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Volumn 5, Issue 1, 2010, Pages 35-46

Regulation of intracellular signaling by extracellular glycan remodeling

Author keywords

[No Author keywords available]

Indexed keywords

B LYMPHOCYTE RECEPTOR; CATHEPSIN; FIBROBLAST GROWTH FACTOR 2; FIBROBLAST GROWTH FACTOR RECEPTOR 1; GANGLIOSIDE; GLUCOSAMINE; GLUCURONIC ACID; GLYCAN; GLYCOPROTEIN; HEPARIN; OLIGOSACCHARIDE; PROTEOGLYCAN; SIALIC ACID; SIALIDASE; VASCULOTROPIN; WNT PROTEIN;

EID: 75749084864     PISSN: 15548929     EISSN: None     Source Type: Journal    
DOI: 10.1021/cb9002514     Document Type: Review
Times cited : (86)

References (114)
  • 1
    • 0035834665 scopus 로고    scopus 로고
    • Reflections on glycobiology
    • Roseman, S. (2001) Reflections on glycobiology, J. Biol. Chem. 276, 41527-41542.
    • (2001) J. Biol. Chem , vol.276 , pp. 41527-41542
    • Roseman, S.1
  • 3
    • 70349871692 scopus 로고    scopus 로고
    • Gangliosides in cell recognition and membrane protein regulation
    • Lopez, P. H., and Schnaar, R. L. (2009) Gangliosides in cell recognition and membrane protein regulation, Curr. Opin. Struct. Biol. 19, 549-557.
    • (2009) Curr. Opin. Struct. Biol , vol.19 , pp. 549-557
    • Lopez, P.H.1    Schnaar, R.L.2
  • 4
    • 0036816590 scopus 로고    scopus 로고
    • Regulation of signal transduction pathways in development by glycosylation
    • Haltiwanger, R. S. (2002) Regulation of signal transduction pathways in development by glycosylation, Curr. Opin. Struct. Biol. 12, 593-598.
    • (2002) Curr. Opin. Struct. Biol , vol.12 , pp. 593-598
    • Haltiwanger, R.S.1
  • 5
    • 35549010538 scopus 로고    scopus 로고
    • Regulation of Notch signaling by glycosylation
    • Stanley, P. (2007) Regulation of Notch signaling by glycosylation, Curr. Opin. Struct. Biol. 17, 530-535.
    • (2007) Curr. Opin. Struct. Biol , vol.17 , pp. 530-535
    • Stanley, P.1
  • 6
    • 34948855519 scopus 로고    scopus 로고
    • Gangliosides and Nogo receptors independently mediate myelin-associated glycoprotein inhibition of neurite outgrowth in different nerve cells
    • Mehta, N. R., Lopez, P. H. H., Vyas, A. A., and Schnaar, R. L. (2007) Gangliosides and Nogo receptors independently mediate myelin-associated glycoprotein inhibition of neurite outgrowth in different nerve cells, J. Biol. Chem. 282, 27875-27886.
    • (2007) J. Biol. Chem , vol.282 , pp. 27875-27886
    • Mehta, N.R.1    Lopez, P.H.H.2    Vyas, A.A.3    Schnaar, R.L.4
  • 7
    • 33745485499 scopus 로고    scopus 로고
    • ST6Gal-I restrains CD22-dependent antigen receptor endocytosis and Shp-1 recruitment in normal and pathogenic immune signaling
    • Grewal, P. K., Boton, M., Ramirez, K., Collins, B. E., Saito, A., Green, R. S., Ohtsubo, K., Chui, D., and Marth, J. D. (2006) ST6Gal-I restrains CD22-dependent antigen receptor endocytosis and Shp-1 recruitment in normal and pathogenic immune signaling, Mol. Cell. Biol. 26, 4970-4981.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 4970-4981
    • Grewal, P.K.1    Boton, M.2    Ramirez, K.3    Collins, B.E.4    Saito, A.5    Green, R.S.6    Ohtsubo, K.7    Chui, D.8    Marth, J.D.9
  • 8
    • 33846587098 scopus 로고    scopus 로고
    • Structural and mechanistic features of protein O-glycosylation linked to CD8+ T-cell apoptosis
    • Van Dyken, S. J., Green, R. S., and Marth, J. D. (2007) Structural and mechanistic features of protein O-glycosylation linked to CD8+ T-cell apoptosis, Mol. Cell. Biol. 27, 1096-1111.
    • (2007) Mol. Cell. Biol , vol.27 , pp. 1096-1111
    • Van Dyken, S.J.1    Green, R.S.2    Marth, J.D.3
  • 10
    • 33947724303 scopus 로고    scopus 로고
    • Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation
    • Lau, K. S., Partridge, E. A., Grigorian, A., Silvescu, C. I., Reinhold, V. N., Demetriou, M., and Dennis, J. W. (2007) Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation, Cell 129, 123-134.
    • (2007) Cell , vol.129 , pp. 123-134
    • Lau, K.S.1    Partridge, E.A.2    Grigorian, A.3    Silvescu, C.I.4    Reinhold, V.N.5    Demetriou, M.6    Dennis, J.W.7
  • 12
    • 70349326274 scopus 로고    scopus 로고
    • The repertoire of glycan determinants in the human glycome
    • Cummings, R. D. (2009) The repertoire of glycan determinants in the human glycome, Mol. Biosyst. 5, 1087-1104.
    • (2009) Mol. Biosyst , vol.5 , pp. 1087-1104
    • Cummings, R.D.1
  • 13
    • 34247565506 scopus 로고    scopus 로고
    • Glycan-based interactions involving vertebrate sialic-acid-recognizing proteins
    • Varki, A. (2007) Glycan-based interactions involving vertebrate sialic-acid-recognizing proteins, Nature 446, 1023-1029.
