메뉴 건너뛰기




Volumn 24, Issue 2, 2007, Pages 153-166

Molecular and cellular mechanisms of syndecans in tissue injury and inflammation

Author keywords

Chemokine; Heparan sulfate; Host defense; Infection; Microbial pathogenesis; Pneumonia; Proteoglycan; Tissue repair

Indexed keywords

CHEMOKINE; CYTOKINE; GROWTH FACTOR; HEPARAN SULFATE; PROTEINASE; PROTEOGLYCAN; SCLEROPROTEIN; SYNDECAN; SYNDECAN 1; SYNDECAN 2; SYNDECAN 4;

EID: 36549089044     PISSN: 10168478     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Short Survey
Times cited : (84)

References (145)
  • 1
    • 0033934447 scopus 로고    scopus 로고
    • Syndecan-1 is required for Wnt-1-induced mammary tumorigenesis in mice
    • Alexander, C. M., Reichsman, F., Hinkes, M. T., Lincecum, J., Becker, K. A., et al. (2000) Syndecan-1 is required for Wnt-1-induced mammary tumorigenesis in mice. Nat. Genet. 25, 329-332.
    • (2000) Nat. Genet , vol.25 , pp. 329-332
    • Alexander, C.M.1    Reichsman, F.2    Hinkes, M.T.3    Lincecum, J.4    Becker, K.A.5
  • 3
    • 20144362882 scopus 로고    scopus 로고
    • Porphyromonas gingivalis lipopolysaccharide induces shedding of syndecan-1 expressed by gingival epithelial cells
    • Andrian, E., Grenier, D., and Rouabhia, M. (2005) Porphyromonas gingivalis lipopolysaccharide induces shedding of syndecan-1 expressed by gingival epithelial cells. J. Cell. Physiol. 204, 178-183.
    • (2005) J. Cell. Physiol , vol.204 , pp. 178-183
    • Andrian, E.1    Grenier, D.2    Rouabhia, M.3
  • 4
    • 0036882397 scopus 로고    scopus 로고
    • Protein ectodomain shedding
    • Arribas, J. and Borroto, A. (2002) Protein ectodomain shedding. Chem. Rev. 102, 4627-4638.
    • (2002) Chem. Rev , vol.102 , pp. 4627-4638
    • Arribas, J.1    Borroto, A.2
  • 5
    • 0042338645 scopus 로고    scopus 로고
    • Matrix metalloproteinase-dependent shedding of syndecan-3, a transmembrane heparan sulfate proteoglycan, in Schwarnn cells
    • Asundi, V. K., Erdman, R., Stahl, R. C., and Carey, D. J. (2003) Matrix metalloproteinase-dependent shedding of syndecan-3, a transmembrane heparan sulfate proteoglycan, in Schwarnn cells. J. Neurosci. Res. 73, 593-602.
    • (2003) J. Neurosci. Res , vol.73 , pp. 593-602
    • Asundi, V.K.1    Erdman, R.2    Stahl, R.C.3    Carey, D.J.4
  • 6
    • 5444242206 scopus 로고    scopus 로고
    • The syndecan-1 ectodomain regulates alphavbeta3 integrin activity in human mammary carcinoma cells
    • Beauvais, D. M., Burbach, B. J., and Rapraeger, A. C. (2004) The syndecan-1 ectodomain regulates alphavbeta3 integrin activity in human mammary carcinoma cells. J. Cell Biol. 167, 171-181.
    • (2004) J. Cell Biol , vol.167 , pp. 171-181
    • Beauvais, D.M.1    Burbach, B.J.2    Rapraeger, A.C.3
  • 7
    • 0031912785 scopus 로고    scopus 로고
    • Cytokine kinetics and other host factors in response to pneumococcal pulmonary infection in mice
    • Bergeron, Y., Ouellet, N., Deslauriers, A. M., Simard, M., Olivier, M., et al. (1998) Cytokine kinetics and other host factors in response to pneumococcal pulmonary infection in mice. Infect. Immun. 66, 912-922.
    • (1998) Infect. Immun , vol.66 , pp. 912-922
    • Bergeron, Y.1    Ouellet, N.2    Deslauriers, A.M.3    Simard, M.4    Olivier, M.5
  • 9
    • 0026685854 scopus 로고
    • Biology of the syndecans: A family of transmembrane heparan sulfate proteoglycans
    • Bernfield, M., Kokenyesi, R., Kato, M., Hinkes, M. T., Spring, J., et al. (1992) Biology of the syndecans: a family of transmembrane heparan sulfate proteoglycans. Annu. Rev. Cell Biol. 8, 365-393.
    • (1992) Annu. Rev. Cell Biol , vol.8 , pp. 365-393
    • Bernfield, M.1    Kokenyesi, R.2    Kato, M.3    Hinkes, M.T.4    Spring, J.5
  • 10
    • 0036185667 scopus 로고    scopus 로고
    • Functional and biochemical characterization of ADAMs and their predicted role in protein ectodomain shedding
    • Blobel, C. P. (2002) Functional and biochemical characterization of ADAMs and their predicted role in protein ectodomain shedding. Inflamm. Res. 51, 83-84.
    • (2002) Inflamm. Res , vol.51 , pp. 83-84
    • Blobel, C.P.1
  • 11
    • 33845803152 scopus 로고    scopus 로고
    • Cell-free human immunodeficiency virus type 1 transcytosis though primary genital epithelial cells
    • Bobardt, M. D., Chatterji, U., Selvarajah, S., Van der Schueren, B., David, G., et al. (2007) Cell-free human immunodeficiency virus type 1 transcytosis though primary genital epithelial cells. J. Virol. 81, 395-405.
    • (2007) J. Virol , vol.81 , pp. 395-405
    • Bobardt, M.D.1    Chatterji, U.2    Selvarajah, S.3    Van der Schueren, B.4    David, G.5
  • 12
    • 17644411447 scopus 로고    scopus 로고
    • Heparan sulfate depletion amplifies TNF-alpha-induced protein leakage in an in vitro model of protein-losing enteropathy
    • Bode, L., Eklund, E. A., Murch, S., and Freeze, H. H. (2005) Heparan sulfate depletion amplifies TNF-alpha-induced protein leakage in an in vitro model of protein-losing enteropathy. Am. J. Physiol. Gastrointest. Liver Physiol. 288, G1015-1023.
    • (2005) Am. J. Physiol. Gastrointest. Liver Physiol , vol.288
    • Bode, L.1    Eklund, E.A.2    Murch, S.3    Freeze, H.H.4
  • 13
    • 33646349227 scopus 로고    scopus 로고
    • Heparan sulfate plays a central role in a dynamic in vitro model of protein-losing enteropathy
    • Bode, L., Murch, S., and Freeze, H. H. (2006) Heparan sulfate plays a central role in a dynamic in vitro model of protein-losing enteropathy. J. Biol. Chem. 281, 7809-7815.
    • (2006) J. Biol. Chem , vol.281 , pp. 7809-7815
    • Bode, L.1    Murch, S.2    Freeze, H.H.3
  • 14
    • 33646863047 scopus 로고    scopus 로고
    • The shedding of syndecan-4 and syndecan-1 from HeLa cells and human primary macrophages is accelerated by SDF-1/CXCL12 and mediated by the matrix metalloproteinase-9
    • Brule, S., Charnaux, N., Sutton, A., Ledoux, D., Chaigneau, T., et al. (2006) The shedding of syndecan-4 and syndecan-1 from HeLa cells and human primary macrophages is accelerated by SDF-1/CXCL12 and mediated by the matrix metalloproteinase-9. Glycobiology 16, 488-501.
    • (2006) Glycobiology , vol.16 , pp. 488-501
    • Brule, S.1    Charnaux, N.2    Sutton, A.3    Ledoux, D.4    Chaigneau, T.5
  • 15
    • 0030660196 scopus 로고    scopus 로고
    • Syndecans: Multifunctional cell-surface coreceptors
    • Carey, D. J. (1997) Syndecans: multifunctional cell-surface coreceptors. Biochem. J. 327, 1-16.
    • (1997) Biochem. J , vol.327 , pp. 1-16
    • Carey, D.J.1
  • 16
    • 20844452036 scopus 로고    scopus 로고
    • RANTES (CCL5) induces a CCR5-dependent accelerated shedding of syndecan-1 (CD138) and syndecan-4 from HeLa cells and forms complexes with the shed ectodomains of these proteoglycans as well as with those of CD44
    • Charnaux, N., Brule, S., Chaigneau, T., Saffar, L., Sutton, A., et al. (2005) RANTES (CCL5) induces a CCR5-dependent accelerated shedding of syndecan-1 (CD138) and syndecan-4 from HeLa cells and forms complexes with the shed ectodomains of these proteoglycans as well as with those of CD44. Glycobiology 15, 119-130.
    • (2005) Glycobiology , vol.15 , pp. 119-130
    • Charnaux, N.1    Brule, S.2    Chaigneau, T.3    Saffar, L.4    Sutton, A.5
  • 17
    • 1442356942 scopus 로고    scopus 로고
    • Syndecan-2 is essential for angiogenic sprouting during zebrafish development
    • Chen, E., Hermanson, S., and Ekker, S. C. (2004a) Syndecan-2 is essential for angiogenic sprouting during zebrafish development. Blood 103, 1710-1719.
    • (2004) Blood , vol.103 , pp. 1710-1719
    • Chen, E.1    Hermanson, S.2    Ekker, S.C.3
  • 18
    • 1942501852 scopus 로고    scopus 로고
    • Syndecan-2 regulates transforming growth factor-beta signaling
    • Chen, L., Klass, C., and Woods, A. (2004b) Syndecan-2 regulates transforming growth factor-beta signaling. J. Biol. Chem. 279, 15715-15718.
