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Volumn 48, Issue 2, 2010, Pages 253-259

Binding activity of recombinant human L-selectin-Fcγ is modified by sialylation

Author keywords

L selectin; Neuraminidase; Recombinant protein production; Sialic acid; Sialylation; Surface plasmon resonance

Indexed keywords

L-SELECTIN; NEURAMINIDASE; RECOMBINANT PROTEIN PRODUCTIONS; SIALIC ACIDS; SIALYLATION;

EID: 72149105585     PISSN: 1369703X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bej.2009.10.022     Document Type: Article
Times cited : (3)

References (37)
  • 1
    • 0027982876 scopus 로고
    • Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm
    • Springer T.A. Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm. Cell 76 (1994) 301-314
    • (1994) Cell , vol.76 , pp. 301-314
    • Springer, T.A.1
  • 2
    • 0026342111 scopus 로고
    • Leukocyte-endothelial cell recognition-three (or more) steps to specificity and diversity
    • Butcher E.C. Leukocyte-endothelial cell recognition-three (or more) steps to specificity and diversity. Cell 67 (1991) 1033-1036
    • (1991) Cell , vol.67 , pp. 1033-1036
    • Butcher, E.C.1
  • 3
    • 1942542931 scopus 로고    scopus 로고
    • Ligands for L-selectin: homing, inflammation, and beyond
    • Rosen S.D. Ligands for L-selectin: homing, inflammation, and beyond. Annu. Rev. Immunol. 22 (2004) 129-156
    • (2004) Annu. Rev. Immunol. , vol.22 , pp. 129-156
    • Rosen, S.D.1
  • 5
    • 0037103146 scopus 로고    scopus 로고
    • L-selectin serves as an E-selectin ligand on cultured human T lymphoblasts
    • Jutila M.A., Kurk S., Jackiw L., Knibbs R.N., and Stoolman L.M. L-selectin serves as an E-selectin ligand on cultured human T lymphoblasts. J. Immunol. 169 (2002) 1768-1773
    • (2002) J. Immunol. , vol.169 , pp. 1768-1773
    • Jutila, M.A.1    Kurk, S.2    Jackiw, L.3    Knibbs, R.N.4    Stoolman, L.M.5
  • 6
    • 0029001510 scopus 로고
    • Selectin-carbohydrate interactions and the initiation of the inflammatory response
    • Lasky L.A. Selectin-carbohydrate interactions and the initiation of the inflammatory response. Annu. Rev. Biochem. 64 (1995) 113-139
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 113-139
    • Lasky, L.A.1
  • 7
    • 0034721650 scopus 로고    scopus 로고
    • Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of P- and E-selectin bound to SLe(x) and PSGL-1
    • Somers W.S., Tang J., Shaw G.D., and Camphausen R.T. Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of P- and E-selectin bound to SLe(x) and PSGL-1. Cell 103 (2000) 467-479
    • (2000) Cell , vol.103 , pp. 467-479
    • Somers, W.S.1    Tang, J.2    Shaw, G.D.3    Camphausen, R.T.4
  • 8
    • 0037698348 scopus 로고    scopus 로고
    • Model glycosulfopeptides from P-selectin glycoprotein ligand-1 require tyrosine sulfation and a core 2-branched O-glycan to bind to L-selectin
    • Leppänen A., Yago T., Otto V.I., McEver R.P., and Cummings R.D. Model glycosulfopeptides from P-selectin glycoprotein ligand-1 require tyrosine sulfation and a core 2-branched O-glycan to bind to L-selectin. J. Biol. Chem. 278 (2003) 26391-26400
    • (2003) J. Biol. Chem. , vol.278 , pp. 26391-26400
    • Leppänen, A.1    Yago, T.2    Otto, V.I.3    McEver, R.P.4    Cummings, R.D.5
  • 9
    • 13544251395 scopus 로고    scopus 로고
    • Highly glycosylated human salivary molecules present oligosaccharides that mediate adhesion of leukocytes and Heliobacter pylori
    • Prakobphol A., Borén T., Max W., Zhixiang P., and Fisher S.J. Highly glycosylated human salivary molecules present oligosaccharides that mediate adhesion of leukocytes and Heliobacter pylori. Biochemistry 144 (2005) 2216-2224
    • (2005) Biochemistry , vol.144 , pp. 2216-2224
    • Prakobphol, A.1    Borén, T.2    Max, W.3    Zhixiang, P.4    Fisher, S.J.5
  • 10
    • 0041846397 scopus 로고    scopus 로고
    • Endoglycan, a member of the CD34 family, functions as an L-selectin ligand through modification with tyrosine sulfation and sialyl Lewis x
    • Fieger C.B., Sassetti C.M., and Rosen S.D. Endoglycan, a member of the CD34 family, functions as an L-selectin ligand through modification with tyrosine sulfation and sialyl Lewis x. J. Biol. Chem. 278 (2003) 27390-27398
