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Volumn 39, Issue 9, 2007, Pages 1625-1636

Requirement of N-glycosylation for the secretion of recombinant extracellular domain of human Fas in HeLa cells

Author keywords

Apoptosis; Fas; Glycoprotein; Glycosylation; Glycosyltransferases; HeLa cells

Indexed keywords

CELL SURFACE RECEPTOR; FAS ANTIBODY; FAS ANTIGEN; GLYCOPROTEIN; GLYCOSYLTRANSFERASE; HYBRID PROTEIN; RECOMBINANT PROTEIN; TUNICAMYCIN;

EID: 34547098850     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2007.04.002     Document Type: Article
Times cited : (25)

References (48)
  • 1
    • 0034843704 scopus 로고    scopus 로고
    • Neutralization of pH in the Golgi apparatus causes redistribution of glycosyltransferases and changes in the O-glycosylation of mucins
    • Axelsson M.A., Karlsson N.G., Steel D.M., Ouwendijk J., Nilsson T., and Hansson G.C. Neutralization of pH in the Golgi apparatus causes redistribution of glycosyltransferases and changes in the O-glycosylation of mucins. Glycobiology 11 (2001) 633-644
    • (2001) Glycobiology , vol.11 , pp. 633-644
    • Axelsson, M.A.1    Karlsson, N.G.2    Steel, D.M.3    Ouwendijk, J.4    Nilsson, T.5    Hansson, G.C.6
  • 2
    • 0032764980 scopus 로고    scopus 로고
    • Analysis of Fas-ligand interactions using a molecular model of the receptor-ligand interface
    • Bajorath J. Analysis of Fas-ligand interactions using a molecular model of the receptor-ligand interface. Computer Aided Molecular Design 13 (1999) 409-418
    • (1999) Computer Aided Molecular Design , vol.13 , pp. 409-418
    • Bajorath, J.1
  • 3
    • 0027301549 scopus 로고
    • Double immunofluorescent staining of alpha-2,6-sialyltransferase and beta-1,4-galactosyltransferase in monensin-treated cells: Evidence for different Golgi compartments?
    • Berger E.G., Grimm K., Bachi T., Bosshart H., Kleene R., and Muller U. Double immunofluorescent staining of alpha-2,6-sialyltransferase and beta-1,4-galactosyltransferase in monensin-treated cells: Evidence for different Golgi compartments?. Journal of Cellular Biochemistry 52 (1993) 275-288
    • (1993) Journal of Cellular Biochemistry , vol.52 , pp. 275-288
    • Berger, E.G.1    Grimm, K.2    Bachi, T.3    Bosshart, H.4    Kleene, R.5    Muller, U.6
  • 4
    • 0023518707 scopus 로고
    • Galactosyltransferase and sialyltransferase are located in different subcellular compartments in HeLa cells
    • Berger E.G., Thurnher M., and Muller U. Galactosyltransferase and sialyltransferase are located in different subcellular compartments in HeLa cells. Experimental Cell Research 173 (1987) 267-273
    • (1987) Experimental Cell Research , vol.173 , pp. 267-273
    • Berger, E.G.1    Thurnher, M.2    Muller, U.3
  • 6
    • 0032760680 scopus 로고    scopus 로고
    • Pathways of O-glycan biosynthesis in cancer cells
    • Brockhausen I. Pathways of O-glycan biosynthesis in cancer cells. Biochimica et Biophysica Acta 1473 (1999) 67-95
    • (1999) Biochimica et Biophysica Acta , vol.1473 , pp. 67-95
    • Brockhausen, I.1
  • 7
    • 33750530797 scopus 로고    scopus 로고
    • The role of galactosyltransferases in cell surface functions and in the immune system
    • Brockhausen I. The role of galactosyltransferases in cell surface functions and in the immune system. Drug News and Perspectives 19 (2006) 401-409
    • (2006) Drug News and Perspectives , vol.19 , pp. 401-409
    • Brockhausen, I.1
  • 8
    • 0036122866 scopus 로고    scopus 로고
    • Glycoprotein biosynthesis in porcine aortic endothelial cells and changes in the apoptotic cell population