    • (2004) J. Biol. Chem , vol.279 , pp. 15715-15718
    • Chen, L.1    Klass, C.2    Woods, A.3
  • 19
    • 0030764559 scopus 로고    scopus 로고
    • Dengue virus infectivity depends on envelope protein binding to target cell heparan sulfate
    • Chen, Y., Maguire, T., Hileman, R. E., Fromm, J. R., Esko, J. D., et al. (1997) Dengue virus infectivity depends on envelope protein binding to target cell heparan sulfate. Nat. Med. 3, 866-871.
    • (1997) Nat. Med , vol.3 , pp. 866-871
    • Chen, Y.1    Maguire, T.2    Hileman, R.E.3    Fromm, J.R.4    Esko, J.D.5
  • 20
    • 33846979112 scopus 로고    scopus 로고
    • Streptococcus pneumoniae sheds syndecan-1 ectodomains through ZmpC, a metalloproteinase virulence factor
    • Chen, Y., Hayashida, A., Bennett, A. E., Hollingshead, S. K., and Park, P. W. (2007) Streptococcus pneumoniae sheds syndecan-1 ectodomains through ZmpC, a metalloproteinase virulence factor. J. Biol. Chem. 282, 159-167.
    • (2007) J. Biol. Chem , vol.282 , pp. 159-167
    • Chen, Y.1    Hayashida, A.2    Bennett, A.E.3    Hollingshead, S.K.4    Park, P.W.5
  • 21
    • 33845967489 scopus 로고    scopus 로고
    • Secreted neutral metalloproteases of Bacillus anthracis as candidate pathogenic factors
    • Chung, M. C., Popova, T. G., Millis, B. A., Mukherjee, D. W., Zhou, W., et al. (2006) Secreted neutral metalloproteases of Bacillus anthracis as candidate pathogenic factors. J. Biol. Chem. 281, 31408-31418.
    • (2006) J. Biol. Chem , vol.281 , pp. 31408-31418
    • Chung, M.C.1    Popova, T.G.2    Millis, B.A.3    Mukherjee, D.W.4    Zhou, W.5
  • 22
    • 0028970195 scopus 로고
    • Receptors involved in carbohydrate binding modulate intestinal epithelial-neutrophil interactions
    • Colgan, S. P., Parkos, C. A., McGuirk, D., Brady, H. R., Papayianni, A. A., et al. (1995) Receptors involved in carbohydrate binding modulate intestinal epithelial-neutrophil interactions. J. Biol. Chem. 270, 10531-10539.
    • (1995) J. Biol. Chem , vol.270 , pp. 10531-10539
    • Colgan, S.P.1    Parkos, C.A.2    McGuirk, D.3    Brady, H.R.4    Papayianni, A.A.5
  • 23
    • 0034801719 scopus 로고    scopus 로고
    • Syndecan-2 expression in colorectal cancer-derived HT-29 M6 epithelial cells induces a migratory phenotype
    • Contreras, H. R., Fabre, M., Granes, F., Casaroli-Marano, R., Rocamora, N., et al. (2001) Syndecan-2 expression in colorectal cancer-derived HT-29 M6 epithelial cells induces a migratory phenotype. Biochem. Biophys. Res. Commun. 286, 742-751.
    • (2001) Biochem. Biophys. Res. Commun , vol.286 , pp. 742-751
    • Contreras, H.R.1    Fabre, M.2    Granes, F.3    Casaroli-Marano, R.4    Rocamora, N.5
  • 24
    • 0029953925 scopus 로고    scopus 로고
    • Syndecans, signaling, and cell adhesion
    • Couchman, J. R. and Woods, A. (1996) Syndecans, signaling, and cell adhesion. J. Cell. Physiol. 61, 578-584.
    • (1996) J. Cell. Physiol , vol.61 , pp. 578-584
    • Couchman, J.R.1    Woods, A.2
  • 26
    • 0033519974 scopus 로고    scopus 로고
    • Heparin, cell adhesion, and pathogenesis of inflammatory bowel disease
    • Day, R. and Forbes, A. (1999) Heparin, cell adhesion, and pathogenesis of inflammatory bowel disease. Lancet 354, 62-65.
    • (1999) Lancet , vol.354 , pp. 62-65
    • Day, R.1    Forbes, A.2
  • 27
    • 0038798579 scopus 로고    scopus 로고
    • Regulation of epithelial syndecan-1 expression by inflammatory cytokines
    • Day, R. M., Mitchell, T. J., Knight, S. C., and Forbes, A. (2003) Regulation of epithelial syndecan-1 expression by inflammatory cytokines. Cytokine 21, 224-233.
    • (2003) Cytokine , vol.21 , pp. 224-233
    • Day, R.M.1    Mitchell, T.J.2    Knight, S.C.3    Forbes, A.4
  • 28
    • 28244483280 scopus 로고    scopus 로고
    • A highly conserved arginine in gp 120 governs HIV-1 binding to both syndecans and CCR5 via sulfated motifs
    • de Parseval, A., Bobardt, M. D., Chatterji, A., Chatterji, U., Elder, J. H., et al. (2005) A highly conserved arginine in gp 120 governs HIV-1 binding to both syndecans and CCR5 via sulfated motifs. J. Biol. Chem. 280, 39493-39504.
    • (2005) J. Biol. Chem , vol.280 , pp. 39493-39504
    • de Parseval, A.1    Bobardt, M.D.2    Chatterji, A.3    Chatterji, U.4    Elder, J.H.5
  • 29
    • 0029166397 scopus 로고
    • Heparin is an adhesive ligand for the leukocyte integrin Mac-1 (CD11b/CD18)
    • Diamond, M. S., Alon, R., Parkos, C. A., Quinn, M. T., and Springer, T. A. (1995) Heparin is an adhesive ligand for the leukocyte integrin Mac-1 (CD11b/CD18). J. Cell Biol. 130, 1473-1482.
    • (1995) J. Cell Biol , vol.130 , pp. 1473-1482
    • Diamond, M.S.1    Alon, R.2    Parkos, C.A.3    Quinn, M.T.4    Springer, T.A.5
  • 31
    • 27944469616 scopus 로고    scopus 로고
    • Growth factor-induced shedding of syndecan-1 confers glypican-1 dependence on mitogenic responses of cancer cells
    • Ding, K., Lopez-Burks, M., Sánchez-Duran, J. A., Korc, M., and Lander, M. D. (2005) Growth factor-induced shedding of syndecan-1 confers glypican-1 dependence on mitogenic responses of cancer cells. J. Cell Biol. 171, 729-738.
    • (2005) J. Cell Biol , vol.171 , pp. 729-738
    • Ding, K.1    Lopez-Burks, M.2    Sánchez-Duran, J.A.3    Korc, M.4    Lander, M.D.5
  • 33
    • 0026672733 scopus 로고
    • Growth factors induce 3T3 cells to express bFGF-binding syndecan
    • Elenius, K., Määttä A., Salmivirta, M., and Jalkanen, M. (1992) Growth factors induce 3T3 cells to express bFGF-binding syndecan. J. Biol. Chem. 267, 6435-6441.
    • (1992) J. Biol. Chem , vol.267 , pp. 6435-6441
    • Elenius, K.1    Määttä, A.2    Salmivirta, M.3    Jalkanen, M.4
  • 34
    • 4744368711 scopus 로고    scopus 로고
    • Inhibition by the soluble syndecan-1 ectodomains delays wound repair in mice overexpressing syndecan-1
    • Elenius, V., Götte, M., Reizes, O., Elenius, K., and Bernfield, M. (2004) Inhibition by the soluble syndecan-1 ectodomains delays wound repair in mice overexpressing syndecan-1. J. Biol. Chem. 279, 41928-41935.
    • (2004) J. Biol. Chem , vol.279 , pp. 41928-41935
    • Elenius, V.1    Götte, M.2    Reizes, O.3    Elenius, K.4    Bernfield, M.5
  • 35
    • 8544247193 scopus 로고    scopus 로고
    • Time-dependent increases in syndecan-1 and fibroglycan messenger RNA expression in the infarct zone after experimentally induced myocardial infarction in rats
    • Endo, C., Kusachi, S., Yamamoto, K., Murakami, M., Murakami, T., et al. (1997) Time-dependent increases in syndecan-1 and fibroglycan messenger RNA expression in the infarct zone after experimentally induced myocardial infarction in rats. Coron. Artery Dis. 8, 155-161.
    • (1997) Coron. Artery Dis , vol.8 , pp. 155-161
    • Endo, C.1    Kusachi, S.2    Yamamoto, K.3    Murakami, M.4    Murakami, T.5
  • 36
    • 0142103466 scopus 로고    scopus 로고
    • Cleavage of syndecan-1 by membrane tpye matrix metalloproteinase-1 stimulates cell migration
    • Endo, K., Takino, T., Miyamori, H., Kinsen, H., Yoshizaki, R., et al. (2003) Cleavage of syndecan-1 by membrane tpye matrix metalloproteinase-1 stimulates cell migration. J. Biol. Chem. 278, 40764-40770.
    • (2003) J. Biol. Chem , vol.278 , pp. 40764-40770
    • Endo, K.1    Takino, T.2    Miyamori, H.3    Kinsen, H.4    Yoshizaki, R.5
  • 37
    • 0034947648 scopus 로고    scopus 로고
    • Molecular diversity of heparan sulfate
    • Esko, J. D. and Lindahl, U. (2001) Molecular diversity of heparan sulfate. J. Clin. Invest. 108, 169-173.