    • (2003) J. Biol. Chem. , vol.278 , pp. 27390-27398
    • Fieger, C.B.1    Sassetti, C.M.2    Rosen, S.D.3
  • 11
    • 33645741356 scopus 로고    scopus 로고
    • Identification of cutaneous lymphocyte-associated antigen as sialyl 6-sulfo Lewis X, a selectin ligand expressed on a subset of skin-homing helper memory T cells
    • Ohmori K., Fukui F., Kiso M., Imai T., Yoshie O., Hasegawa H., Matsushima K., and Kannagi R. Identification of cutaneous lymphocyte-associated antigen as sialyl 6-sulfo Lewis X, a selectin ligand expressed on a subset of skin-homing helper memory T cells. Blood 107 (2006) 3197-3204
    • (2006) Blood , vol.107 , pp. 3197-3204
    • Ohmori, K.1    Fukui, F.2    Kiso, M.3    Imai, T.4    Yoshie, O.5    Hasegawa, H.6    Matsushima, K.7    Kannagi, R.8
  • 12
    • 0030995665 scopus 로고    scopus 로고
    • Valency dependent patterns of binding of human L-selectin toward sialyl and sulfated oligosaccharides of Le(a) and Le(x) types: relevance to anti-adhesion therapeutics
    • Galustian C., Childs R.A., Yuen C.T., Hasegawa A., Kiso M., Lubineau A., Shaw G., and Feizi T. Valency dependent patterns of binding of human L-selectin toward sialyl and sulfated oligosaccharides of Le(a) and Le(x) types: relevance to anti-adhesion therapeutics. Biochemistry 36 (1997) 5260-5266
    • (1997) Biochemistry , vol.36 , pp. 5260-5266
    • Galustian, C.1    Childs, R.A.2    Yuen, C.T.3    Hasegawa, A.4    Kiso, M.5    Lubineau, A.6    Shaw, G.7    Feizi, T.8
  • 14
    • 34548570914 scopus 로고    scopus 로고
    • Inhibition of L-selectin binding by polyacrylamide-based conjugates under defined flow conditions
    • Enders S., Bernhard G., Zakrzewicz A., and Tauber R. Inhibition of L-selectin binding by polyacrylamide-based conjugates under defined flow conditions. Biochim Biophys. Acta 1770 (2007) 1441-1449
    • (2007) Biochim Biophys. Acta , vol.1770 , pp. 1441-1449
    • Enders, S.1    Bernhard, G.2    Zakrzewicz, A.3    Tauber, R.4
  • 15
    • 56349085126 scopus 로고    scopus 로고
    • Modular synthesis of multivalent glycoarchitecturs and their unique selectin binding behaviour
    • Papp I., Dernedde J., Enders S., and Haag R. Modular synthesis of multivalent glycoarchitecturs and their unique selectin binding behaviour. Chem. Commun. (Camb.) 44 (2008) 5851-5853
    • (2008) Chem. Commun. (Camb.) , Issue.44 , pp. 5851-5853
    • Papp, I.1    Dernedde, J.2    Enders, S.3    Haag, R.4
  • 17
    • 0032968007 scopus 로고    scopus 로고
    • H (0) blood group determinant is present in soluble L-selectin expressed in BHK-cells
    • Gohlke M., Mach U., Nuck R., Volz B., Fieger C., Tauber R., and Reutter W. H (0) blood group determinant is present in soluble L-selectin expressed in BHK-cells. FEBS Lett. 450 (1999) 111-116
    • (1999) FEBS Lett. , vol.450 , pp. 111-116
    • Gohlke, M.1    Mach, U.2    Nuck, R.3    Volz, B.4    Fieger, C.5    Tauber, R.6    Reutter, W.7
  • 20
    • 0027369489 scopus 로고
    • Enzymatic modelling of the oligosaccharide chains of glycoproteins immobilized onto polystyrene surfaces
    • Orberger G., Gessner R., Fuchs H., Volz B., Köttgen E., and Tauber R. Enzymatic modelling of the oligosaccharide chains of glycoproteins immobilized onto polystyrene surfaces. Anal. Biochem. 214 (1993) 195-204
    • (1993) Anal. Biochem. , vol.214 , pp. 195-204
    • Orberger, G.1    Gessner, R.2    Fuchs, H.3    Volz, B.4    Köttgen, E.5    Tauber, R.6
  • 22
    • 0023175723 scopus 로고
    • Fluorometric high-performance liquid chromatography of N-acetyl- and N-glycolylneuraminic acids and its application to their microdetermination in human and animal sera, glycoproteins, and glycolipids
    • Hara S., Takemori Y., Yamaquchi M., Nakamura M., and Ohkura Y. Fluorometric high-performance liquid chromatography of N-acetyl- and N-glycolylneuraminic acids and its application to their microdetermination in human and animal sera, glycoproteins, and glycolipids. Anal. Biochem. 164 (1987) 138-145
    • (1987) Anal. Biochem. , vol.164 , pp. 138-145
    • Hara, S.1    Takemori, Y.2    Yamaquchi, M.3    Nakamura, M.4    Ohkura, Y.5
  • 24
    • 0024391397 scopus 로고
    • Human homologue of mouse lymph node homing receptor: evolutionary conservation at tandem cell interaction domains