    • (2007) Nature , vol.446 , pp. 1023-1029
    • Varki, A.1
  • 14
    • 0036462606 scopus 로고    scopus 로고
    • Chemical diversity in the sialic acids and related alpha-keto acids: An evolutionary perspective
    • Angata, T., and Varki, A. (2002) Chemical diversity in the sialic acids and related alpha-keto acids: an evolutionary perspective, Chem. Rev. 102, 439-469.
    • (2002) Chem. Rev , vol.102 , pp. 439-469
    • Angata, T.1    Varki, A.2
  • 15
    • 33847755495 scopus 로고    scopus 로고
    • Carbohydrate post-glycosylational modifications
    • Yu, H., and Chen, X. (2007) Carbohydrate post-glycosylational modifications, Org. Biomol. Chem. 5, 865-872.
    • (2007) Org. Biomol. Chem , vol.5 , pp. 865-872
    • Yu, H.1    Chen, X.2
  • 16
    • 0342745990 scopus 로고
    • Neuraminidase: The specific enzyme of influenza virus and Vibrio cholerae
    • Gottschalk, A. (1957) Neuraminidase: the specific enzyme of influenza virus and Vibrio cholerae, Biochim. Biophys. Acta 23, 645-646.
    • (1957) Biochim. Biophys. Acta , vol.23 , pp. 645-646
    • Gottschalk, A.1
  • 17
    • 0027486980 scopus 로고
    • Molecular cloning and expression of cDNA encoding rat skeletal muscle cytosolic sialidase
    • Miyagi, T., Konno, K., Emori, Y., Kawasaki, H., Suzuki, K., Yasui, A., and Tsuik, S. (1993) Molecular cloning and expression of cDNA encoding rat skeletal muscle cytosolic sialidase, J. Biol. Chem. 268, 26435-26440.
    • (1993) J. Biol. Chem , vol.268 , pp. 26435-26440
    • Miyagi, T.1    Konno, K.2    Emori, Y.3    Kawasaki, H.4    Suzuki, K.5    Yasui, A.6    Tsuik, S.7
  • 18
    • 0033118290 scopus 로고    scopus 로고
    • Cloning and characterization of NEU2, a human gene homologous to rodent soluble sialidases
    • Monti, E., Preti, A., Rossi, E., Ballabio, A., and Borsani, G. (1999) Cloning and characterization of NEU2, a human gene homologous to rodent soluble sialidases, Genomics 57, 137-143.
    • (1999) Genomics , vol.57 , pp. 137-143
    • Monti, E.1    Preti, A.2    Rossi, E.3    Ballabio, A.4    Borsani, G.5
  • 19
    • 0030451974 scopus 로고    scopus 로고
    • Characterization of human lysosomal neuraminidase defines the molecular basis of the metabolic storage disorder sialidosis
    • Bonten, E., van der Spoel, A., Fornerod, M., Grosveld, G., and d'Azzo, A. (1996) Characterization of human lysosomal neuraminidase defines the molecular basis of the metabolic storage disorder sialidosis, Genes Dev. 10, 3156-3169.
    • (1996) Genes Dev , vol.10 , pp. 3156-3169
    • Bonten, E.1    van der Spoel, A.2    Fornerod, M.3    Grosveld, G.4    d'Azzo, A.5
  • 20
    • 0027256304 scopus 로고
    • Differential effect of various inhibitors on four types of rat sialidase
    • Miyagi, T., Hata, K., Hasegawa, T., and Aoyagi, T. (1993) Differential effect of various inhibitors on four types of rat sialidase, Glycoconjugate J. 10, 45-49.
    • (1993) Glycoconjugate J , vol.10 , pp. 45-49
    • Miyagi, T.1    Hata, K.2    Hasegawa, T.3    Aoyagi, T.4
  • 21
    • 33748754053 scopus 로고    scopus 로고
    • Monocyte differentiation up-regulates the expression of the lysosomal sialidase, Neu1, and triggers its targeting to the plasma membrane via major histocompatibility complex class II-positive compartments
    • Liang, F., Seyrantepe, V., Landry, K., Ahmad, R., Ahmad, A., Stamatos, N. M., and Pshezhetsky, A. V. (2006) Monocyte differentiation up-regulates the expression of the lysosomal sialidase, Neu1, and triggers its targeting to the plasma membrane via major histocompatibility complex class II-positive compartments, J. Biol. Chem. 281, 27526-27538.
    • (2006) J. Biol. Chem , vol.281 , pp. 27526-27538
    • Liang, F.1    Seyrantepe, V.2    Landry, K.3    Ahmad, R.4    Ahmad, A.5    Stamatos, N.M.6    Pshezhetsky, A.V.7
  • 25
    • 0031959479 scopus 로고    scopus 로고
    • Purification and characterization of a membrane-associated ganglioside sialidase from bovine brain
    • Hata, K., Wada, T., Hasegawa, A., Kiso, M., and Miyagi, T. (1998) Purification and characterization of a membrane-associated ganglioside sialidase from bovine brain, J. Biochem. 123, 899-905.
    • (1998) J. Biochem , vol.123 , pp. 899-905
    • Hata, K.1    Wada, T.2    Hasegawa, A.3    Kiso, M.4    Miyagi, T.5
  • 27
    • 0037135588 scopus 로고    scopus 로고
    • A close association of the ganglioside-specific sialidase Neu3 with caveolin in membrane microdomains
    • Wang, Y., Yamaguchi, K., Wada, T., Hata, K., Zhao, X. J., Fujimoto, T., and Miyagi, T. (2002) A close association of the ganglioside-specific sialidase Neu3 with caveolin in membrane microdomains, J. Biol. Chem. 277, 26252-26259.
    • (2002) J. Biol. Chem , vol.277 , pp. 26252-26259
    • Wang, Y.1    Yamaguchi, K.2    Wada, T.3    Hata, K.4    Zhao, X.J.5    Fujimoto, T.6    Miyagi, T.7
  • 28
    • 0242493195 scopus 로고    scopus 로고
    • Identification and expression of Neu4, a novel murine sialidase
    • Comelli, E. M., Amado, M., Lustig, S. R., and Paulson, J. C. (2003) Identification and expression of Neu4, a novel murine sialidase, Gene 321, 155-161.
