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Volumn 11, Issue 14, 2011, Pages 2812-2829

MS-based glycomic strategies for probing the structural details of polylactosaminoglycan chain on N-glycans and glycoproteomic identification of its protein carriers

Author keywords

Glycomics; Glycoproteomics; MS; Polylactosaminoglycans; Tomato lectin

Indexed keywords

ENDO BETA GALACTOSIDASE; GLYCOPROTEIN; GLYCOSIDASE; LECTIN; POLYLACTOSAMINOGLYCAN; UNCLASSIFIED DRUG;

EID: 79959727334     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201000794     Document Type: Article
Times cited : (6)

References (67)
  • 1
    • 0021265108 scopus 로고
    • Structure of branched lactosaminoglycan, the carbohydrate moiety of band 3 isolated from adult human erythrocytes
    • Fukuda, M., Dell, A., Oates, J. E., Fukuda, M. N., Structure of branched lactosaminoglycan, the carbohydrate moiety of band 3 isolated from adult human erythrocytes. J. Biol. Chem. 1984, 259, 8260-8273.
    • (1984) J. Biol. Chem. , vol.259 , pp. 8260-8273
    • Fukuda, M.1    Dell, A.2    Oates, J.E.3    Fukuda, M.N.4
  • 2
    • 0033515687 scopus 로고    scopus 로고
    • Regulation of I-branched poly-N-acetyllactosamine synthesis. Concerted actions by I-extension enzyme, I-branching enzyme, and beta1,4-galactosyltransferase I
    • Ujita, M., McAuliffe, J., Suzuki, M., Hindsgaul, O. et al., Regulation of I-branched poly-N-acetyllactosamine synthesis. Concerted actions by I-extension enzyme, I-branching enzyme, and beta1, 4-galactosyltransferase I. J. Biol. Chem. 1999, 274, 9296-9304.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9296-9304
    • Ujita, M.1    McAuliffe, J.2    Suzuki, M.3    Hindsgaul, O.4
  • 3
    • 0033546414 scopus 로고    scopus 로고
    • Poly-N-acetyllactosamine synthesis in branched N-glycans is controlled by complemental branch specificity of I-extension enzyme and beta1,4-galactosyltransferase I
    • Ujita, M., McAuliffe, J., Hindsgaul, O., Sasaki, K. et al., Poly-N-acetyllactosamine synthesis in branched N-glycans is controlled by complemental branch specificity of I-extension enzyme and beta1, 4-galactosyltransferase I. J. Biol. Chem. 1999, 274, 16717-16726.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16717-16726
    • Ujita, M.1    McAuliffe, J.2    Hindsgaul, O.3    Sasaki, K.4
  • 4
    • 0032504181 scopus 로고    scopus 로고
    • Biosynthesis of branched polylactosaminoglycans. Embryonal carcinoma cells express midchain beta1,6-N-acetylglucosaminyltransferase activity that generates branches to preformed linear backbones
    • Leppanen, A., Zhu, Y., Maaheimo, H., Helin, J. et al., Biosynthesis of branched polylactosaminoglycans. Embryonal carcinoma cells express midchain beta1, 6-N-acetylglucosaminyltransferase activity that generates branches to preformed linear backbones. J. Biol. Chem. 1998, 273, 17399-17405.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17399-17405
    • Leppanen, A.1    Zhu, Y.2    Maaheimo, H.3    Helin, J.4
  • 6
    • 0033769926 scopus 로고    scopus 로고
    • Enzymatic in vitro synthesis of I-branches of mammalian polylactosamines: generation of scaffolds for multiple selectin-binding saccharide determinants
    • Renkonen, O., Enzymatic in vitro synthesis of I-branches of mammalian polylactosamines: generation of scaffolds for multiple selectin-binding saccharide determinants. Cell. Mol. Life Sci. 2000, 57, 1423-1439.
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 1423-1439
    • Renkonen, O.1
  • 7
    • 40549138776 scopus 로고    scopus 로고
    • Embryonic stem cells deficient in I beta1,6-N-acetylglucosaminyltransferase exhibit reduced expression of embryoglycan and the loss of a Lewis X antigen, 4C9
    • Muramatsu, H., Kusano, T., Sato, M., Oda, Y. et al., Embryonic stem cells deficient in I beta1, 6-N-acetylglucosaminyltransferase exhibit reduced expression of embryoglycan and the loss of a Lewis X antigen, 4C9. Glycobiology 2008, 18, 242-249.