    • (2001) J. Clin. Invest , vol.108 , pp. 169-173
    • Esko, J.D.1    Lindahl, U.2
  • 38
    • 0035997376 scopus 로고    scopus 로고
    • Order out of chaos: Assembly of ligand binding sites in heparan sulfate
    • Esko, J. D. and Selleck, S. B. (2002) Order out of chaos: assembly of ligand binding sites in heparan sulfate. Annu. Rev. Biochem. 71, 435-471.
    • (2002) Annu. Rev. Biochem , vol.71 , pp. 435-471
    • Esko, J.D.1    Selleck, S.B.2
  • 40
    • 0030816854 scopus 로고    scopus 로고
    • Treatment of corticosteroid-resistant ulcerative colitis with heparin-a report of 16 cases
    • Evans, R. C., Wong, V. S, Morris, A. L, and Rhodes, J. M. (1997) Treatment of corticosteroid-resistant ulcerative colitis with heparin-a report of 16 cases. Aliment. Pharmacol. Ther. 11, 1037-1040.
    • (1997) Aliment. Pharmacol. Ther , vol.11 , pp. 1037-1040
    • Evans, R.C.1    Wong, V.S.2    Morris, A.L.3    Rhodes, J.M.4
  • 41
    • 33749441307 scopus 로고    scopus 로고
    • The role of syndecans in disease and wound healing
    • Fears, C. Y. and Woods, A. (2006) The role of syndecans in disease and wound healing. Matrix Biol. 25, 443-456.
    • (2006) Matrix Biol , vol.25 , pp. 443-456
    • Fears, C.Y.1    Woods, A.2
  • 42
    • 33744951974 scopus 로고    scopus 로고
    • Syndecan-2 is expressed in the microvasculature of gliomas and regulates angiogenic processes in microasoular endothelial cells
    • Fears, C. Y., Gladson, C. L., and Woods, A. (2006) Syndecan-2 is expressed in the microvasculature of gliomas and regulates angiogenic processes in microasoular endothelial cells. J. Biol. Chem. 281, 14533-14536.
    • (2006) J. Biol. Chem , vol.281 , pp. 14533-14536
    • Fears, C.Y.1    Gladson, C.L.2    Woods, A.3
  • 43
    • 1842482657 scopus 로고    scopus 로고
    • Increased syndecan expression following myocardial infarction indicates a role in cardiac remodeling
    • Finsen, A. V., Woldbaek, P. R., Li, J., Wu, J., Lyberg, T., et al. (2004) Increased syndecan expression following myocardial infarction indicates a role in cardiac remodeling. Physiol. Genomics 16, 301-308.
    • (2004) Physiol. Genomics , vol.16 , pp. 301-308
    • Finsen, A.V.1    Woldbaek, P.R.2    Li, J.3    Wu, J.4    Lyberg, T.5
  • 44
    • 0034695918 scopus 로고    scopus 로고
    • Shedding of syndecan-1 and -4 ectodomains is regulated by multiple signaling pathways and mediated by a TIMP-3 sensitive metalloproteinase
    • Fitzgerald, M. L., Wang, Z., Park, P. W., Murphy, GL, and Bernfield, M. (2000) Shedding of syndecan-1 and -4 ectodomains is regulated by multiple signaling pathways and mediated by a TIMP-3 sensitive metalloproteinase. J. Cell Biol. 148, 81-824.
    • (2000) J. Cell Biol , vol.148 , pp. 81-824
    • Fitzgerald, M.L.1    Wang, Z.2    Park, P.W.3    Murphy, G.L.4    Bernfield, M.5
  • 46
    • 0028814834 scopus 로고
    • Paradoxical response to heparin in 10 patients with ulcerative colitis
    • Gaffhey, P. R., Doyle, C. T., Gaffney, A., Hogan, J., Hayes, D. P., et al. (1995) Paradoxical response to heparin in 10 patients with ulcerative colitis. Am. J Gastroenterol. 90, 220-223.
    • (1995) Am. J Gastroenterol , vol.90 , pp. 220-223
    • Gaffhey, P.R.1    Doyle, C.T.2    Gaffney, A.3    Hogan, J.4    Hayes, D.P.5
  • 47
    • 0025976992 scopus 로고
    • Response to heparin in patients with ulcerative colitis
    • Gaffney, P. R., O'Leary, J. J., Doyle, C. T., Gaffney, A., Hogan, J., et al. (1991) Response to heparin in patients with ulcerative colitis. Lancet 337, 238-239.
    • (1991) Lancet , vol.337 , pp. 238-239
    • Gaffney, P.R.1    O'Leary, J.J.2    Doyle, C.T.3    Gaffney, A.4    Hogan, J.5
  • 48
    • 0034907578 scopus 로고    scopus 로고
    • Heparan sulfate: Growth control with a restricted sequence menu
    • Gallagher, J. T. (2001) Heparan sulfate: growth control with a restricted sequence menu. J. Clin. Invest. 108, 357-361.
    • (2001) J. Clin. Invest , vol.108 , pp. 357-361
    • Gallagher, J.T.1
  • 49
    • 2542422996 scopus 로고    scopus 로고
    • Syndecans and HIV-1 pathogenesis
    • Gallay, P. (2004) Syndecans and HIV-1 pathogenesis. Microbes. Infect. 6, 617-622.
    • (2004) Microbes. Infect , vol.6 , pp. 617-622
    • Gallay, P.1
  • 50
    • 33746928340 scopus 로고    scopus 로고
    • Emerging roles for ectodomain shedding in the regulation of inflammatory responses
    • Garton, K. J., Gough, P. J., and Raines, E. W. (2006) Emerging roles for ectodomain shedding in the regulation of inflammatory responses. J. Leukoc. Biol. 79, 1105-1116.
    • (2006) J. Leukoc. Biol , vol.79 , pp. 1105-1116
    • Garton, K.J.1    Gough, P.J.2    Raines, E.W.3
  • 51
    • 0033574278 scopus 로고    scopus 로고
    • Glypican-1 is a VEGF 165 binding proteoglycan that acts as an extracellular chaperone for VEGF 165
    • Gengrinovitch, S., Berman, B., David, G., Witte, L., Neufeld, G., et al. (1999) Glypican-1 is a VEGF 165 binding proteoglycan that acts as an extracellular chaperone for VEGF 165. J. Biol. Chem. 274, 10816-10822.
    • (1999) J. Biol. Chem , vol.274 , pp. 10816-10822
    • Gengrinovitch, S.1    Berman, B.2    David, G.3    Witte, L.4    Neufeld, G.5
  • 52
    • 0031028665 scopus 로고    scopus 로고
    • Monocyte adhesion to activated aortic endothelium: Role of L-selectin and heparan sulfate proteoglycans
    • Giuffre, L., Cordey, A. S., Monai, N., Tardy, Y., Schapira, M., et al. (1997) Monocyte adhesion to activated aortic endothelium: role of L-selectin and heparan sulfate proteoglycans. J. Cell Biol. 136, 945-956.
    • (1997) J. Cell Biol , vol.136 , pp. 945-956
    • Giuffre, L.1    Cordey, A.S.2    Monai, N.3    Tardy, Y.4    Schapira, M.5
  • 53
    • 0037387945 scopus 로고    scopus 로고
    • Syndecans in inflammation
    • Götte, M. (2003) Syndecans in inflammation. Faseb J. 17, 575-591.
    • (2003) Faseb J , vol.17 , pp. 575-591
    • Götte, M.1
  • 54
    • 0036210319 scopus 로고    scopus 로고
    • Role of syndecan-1 in leukocyte-endothelial interactions in the ocular vasculature
    • Götte, M., Joussen, A., M., Klein, C., Andre, P., Wagner, D. D., et al. (2002) Role of syndecan-1 in leukocyte-endothelial interactions in the ocular vasculature. Invest. Ophthalmol. Vis. Sci. 43, 1135-1141.
    • (2002) Invest. Ophthalmol. Vis. Sci , vol.43 , pp. 1135-1141
    • Götte, M.1    Joussen, A.M.2    Klein, C.3    Andre, P.4    Wagner, D.D.5
  • 55
    • 0030775369 scopus 로고    scopus 로고
    • Acidic sphingomyelinase mediates entry of N. gonorrhoeae into nonphagocytic cells
    • Grassmé, H., Gulbins, E., Brenner, B., Ferlinz, K., Sandhoff, K., et al. (1997) Acidic sphingomyelinase mediates entry of N. gonorrhoeae into nonphagocytic cells. Cell 91, 605-615.
    • (1997) Cell , vol.91 , pp. 605-615
    • Grassmé, H.1    Gulbins, E.2    Brenner, B.3    Ferlinz, K.4    Sandhoff, K.5
  • 56
    • 0345471071 scopus 로고    scopus 로고
    • Normal levels of anticoagulant heparan sulfate are not essential for normal hemostasis
    • HajMohammadi, S., Enjyoji, K., Princivalle, M., Christi, P., Lech, M., et al. (2003) Normal levels of anticoagulant heparan sulfate are not essential for normal hemostasis. J. Clin. Invest. 111, 989-999.
    • (2003) J. Clin. Invest , vol.111 , pp. 989-999
    • HajMohammadi, S.1    Enjyoji, K.2    Princivalle, M.3    Christi, P.4    Lech, M.5
  • 57
    • 0942279499 scopus 로고    scopus 로고
    • Interleukin-8 binds to syndecan-2 on human endothelial cells
    • Halden, Y., Rek, A., Atzenhofer, W., Szilak, L., Walmig, A., et al. (2004) Interleukin-8 binds to syndecan-2 on human endothelial cells. Biochem. J. 377, 533-539.