    • Siegelman M.H., and Weissman I.L. Human homologue of mouse lymph node homing receptor: evolutionary conservation at tandem cell interaction domains. Proc. Natl. Acad. Sci. U.S.A. 86 (1989) 5562-5566
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 5562-5566
    • Siegelman, M.H.1    Weissman, I.L.2
  • 26
    • 0024321508 scopus 로고
    • Alteration of terminal glycosylation sequences on N-linked oligosaccharides of Chinese hamster ovary cells by expression of beta-galactoside alpha 2,6-sialyltransferase
    • Lee E.U., Roth J., and Paulson J.C. Alteration of terminal glycosylation sequences on N-linked oligosaccharides of Chinese hamster ovary cells by expression of beta-galactoside alpha 2,6-sialyltransferase. J. Biol. Chem. 264 (1989) 13848-13855
    • (1989) J. Biol. Chem. , vol.264 , pp. 13848-13855
    • Lee, E.U.1    Roth, J.2    Paulson, J.C.3
  • 27
    • 0032551285 scopus 로고    scopus 로고
    • Improvement of interferon-gamma sialylation in Chinese hamster ovary cell culture by feeding of N-acetylmannosamine
    • Gu X., and Wang D.I. Improvement of interferon-gamma sialylation in Chinese hamster ovary cell culture by feeding of N-acetylmannosamine. Biotechnol. Bioeng. 58 (1998) 642-648
    • (1998) Biotechnol. Bioeng. , vol.58 , pp. 642-648
    • Gu, X.1    Wang, D.I.2
  • 29
    • 33746163433 scopus 로고    scopus 로고
    • Remodeling of the lectin-EGF-like domain interface in P- and L-selectin increases adhesiveness and shear resistance under hydrodynamic force
    • Phan U.T., Waldron T.T., and Springer T.A. Remodeling of the lectin-EGF-like domain interface in P- and L-selectin increases adhesiveness and shear resistance under hydrodynamic force. Nat. Immunol. 7 (2006) 883-889
    • (2006) Nat. Immunol. , vol.7 , pp. 883-889
    • Phan, U.T.1    Waldron, T.T.2    Springer, T.A.3
  • 31
    • 0033557570 scopus 로고    scopus 로고
    • Sialylation of the sialic acid binding lectin sialoadhesin regulates its ability to mediate cell adhesion
    • Barnes Y.C., Skelton T.P., Stamenkovic I., and Sgroi D.C. Sialylation of the sialic acid binding lectin sialoadhesin regulates its ability to mediate cell adhesion. Blood 93 (1999) 1245-1252
    • (1999) Blood , vol.93 , pp. 1245-1252
    • Barnes, Y.C.1    Skelton, T.P.2    Stamenkovic, I.3    Sgroi, D.C.4
  • 32
  • 33
    • 0019318664 scopus 로고
    • Sialic acid residues inhibit proteolytic degradation of dopamine beta-hydroxylase
    • Aquino D., Wong R., Margolis R.U., and Margolis R.K. Sialic acid residues inhibit proteolytic degradation of dopamine beta-hydroxylase. FEBS Lett. 112 (1980) 195-198
    • (1980) FEBS Lett. , vol.112 , pp. 195-198
    • Aquino, D.1    Wong, R.2    Margolis, R.U.3    Margolis, R.K.4
  • 35
    • 0038458983 scopus 로고    scopus 로고
    • Effect of culture conditions on the degree of sialylation of a recombinant glycoprotein expressed in insect cells
    • Joosten C.E., and Shuler M.L. Effect of culture conditions on the degree of sialylation of a recombinant glycoprotein expressed in insect cells. Biotechnol. Prog. 19 (2003) 739-749
    • (2003) Biotechnol. Prog. , vol.19 , pp. 739-749
    • Joosten, C.E.1    Shuler, M.L.2
  • 36
    • 0347362787 scopus 로고    scopus 로고
    • Lec3 Chinese hamster ovary mutants lack UDP-acetylglucosamine 2-epimerase activity because of mutations in the epimerase domain of the Gne gene
    • Hong Y., and Stanley P. Lec3 Chinese hamster ovary mutants lack UDP-acetylglucosamine 2-epimerase activity because of mutations in the epimerase domain of the Gne gene. J. Biol. Chem. 278 (2003) 53045-53054
    • (2003) J. Biol. Chem. , vol.278 , pp. 53045-53054
    • Hong, Y.1    Stanley, P.2
  • 37
    • 0042160074 scopus 로고    scopus 로고
    • Epigenetically mediated loss of UDP-GlcNAc 2-epimerase/ManNAc kinase expression in hyposialylated cell lines
    • Oetke C., Hinderlich S., Reutter W., and Pawlita M. Epigenetically mediated loss of UDP-GlcNAc 2-epimerase/ManNAc kinase expression in hyposialylated cell lines. Biochem. Biophys. Res. Commun. 308 (2003) 892-898
    • (2003) Biochem. Biophys. Res. Commun. , vol.308 , pp. 892-898
    • Oetke, C.1    Hinderlich, S.2    Reutter, W.3    Pawlita, M.4


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