    • (2008) Glycobiology , vol.18 , pp. 242-249
    • Muramatsu, H.1    Kusano, T.2    Sato, M.3    Oda, Y.4
  • 8
    • 35648958775 scopus 로고    scopus 로고
    • Polylactosamine on glycoproteins influences basal levels of lymphocyte and macrophage activation
    • Togayachi, A., Kozono, Y., Ishida, H., Abe, S. et al., Polylactosamine on glycoproteins influences basal levels of lymphocyte and macrophage activation. Proc. Natl. Acad. Sci. USA 2007, 104, 15829-15834.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 15829-15834
    • Togayachi, A.1    Kozono, Y.2    Ishida, H.3    Abe, S.4
  • 9
    • 0026657798 scopus 로고
    • Differential glycosylation and cell surface expression of lysosomal membrane glycoproteins in sublines of a human colon cancer exhibiting distinct metastatic potentials
    • Saitoh, O., Wang, W. C., Lotan, R., Fukuda, M., Differential glycosylation and cell surface expression of lysosomal membrane glycoproteins in sublines of a human colon cancer exhibiting distinct metastatic potentials. J. Biol. Chem. 1992, 267, 5700-5711.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5700-5711
    • Saitoh, O.1    Wang, W.C.2    Lotan, R.3    Fukuda, M.4
  • 10
    • 64149125582 scopus 로고    scopus 로고
    • Poly N-acetyllactosamine substitutions on N- and not O-oligosaccharides or Thomsen-Friedenreich antigen facilitate lung specific metastasis of melanoma cells via galectin-3
    • Srinivasan, N., Bane, S. M., Ahire, S. D., Ingle, A. D., Kalraiya, R. D., Poly N-acetyllactosamine substitutions on N- and not O-oligosaccharides or Thomsen-Friedenreich antigen facilitate lung specific metastasis of melanoma cells via galectin-3. Glycoconj. J. 2009, 26, 445-456.
    • (2009) Glycoconj. J. , vol.26 , pp. 445-456
    • Srinivasan, N.1    Bane, S.M.2    Ahire, S.D.3    Ingle, A.D.4    Kalraiya, R.D.5
  • 11
    • 0028266470 scopus 로고
    • Identification of a major poly-N-acetyllactosamine-containing cell-surface glycoprotein of mouse teratocarcinoma cells. Appearance on cells induced to primitive endoderm but not parietal endoderm differentiation
    • Spillmann, D., Finne, J., Identification of a major poly-N-acetyllactosamine-containing cell-surface glycoprotein of mouse teratocarcinoma cells. Appearance on cells induced to primitive endoderm but not parietal endoderm differentiation. Eur. J. Biochem. 1994, 220, 385-394.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 385-394
    • Spillmann, D.1    Finne, J.2
  • 12
    • 0023672037 scopus 로고
    • Developmentally regulated expression of cell surface carbohydrates during mouse embryogenesis
    • Muramatsu, T., Developmentally regulated expression of cell surface carbohydrates during mouse embryogenesis. J. Cell. Biochem. 1988, 36, 1-14.
    • (1988) J. Cell. Biochem. , vol.36 , pp. 1-14
    • Muramatsu, T.1
  • 13
    • 52949084643 scopus 로고    scopus 로고
    • Characterisation of alpha3beta1 and alpha(v)beta3 integrin N-oligosaccharides in metastatic melanoma WM9 and WM239 cell lines
    • Kremser, M. E., Przybylo, M., Hoja-Lukowicz, D., Pochec, E. et al., Characterisation of alpha3beta1 and alpha(v)beta3 integrin N-oligosaccharides in metastatic melanoma WM9 and WM239 cell lines. Biochim. Biophys. Acta. 2008, 1780, 1421-1431.
    • (2008) Biochim. Biophys. Acta. , vol.1780 , pp. 1421-1431
    • Kremser, M.E.1    Przybylo, M.2    Hoja-Lukowicz, D.3    Pochec, E.4
  • 14
    • 41149083080 scopus 로고    scopus 로고
    • Characterization of the N-glycosylation phenotype of erythrocyte membrane proteins in congenital dyserythropoietic anemia type II (CDA II/HEMPAS)
    • Denecke, J., Kranz, C., Nimtz, M., Conradt, H. S. et al., Characterization of the N-glycosylation phenotype of erythrocyte membrane proteins in congenital dyserythropoietic anemia type II (CDA II/HEMPAS). Glycoconj. J. 2008, 25, 375-382.