    • (2003) Gene , vol.321 , pp. 155-161
    • Comelli, E.M.1    Amado, M.2    Lustig, S.R.3    Paulson, J.C.4
  • 31
    • 4344608107 scopus 로고    scopus 로고
    • Neu4, a novel human lysosomal lumen sialidase, confers normal phenotype to sialidosis and galactosialidosis cells
    • Seyrantepe, V., Landry, K., Trudel, S., Hassan, J. A., Morales, C. R., and Pshezhetsky, A. V. (2004) Neu4, a novel human lysosomal lumen sialidase, confers normal phenotype to sialidosis and galactosialidosis cells, J. Biol. Chem. 279, 37021-37029.
    • (2004) J. Biol. Chem , vol.279 , pp. 37021-37029
    • Seyrantepe, V.1    Landry, K.2    Trudel, S.3    Hassan, J.A.4    Morales, C.R.5    Pshezhetsky, A.V.6
  • 32
    • 47749148805 scopus 로고    scopus 로고
    • Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1
    • Cha, S. K., Ortega, B., Kurosu, H., Rosenblatt, K. P., Kuro-O, M., and Huang, C. L. (2008) Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1, Proc. Natl. Acad. Sci. U.S.A. 105, 9805-9810.
    • (2008) Proc. Natl. Acad. Sci. U.S.A , vol.105 , pp. 9805-9810
    • Cha, S.K.1    Ortega, B.2    Kurosu, H.3    Rosenblatt, K.P.4    Kuro-O, M.5    Huang, C.L.6
  • 33
    • 0031908464 scopus 로고    scopus 로고
    • Induction of sialic acid 9-O-acetylation by diverse gene products: Implications for the expression cloning of sialic acid O-acetyltransferases
    • Shi, W. X., Chammas, R., and Varki, A. (1998) Induction of sialic acid 9-O-acetylation by diverse gene products: implications for the expression cloning of sialic acid O-acetyltransferases, Glycobiology 8, 199-205.
    • (1998) Glycobiology , vol.8 , pp. 199-205
    • Shi, W.X.1    Chammas, R.2    Varki, A.3
  • 34
    • 33646343214 scopus 로고    scopus 로고
    • 9-O-Acetylation of exogenously added ganglioside GD3
    • Chen, H. Y., Challa, A. K., and Varki, A. (2006) 9-O-Acetylation of exogenously added ganglioside GD3, J. Biol. Chem. 281, 7825-7833.
    • (2006) J. Biol. Chem , vol.281 , pp. 7825-7833
    • Chen, H.Y.1    Challa, A.K.2    Varki, A.3
  • 35
    • 0033520481 scopus 로고    scopus 로고
    • Lysosomal and cytosolic sialic acid 9-O-acetylesterase activities can be encoded by one gene via differential usage of a signal peptide-encoding exon at the N terminus
    • Takematsu, H., Diaz, S., Stoddart, A., Zhang, Y., and Varki, A. (1999) Lysosomal and cytosolic sialic acid 9-O-acetylesterase activities can be encoded by one gene via differential usage of a signal peptide-encoding exon at the N terminus, J. Biol. Chem. 274, 25623-25631.
    • (1999) J. Biol. Chem , vol.274 , pp. 25623-25631
    • Takematsu, H.1    Diaz, S.2    Stoddart, A.3    Zhang, Y.4    Varki, A.5
  • 37
    • 12344310615 scopus 로고    scopus 로고
    • Functions of heparan sulfate proteoglycans in cell signaling during development
    • Lin, X. (2004) Functions of heparan sulfate proteoglycans in cell signaling during development, Development 131, 6009-6021.
    • (2004) Development , vol.131 , pp. 6009-6021
    • Lin, X.1
  • 38
    • 27744490621 scopus 로고    scopus 로고
    • Chemical approaches to deciphering the glycosaminoglycan code
    • Gama, C. I., and Hsieh-Wilson, L. C. (2005) Chemical approaches to deciphering the glycosaminoglycan code, Curr. Opin. Chem. Biol. 9, 609-619.
    • (2005) Curr. Opin. Chem. Biol , vol.9 , pp. 609-619
    • Gama, C.I.1    Hsieh-Wilson, L.C.2
  • 39
    • 0037147259 scopus 로고    scopus 로고
    • Cloning and characterization of two extracellular heparin-degrading endosulfatases in mice and humans
    • Morimoto-Tomita, M., Uchimura, K., Werb, Z., Hemmerich, S., and Rosen, S. D. (2002) Cloning and characterization of two extracellular heparin-degrading endosulfatases in mice and humans, J. Biol. Chem. 277, 49175-49185.
    • (2002) J. Biol. Chem , vol.277 , pp. 49175-49185
    • Morimoto-Tomita, M.1    Uchimura, K.2    Werb, Z.3    Hemmerich, S.4    Rosen, S.D.5
  • 40
    • 33646188185 scopus 로고    scopus 로고
    • Substrate specificity and domain functions of extracellular heparan sulfate 6-O-endosulfatases, QSulf1 and QSulf2
    • Ai, X., Do, A. T., Kusche-Gullberg, M., Lindahl, U., Lu, K., and Emerson, C. P., Jr. (2006) Substrate specificity and domain functions of extracellular heparan sulfate 6-O-endosulfatases, QSulf1 and QSulf2, J. Biol. Chem. 281, 4969-4976.
