, A.9
  • 192
    • 18144403762 scopus 로고    scopus 로고
    • Chondroitin synthase 1 is a key molecule in myeloma cell-osteoclast interactions
    • Yin L. Chondroitin synthase 1 is a key molecule in myeloma cell-osteoclast interactions. J. Biol. Chem. 280 (2005) 15666-15672
    • (2005) J. Biol. Chem. , vol.280 , pp. 15666-15672
    • Yin, L.1
  • 193
    • 0030760779 scopus 로고    scopus 로고
    • Disaccharide analysis of skin glycosaminoglycan in localized scleroderma
    • Yokoyama Y., Ishikawa O., and Miyachi Y. Disaccharide analysis of skin glycosaminoglycan in localized scleroderma. Dermatology 194 (1997) 329-333
    • (1997) Dermatology , vol.194 , pp. 329-333
    • Yokoyama, Y.1    Ishikawa, O.2    Miyachi, Y.3
  • 194
    • 0033230988 scopus 로고    scopus 로고
    • Biosynthesis of glycosaminoglycans and aggrecan by tumor cells in salivary pleomorphic adenoma: Ultrastructural evidence
    • Zhao M., Takata T., Kudo Y., Sato S., Ogawa I., Wakida K., Uchida T., and Nikai H. Biosynthesis of glycosaminoglycans and aggrecan by tumor cells in salivary pleomorphic adenoma: Ultrastructural evidence. J. Oral Pathol. Med. 28 (1999) 442-450
    • (1999) J. Oral Pathol. Med. , vol.28 , pp. 442-450
    • Zhao, M.1    Takata, T.2    Kudo, Y.3    Sato, S.4    Ogawa, I.5    Wakida, K.6    Uchida, T.7    Nikai, H.8


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