    • Brockhausen I., Lehotay M., Yang J.M., Qin W., Young D., Lucien J., et al. Glycoprotein biosynthesis in porcine aortic endothelial cells and changes in the apoptotic cell population. Glycobiology 12 (2002) 33-45
    • (2002) Glycobiology , vol.12 , pp. 33-45
    • Brockhausen, I.1    Lehotay, M.2    Yang, J.M.3    Qin, W.4    Young, D.5    Lucien, J.6
  • 9
    • 0031723937 scopus 로고    scopus 로고
    • Glycoproteins and their relationship to human disease
    • Brockhausen I., Schutzbach J.S., and Kuhns W. Glycoproteins and their relationship to human disease. Acta Anatomica 161 (1998) 36-78
    • (1998) Acta Anatomica , vol.161 , pp. 36-78
    • Brockhausen, I.1    Schutzbach, J.S.2    Kuhns, W.3
  • 10
    • 0035083062 scopus 로고    scopus 로고
    • Pathways of mucin O-glycosylation in normal and malignant rat colonic epithelial cells reveal a mechanism for cancer-associated Sialyl-Tn antigen expression
    • Brockhausen I., Yang J., Lehotay M., Ogata S., and Itzkowitz S. Pathways of mucin O-glycosylation in normal and malignant rat colonic epithelial cells reveal a mechanism for cancer-associated Sialyl-Tn antigen expression. Biological Chemistry 382 (2001) 219-232
    • (2001) Biological Chemistry , vol.382 , pp. 219-232
    • Brockhausen, I.1    Yang, J.2    Lehotay, M.3    Ogata, S.4    Itzkowitz, S.5
  • 12
    • 0024245391 scopus 로고
    • Isolation and characterization of human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2. Major sialoglycoproteins carrying polylactosaminoglycan
    • Carlsson S.R., Roth J., Piller F., and Fukuda M. Isolation and characterization of human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2. Major sialoglycoproteins carrying polylactosaminoglycan. Journal of Biological Chemistry 263 (1988) 18911-18919
    • (1988) Journal of Biological Chemistry , vol.263 , pp. 18911-18919
    • Carlsson, S.R.1    Roth, J.2    Piller, F.3    Fukuda, M.4
  • 13
    • 0029935762 scopus 로고    scopus 로고
    • Specific toxicity of tunicamycin in induction of programmed cell death of sympathetic neurons
    • Chang J.Y., and Korolev V.V. Specific toxicity of tunicamycin in induction of programmed cell death of sympathetic neurons. Experimental Neurology 137 (1996) 201-211
    • (1996) Experimental Neurology , vol.137 , pp. 201-211
    • Chang, J.Y.1    Korolev, V.V.2
  • 14
    • 0035815609 scopus 로고    scopus 로고
    • The relative activities of the C2GnT1 and ST3Gal-I glycosyltransferases determine O-glycan structure and expression of a tumor-associated epitope on MUC1
    • Dalziel M., Whitehouse C., McFarlane I., Brockhausen I., Gschmeissner S., Schwientek T., et al. The relative activities of the C2GnT1 and ST3Gal-I glycosyltransferases determine O-glycan structure and expression of a tumor-associated epitope on MUC1. Journal of Biological Chemistry 276 (2001) 11007-11015
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 11007-11015
    • Dalziel, M.1    Whitehouse, C.2    McFarlane, I.3    Brockhausen, I.4    Gschmeissner, S.5    Schwientek, T.6
  • 15
    • 0035211552 scopus 로고    scopus 로고
    • Site-directed mutagenesis of heparin-binding EGF-like growth factor (HB-EGF): Analysis of O-glycosylation sites and properties
    • Davis-Fleische K.M., Brigstock D.R., and Besner G.E. Site-directed mutagenesis of heparin-binding EGF-like growth factor (HB-EGF): Analysis of O-glycosylation sites and properties. Growth Factors 19 (2001) 127-143
    • (2001) Growth Factors , vol.19 , pp. 127-143
    • Davis-Fleische, K.M.1    Brigstock, D.R.2    Besner, G.E.3
  • 16
    • 0028265466 scopus 로고
    • High expression of APO-1 (CD95) on T lymphocytes from human immunodeficiency virus-1-infected children