    • (2006) J. Biol. Chem , vol.281 , pp. 4969-4976
    • Ai, X.1    Do, A.T.2    Kusche-Gullberg, M.3    Lindahl, U.4    Lu, K.5    Emerson Jr., C.P.6
  • 42
    • 0035979765 scopus 로고    scopus 로고
    • Regulation of Wnt signaling and embryo patterning by an extracellular sulfatase
    • Dhoot, G. K., Gustafsson, M. K., Ai, X., Sun, W., Standiford, D. M., and Emerson, C. P., Jr. (2001) Regulation of Wnt signaling and embryo patterning by an extracellular sulfatase, Science 293, 1663-1666.
    • (2001) Science , vol.293 , pp. 1663-1666
    • Dhoot, G.K.1    Gustafsson, M.K.2    Ai, X.3    Sun, W.4    Standiford, D.M.5    Emerson Jr., C.P.6
  • 43
    • 0041671071 scopus 로고    scopus 로고
    • QSulf1 remodels the 6-O sulfation states of cell surface heparan sulfate proteoglycans to promote Wnt signaling
    • Ai, X., Do, A.-T., Lozynska, O., Kusche-Gullberg, M., Lindahl, U., and Emerson, C. P., Jr. (2003) QSulf1 remodels the 6-O sulfation states of cell surface heparan sulfate proteoglycans to promote Wnt signaling, J. Cell Biol. 162, 341-351.
    • (2003) J. Cell Biol , vol.162 , pp. 341-351
    • Ai, X.1    Do, A.-T.2    Lozynska, O.3    Kusche-Gullberg, M.4    Lindahl, U.5    Emerson Jr., C.P.6
  • 44
    • 1842737772 scopus 로고    scopus 로고
    • QSulf1, a heparan sulfate 6-O-endosulfatase, inhibits fibroblast growth factor signaling in mesoderm induction and angiogenesis
    • Wang, S., Ai, X., Freeman, S. D., Pownall, M. E., Lu, Q., Kessler, D. S., and Emerson, C. P. (2004) QSulf1, a heparan sulfate 6-O-endosulfatase, inhibits fibroblast growth factor signaling in mesoderm induction and angiogenesis, Proc. Natl. Acad. Sci. U.S.A. 101, 4833-4838.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 4833-4838
    • Wang, S.1    Ai, X.2    Freeman, S.D.3    Pownall, M.E.4    Lu, Q.5    Kessler, D.S.6    Emerson, C.P.7
  • 46
    • 39749201086 scopus 로고    scopus 로고
    • Redundant function of the heparan sulfate 6-O-endosulfatases Sulf1 and Sulf2 during skeletal development
    • Ratzka, A., Kalus, I., Moser, M., Dierks, T., Mundlos, S., and Vortkamp, A. (2008) Redundant function of the heparan sulfate 6-O-endosulfatases Sulf1 and Sulf2 during skeletal development, Dev. Dyn. 237, 339-353.
    • (2008) Dev. Dyn , vol.237 , pp. 339-353
    • Ratzka, A.1    Kalus, I.2    Moser, M.3    Dierks, T.4    Mundlos, S.5    Vortkamp, A.6
  • 48
    • 0037250476 scopus 로고    scopus 로고
    • Consequences of knocking out BMP signaling in the mouse
    • Zhao, G.-Q. (2003) Consequences of knocking out BMP signaling in the mouse, Genesis 35, 43-56.
    • (2003) Genesis , vol.35 , pp. 43-56
    • Zhao, G.-Q.1
  • 50
    • 1242272044 scopus 로고    scopus 로고
    • Domain-specific modification of heparan sulfate by Qsulf1 modulates the binding of the bone morphogenetic protein antagonist Noggin
    • Viviano, B. L., Paine-Saunders, S., Gasiunas, N., Gallagher, J., and Saunders, S. (2004) Domain-specific modification of heparan sulfate by Qsulf1 modulates the binding of the bone morphogenetic protein antagonist Noggin, J. Biol. Chem. 279, 5604-5611.
    • (2004) J. Biol. Chem , vol.279 , pp. 5604-5611
    • Viviano, B.L.1    Paine-Saunders, S.2    Gasiunas, N.3    Gallagher, J.4    Saunders, S.5
  • 51
    • 66849097625 scopus 로고    scopus 로고
    • NDST1-dependent heparan sulfate regulates BMP signaling and internalization in lung development
    • Hu, Z., Wang, C., Xiao, Y., Sheng, N., Chen, Y., Xu, Y., Zhang, L., Mo, W., Jing, N., and Hu, G. (2009) NDST1-dependent heparan sulfate regulates BMP signaling and internalization in lung development, J. Cell. Sci. 122, 1145-1154.
    • (2009) J. Cell. Sci , vol.122 , pp. 1145-1154
    • Hu, Z.1    Wang, C.2    Xiao, Y.3    Sheng, N.4    Chen, Y.5    Xu, Y.6    Zhang, L.7    Mo, W.8    Jing, N.9    Hu, G.10
  • 53
    • 55549104048 scopus 로고    scopus 로고
    • Sulf loss influences N-, 2-O-, and 6-O-sulfation of multiple heparan sulfate proteoglycans and modulates fibroblast growth factor signaling
    • Lamanna, W. C., Frese, M. A., Balleininger, M., and Dierks, T. (2008) Sulf loss influences N-, 2-O-, and 6-O-sulfation of multiple heparan sulfate proteoglycans and modulates fibroblast growth factor signaling, J. Biol. Chem. 283, 27724-27735.
    • (2008) J. Biol. Chem , vol.283 , pp. 27724-27735
    • Lamanna, W.C.1    Frese, M.A.2    Balleininger, M.3    Dierks, T.4
  • 56
    • 69849092570 scopus 로고    scopus 로고
    • The tumor suppressor function of human sulfatase 1 (SULF1) in carcinogenesis
    • Lai, J., Sandhu, D. S., Shire, A. M., and Roberts, L. R. (2008) The tumor suppressor function of human sulfatase 1 (SULF1) in carcinogenesis, J. Gastrointest. Cancer 39, 149-158.