    • (2004) Biochem. J , vol.377 , pp. 533-539
    • Halden, Y.1    Rek, A.2    Atzenhofer, W.3    Szilak, L.4    Walmig, A.5
  • 58
    • 22244448718 scopus 로고    scopus 로고
    • Regulation of protein function by glycosaminoglycans - as exemplified by chemokines
    • Handel, T. M., Johnson, Z., Crown, S. E, Lau, E. K., and Proudfoot, A. E. (2005) Regulation of protein function by glycosaminoglycans - as exemplified by chemokines. Annu. Rev. Biochem. 74, 385-410.
    • (2005) Annu. Rev. Biochem , vol.74 , pp. 385-410
    • Handel, T.M.1    Johnson, Z.2    Crown, S.E.3    Lau, E.K.4    Proudfoot, A.E.5
  • 59
    • 33747727571 scopus 로고    scopus 로고
    • Syndecan-1 expression in epithelial cells is induced by TGFβ through a PKA-dependent pathway
    • Hayashida, K., Johnston, D. R., Goldberger, O., and Park, P. W. (2006) Syndecan-1 expression in epithelial cells is induced by TGFβ through a PKA-dependent pathway. J. Biol. Chem. 281, 24365-24374.
    • (2006) J. Biol. Chem , vol.281 , pp. 24365-24374
    • Hayashida, K.1    Johnston, D.R.2    Goldberger, O.3    Park, P.W.4
  • 60
    • 28444451902 scopus 로고    scopus 로고
    • Syndecan-1 shedding contributes to Pseudomonas aeruginosa sepsis
    • Haynes, A., Ruda, 3rd, F., Oliver, J., Hamood, A. N., Griswold, J. A., et al. (2005a) Syndecan-1 shedding contributes to Pseudomonas aeruginosa sepsis. Infect. Immun. 73, 7914-7921.
    • (2005) Infect. Immun , vol.73 , pp. 7914-7921
    • Haynes, A.1    Ruda 3rd, F.2    Oliver, J.3    Hamood, A.N.4    Griswold, J.A.5
  • 61
    • 11844296684 scopus 로고    scopus 로고
    • Protamine sulfate reduces the susceptibility of thermally injured mice to Pseudomonas aeruginosa infection
    • Haynes, A., Rumbaugh, 3rd, K. P., Park, P. W., Hamood, A. N., and Griswold, J. A. (2005b) Protamine sulfate reduces the susceptibility of thermally injured mice to Pseudomonas aeruginosa infection. J. Surg. Res. 123, 109-117.
    • (2005) J. Surg. Res , vol.123 , pp. 109-117
    • Haynes, A.1    Rumbaugh 3rd, K.P.2    Park, P.W.3    Hamood, A.N.4    Griswold, J.A.5
  • 62
    • 33646781306 scopus 로고    scopus 로고
    • Ability of the heparan sulfate proteoglycan syndecan-1 to participate in bacterial translocation across the intestinal epithelial barrier
    • Henry-Stanley, M. J., Hess, D. J., Erlandsen, S. L., and Wells, C. L. (2005) Ability of the heparan sulfate proteoglycan syndecan-1 to participate in bacterial translocation across the intestinal epithelial barrier. Shock 24, 571-576.
    • (2005) Shock , vol.24 , pp. 571-576
    • Henry-Stanley, M.J.1    Hess, D.J.2    Erlandsen, S.L.3    Wells, C.L.4
  • 63
    • 33747113334 scopus 로고    scopus 로고
    • Synergistic effect of tumor necrosis factor-alpha and interferon-gamma on enterocyte shedding of syndecan-1 and associated decreases in internalization of Listeria monocytogenes and Staphylococcus aureus
    • Henry-Stanley, M. J., Zhang, B., Erlandsen, S. L., and Wells, C. L. (2006) Synergistic effect of tumor necrosis factor-alpha and interferon-gamma on enterocyte shedding of syndecan-1 and associated decreases in internalization of Listeria monocytogenes and Staphylococcus aureus. Cytokine 34, 252-259.
    • (2006) Cytokine , vol.34 , pp. 252-259
    • Henry-Stanley, M.J.1    Zhang, B.2    Erlandsen, S.L.3    Wells, C.L.4
  • 64
    • 33748857194 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans mediate Staphylococcus aureus interactions with intestinal epithelium
    • Hess, D. J., Henry-Stanley, M., J.; Erlandsen, S. L., and Wells, C. J. (2006) Heparan sulfate proteoglycans mediate Staphylococcus aureus interactions with intestinal epithelium. Med. Microbiol. Immunol. 195, 133-141.
    • (2006) Med. Microbiol. Immunol , vol.195 , pp. 133-141
    • Hess, D.J.1    Henry-Stanley, M.J.2    Erlandsen, S.L.3    Wells, C.J.4
  • 66
    • 0035861669 scopus 로고    scopus 로고
    • Syndecan-4 deficiency leads to high mortality of lipopolysaccharide-injected mice
    • Ishiguro, K., Kadomatsu, K., Kojima, T., Muramatsu, H., Iwase, M., et al. (2001a) Syndecan-4 deficiency leads to high mortality of lipopolysaccharide-injected mice. J. Biol. Chem. 276, 47483-47488.
    • (2001) J. Biol. Chem , vol.276 , pp. 47483-47488
    • Ishiguro, K.1    Kadomatsu, K.2    Kojima, T.3    Muramatsu, H.4    Iwase, M.5
  • 67
    • 0035051269 scopus 로고    scopus 로고
    • Syndecan-4 deficiency increases susceptibility to kappa-carrageenan-induced renal damage
    • Ishiguro, K., Kadomatsu, K., Kojima, T., Muramatsu, H., Matsuo, S., et al. (2001b) Syndecan-4 deficiency increases susceptibility to kappa-carrageenan-induced renal damage. Lab. Invest. 81, 509-516.
    • (2001) Lab. Invest , vol.81 , pp. 509-516
    • Ishiguro, K.1    Kadomatsu, K.2    Kojima, T.3    Muramatsu, H.4    Matsuo, S.5
  • 68
    • 0033672202 scopus 로고    scopus 로고
    • Syndecan-4 deficiency impairs the fetal vessels in the placental labyrinth
    • Ishiguro, K., Kadomatsu, K., Kojima, T., Muramatsu, H., Nakamura, E., et al. (2000a) Syndecan-4 deficiency impairs the fetal vessels in the placental labyrinth. Dev. Dyn. 219, 539-544.
    • (2000) Dev. Dyn , vol.219 , pp. 539-544
    • Ishiguro, K.1    Kadomatsu, K.2    Kojima, T.3    Muramatsu, H.4    Nakamura, E.5
  • 69
    • 0034050724 scopus 로고    scopus 로고
    • Syndecan-4 deficiency impairs focal adhesion formation only under restricted conditions
    • Ishiguro, K., Kadomatsu, K., Kojima, T., Muramatsu, H., Tsuzuki, S., et al. (2000b) Syndecan-4 deficiency impairs focal adhesion formation only under restricted conditions. J. Biol. Chem. 275, 5249-5252.
    • (2000) J. Biol. Chem , vol.275 , pp. 5249-5252
    • Ishiguro, K.1    Kadomatsu, K.2    Kojima, T.3    Muramatsu, H.4    Tsuzuki, S.5
  • 70
    • 0023550962 scopus 로고
    • Cell surface proteoglycan of mouse mammary epithelial cells is shed by cleavage of its matrix-binding ectodomain from its membrane-associated domain
    • Jalkanen, M., Rapraeger, A., Saunders, S., and Bernfield, M. (1987) Cell surface proteoglycan of mouse mammary epithelial cells is shed by cleavage of its matrix-binding ectodomain from its membrane-associated domain. J Cell Biol. 105, 3087-3096.
    • (1987) J Cell Biol , vol.105 , pp. 3087-3096
    • Jalkanen, M.1    Rapraeger, A.2    Saunders, S.3    Bernfield, M.4
  • 71
    • 6344269426 scopus 로고    scopus 로고
    • Interference with heparin binding and oligomerization creates a novel anti-inflammatory strategy targeting the chemokine system
    • Johnson, Z., Kosco-Vilbois, M., H., Herren, S., Cirillo, R., Muzio, V., et al. (2004) Interference with heparin binding and oligomerization creates a novel anti-inflammatory strategy targeting the chemokine system. J Immunol. 173, 5776-5785.
    • (2004) J Immunol , vol.173 , pp. 5776-5785
    • Johnson, Z.1    Kosco-Vilbois, M.H.2    Herren, S.3    Cirillo, R.4    Muzio, V.5
  • 72
    • 0036396896 scopus 로고    scopus 로고
    • Syndecan-3-deficient mice exhibit enhanced LTP and impaired hippocampus-dependent memory
    • Kaksonen, M., Pavlov, I., Voikar, V., Lauri, S. E., Hienola, A., et al. (2002) Syndecan-3-deficient mice exhibit enhanced LTP and impaired hippocampus-dependent memory. Mol. Cell Neurosci. 21, 158-172.