    • Debatin K.M., Fahrig-Faissner A., Enenkel-Stoodt S., Kreuz W., Benner A., and Krammer P.H. High expression of APO-1 (CD95) on T lymphocytes from human immunodeficiency virus-1-infected children. Blood 83 (1994) 3101-3103
    • (1994) Blood , vol.83 , pp. 3101-3103
    • Debatin, K.M.1    Fahrig-Faissner, A.2    Enenkel-Stoodt, S.3    Kreuz, W.4    Benner, A.5    Krammer, P.H.6
  • 17
    • 0031884694 scopus 로고    scopus 로고
    • A three-dimensional model of the Fas/APO-1 molecule: Cross-reactivity of anti-Fas antibodies explained by structural mimicry of antigenic sites
    • Fadeel B., Lindberg J., Achour A., and Chiodi F. A three-dimensional model of the Fas/APO-1 molecule: Cross-reactivity of anti-Fas antibodies explained by structural mimicry of antigenic sites. International Immunology 10 (1998) 131-140
    • (1998) International Immunology , vol.10 , pp. 131-140
    • Fadeel, B.1    Lindberg, J.2    Achour, A.3    Chiodi, F.4
  • 18
    • 0029592026 scopus 로고
    • Mapping the linear site on the Fas/APO-1 molecule targeted by the prototypic anti-Fas mAb
    • Fadeel B., Thorpe J., and Chiodi F. Mapping the linear site on the Fas/APO-1 molecule targeted by the prototypic anti-Fas mAb. International Immunology 7 (1995) 1967-1975
    • (1995) International Immunology , vol.7 , pp. 1967-1975
    • Fadeel, B.1    Thorpe, J.2    Chiodi, F.3
  • 19
    • 0034850491 scopus 로고    scopus 로고
    • Probing the cons and pros of lectin-induced immunomodulation: Case studies for the mistletoe lectin and galectin-1
    • Gabius H.J. Probing the cons and pros of lectin-induced immunomodulation: Case studies for the mistletoe lectin and galectin-1. Biochimie 83 (2001) 659-666
    • (2001) Biochimie , vol.83 , pp. 659-666
    • Gabius, H.J.1
  • 22
    • 0027338125 scopus 로고
    • Le(y) antigen expression is correlated with apoptosis (programmed cell death)
    • Hiraishi K., Suzuki K., Hakomori S., and Adachi M. Le(y) antigen expression is correlated with apoptosis (programmed cell death). Glycobiology 3 (1993) 381-390
    • (1993) Glycobiology , vol.3 , pp. 381-390
    • Hiraishi, K.1    Suzuki, K.2    Hakomori, S.3    Adachi, M.4
  • 23
    • 0033046601 scopus 로고    scopus 로고
    • Differential sialylation of cell surface glycoconjugates in a human B lymphoma cell line regulates susceptibility for CD95 (APO-1/Fas)-mediated apoptosis and for infection by a lymphotropic virus
    • Keppler O.T., Peter M.E., Hinderlich S., Moldenhauer G., Stehling P., Schmitz I., et al. Differential sialylation of cell surface glycoconjugates in a human B lymphoma cell line regulates susceptibility for CD95 (APO-1/Fas)-mediated apoptosis and for infection by a lymphotropic virus. Glycobiology 9 (1999) 557-569
    • (1999) Glycobiology , vol.9 , pp. 557-569
    • Keppler, O.T.1    Peter, M.E.2    Hinderlich, S.3    Moldenhauer, G.4    Stehling, P.5    Schmitz, I.6
  • 24
    • 0026562067 scopus 로고
    • Inhibition of selectin-dependent tumor cell adhesion to endothelial cells and platelets by blocking O-glycosylation of these cells
    • Kojima N., Handa K., Newman W., and Hakomori S. Inhibition of selectin-dependent tumor cell adhesion to endothelial cells and platelets by blocking O-glycosylation of these cells. Biochemical and Biophysical Research Communications 182 (1992) 1288-1295
    • (1992) Biochemical and Biophysical Research Communications , vol.182 , pp. 1288-1295
    • Kojima, N.1    Handa, K.2    Newman, W.3    Hakomori, S.4
  • 25
    • 0034471661 scopus 로고    scopus 로고