    • (2008) J. Gastrointest. Cancer , vol.39 , pp. 149-158
    • Lai, J.1    Sandhu, D.S.2    Shire, A.M.3    Roberts, L.R.4
  • 59
    • 55349119506 scopus 로고    scopus 로고
    • Extracellular sulfatases, elements of the Wnt signaling pathway, positively regulate growth and tumorigenicity of human pancreatic cancer cells
    • Nawroth, R., van Zante, A., Cervantes, S., McManus, M., Hebrok, M., and Rosen, S. D. (2007) Extracellular sulfatases, elements of the Wnt signaling pathway, positively regulate growth and tumorigenicity of human pancreatic cancer cells, PLoS One 2, e392.
    • (2007) PLoS One , vol.2
    • Nawroth, R.1    van Zante, A.2    Cervantes, S.3    McManus, M.4    Hebrok, M.5    Rosen, S.D.6
  • 62
    • 59449085594 scopus 로고    scopus 로고
    • Evidence that molecular changes in cells occur before morphological alterations during the progression of breast ductal carcinoma
    • Castro, N., Osorio, C., Torres, C., Bastos, E., Mourao-Neto, M., Soares, F., Brentani, H., and Carraro, D. (2008) Evidence that molecular changes in cells occur before morphological alterations during the progression of breast ductal carcinoma, Breast Cancer Res. 10, R87.
    • (2008) Breast Cancer Res , vol.10
    • Castro, N.1    Osorio, C.2    Torres, C.3    Bastos, E.4    Mourao-Neto, M.5    Soares, F.6    Brentani, H.7    Carraro, D.8
  • 63
    • 33746895756 scopus 로고    scopus 로고
    • Periostin promotes invasion and anchorage-independent growth in the metastatic process of head and neck cancer
    • Kudo, Y., Ogawa, I., Kitajima, S., Kitagawa, M., Kawai, H., Gaffney, P. M., Miyauchi, M., and Takata, T. (2006) Periostin promotes invasion and anchorage-independent growth in the metastatic process of head and neck cancer, Cancer Res. 66, 6928-6935.
    • (2006) Cancer Res , vol.66 , pp. 6928-6935
    • Kudo, Y.1    Ogawa, I.2    Kitajima, S.3    Kitagawa, M.4    Kawai, H.5    Gaffney, P.M.6    Miyauchi, M.7    Takata, T.8
  • 65
    • 33644657201 scopus 로고    scopus 로고
    • HSulf-2, an extracellular endoglucosamine-6-sulfatase, selectively mobilizes heparinbound growth factors and chemokines: Effects on VEGF, FGF-1, and SDF-1
    • Uchimura, K., Morimoto-Tomita, M., Bistrup, A., Li, J., Lyon, M., Gallagher, J., Werb, Z., and Rosen, S. D. (2006) HSulf-2, an extracellular endoglucosamine-6-sulfatase, selectively mobilizes heparinbound growth factors and chemokines: effects on VEGF, FGF-1, and SDF-1, BMC Biochem. 7, 2.
    • (2006) BMC Biochem , vol.7 , pp. 2
    • Uchimura, K.1    Morimoto-Tomita, M.2    Bistrup, A.3    Li, J.4    Lyon, M.5    Gallagher, J.6    Werb, Z.7    Rosen, S.D.8
  • 69
    • 0034904048 scopus 로고    scopus 로고
    • Molecular properties and involvement of heparanase in cancer metastasis and angiogenesis
    • Vlodavsky, I., and Friedmann, Y. (2001) Molecular properties and involvement of heparanase in cancer metastasis and angiogenesis, J. Clin. Invest. 108, 341-347.
    • (2001) J. Clin. Invest , vol.108 , pp. 341-347
    • Vlodavsky, I.1    Friedmann, Y.2
  • 71
    • 34547313009 scopus 로고    scopus 로고
    • Mammalian heparanase: What is the message?
    • Vreys, V., and David, G. (2007) Mammalian heparanase: what is the message? J. Cell. Mol. Med. 11, 427-452.
    • (2007) J. Cell. Mol. Med , vol.11 , pp. 427-452
    • Vreys, V.1    David, G.2
  • 74
    • 0036678137 scopus 로고    scopus 로고
    • Up-regulation of plasma membrane-associated ganglioside sialidase (Neu3) in human colon cancer and its involvement in apoptosis suppression
    • Kakugawa, Y., Wada, T., Yamaguchi, K., Yamanami, H., Ouchi, K., Sato, I., and Miyagi, T. (2002) Up-regulation of plasma membrane-associated ganglioside sialidase (Neu3) in human colon cancer and its involvement in apoptosis suppression, Proc. Nat. Acad. Sci. U.S.A. 99, 10718-10723.
    • (2002) Proc. Nat. Acad. Sci. U.S.A , vol.99 , pp. 10718-10723
    • Kakugawa, Y.1    Wada, T.2    Yamaguchi, K.3    Yamanami, H.4    Ouchi, K.5    Sato, I.6    Miyagi, T.7
  • 75
    • 33646355707 scopus 로고    scopus 로고
    • Plasma membrane-associated sialidase is up-regulated in renal cell carcinoma and promotes interleukin-6-induced apoptosis suppression and cell motility
    • Ueno, S., Saito, S., Wada, T., Yamaguchi, K., Satoh, M., Arai, Y., and Miyagi, T. (2006) Plasma membrane-associated sialidase is up-regulated in renal cell carcinoma and promotes interleukin-6-induced apoptosis suppression and cell motility, J. Biol. Chem. 281, 7756-7764.