    • (2008) Glycoconj. J. , vol.25 , pp. 375-382
    • Denecke, J.1    Kranz, C.2    Nimtz, M.3    Conradt, H.S.4
  • 15
    • 72649096402 scopus 로고    scopus 로고
    • Structural characterisation of neutrophil glycans by ultra sensitive mass spectrometric glycomics methodology
    • Babu, P., North, S. J., Jang-Lee, J., Chalabi, S. et al., Structural characterisation of neutrophil glycans by ultra sensitive mass spectrometric glycomics methodology. Glycoconj. J. 2009, 26, 975-986.
    • (2009) Glycoconj. J. , vol.26 , pp. 975-986
    • Babu, P.1    North, S.J.2    Jang-Lee, J.3    Chalabi, S.4
  • 16
    • 0020356007 scopus 로고
    • A mouse lymphoma cell line resistant to the leukoagglutinating lectin from Phaseolus vulgaris is deficient in UDP-GlcNAc: alpha-D-mannoside beta 1,6 N-acetylglucosaminyltransferase
    • Cummings, R. D., Trowbridge, I. S., Kornfeld, S., A mouse lymphoma cell line resistant to the leukoagglutinating lectin from Phaseolus vulgaris is deficient in UDP-GlcNAc: alpha-D-mannoside beta 1, 6 N-acetylglucosaminyltransferase. J. Biol. Chem. 1982, 257, 13421-13427.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13421-13427
    • Cummings, R.D.1    Trowbridge, I.S.2    Kornfeld, S.3
  • 17
    • 0028332517 scopus 로고
    • cDNA cloning and chromosomal mapping of human N-acetylglucosaminyltransferase V+
    • Saito, H., Nishikawa, A., Gu, J., Ihara, Y. et al., cDNA cloning and chromosomal mapping of human N-acetylglucosaminyltransferase V+. Biochem. Biophys. Res. Commun. 1994, 198, 318-327.
    • (1994) Biochem. Biophys. Res. Commun. , vol.198 , pp. 318-327
    • Saito, H.1    Nishikawa, A.2    Gu, J.3    Ihara, Y.4
  • 18
    • 0035825644 scopus 로고    scopus 로고
    • Negative regulation of T-cell activation and autoimmunity by Mgat5 N-glycosylation
    • Demetriou, M., Granovsky, M., Quaggin, S., Dennis, J. W., Negative regulation of T-cell activation and autoimmunity by Mgat5 N-glycosylation. Nature 2001, 409, 733-739.
    • (2001) Nature , vol.409 , pp. 733-739
    • Demetriou, M.1    Granovsky, M.2    Quaggin, S.3    Dennis, J.W.4
  • 19
    • 0037524469 scopus 로고    scopus 로고
    • GnT-V, macrophage and cancer metastasis: a common link
    • Chakraborty, A. K., Pawelek, J. M., GnT-V, macrophage and cancer metastasis: a common link. Clin. Exp. Metastasis 2003, 20, 365-373.
    • (2003) Clin. Exp. Metastasis , vol.20 , pp. 365-373
    • Chakraborty, A.K.1    Pawelek, J.M.2
  • 20
    • 33645822097 scopus 로고    scopus 로고
    • Galectin binding to Mgat5-modified N-glycans regulates fibronectin matrix remodeling in tumor cells
    • Lagana, A., Goetz, J. G., Cheung, P., Raz, A. et al., Galectin binding to Mgat5-modified N-glycans regulates fibronectin matrix remodeling in tumor cells. Mol. Cell. Biol. 2006, 26, 3181-3193.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3181-3193
    • Lagana, A.1    Goetz, J.G.2    Cheung, P.3    Raz, A.4
  • 21
    • 34547610472 scopus 로고    scopus 로고
    • Inhibition of a specific N-glycosylation activity results in attenuation of breast carcinoma cell invasiveness-related phenotypes: inhibition of epidermal growth factor-induced dephosphorylation of focal adhesion kinase
    • Guo, H. B., Randolph, M., Pierce, M., Inhibition of a specific N-glycosylation activity results in attenuation of breast carcinoma cell invasiveness-related phenotypes: inhibition of epidermal growth factor-induced dephosphorylation of focal adhesion kinase. J. Biol. Chem. 2007, 282, 22150-22162.