    • (2002) Mol. Cell Neurosci , vol.21 , pp. 158-172
    • Kaksonen, M.1    Pavlov, I.2    Voikar, V.3    Lauri, S.E.4    Hienola, A.5
  • 73
    • 0029005076 scopus 로고
    • Loss of cell surface syndecan-1 causes epithelia to transform into anchorage-independent mesenchyme-like cells
    • Kato, M., Saunders, S., Nguyen, H., and Bernfield, M. (1995) Loss of cell surface syndecan-1 causes epithelia to transform into anchorage-independent mesenchyme-like cells. Mol. Biol. Cell. 6, 559-576.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 559-576
    • Kato, M.1    Saunders, S.2    Nguyen, H.3    Bernfield, M.4
  • 74
    • 0036182433 scopus 로고    scopus 로고
    • Role of inflammatory mediators in resistance and susceptibility to pneumococcal infection
    • Kerr, A. R., Irvine, J. J., Search, J. J., Gingles, N. A., Kadioglu, A., et al. (2002) Role of inflammatory mediators in resistance and susceptibility to pneumococcal infection. Infect. Immun. 70, 1547-1557.
    • (2002) Infect. Immun , vol.70 , pp. 1547-1557
    • Kerr, A.R.1    Irvine, J.J.2    Search, J.J.3    Gingles, N.A.4    Kadioglu, A.5
  • 75
    • 0028016404 scopus 로고
    • Members of the syndecan family of heparan sulfate proteoglycans are expressed in distinct cell-, tissue-, and development-specific patterns
    • Kim, C. W., Goldberger, O. A., Gallo, R. L., and Bernfield, M. (1994) Members of the syndecan family of heparan sulfate proteoglycans are expressed in distinct cell-, tissue-, and development-specific patterns. Mol. Biol. Cell. 5, 797-805.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 797-805
    • Kim, C.W.1    Goldberger, O.A.2    Gallo, R.L.3    Bernfield, M.4
  • 76
    • 1542327294 scopus 로고    scopus 로고
    • Role of syndecan-4 in the cellular invasion of Orientia tsutsugamushi
    • Kim, H. R., Choi, M. S., and Kim, I. S. (2004) Role of syndecan-4 in the cellular invasion of Orientia tsutsugamushi. Microb. Pathog. 36, 219-225.
    • (2004) Microb. Pathog , vol.36 , pp. 219-225
    • Kim, H.R.1    Choi, M.S.2    Kim, I.S.3
  • 77
    • 0035020956 scopus 로고    scopus 로고
    • Plasma levels of syndecan-4 (ryudocan) are elevated in patients with acute myocardial infarction
    • Kojima, T., Takagi, A., Maeda, M., Segawa, T., Shimizu, A., et al. (2001) Plasma levels of syndecan-4 (ryudocan) are elevated in patients with acute myocardial infarction. Thromb. Haemost. 85, 793-799.
    • (2001) Thromb. Haemost , vol.85 , pp. 793-799
    • Kojima, T.1    Takagi, A.2    Maeda, M.3    Segawa, T.4    Shimizu, A.5
  • 78
    • 0033613247 scopus 로고    scopus 로고
    • Glycosaminoglycans interact selectively with chemokines and modulate receptor binding and cellular responses
    • Kuschert, G. S. V., Coulin, F., Power, C. A., Proudfoot, A. E. I., Hubbard, R. E., et al. (1999) Glycosaminoglycans interact selectively with chemokines and modulate receptor binding and cellular responses. Biochemistry 38, 12959-12968.
    • (1999) Biochemistry , vol.38 , pp. 12959-12968
    • Kuschert, G.S.V.1    Coulin, F.2    Power, C.A.3    Proudfoot, A.E.I.4    Hubbard, R.E.5
  • 79
    • 33847309856 scopus 로고    scopus 로고
    • Staphylococcus aureus Panton-Valentine leukocidin causes necrotizing pneumonia
    • Labandeira-Rey, M., Couzon, F., Boisset, S., Brown, E. L., Bes, M., et al. (2007) Staphylococcus aureus Panton-Valentine leukocidin causes necrotizing pneumonia. Science 315, 1130-1133.
    • (2007) Science , vol.315 , pp. 1130-1133
    • Labandeira-Rey, M.1    Couzon, F.2    Boisset, S.3    Brown, E.L.4    Bes, M.5
  • 80
    • 13544267411 scopus 로고    scopus 로고
    • Identification of an invasion regulatory domain within the core protein of syndecan-1
    • Langford, J. K., Yang, Y., Kieber-Emmons, T., and Sanderson, R. D. (2005) Identification of an invasion regulatory domain within the core protein of syndecan-1. J. Biol. Chem. 280, 3467-3473.
    • (2005) J. Biol. Chem , vol.280 , pp. 3467-3473
    • Langford, J.K.1    Yang, Y.2    Kieber-Emmons, T.3    Sanderson, R.D.4
  • 81
    • 18744383614 scopus 로고    scopus 로고
    • Matrilysin shedding of syndecan-1 regulates chemokine mobilization and transepithelial efflux of neutrophils in acute lung injury
    • Li, Q., Park, P. W., Wilson, C. L., and Parks, W. C. (2002) Matrilysin shedding of syndecan-1 regulates chemokine mobilization and transepithelial efflux of neutrophils in acute lung injury. Cell 111, 635-646.
    • (2002) Cell , vol.111 , pp. 635-646
    • Li, Q.1    Park, P.W.2    Wilson, C.L.3    Parks, W.C.4
  • 82
    • 0032500662 scopus 로고    scopus 로고
    • The putative tumor suppressors EXT1 and EXT2 are glycosyltransferases required for the biosynthesis of heparan sulfate
    • Lind, T., Tufaro, F., McCormick, C., Lindahl, U., and Lidholt, K. (1998) The putative tumor suppressors EXT1 and EXT2 are glycosyltransferases required for the biosynthesis of heparan sulfate. J. Biol. Chem. 273, 26265-26268.
    • (1998) J. Biol. Chem , vol.273 , pp. 26265-26268
    • Lind, T.1    Tufaro, F.2    McCormick, C.3    Lindahl, U.4    Lidholt, K.5
  • 84
    • 0037022280 scopus 로고    scopus 로고
    • Structural diversity of heparan sulfate binding domains in chemokines
    • Lortat-Jacob, H., Grosdidier, A., and Imberty, A. (2002) Structural diversity of heparan sulfate binding domains in chemokines. Proc. Natl. Acad. Sci. USA 99, 1229-1234.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1229-1234
    • Lortat-Jacob, H.1    Grosdidier, A.2    Imberty, A.3
  • 85
    • 0036696903 scopus 로고    scopus 로고
    • Glycosylation in the control of selectin counter-receptor structure and function
    • Lowe, J. B. (2002) Glycosylation in the control of selectin counter-receptor structure and function. Immunol. Rev. 186, 19-36.
    • (2002) Immunol. Rev , vol.186 , pp. 19-36
    • Lowe, J.B.1
  • 86
    • 33748121374 scopus 로고    scopus 로고
    • Heparanase deglycanation of syndecan-1 is required for binding of the epithelial-restricted prosecretory mitogen lacritin
    • Ma, P., Beck, S. L., Raab, R. W., McKown, R. L., Coffman, G. L., et al. (2006) Heparanase deglycanation of syndecan-1 is required for binding of the epithelial-restricted prosecretory mitogen lacritin. J. Cell Biol. 174, 1097-1106.
    • (2006) J. Cell Biol , vol.174 , pp. 1097-1106
    • Ma, P.1    Beck, S.L.2    Raab, R.W.3    McKown, R.L.4    Coffman, G.L.5
  • 87
    • 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
    • McCormick, C., Duncan, G., Goutsos, K. T., and 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
  • 88
    • 0029838994 scopus 로고    scopus 로고
    • Identification of a heparin-binding hemagglutinin present in mycobacteria
    • Menozzi, F. D., Rouse, J. H., Alavi, M., Laude-Sharp, M., Muller, J., et al. (1996) Identification of a heparin-binding hemagglutinin present in mycobacteria. J. Exp. Med. 184, 993-1001.
    • (1996) J. Exp. Med , vol.184 , pp. 993-1001
    • Menozzi, F.D.1    Rouse, J.H.2    Alavi, M.3    Laude-Sharp, M.4    Muller, J.5
  • 89
    • 0030704740 scopus 로고    scopus 로고
    • Transcytosis and surface presentation of IL-8 by venular endothelial cells
    • Middleton, J., Neil, S., Wintle, J., Clark-Lewis, I., Moore, H., et al. (1997) Transcytosis and surface presentation of IL-8 by venular endothelial cells. Cell 91, 385-395.
    • (1997) Cell , vol.91 , pp. 385-395
    • Middleton, J.1    Neil, S.2    Wintle, J.3    Clark-Lewis, I.4    Moore, H.5
  • 90
    • 0036892646 scopus 로고    scopus 로고
    • Leukocyte extravasation: Chemokine transport and presentation by the endothelium
    • Middleton, J., Patterson, A. M., Gardner, L., Schmutz, C., and Ashton, B. A. (2002) Leukocyte extravasation: chemokine transport and presentation by the endothelium. Blood 100, 3853-3860.
    • (2002) Blood , vol.100 , pp. 3853-3860
    • Middleton, J.1    Patterson, A.M.2    Gardner, L.3    Schmutz, C.4    Ashton, B.A.5
  • 91
    • 9444297917 scopus 로고    scopus 로고
    • Coregulation of fibronectin signaling and matrix contraction by tenascin-C and syndecan-4
    • Midwood, K. S., Valenick, L. V., Hsia, H. C., and Schwarzbauer, J. E. (2004) Coregulation of fibronectin signaling and matrix contraction by tenascin-C and syndecan-4. Mol. Biol. Cell. 15, 5670-5677.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5670-5677
    • Midwood, K.S.1    Valenick, L.V.2    Hsia, H.C.3    Schwarzbauer, J.E.4
  • 92
    • 0038180539 scopus 로고    scopus 로고
    • Leukocyte-endothelial-cell interactions in leukocyte transmigration and the inflammatory response
    • Muller, W. A. (2003) Leukocyte-endothelial-cell interactions in leukocyte transmigration and the inflammatory response. Trends Immunol. 24, 327-334.