    • (2006) J. Biol. Chem , vol.281 , pp. 7756-7764
    • Ueno, S.1    Saito, S.2    Wada, T.3    Yamaguchi, K.4    Satoh, M.5    Arai, Y.6    Miyagi, T.7
  • 76
    • 34147124256 scopus 로고    scopus 로고
    • Expression of NEU3 (plasma membrane-associated sialidase) in clear cell adenocarcinoma of the ovary: Its relationship with T factor of pTNM classification
    • Nomura, H., Tamada, Y., Miyagi, T., Suzuki, A., Taira, M., Suzuki, N., Susumu, N., Irimura, T., and Aoki, D. (2006) Expression of NEU3 (plasma membrane-associated sialidase) in clear cell adenocarcinoma of the ovary: its relationship with T factor of pTNM classification, Oncol. Res. 16, 289-297.
    • (2006) Oncol. Res , vol.16 , pp. 289-297
    • Nomura, H.1    Tamada, Y.2    Miyagi, T.3    Suzuki, A.4    Taira, M.5    Suzuki, N.6    Susumu, N.7    Irimura, T.8    Aoki, D.9
  • 77
    • 57649217883 scopus 로고    scopus 로고
    • Silencing of membrane-associated sialidase Neu3 diminishes apoptosis resistance and triggers megakaryocytic differentiation of chronic myeloid leukemic cells K562 through the increase of ganglioside GM3
    • Tringali, C., Lupo, B., Cirillo, F., Papini, N., Anastasia, L., Lamorte, G., Colombi, P., Bresciani, R., Monti, E., Tettamanti, G., and Venerando, B. (2009) Silencing of membrane-associated sialidase Neu3 diminishes apoptosis resistance and triggers megakaryocytic differentiation of chronic myeloid leukemic cells K562 through the increase of ganglioside GM3, Cell Death Differ. 16, 164-174.
    • (2009) Cell Death Differ , vol.16 , pp. 164-174
    • Tringali, C.1    Lupo, B.2    Cirillo, F.3    Papini, N.4    Anastasia, L.5    Lamorte, G.6    Colombi, P.7    Bresciani, R.8    Monti, E.9    Tettamanti, G.10    Venerando, B.11
  • 78
    • 34447641458 scopus 로고    scopus 로고
    • Epidermal growth factor receptor tyrosine kinase is modulated by GM3 interaction with N-linked GlcNAc termini of the receptor
    • Yoon, S. J., Nakayama, K., Hikita, T., Handa, K., and Hakomori, S. I. (2006) Epidermal growth factor receptor tyrosine kinase is modulated by GM3 interaction with N-linked GlcNAc termini of the receptor, Proc. Natl. Acad. Sci. U.S.A. 103, 18987-18991.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 18987-18991
    • Yoon, S.J.1    Nakayama, K.2    Hikita, T.3    Handa, K.4    Hakomori, S.I.5
  • 80
    • 33645010460 scopus 로고    scopus 로고
    • Plasma-membrane-associated sialidase (NEU3) differentially regulates integrin-mediated cell proliferation through laminin- and fibronectinderived signalling
    • Kato, K., Shiga, K., Yamaguchi, K., Hata, K., Kobayashi, T., Miyazaki, K., Saijo, S., and Miyagi, T. (2006) Plasma-membrane-associated sialidase (NEU3) differentially regulates integrin-mediated cell proliferation through laminin- and fibronectinderived signalling, Biochem. J. 394, 647-656.
    • (2006) Biochem. J , vol.394 , pp. 647-656
    • Kato, K.1    Shiga, K.2    Yamaguchi, K.3    Hata, K.4    Kobayashi, T.5    Miyazaki, K.6    Saijo, S.7    Miyagi, T.8
  • 81
    • 18144421905 scopus 로고    scopus 로고
    • Effect of ganglioside and tetraspanins in microdomains on interaction of integrins with fibroblast growth factor receptor
    • Toledo, M. S., Suzuki, E., Handa, K., and Hakomori, S. (2005) Effect of ganglioside and tetraspanins in microdomains on interaction of integrins with fibroblast growth factor receptor, J. Biol. Chem. 280, 16227-16234.
    • (2005) J. Biol. Chem , vol.280 , pp. 16227-16234
    • Toledo, M.S.1    Suzuki, E.2    Handa, K.3    Hakomori, S.4
  • 82
    • 4644245297 scopus 로고    scopus 로고
    • Cholesterol alters the interaction of glycosphingolipid GM3 with alpha5beta1 integrin and increases integrin-mediated cell adhesion to fibronectin
    • Gopalakrishna, P., Rangaraj, N., and Pande, G. (2004) Cholesterol alters the interaction of glycosphingolipid GM3 with alpha5beta1 integrin and increases integrin-mediated cell adhesion to fibronectin, Exp. Cell Res. 300, 43-53.
    • (2004) Exp. Cell Res , vol.300 , pp. 43-53
    • Gopalakrishna, P.1    Rangaraj, N.2    Pande, G.3
  • 83
    • 33645640140 scopus 로고    scopus 로고
    • Lysosomal sialidase (neuraminidase-1) is targeted to the cell surface in a multiprotein complex that facilitates elastic fiber assembly
    • Hinek, A., Pshezhetsky, A. V., von Itzstein, M., and Starcher, B. (2006) Lysosomal sialidase (neuraminidase-1) is targeted to the cell surface in a multiprotein complex that facilitates elastic fiber assembly, J. Biol. Chem. 281, 3698-3710.
    • (2006) J. Biol. Chem , vol.281 , pp. 3698-3710
    • Hinek, A.1    Pshezhetsky, A.V.2    von Itzstein, M.3    Starcher, B.4
  • 84
    • 56249093847 scopus 로고    scopus 로고
    • CD15 expression in human myeloid cell differentiation is regulated by sialidase activity
    • Gadhoum, S. Z., and Sackstein, R. (2008) CD15 expression in human myeloid cell differentiation is regulated by sialidase activity, Nat. Chem. Biol. 4, 751-757.