    • (2007) J. Biol. Chem. , vol.282 , pp. 22150-22162
    • Guo, H.B.1    Randolph, M.2    Pierce, M.3
  • 22
    • 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. et al., Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation. Cell 2007, 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
  • 23
    • 0020479688 scopus 로고
    • Characterization of the structural determinants required for the high affinity interaction of asparagine-linked oligosaccharides with immobilized Phaseolus vulgaris leukoagglutinating and erythroagglutinating lectins
    • Cummings, R. D., Kornfeld, S., Characterization of the structural determinants required for the high affinity interaction of asparagine-linked oligosaccharides with immobilized Phaseolus vulgaris leukoagglutinating and erythroagglutinating lectins. J. Biol. Chem. 1982, 257, 11230-11234.
    • (1982) J. Biol. Chem. , vol.257 , pp. 11230-11234
    • Cummings, R.D.1    Kornfeld, S.2
  • 24
    • 0021227742 scopus 로고
    • The distribution of repeating [Gal beta 1,4GlcNAc beta 1,3] sequences in asparagine-linked oligosaccharides of the mouse lymphoma cell lines BW5147 and PHAR 2.1
    • Cummings, R. D., Kornfeld, S., The distribution of repeating [Gal beta 1, 4GlcNAc beta 1, 3] sequences in asparagine-linked oligosaccharides of the mouse lymphoma cell lines BW5147 and PHAR 2.1. J. Biol. Chem. 1984, 259, 6253-6260.
    • (1984) J. Biol. Chem. , vol.259 , pp. 6253-6260
    • Cummings, R.D.1    Kornfeld, S.2
  • 25
    • 0023644519 scopus 로고
    • Carbohydrate binding properties of complex-type oligosaccharides on immobilized Datura stramonium lectin
    • Yamashita, K., Totani, K., Ohkura, T., Takasaki, S. et al., Carbohydrate binding properties of complex-type oligosaccharides on immobilized Datura stramonium lectin. J. Biol. Chem. 1987, 262, 1602-1607.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1602-1607
    • Yamashita, K.1    Totani, K.2    Ohkura, T.3    Takasaki, S.4
  • 26
    • 0023655294 scopus 로고
    • Relationship of the terminal sequences to the length of poly-N-acetyllactosamine chains in asparagine-linked oligosaccharides from the mouse lymphoma cell line BW5147. Immobilized tomato lectin interacts with high affinity with glycopeptides containing long poly-N-acetyllactosamine chains
    • Merkle, R. K., Cummings, R. D., Relationship of the terminal sequences to the length of poly-N-acetyllactosamine chains in asparagine-linked oligosaccharides from the mouse lymphoma cell line BW5147. Immobilized tomato lectin interacts with high affinity with glycopeptides containing long poly-N-acetyllactosamine chains. J. Biol. Chem. 1987, 262, 8179-8189.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8179-8189
    • Merkle, R.K.1    Cummings, R.D.2
  • 27
    • 0025223278 scopus 로고
    • Granulocytic differentiation of HL-60 cells is associated with increase of poly-N-acetyllactosamine in Asn-linked oligosaccharides attached to human lysosomal membrane glycoproteins
    • Lee, N., Wang, W. C., Fukuda, M., Granulocytic differentiation of HL-60 cells is associated with increase of poly-N-acetyllactosamine in Asn-linked oligosaccharides attached to human lysosomal membrane glycoproteins. J. Biol. Chem. 1990, 265, 20476-20487.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20476-20487
    • Lee, N.1    Wang, W.C.2    Fukuda, M.3
  • 28
    • 0033888016 scopus 로고    scopus 로고
    • Galectin-3 induces endothelial cell morphogenesis and angiogenesis
    • Nangia-Makker, P., Honjo, Y., Sarvis, R., Akahani, S. et al., Galectin-3 induces endothelial cell morphogenesis and angiogenesis. Am. J. Pathol. 2000, 156, 899-909.
    • (2000) Am. J. Pathol. , vol.156 , pp. 899-909
    • Nangia-Makker, P.1    Honjo, Y.2    Sarvis, R.3    Akahani, S.4
  • 29
    • 34748837860 scopus 로고    scopus 로고
    • Aminopeptidase N/CD13 induces angiogenesis through interaction with a pro-angiogenic protein, galectin-3
    • Yang, E., Shim, J. S., Woo, H. J., Kim, K. W., Kwon, H. J., Aminopeptidase N/CD13 induces angiogenesis through interaction with a pro-angiogenic protein, galectin-3. Biochem. Biophys. Res. Commun. 2007, 363, 336-341.