    • (2003) Trends Immunol , vol.24 , pp. 327-334
    • Muller, W.A.1
  • 93
    • 34948867377 scopus 로고    scopus 로고
    • A novel function of syndecan-2, suppression of MMP-2 activation, which causes suppression of metastasis
    • Munesue, S., Yoshitomi, Y., Kusano, Y., Koyama, Y., Nishiyama, A., et al. (2007) A novel function of syndecan-2, suppression of MMP-2 activation, which causes suppression of metastasis. J. Biol. Chem. 282, 28167-28174
    • (2007) J. Biol. Chem , vol.282 , pp. 28167-28174
    • Munesue, S.1    Yoshitomi, Y.2    Kusano, Y.3    Koyama, Y.4    Nishiyama, A.5
  • 94
    • 0027248439 scopus 로고
    • Calcium-dependent heparin-like ligands for L-selectin in nonlymphoid endothelial cells
    • Norgard-Sumnicht, K. E., Varki, N. M., and Varki, A. (1993) Calcium-dependent heparin-like ligands for L-selectin in nonlymphoid endothelial cells. Science 261, 480-483.
    • (1993) Science , vol.261 , pp. 480-483
    • Norgard-Sumnicht, K.E.1    Varki, N.M.2    Varki, A.3
  • 95
    • 36549053950 scopus 로고    scopus 로고
    • Ectopic expression of syndecan-1 in basal epidermis affects keratinocyte proliferation and wound reepithelialization
    • in press
    • Ojeh, N., Hiilesvuo, K., Warri, A., Silmivirta, M., Henttinen, T., et al. (2007) Ectopic expression of syndecan-1 in basal epidermis affects keratinocyte proliferation and wound reepithelialization. J. Invest. Dermatol. (in press).
    • (2007) J. Invest. Dermatol
    • Ojeh, N.1    Hiilesvuo, K.2    Warri, A.3    Silmivirta, M.4    Henttinen, T.5
  • 96
    • 0025943946 scopus 로고
    • A novel T. cruzi heparin-binding protein promotes fibroblast adhesion and penetration of engineered bacteria and trypanosomes into mammalian cells
    • Ortega-Barria, E. and Pereira, M. E. (1991) A novel T. cruzi heparin-binding protein promotes fibroblast adhesion and penetration of engineered bacteria and trypanosomes into mammalian cells. Cell 67, 411-421.
    • (1991) Cell , vol.67 , pp. 411-421
    • Ortega-Barria, E.1    Pereira, M.E.2
  • 97
    • 0026716363 scopus 로고
    • Malaria sporozoites and circumsporozoite proteins bind specifically to sulfated glycoconjugates
    • Pancake, S. J., Holt, G. D., Mellouk, S., and Hoffman, S. L. (1992) Malaria sporozoites and circumsporozoite proteins bind specifically to sulfated glycoconjugates. J. Cell Biol. 117, 1351-1357.
    • (1992) J. Cell Biol , vol.117 , pp. 1351-1357
    • Pancake, S.J.1    Holt, G.D.2    Mellouk, S.3    Hoffman, S.L.4
  • 98
    • 33748048179 scopus 로고    scopus 로고
    • The role of heparan sulphate in inflammation
    • Parish, C. R. (2006) The role of heparan sulphate in inflammation. Nat. Rev. Immunol. 6, 633-643.
    • (2006) Nat. Rev. Immunol , vol.6 , pp. 633-643
    • Parish, C.R.1
  • 99
    • 0007855988 scopus 로고    scopus 로고
    • Syndecan-1 shedding is enhanced by LasA, a secreted virulence factor of Pseudomonas aeruginosa
    • Park, P. W., Pier, G. B., Preston, M., J., Goldberger, O., Fitzgerald, M. L., et al. (2000a) Syndecan-1 shedding is enhanced by LasA, a secreted virulence factor of Pseudomonas aeruginosa. J. Biol. Chem. 275, 3057-3064.
    • (2000) J. Biol. Chem , vol.275 , pp. 3057-3064
    • Park, P.W.1    Pier, G.B.2    Preston, M.J.3    Goldberger, O.4    Fitzgerald, M.L.5
  • 100
    • 0034730728 scopus 로고    scopus 로고
    • Cell surface heparan sulfate proteoglycans: Selective regulators of ligand-receptor encounters
    • Park, P. W., Reizes, O., and Bernfield, M. (2000b) Cell surface heparan sulfate proteoglycans: selective regulators of ligand-receptor encounters. J. Biol. Chem. 275, 29923-29926.
    • (2000) J. Biol. Chem , vol.275 , pp. 29923-29926
    • Park, P.W.1    Reizes, O.2    Bernfield, M.3
  • 101
    • 0035799627 scopus 로고    scopus 로고
    • Exploitation of syndecan-1 shedding by Pseudomonas aeruginosa enhances virulence
    • Park, P. W., Pier, G. B., Hinkes, M. T., and Bernfield, M. (2001) Exploitation of syndecan-1 shedding by Pseudomonas aeruginosa enhances virulence. Nature 411, 98-102.
    • (2001) Nature , vol.411 , pp. 98-102
    • Park, P.W.1    Pier, G.B.2    Hinkes, M.T.3    Bernfield, M.4
  • 102
    • 0345791535 scopus 로고    scopus 로고
    • Activation of syndecan-1 ectodomain shedding by Staphylococcus aureus α-toxin and β-toxin
    • Park, P. W., Foster, T. J., Nishi, E., Duncan, S. J., Klagsbrun, M., et al. (2004) Activation of syndecan-1 ectodomain shedding by Staphylococcus aureus α-toxin and β-toxin. J. Biol. Chem. 279, 251-258.
    • (2004) J. Biol. Chem , vol.279 , pp. 251-258
    • Park, P.W.1    Foster, T.J.2    Nishi, E.3    Duncan, S.J.4    Klagsbrun, M.5
  • 103
    • 3543134126 scopus 로고    scopus 로고
    • Matrix metalloproteinases as modulators of inflammation and innate immunity
    • Parks, W. C., Wilson, C. L., and López-Boado, Y. S. (2004) Matrix metalloproteinases as modulators of inflammation and innate immunity. Nat. Rev. Immunol. 4, 617-629.
    • (2004) Nat. Rev. Immunol , vol.4 , pp. 617-629
    • Parks, W.C.1    Wilson, C.L.2    López-Boado, Y.S.3
  • 104
    • 0036024085 scopus 로고    scopus 로고
    • Selectins: Critical mediators of leukocyte recruitment
    • Patel, K. D., Cuvelier, S. L., and Wiehler, S. (2002) Selectins: critical mediators of leukocyte recruitment. Semin. Immunol. 14, 73-81.
    • (2002) Semin. Immunol , vol.14 , pp. 73-81
    • Patel, K.D.1    Cuvelier, S.L.2    Wiehler, S.3
  • 105
    • 33847694909 scopus 로고    scopus 로고
    • Pathogenesis of avian flu H5N1 and SARS
    • Peiris, M. (2006) Pathogenesis of avian flu H5N1 and SARS. Novartis Found Symp. 279, 56-60.
    • (2006) Novartis Found Symp , vol.279 , pp. 56-60
    • Peiris, M.1
  • 106
    • 33644648573 scopus 로고    scopus 로고
    • Acceleration of epithelial cell syndecan-1 shedding by anthrax hcmolytic virulence factors
    • Popova, T. G., Millis, B., Bradburne, C., Nazarenko, S., Bailey, C., et al. (2006) Acceleration of epithelial cell syndecan-1 shedding by anthrax hcmolytic virulence factors. BMC Microbiol. 6, 8-24.
    • (2006) BMC Microbiol , vol.6 , pp. 8-24
    • Popova, T.G.1    Millis, B.2    Bradburne, C.3    Nazarenko, S.4    Bailey, C.5
  • 107
    • 33746820209 scopus 로고    scopus 로고
    • Differential immunohistochemical expression of syndecan-1 and tumor necrosis factor alpha in colonic mucosa of patients with Crohn's disease
    • Principi, M., Day, R., Marangi, S., Burattini, O., De Francesco, V., et al. (2006) Differential immunohistochemical expression of syndecan-1 and tumor necrosis factor alpha in colonic mucosa of patients with Crohn's disease. Immunopharmacol. Immunotoxicol. 28, 185-195.
    • (2006) Immunopharmacol. Immunotoxicol , vol.28 , pp. 185-195
    • Principi, M.1    Day, R.2    Marangi, S.3    Burattini, O.4    De Francesco, V.5
  • 108
    • 0037452728 scopus 로고    scopus 로고
    • Glycosaminoglycan binding and oligomerization are essential for the in vivo activity of certain chemokines
    • Proudfoot, A. E., Handel, T. M., Johnson, Z., Lau, E. K., Li-Wang, P., et al. (2003) Glycosaminoglycan binding and oligomerization are essential for the in vivo activity of certain chemokines. Proc. Natl. Acad. Sci. USA 100, 1885-1890.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 1885-1890
    • Proudfoot, A.E.1    Handel, T.M.2    Johnson, Z.3    Lau, E.K.4    Li-Wang, P.5
  • 109
    • 0031672037 scopus 로고    scopus 로고
    • Molecular interactions of the syndecan core proteins
    • Rapraeger, A. and Ott, V. L. (1998) Molecular interactions of the syndecan core proteins. Curr. Opin. Cell Biol. 10, 620-628.