    • (2008) Nat. Chem. Biol , vol.4 , pp. 751-757
    • Gadhoum, S.Z.1    Sackstein, R.2
  • 85
    • 62049084618 scopus 로고    scopus 로고
    • Contribution of sialidase NEU1 to suppression of metastasis of human colon cancer cells through desialylation of integrin beta 4
    • Uemura, T., Shiozaki, K., Yamaguchi, K., Miyazaki, S., Satomi, S., Kato, K., Sakuraba, H., and Miyagi, T. (2009) Contribution of sialidase NEU1 to suppression of metastasis of human colon cancer cells through desialylation of integrin beta 4, Oncogene 28, 1218-1229.
    • (2009) Oncogene , vol.28 , pp. 1218-1229
    • Uemura, T.1    Shiozaki, K.2    Yamaguchi, K.3    Miyazaki, S.4    Satomi, S.5    Kato, K.6    Sakuraba, H.7    Miyagi, T.8
  • 89
    • 18244389671 scopus 로고    scopus 로고
    • Neutrophils mediate immune modulation of dendritic cells through glycosylation-dependent interactions between Mac-1 and DC-SIGN
    • van Gisbergen, K. P. J. M., Sanchez-Hernandez, M., Geijtenbeek, T. B. H., and van Kooyk, Y. (2005) Neutrophils mediate immune modulation of dendritic cells through glycosylation-dependent interactions between Mac-1 and DC-SIGN, J. Exp. Med. 201, 1281-1292.
    • (2005) J. Exp. Med , vol.201 , pp. 1281-1292
    • van Gisbergen, K.P.J.M.1    Sanchez-Hernandez, M.2    Geijtenbeek, T.B.H.3    van Kooyk, Y.4
  • 90
    • 66949130737 scopus 로고    scopus 로고
    • Developmental acquisition of the Lyn-CD22-SHP-1 inhibitory pathway promotes B cell tolerance
    • Gross, A. J., Lyandres, J. R., Panigrahi, A. K., Prak, E. T. L., and De-Franco, A. L. (2009) Developmental acquisition of the Lyn-CD22-SHP-1 inhibitory pathway promotes B cell tolerance, J. Immunol. 182, 5382-5392.
    • (2009) J. Immunol , vol.182 , pp. 5382-5392
    • Gross, A.J.1    Lyandres, J.R.2    Panigrahi, A.K.3    Prak, E.T.L.4    De-Franco, A.L.5
  • 92
    • 70349559578 scopus 로고    scopus 로고
    • Esterases and autoimmunity: The sialic acid acetylesterase pathway and the regulation of peripheral B cell tolerance
    • Pillai, S., Cariappa, A., and Pirnie, S. P. (2009) Esterases and autoimmunity: the sialic acid acetylesterase pathway and the regulation of peripheral B cell tolerance, Trends Immunol. 30, 488-493.
    • (2009) Trends Immunol , vol.30 , pp. 488-493
    • Pillai, S.1    Cariappa, A.2    Pirnie, S.P.3
  • 95
    • 70349659193 scopus 로고    scopus 로고
    • Klotho gene delivery prevents the progression of spontaneous hypertension and renal damage
    • Wang, Y., and Sun, Z. (2009) Klotho gene delivery prevents the progression of spontaneous hypertension and renal damage, Hypertension 54, 810-817.
    • (2009) Hypertension , vol.54 , pp. 810-817
    • Wang, Y.1    Sun, Z.2
  • 96
    • 0035503727 scopus 로고    scopus 로고
    • Plasma membrane ganglioside sialidase regulates axonal growth and regeneration in hippocampal neurons in culture
    • Rodriguez, J. A., Piddini, E., Hasegawa, T., Miyagi, T., and Dotti, C. G. (2001) Plasma membrane ganglioside sialidase regulates axonal growth and regeneration in hippocampal neurons in culture, J. Neurosci. 21, 8387-8395.
    • (2001) J. Neurosci , vol.21 , pp. 8387-8395
    • Rodriguez, J.A.1    Piddini, E.2    Hasegawa, T.3    Miyagi, T.4    Dotti, C.G.5
  • 97
    • 0030929378 scopus 로고    scopus 로고
    • Ganglioside GM1 enhances induction by nerve growth factor of a putative dimer of TrkA
    • Farooqui, T., Franklin, T., Pearl, D. K., and Yates, A. (1997) Ganglioside GM1 enhances induction by nerve growth factor of a putative dimer of TrkA, J. Neurochem. 68, 2348-2355.
    • (1997) J. Neurochem , vol.68 , pp. 2348-2355
    • Farooqui, T.1    Franklin, T.2    Pearl, D.K.3    Yates, A.4
  • 98
    • 33846238468 scopus 로고    scopus 로고
    • Induction of axonal differentiation by silencing plasma membrane-associated sialidase Neu3 in neuroblastoma cells
    • Valaperta, R., Valsecchi, M., Rocchetta, F., Aureli, M., Prioni, S., Prinetti, A., Chigorno, V., and Sonnino, S. (2007) Induction of axonal differentiation by silencing plasma membrane-associated sialidase Neu3 in neuroblastoma cells, J. Neurochem. 100, 708-719.
    • (2007) J. Neurochem , vol.100 , pp. 708-719
    • Valaperta, R.1    Valsecchi, M.2    Rocchetta, F.3    Aureli, M.4    Prioni, S.5    Prinetti, A.6    Chigorno, V.7    Sonnino, S.8
  • 99
    • 0036695474 scopus 로고    scopus 로고
    • Modulation of neuritogenesis by ganglioside-specific sialidase (Neu 3) in human neuroblastoma NB-1 cells
    • Proshin, S., Yamaguchi, K., Wada, T., and Miyagi, T. (2002) Modulation of neuritogenesis by ganglioside-specific sialidase (Neu 3) in human neuroblastoma NB-1 cells, Neurochem. Res. 27, 841-846.