    • (2007) Biochem. Biophys. Res. Commun. , vol.363 , pp. 336-341
    • Yang, E.1    Shim, J.S.2    Woo, H.J.3    Kim, K.W.4    Kwon, H.J.5
  • 30
    • 0001637870 scopus 로고
    • Permanent cell line expressing human factor VIII-related antigen established by hybridization
    • Edgell, C. J., McDonald, C. C., Graham, J. B., Permanent cell line expressing human factor VIII-related antigen established by hybridization. Proc. Natl. Acad. Sci. USA 1983, 80, 3734-3737.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 3734-3737
    • Edgell, C.J.1    McDonald, C.C.2    Graham, J.B.3
  • 31
    • 56349164708 scopus 로고    scopus 로고
    • Acute hypoxia enhances proteins S-nitrosylation in endothelial cells
    • Chen, S. C., Huang, B., Liu, Y. C., Shyu, K. G. et al., Acute hypoxia enhances proteins S-nitrosylation in endothelial cells. Biochem. Biophys. Res. Commun. 2008, 377, 1274-1278.
    • (2008) Biochem. Biophys. Res. Commun. , vol.377 , pp. 1274-1278
    • Chen, S.C.1    Huang, B.2    Liu, Y.C.3    Shyu, K.G.4
  • 32
    • 0028344521 scopus 로고
    • Mass spectrometry of carbohydrate-containing biopolymers
    • Dell, A., Reason, A. J., Khoo, K. H., Panico, M. et al., Mass spectrometry of carbohydrate-containing biopolymers. Methods Enzymol. 1994, 230, 108-132.
    • (1994) Methods Enzymol. , vol.230 , pp. 108-132
    • Dell, A.1    Reason, A.J.2    Khoo, K.H.3    Panico, M.4
  • 33
    • 33746895191 scopus 로고    scopus 로고
    • Distinctive characteristics of MALDI-Q/TOF and TOF/TOF tandem mass spectrometry for sequencing of permethylated complex type N-glycans
    • Yu, S. Y., Wu, S. W., Khoo, K. H., Distinctive characteristics of MALDI-Q/TOF and TOF/TOF tandem mass spectrometry for sequencing of permethylated complex type N-glycans. Glycoconj. J. 2006, 23, 355-369.
    • (2006) Glycoconj. J. , vol.23 , pp. 355-369
    • Yu, S.Y.1    Wu, S.W.2    Khoo, K.H.3
  • 34
    • 34247849493 scopus 로고    scopus 로고
    • Dynamic developmental elaboration of N-linked glycan complexity in the Drosophila melanogaster embryo
    • Aoki, K., Perlman, M., Lim, J. M., Cantu, R. et al., Dynamic developmental elaboration of N-linked glycan complexity in the Drosophila melanogaster embryo. J. Biol. Chem. 2007, 282, 9127-9142.
    • (2007) J. Biol. Chem. , vol.282 , pp. 9127-9142
    • Aoki, K.1    Perlman, M.2    Lim, J.M.3    Cantu, R.4
  • 35
    • 16844385691 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha up-regulates the expression of beta1,4-galactosyltransferase I in primary human endothelial cells by mRNA stabilization
    • Garcia-Vallejo, J. J., van Dijk, W., van Die, I., Gringhuis, S. I., Tumor necrosis factor-alpha up-regulates the expression of beta1, 4-galactosyltransferase I in primary human endothelial cells by mRNA stabilization. J. Biol. Chem. 2005, 280, 12676-12682.
    • (2005) J. Biol. Chem. , vol.280 , pp. 12676-12682
    • Garcia-Vallejo, J.J.1    van Dijk, W.2    van Die, I.3    Gringhuis, S.I.4
  • 36
    • 28444485987 scopus 로고    scopus 로고
    • Activation of human endothelial cells by tumor necrosis factor-alpha results in profound changes in the expression of glycosylation-related genes
    • Garcia-Vallejo, J. J., Van Dijk, W., Van Het Hof, B., Van Die, I. et al., Activation of human endothelial cells by tumor necrosis factor-alpha results in profound changes in the expression of glycosylation-related genes. J. Cell. Physiol. 2006, 206, 203-210.