    • (1998) Curr. Opin. Cell Biol , vol.10 , pp. 620-628
    • Rapraeger, A.1    Ott, V.L.2
  • 110
    • 20444486909 scopus 로고    scopus 로고
    • Syndecan-4 is required for thrombin-induced migration and proliferation in human vascular smooth muscle cells
    • Rauch, B. H., Millette, E., Kenagy, R. D., Daum, G., Fischer, J. W., et al. (2005) Syndecan-4 is required for thrombin-induced migration and proliferation in human vascular smooth muscle cells. J. Biol. Chem. 280, 17507-17511.
    • (2005) J. Biol. Chem , vol.280 , pp. 17507-17511
    • Rauch, B.H.1    Millette, E.2    Kenagy, R.D.3    Daum, G.4    Fischer, J.W.5
  • 111
    • 17844372731 scopus 로고    scopus 로고
    • Transgenic expression of syndecan-1 uncovers a physiological control of feeding behavior by syndecan-3
    • Reizes, O., Lincecum, J., Wang, Z., Goldberger, O., Huang, L., et al. (2001) Transgenic expression of syndecan-1 uncovers a physiological control of feeding behavior by syndecan-3. Cell 106, 105-116.
    • (2001) Cell , vol.106 , pp. 105-116
    • Reizes, O.1    Lincecum, J.2    Wang, Z.3    Goldberger, O.4    Huang, L.5
  • 113
    • 0031023713 scopus 로고    scopus 로고
    • Microbial adherence to and invasion through proteoglycans
    • Rostand, K. S. and Esko, J. D. (1997) Microbial adherence to and invasion through proteoglycans. Infect. Immun. 65, 1-8.
    • (1997) Infect. Immun , vol.65 , pp. 1-8
    • Rostand, K.S.1    Esko, J.D.2
  • 114
    • 2542428442 scopus 로고    scopus 로고
    • Chemokines in innate and adaptive host defense: Basic chemokinese grammar for immune cells
    • Rot, A. and von Andrian, U. H. (2004) Chemokines in innate and adaptive host defense: basic chemokinese grammar for immune cells. Annu. Rev. Immunol. 22, 891-928.
    • (2004) Annu. Rev. Immunol , vol.22 , pp. 891-928
    • Rot, A.1    von Andrian, U.H.2
  • 115
    • 6344284808 scopus 로고    scopus 로고
    • Heparan sulfate/heparin oligosaccharides protect stromal cell-derived factor-1 (SDF-1)/CXCL12 against proteolysis induced by CD26/dipeptidyl peptidase IV
    • Sadir, R., Imberty, A., Baleux, F., and Lortat-Jacob, H. (2004) Heparan sulfate/heparin oligosaccharides protect stromal cell-derived factor-1 (SDF-1)/CXCL12 against proteolysis induced by CD26/dipeptidyl peptidase IV. J. Biol. Chem. 279, 43854-43860.
    • (2004) J. Biol. Chem , vol.279 , pp. 43854-43860
    • Sadir, R.1    Imberty, A.2    Baleux, F.3    Lortat-Jacob, H.4
  • 116
    • 27144526268 scopus 로고    scopus 로고
    • Plasmin- and thrombin-accelerated shedding of syndecan-4 ectodomain generates cleavage sites at Lys(114)-Arg(115) and Lys(129)-Val(130) bonds
    • Schmidt, A., Echtermeyer, F., Alozie, A., Brands, K., and Buddecke, E. (2005) Plasmin- and thrombin-accelerated shedding of syndecan-4 ectodomain generates cleavage sites at Lys(114)-Arg(115) and Lys(129)-Val(130) bonds. J. Biol. Chem. 280, 34441-34446.
    • (2005) J. Biol. Chem , vol.280 , pp. 34441-34446
    • Schmidt, A.1    Echtermeyer, F.2    Alozie, A.3    Brands, K.4    Buddecke, E.5
  • 117
    • 0026551062 scopus 로고
    • Cell surface receptors for herpes simplex virus are heparan sulfate proteoglycans
    • Shieh, M. T., WuDunn, D., Montgomery, R. I., Esko, J. D., and Spear, P. G. (1992) Cell surface receptors for herpes simplex virus are heparan sulfate proteoglycans. J. Cell Biol. 116, 1273-1281.
    • (1992) J. Cell Biol , vol.116 , pp. 1273-1281
    • Shieh, M.T.1    WuDunn, D.2    Montgomery, R.I.3    Esko, J.D.4    Spear, P.G.5
  • 118
    • 0034883314 scopus 로고    scopus 로고
    • Herpesviruses and heparan sulfate: An intimate relationship in aid of viral entry
    • Shukla, D. and Spear, P. G. (2001) Herpesviruses and heparan sulfate: an intimate relationship in aid of viral entry. J. Clin. Invest. 108, 503-510.
    • (2001) J. Clin. Invest , vol.108 , pp. 503-510
    • Shukla, D.1    Spear, P.G.2
  • 119
    • 0033215527 scopus 로고    scopus 로고
    • A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry
    • Shukla, D., Liu, J., Blaiklock, P., Shworak, N. W., Bai, Z., et al. (1999) A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry. Cell 99, 13-22.
    • (1999) Cell , vol.99 , pp. 13-22
    • Shukla, D.1    Liu, J.2    Blaiklock, P.3    Shworak, N.W.4    Bai, Z.5
  • 120
    • 0141730222 scopus 로고    scopus 로고
    • Binding of the CC-chemokine RANTES to syndecan-1 and syndecan-4 expressed on HeLa cells
    • Slimani, H., Charnaux, N., Mbemba, E., Saffar, L., Vassy, R., et al. (2003) Binding of the CC-chemokine RANTES to syndecan-1 and syndecan-4 expressed on HeLa cells. Glycobiology 13, 623-634.
    • (2003) Glycobiology , vol.13 , pp. 623-634
    • Slimani, H.1    Charnaux, N.2    Mbemba, E.3    Saffar, L.4    Vassy, R.5
  • 121
    • 33144482986 scopus 로고    scopus 로고
    • Helicobacter pylori and toll-like receptor agonists induce syndecan-4 expression in an NF-kB-dependent manner
    • Smith, M. F., Novotony, J., Carl, V. S., and Comeau, L. D. (2006) Helicobacter pylori and toll-like receptor agonists induce syndecan-4 expression in an NF-kB-dependent manner. Glycobiology 16, 221-229.
    • (2006) Glycobiology , vol.16 , pp. 221-229
    • Smith, M.F.1    Novotony, J.2    Carl, V.S.3    Comeau, L.D.4
  • 122
    • 12244305625 scopus 로고    scopus 로고
    • Defects in keratinocyte activation during wound healing in the syndecan-1-deficient mouse
    • Stepp, M. A., Gibson, H. E., Gala, P. H., Iglesia, D. D., Pajoohesh-Ganji, A., et al. (2002) Defects in keratinocyte activation during wound healing in the syndecan-1-deficient mouse. J. Cell Sci. 115, 4517-4531.
    • (2002) J. Cell Sci , vol.115 , pp. 4517-4531
    • Stepp, M.A.1    Gibson, H.E.2    Gala, P.H.3    Iglesia, D.D.4    Pajoohesh-Ganji, A.5
  • 123
    • 34548586975 scopus 로고    scopus 로고
    • Reduced migration, altered matrix and enhanced TGFbeta1 signaling are signatures of mouse keratinocytes lacking Sdc1
    • Stepp, M. A., Liu, Y., Pal-Ghosh, S., Jurjus, R. A., Tadvalkar, G, et al. (2007) Reduced migration, altered matrix and enhanced TGFbeta1 signaling are signatures of mouse keratinocytes lacking Sdc1. J. Cell Sci. 120, 2851-2863.
    • (2007) J. Cell Sci , vol.120 , pp. 2851-2863
    • Stepp, M.A.1    Liu, Y.2    Pal-Ghosh, S.3    Jurjus, R.A.4    Tadvalkar, G.5
  • 124
    • 0030967612 scopus 로고    scopus 로고
    • Regulated shedding of syndecan-1 and -4 ectodomains by thrombin and growth factor activation
    • Subramanian, S. V., Fitzgerald, M. L., and Bernfield, M. (1997) Regulated shedding of syndecan-1 and -4 ectodomains by thrombin and growth factor activation. J. Biol. Chem. 272, 14713-14720.
    • (1997) J. Biol. Chem , vol.272 , pp. 14713-14720
    • Subramanian, S.V.1    Fitzgerald, M.L.2    Bernfield, M.3
  • 125
    • 33846985321 scopus 로고    scopus 로고
    • Stromal cell-derived factor-1/chemokine (C-X-C motif) ligand 12 stimulates human hepatoma cell growth, migration, and invasion
    • Sutton, A., Friand, V., Brule-Donneger, S., Chaigneau, T., Ziol, M., et al. (2007) Stromal cell-derived factor-1/chemokine (C-X-C motif) ligand 12 stimulates human hepatoma cell growth, migration, and invasion. Mol. Cancer Res. 5, 21-33.
    • (2007) Mol. Cancer Res , vol.5 , pp. 21-33
    • Sutton, A.1    Friand, V.2    Brule-Donneger, S.3    Chaigneau, T.4    Ziol, M.5
  • 126
  • 127
    • 0032610504 scopus 로고    scopus 로고
    • Heparin in inflammation: Potential therapeutic applications beyond anticoagulation
    • Tyrrell, D. J., Horne, A. P., Holme, K. R., Preuss, J. M., and Page, C. P. (1999) Heparin in inflammation: potential therapeutic applications beyond anticoagulation. Adv. Pharmacol. 46, 151-208.