    • (2002) Neurochem. Res , vol.27 , pp. 841-846
    • Proshin, S.1    Yamaguchi, K.2    Wada, T.3    Miyagi, T.4
  • 100
    • 0034826059 scopus 로고    scopus 로고
    • Differential functional relevance of a plasma membrane ganglioside sialidase in cholinergic and adrenergic neuroblastoma cell lines
    • von Reitzenstein, C., Kopitz, J., Schuhmann, V., and Cantz, M. (2001) Differential functional relevance of a plasma membrane ganglioside sialidase in cholinergic and adrenergic neuroblastoma cell lines, Eur. J. Biochem. 268, 326-333.
    • (2001) Eur. J. Biochem , vol.268 , pp. 326-333
    • von Reitzenstein, C.1    Kopitz, J.2    Schuhmann, V.3    Cantz, M.4
  • 101
    • 0034805645 scopus 로고    scopus 로고
    • The plasma membrane ganglioside sialidase cofractionates with markers of lipid rafts
    • Kalka, D., von Reitzenstein, C., Kopitz, J., and Cantz, M. (2001) The plasma membrane ganglioside sialidase cofractionates with markers of lipid rafts, Biochem. Biophys. Res. Commun. 283, 989-993.
    • (2001) Biochem. Biophys. Res. Commun , vol.283 , pp. 989-993
    • Kalka, D.1    von Reitzenstein, C.2    Kopitz, J.3    Cantz, M.4
  • 104
    • 0031964547 scopus 로고    scopus 로고
    • Cell surface glycoproteins undergo post-biosynthetic modification of their N-glycans by stepwise demannosylation
    • Porwoll, S., Loch, N., Kannicht, C., Nuck, R., Grunow, D., Reutter, W., and Tauber, R. (1998) Cell surface glycoproteins undergo post-biosynthetic modification of their N-glycans by stepwise demannosylation, J. Biol. Chem. 273, 1075-1085.
    • (1998) J. Biol. Chem , vol.273 , pp. 1075-1085
    • Porwoll, S.1    Loch, N.2    Kannicht, C.3    Nuck, R.4    Grunow, D.5    Reutter, W.6    Tauber, R.7
  • 105
    • 0032959798 scopus 로고    scopus 로고
    • Characterization of a soluble class I alpha-mannosidase in human serum
    • Porwoll, S., Fuchs, H., and Tauber, R. (1999) Characterization of a soluble class I alpha-mannosidase in human serum, FEBS Lett. 449, 175-178.
    • (1999) FEBS Lett , vol.449 , pp. 175-178
    • Porwoll, S.1    Fuchs, H.2    Tauber, R.3
  • 106
    • 0037369738 scopus 로고    scopus 로고
    • Purification and characterization of plasma membrane-associated human sperm alpha-L-fucosidase
    • Khunsook, S., Bean, B. S., McGowan, S. R., and Alhadeff, J. A. (2003) Purification and characterization of plasma membrane-associated human sperm alpha-L-fucosidase, Biol. Reprod. 68, 709-716.
    • (2003) Biol. Reprod , vol.68 , pp. 709-716
    • Khunsook, S.1    Bean, B.S.2    McGowan, S.R.3    Alhadeff, J.A.4
  • 107
    • 0036008784 scopus 로고    scopus 로고
    • Purification and characterization of human seminal plasma α-L-fucosidase
    • Khunsook, S., Alhadeff, J. A., and Bean, B. S. (2002) Purification and characterization of human seminal plasma α-L-fucosidase, Mol. Hum. Reprod. 8, 221-227.
    • (2002) Mol. Hum. Reprod , vol.8 , pp. 221-227
    • Khunsook, S.1    Alhadeff, J.A.2    Bean, B.S.3
  • 108
    • 33745435911 scopus 로고    scopus 로고
    • Purification and characterization of alpha-L-fucosidase from human primary hepatocarcinoma tissue
    • Li, C., Qian, J., and Lin, J. S. (2006) Purification and characterization of alpha-L-fucosidase from human primary hepatocarcinoma tissue, World J. Gastroenterol. 12, 3770-3775.
    • (2006) World J. Gastroenterol , vol.12 , pp. 3770-3775
    • Li, C.1    Qian, J.2    Lin, J.S.3
  • 111
    • 0029837484 scopus 로고    scopus 로고
    • Getting the glycosylation right: Implications for the biotechnology industry
    • Jenkins, N., Parekh, R. B., and James, D. C. (1996) Getting the glycosylation right: Implications for the biotechnology industry, Nat. Biotechnol. 14, 975-981.
    • (1996) Nat. Biotechnol , vol.14 , pp. 975-981
    • Jenkins, N.1    Parekh, R.B.2    James, D.C.3
  • 112
    • 0033938852 scopus 로고    scopus 로고
    • Detecting and minimizing glycosidase activities that can hydrolyze sugars from cell culture-produced glycoproteins
    • Gramer, M. J. (2000) Detecting and minimizing glycosidase activities that can hydrolyze sugars from cell culture-produced glycoproteins, Mol. Biotechnol. 15, 69-75.
    • (2000) Mol. Biotechnol , vol.15 , pp. 69-75
    • Gramer, M.J.1
  • 113
    • 34948865783 scopus 로고    scopus 로고
    • Sialic acid utilization by bacterial pathogens
    • Severi, E., Hood, D. W., and Thomas, G. H. (2007) Sialic acid utilization by bacterial pathogens, Microbiology 153, 2817-2822.
    • (2007) Microbiology , vol.153 , pp. 2817-2822
    • Severi, E.1    Hood, D.W.2    Thomas, G.H.3
  • 114
    • 21044451636 scopus 로고    scopus 로고
    • Novel bifidobacterial glycosidases acting on sugar chains of mucin glycoproteins
    • Katayama, T., Fujita, K., and Yamamoto, K. (2005) Novel bifidobacterial glycosidases acting on sugar chains of mucin glycoproteins, J. Biosci. Bioeng. 99, 457-465.
    • (2005) J. Biosci. Bioeng , vol.99 , pp. 457-465
    • Katayama, T.1    Fujita, K.2    Yamamoto, K.3


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