    • (2006) J. Cell. Physiol. , vol.206 , pp. 203-210
    • Garcia-Vallejo, J.J.1    Van Dijk, W.2    Van Het Hof, B.3    Van Die, I.4
  • 37
    • 0023935871 scopus 로고
    • Fibrinolytic properties of a human endothelial hybrid cell line (Ea.hy 926)
    • Emeis, J. J., Edgell, C. J., Fibrinolytic properties of a human endothelial hybrid cell line (Ea.hy 926). Blood 1988, 71, 1669-1675.
    • (1988) Blood , vol.71 , pp. 1669-1675
    • Emeis, J.J.1    Edgell, C.J.2
  • 38
    • 0026322416 scopus 로고
    • Endothelin-1 is expressed and released by a human endothelial hybrid cell line (EA.hy 926)
    • Saijonmaa, O., Nyman, T., Hohenthal, U., Fyhrquist, F., Endothelin-1 is expressed and released by a human endothelial hybrid cell line (EA.hy 926). Biochem. Biophys. Res. Commun. 1991, 181, 529-536.
    • (1991) Biochem. Biophys. Res. Commun. , vol.181 , pp. 529-536
    • Saijonmaa, O.1    Nyman, T.2    Hohenthal, U.3    Fyhrquist, F.4
  • 39
    • 0030836584 scopus 로고    scopus 로고
    • Responses of HUVEC and EAhy926 to heparin and fibroblast growth factors
    • Thomas, S., Robinson, C. J., Gray, E., Responses of HUVEC and EAhy926 to heparin and fibroblast growth factors. In Vitro Cell Dev. Biol. Anim. 1997, 33, 492-494.
    • (1997) In Vitro Cell Dev. Biol. Anim. , vol.33 , pp. 492-494
    • Thomas, S.1    Robinson, C.J.2    Gray, E.3
  • 40
    • 0036433641 scopus 로고    scopus 로고
    • In vitro expression of the endothelial phenotype: comparative study of primary isolated cells and cell lines, including the novel cell line HPMEC-ST1.6R
    • Unger, R. E., Krump-Konvalinkova, V., Peters, K., Kirkpatrick, C. J., In vitro expression of the endothelial phenotype: comparative study of primary isolated cells and cell lines, including the novel cell line HPMEC-ST1.6R. Microvasc. Res. 2002, 64, 384-397.
    • (2002) Microvasc. Res. , vol.64 , pp. 384-397
    • Unger, R.E.1    Krump-Konvalinkova, V.2    Peters, K.3    Kirkpatrick, C.J.4
  • 41
    • 70349275888 scopus 로고    scopus 로고
    • Mass spectrometry in the analysis of N-linked and O-linked glycans
    • North, S. J., Hitchen, P. G., Haslam, S. M., Dell, A., Mass spectrometry in the analysis of N-linked and O-linked glycans. Curr. Opin. Struct. Biol. 2009, 19, 498-506.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 498-506
    • North, S.J.1    Hitchen, P.G.2    Haslam, S.M.3    Dell, A.4
  • 42
    • 51649085326 scopus 로고    scopus 로고
    • Mass spectrometry and the emerging field of glycomics
    • Zaia, J., Mass spectrometry and the emerging field of glycomics. Chem. Biol. 2008, 15, 881-892.
    • (2008) Chem. Biol. , vol.15 , pp. 881-892
    • Zaia, J.1
  • 43
    • 77958604484 scopus 로고    scopus 로고
    • Glycan analysis and influenza A virus infection of primary swine respiratory epithelial cells: the importance of NeuAcalpha2-6 glycans
    • Bateman, A. C., Karamanska, R., Busch, M. G., Dell, A. et al., Glycan analysis and influenza A virus infection of primary swine respiratory epithelial cells: the importance of NeuAcalpha2-6 glycans. J. Biol. Chem. 2010, 285, 34016-34026.
    • (2010) J. Biol. Chem. , vol.285 , pp. 34016-34026
    • Bateman, A.C.1    Karamanska, R.2    Busch, M.G.3    Dell, A.4
  • 44
    • 77949325755 scopus 로고    scopus 로고
    • Glycomics profiling of Chinese hamster ovary cell glycosylation mutants reveals N-glycans of a novel size and complexity
    • North, S. J., Huang, H. H., Sundaram, S., Jang-Lee, J. et al., Glycomics profiling of Chinese hamster ovary cell glycosylation mutants reveals N-glycans of a novel size and complexity. J. Biol. Chem. 2010, 285, 5759-5775.