    • (1999) Adv. Pharmacol , vol.46 , pp. 151-208
    • Tyrrell, D.J.1    Horne, A.P.2    Holme, K.R.3    Preuss, J.M.4    Page, C.P.5
  • 128
    • 0030877411 scopus 로고    scopus 로고
    • Identification of heparan sulphate binding surface proteins of Helicobacter pylori: Inhibition of heparan sulphate binding with sulphated carbohydrate polymers
    • Utt, M. and Wadstrom. T. (1997) Identification of heparan sulphate binding surface proteins of Helicobacter pylori: inhibition of heparan sulphate binding with sulphated carbohydrate polymers. J. Med. Microbiol. 46, 541-546.
    • (1997) J. Med. Microbiol , vol.46 , pp. 541-546
    • Utt, M.1    Wadstrom, T.2
  • 129
    • 0035068436 scopus 로고    scopus 로고
    • Helicobacter pylori vacuolating cytotoxin binding to a putative cell surface receptor, heparan sulfate, studied by surface plasmon resonance
    • Utt, M., Danielsson, B., and Wadstrom, T. (2001) Helicobacter pylori vacuolating cytotoxin binding to a putative cell surface receptor, heparan sulfate, studied by surface plasmon resonance. FEMS Immunol. Med. Microbiol. 30, 109-113.
    • (2001) FEMS Immunol. Med. Microbiol , vol.30 , pp. 109-113
    • Utt, M.1    Danielsson, B.2    Wadstrom, T.3
  • 130
    • 0029027169 scopus 로고
    • Binding of syndecanlike cell surface proteoglycan receptors is required for Neisseria gonorrheae entry into human mucosal cells
    • van Putten, J. P. and Paul, S. M. (1995) Binding of syndecanlike cell surface proteoglycan receptors is required for Neisseria gonorrheae entry into human mucosal cells. EMBO J. 14, 2144-2154.
    • (1995) EMBO J , vol.14 , pp. 2144-2154
    • van Putten, J.P.1    Paul, S.M.2
  • 131
    • 33846570959 scopus 로고    scopus 로고
    • Increased expression of syndecan-1 protects against cardiac dilatation and dysfunction after myocardial infarction
    • Vanhoutte, D., Schellings, M. W., Gotte, M., Swinnen, M., Herias, V., et al. (2007) Increased expression of syndecan-1 protects against cardiac dilatation and dysfunction after myocardial infarction. Circulation 115, 475-482.
    • (2007) Circulation , vol.115 , pp. 475-482
    • Vanhoutte, D.1    Schellings, M.W.2    Gotte, M.3    Swinnen, M.4    Herias, V.5
  • 132
    • 0032904627 scopus 로고    scopus 로고
    • Mechanisms that regulate the function of the selectins and their ligands
    • Vestweber, D. and Blanks, J. E. (1999) Mechanisms that regulate the function of the selectins and their ligands. Physiol. Rev. 79, 181-213.
    • (1999) Physiol. Rev , vol.79 , pp. 181-213
    • Vestweber, D.1    Blanks, J.E.2
  • 133
    • 24944451114 scopus 로고    scopus 로고
    • Endothelial heparan sulfate deficiency impairs L-selectin-and chemokine-mediated neutrophil trafficking during in flammatory responses
    • Wang, L., Fuster, M., Sriramarao, P., and Esko, J. D. (2005) Endothelial heparan sulfate deficiency impairs L-selectin-and chemokine-mediated neutrophil trafficking during in flammatory responses. Nat. 1mmunol. 6, 902-910.
    • (2005) Nat. 1mmunol , vol.6 , pp. 902-910
    • Wang, L.1    Fuster, M.2    Sriramarao, P.3    Esko, J.D.4
  • 134
    • 0027493797 scopus 로고
    • The heparin binding PECAM-1 adhesion molecule is expressed by CD34+ hematopoietic precursor cells with early myeloid and B-lymphoid cell phenotypes
    • Watt, S. M., Williamson, J., Genevier, H., Fawcett, J., Simmons, D. L., et al. (1993) The heparin binding PECAM-1 adhesion molecule is expressed by CD34+ hematopoietic precursor cells with early myeloid and B-lymphoid cell phenotypes. Blood 82, 2649-2663.
    • (1993) Blood , vol.82 , pp. 2649-2663
    • Watt, S.M.1    Williamson, J.2    Genevier, H.3    Fawcett, J.4    Simmons, D.L.5
  • 136
    • 0032802301 scopus 로고    scopus 로고
    • Chemokine receptors and their antagonists in allergic lung disease
    • Wells, T. N. and Proudfoot, A. E. (1999) Chemokine receptors and their antagonists in allergic lung disease. Inflamm. Res. 48, 353-362.
    • (1999) Inflamm. Res , vol.48 , pp. 353-362
    • Wells, T.N.1    Proudfoot, A.E.2
  • 137
    • 0033636903 scopus 로고    scopus 로고
    • Reduced heparan sulfate accumulation in enterocytes contributes to protein-losing enteropathy in a congenital disorder of glycosylation
    • Westphal, V., Murch, S., Kim, S., Srikrishna, Q, Winchester, B., et al. (2000) Reduced heparan sulfate accumulation in enterocytes contributes to protein-losing enteropathy in a congenital disorder of glycosylation. Am. J. Pathol. 157, 1917-1925.
    • (2000) Am. J. Pathol , vol.157 , pp. 1917-1925
    • Westphal, V.1    Murch, S.2    Kim, S.3    Srikrishna, Q.4    Winchester, B.5
  • 138
    • 17844372521 scopus 로고    scopus 로고
    • Endogenous attenuation of allergic lung inflammation by syndecan-1
    • Xu, J., Park, P. W., Kheradmand, F., and Corry, D. B. (2005) Endogenous attenuation of allergic lung inflammation by syndecan-1. J. Immunol. 174, 5758-5765.
    • (2005) J. Immunol , vol.174 , pp. 5758-5765
    • Xu, J.1    Park, P.W.2    Kheradmand, F.3    Corry, D.B.4
  • 139
    • 0037100282 scopus 로고    scopus 로고
    • Soluble syndecan-1 promotes growth of myeloma tumors in vivo
    • Yang, Y., Yaccoby, S., Liu, W., Langford, J. K., Pumphrey, C. Y., et al. (2002) Soluble syndecan-1 promotes growth of myeloma tumors in vivo. Blood 100, 610-617.
    • (2002) Blood , vol.100 , pp. 610-617
    • Yang, Y.1    Yaccoby, S.2    Liu, W.3    Langford, J.K.4    Pumphrey, C.Y.5
  • 140
    • 34250366643 scopus 로고    scopus 로고
    • Heparanase enhances syndecan-1 shedding: A novel mechanism for stimulation of tumor growth and metastasis
    • Yang, Y., Macleod, V., Miao, H. Q., Theus, A., Zhan, F., et al. (2007) Heparanase enhances syndecan-1 shedding: a novel mechanism for stimulation of tumor growth and metastasis. J. Biol. Chem. 282, 13326-13333.
    • (2007) J. Biol. Chem , vol.282 , pp. 13326-13333
    • Yang, Y.1    Macleod, V.2    Miao, H.Q.3    Theus, A.4    Zhan, F.5
  • 141
    • 34547899189 scopus 로고    scopus 로고
    • Glycocalyx modulates the motility and proliferative response of vascular endothelium to fluid shear stress
    • Yao, Y., Rabodzey, A., and Forbes Dewey, C. Jr. (2007) Glycocalyx modulates the motility and proliferative response of vascular endothelium to fluid shear stress. Am. J. Physiol. Heart Circ. Physiol. 293, H1023-1030.
    • (2007) Am. J. Physiol. Heart Circ. Physiol , vol.293
    • Yao, Y.1    Rabodzey, A.2    Forbes Dewey Jr., C.3
  • 142
    • 0034635483 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans as extracellular docking molecules for matrilysin (matrix metalloproteinase 7)
    • Yu, W. H. and Woessner, J. F. (2000) Heparan sulfate proteoglycans as extracellular docking molecules for matrilysin (matrix metalloproteinase 7). J. Biol. Chem. 275, 4183-4191.
    • (2000) J. Biol. Chem , vol.275 , pp. 4183-4191
    • Yu, W.H.1    Woessner, J.F.2
  • 143
    • 0035369013 scopus 로고    scopus 로고
    • Heparin-enhanced zymographic detection of matrilysin and collagenases
    • Yu, W. H. and Woessner, J. F. Jr. (2001) Heparin-enhanced zymographic detection of matrilysin and collagenases. Anal. Biochem. 293, 38-42.
    • (2001) Anal. Biochem , vol.293 , pp. 38-42
    • Yu, W.H.1    Woessner Jr., J.F.2
  • 144
    • 0141644210 scopus 로고    scopus 로고
    • Leukocyte-epithelial interactions
    • Zen, K. and Parkos, C. A. (2003) Leukocyte-epithelial interactions. Curr. Opin. Cell Biol. 15, 557-564.
    • (2003) Curr. Opin. Cell Biol , vol.15 , pp. 557-564
    • Zen, K.1    Parkos, C.A.2
  • 145
    • 0028122383 scopus 로고
    • Amino acid determinants that drive heparan sulfate assembly in a proteoglycan
    • Zhang, L. and Esko, J. D. (1994) Amino acid determinants that drive heparan sulfate assembly in a proteoglycan. J. Biol. Chem. 269, 19295-19299.
    • (1994) J. Biol. Chem , vol.269 , pp. 19295-19299
    • Zhang, L.1    Esko, J.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.