    • Tunicamycin inhibits capillary endothelial cell proliferation by inducing apoptosis. Targeting dolichol-pathway for generation of new anti-angiogenic therapeutics
    • Martinez J.A., Torres-Negrom I., Amigo L.A., Roldan R.A., Mendez A., and Banerjee D.K. Tunicamycin inhibits capillary endothelial cell proliferation by inducing apoptosis. Targeting dolichol-pathway for generation of new anti-angiogenic therapeutics. Advances in Experimental Medicine and Biology 476 (2000) 197-208
    • (2000) Advances in Experimental Medicine and Biology , vol.476 , pp. 197-208
    • Martinez, J.A.1    Torres-Negrom, I.2    Amigo, L.A.3    Roldan, R.A.4    Mendez, A.5    Banerjee, D.K.6
  • 26
    • 33750813509 scopus 로고    scopus 로고
    • Secretory expression of synthetic human Fas ligand extracellular domain gene in Pichia pastoris: Influences of tag addition and N-glycosylation site deletion, and development of a purification method
    • Muraki M. Secretory expression of synthetic human Fas ligand extracellular domain gene in Pichia pastoris: Influences of tag addition and N-glycosylation site deletion, and development of a purification method. Protein Expression and Purification 50 (2006) 137-146
    • (2006) Protein Expression and Purification , vol.50 , pp. 137-146
    • Muraki, M.1
  • 27
    • 0028927607 scopus 로고
    • The Fas death factor
    • Nagata S., and Goldstein P. The Fas death factor. Science 267 (1995) 1449-1456
    • (1995) Science , vol.267 , pp. 1449-1456
    • Nagata, S.1    Goldstein, P.2
  • 28
    • 0028980902 scopus 로고
    • Fas and Fas ligand: lpr and gld mutations
    • Nagata S., and Suda T. Fas and Fas ligand: lpr and gld mutations. Immunology Today 16 (1995) 39-43
    • (1995) Immunology Today , vol.16 , pp. 39-43
    • Nagata, S.1    Suda, T.2
  • 29
    • 0030038568 scopus 로고    scopus 로고
    • N-linked oligosaccharides are required for cell surface expression of the norepinephrine transporter but do not influence substrate or inhibitor recognition
    • Nguyen T.T., and Amara S.G. N-linked oligosaccharides are required for cell surface expression of the norepinephrine transporter but do not influence substrate or inhibitor recognition. Journal of Neurochemistry 67 (1996) 645-655
    • (1996) Journal of Neurochemistry , vol.67 , pp. 645-655
    • Nguyen, T.T.1    Amara, S.G.2
  • 32
    • 0026706261 scopus 로고
    • Purification and molecular cloning of the Apo-1 Cell surface antigen, a member of the tumor necrosis factor-nerve growth factor receptor superfamily. Sequence identity with the Fas antigen
    • Oehm A., Behrmann I., Falk W., Pawlita M., Maier G., Klas C., et al. Purification and molecular cloning of the Apo-1 Cell surface antigen, a member of the tumor necrosis factor-nerve growth factor receptor superfamily. Sequence identity with the Fas antigen. Journal of Biological Chemistry 267 (1992) 10709-10715
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 10709-10715
    • Oehm, A.1    Behrmann, I.2    Falk, W.3    Pawlita, M.4    Maier, G.5    Klas, C.6
  • 33
    • 0031452639 scopus 로고    scopus 로고
    • Separate domains of the human fas ligand dictate self-association and receptor binding
    • Orlinick J.R., Elkon K.B., and Chao M.V. Separate domains of the human fas ligand dictate self-association and receptor binding. Journal of Biological Chemistry 272 (1997) 32221-32229
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 32221-32229
    • Orlinick, J.R.1    Elkon, K.B.2    Chao, M.V.3
  • 34
    • 0028989515 scopus 로고
    • Inhibition of N-linked glycosylation induces early apoptosis in human promyelocytic HL-60 cells
    • Perez-Sala D., and Mollinedo F. Inhibition of N-linked glycosylation induces early apoptosis in human promyelocytic HL-60 cells. Journal of Cellular Physiology 163 (1995) 523-531
    • (1995) Journal of Cellular Physiology , vol.163 , pp. 523-531
    • Perez-Sala, D.1    Mollinedo, F.2
  • 35
    • 0031959770 scopus 로고    scopus 로고
    • Galectins: Versatile modulators of cell adhesion, cell proliferation, and cell death
    • Perillo N.L., Marcus M.E., and Baum L.G. Galectins: Versatile modulators of cell adhesion, cell proliferation, and cell death. Journal of Molecular Medicine 76 (1998) 402-412
    • (1998) Journal of Molecular Medicine , vol.76 , pp. 402-412
    • Perillo, N.L.1    Marcus, M.E.2    Baum, L.G.3
  • 37
    • 20444419772 scopus 로고    scopus 로고
    • Galectins as immunoregulators during infectious processes: From microbial invasion to the resolution of the disease
    • Rabinovich G.A., and Gruppi A. Galectins as immunoregulators during infectious processes: From microbial invasion to the resolution of the disease. Parasite Immunology 27 (2005) 103-114
    • (2005) Parasite Immunology , vol.27 , pp. 103-114
    • Rabinovich, G.A.1    Gruppi, A.2
  • 38
    • 0033434103 scopus 로고    scopus 로고
    • Glycosylation alterations of cells in late phase apoptosis from colon carcinomas
    • Rapoport E., and Le Pendu J. Glycosylation alterations of cells in late phase apoptosis from colon carcinomas. Glycobiology 9 (1999) 1337-1345
    • (1999) Glycobiology , vol.9 , pp. 1337-1345
    • Rapoport, E.1    Le Pendu, J.2
  • 39
    • 0039992226 scopus 로고    scopus 로고
    • Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus
    • Röttger S., White J., Wandall H.H., Olivo J.C., Stark A., Bennett E.P., et al. Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus. Journal of Cell Science 111 (1998) 45-60
    • (1998) Journal of Cell Science , vol.111 , pp. 45-60
    • Röttger, S.1    White, J.2    Wandall, H.H.3    Olivo, J.C.4    Stark, A.5    Bennett, E.P.6
  • 43
    • 0032539963 scopus 로고    scopus 로고
    • Analysis of the ligand binding site in Fas (CD95) by site-directed mutagenesis and comparison with TNFR and CD40
    • Starling G.C., Kiener P.A., Aruffo A., and Bajorath J. Analysis of the ligand binding site in Fas (CD95) by site-directed mutagenesis and comparison with TNFR and CD40. Biochemistry 37 (1998) 3723-3726
    • (1998) Biochemistry , vol.37 , pp. 3723-3726
    • Starling, G.C.1    Kiener, P.A.2    Aruffo, A.3    Bajorath, J.4
  • 44
    • 9644268191 scopus 로고    scopus 로고
    • An inhibitor of O-glycosylation induces apoptosis in NIH3T3 cells and developing mouse embryonic mandibular tissues
    • Tian E., Hagen K.G., Shum L., Hang H.C., Imbert Y., Young Jr. W.W., et al. An inhibitor of O-glycosylation induces apoptosis in NIH3T3 cells and developing mouse embryonic mandibular tissues. Journal of Biological Chemistry 279 (2004) 50382-50390
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 50382-50390
    • Tian, E.1    Hagen, K.G.2    Shum, L.3    Hang, H.C.4    Imbert, Y.5    Young Jr., W.W.6
  • 46
    • 33846318191 scopus 로고    scopus 로고
    • The action of TNFalpha and TGFbeta include specific alterations of the glycosylation of bovine and human chondrocytes
    • Yang X., Yip J., Anastassiades T., Harrison M., and Brockhausen I. The action of TNFalpha and TGFbeta include specific alterations of the glycosylation of bovine and human chondrocytes. Biochimica et Biophysica Acta 1773 (2007) 264-272
    • (2007) Biochimica et Biophysica Acta , vol.1773 , pp. 264-272
    • Yang, X.1    Yip, J.2    Anastassiades, T.3    Harrison, M.4    Brockhausen, I.5


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