    • (2010) J. Biol. Chem. , vol.285 , pp. 5759-5775
    • North, S.J.1    Huang, H.H.2    Sundaram, S.3    Jang-Lee, J.4
  • 45
    • 45549095820 scopus 로고    scopus 로고
    • Targeted glycoproteomic identification of biomarkers for human breast carcinoma
    • Abbott, K. L., Aoki, K., Lim, J. M., Porterfield, M. et al., Targeted glycoproteomic identification of biomarkers for human breast carcinoma. J. Proteome Res. 2008, 7, 1470-1480.
    • (2008) J. Proteome Res. , vol.7 , pp. 1470-1480
    • Abbott, K.L.1    Aoki, K.2    Lim, J.M.3    Porterfield, M.4
  • 46
    • 34447527604 scopus 로고    scopus 로고
    • Analysis of protein-linked glycosylation in a sperm-somatic cell adhesion system
    • Sutton-Smith, M., Wong, N. K., Khoo, K. H., Wu, S. W. et al., Analysis of protein-linked glycosylation in a sperm-somatic cell adhesion system. Glycobiology 2007, 17, 553-567.
    • (2007) Glycobiology , vol.17 , pp. 553-567
    • Sutton-Smith, M.1    Wong, N.K.2    Khoo, K.H.3    Wu, S.W.4
  • 47
    • 70449338884 scopus 로고    scopus 로고
    • Analysis of the human seminal plasma glycome reveals the presence of immunomodulatory carbohydrate functional groups
    • Pang, P. C., Tissot, B., Drobnis, E. Z., Morris, H. R. et al., Analysis of the human seminal plasma glycome reveals the presence of immunomodulatory carbohydrate functional groups. J. Proteome Res. 2009, 8, 4906-4915.
    • (2009) J. Proteome Res. , vol.8 , pp. 4906-4915
    • Pang, P.C.1    Tissot, B.2    Drobnis, E.Z.3    Morris, H.R.4
  • 48
    • 77952302417 scopus 로고    scopus 로고
    • Physiological and glycomic characterization of N-acetylglucosaminyltransferase-IVa and -IVb double deficient mice
    • Takamatsu, S., Antonopoulos, A., Ohtsubo, K., Ditto, D. et al., Physiological and glycomic characterization of N-acetylglucosaminyltransferase-IVa and -IVb double deficient mice. Glycobiology 2010, 20, 485-497.
    • (2010) Glycobiology , vol.20 , pp. 485-497
    • Takamatsu, S.1    Antonopoulos, A.2    Ohtsubo, K.3    Ditto, D.4
  • 49
    • 0017176814 scopus 로고
    • Endo-beta-galactosidase of Escherichia freundii. Purification and endoglycosidic action on keratan sulfates, oligosaccharides, and blood group active glycoprotein
    • Fukuda, M. N., Matsumura, G., Endo-beta-galactosidase of Escherichia freundii. Purification and endoglycosidic action on keratan sulfates, oligosaccharides, and blood group active glycoprotein. J. Biol. Chem. 1976, 251, 6218-6225.
    • (1976) J. Biol. Chem. , vol.251 , pp. 6218-6225
    • Fukuda, M.N.1    Matsumura, G.2
  • 50
    • 0021348368 scopus 로고
    • Structure of fetal lactosaminoglycan. The carbohydrate moiety of Band 3 isolated from human umbilical cord erythrocytes
    • Fukuda, M., Dell, A., Fukuda, M. N., Structure of fetal lactosaminoglycan. The carbohydrate moiety of Band 3 isolated from human umbilical cord erythrocytes. J. Biol. Chem. 1984, 259, 4782-4791.
    • (1984) J. Biol. Chem. , vol.259 , pp. 4782-4791
    • Fukuda, M.1    Dell, A.2    Fukuda, M.N.3
  • 51
    • 0021611610 scopus 로고
    • Structure of sialylated fucosyl lactosaminoglycan isolated from human granulocytes
    • Fukuda, M., Spooncer, E., Oates, J. E., Dell, A., Klock, J. C., Structure of sialylated fucosyl lactosaminoglycan isolated from human granulocytes. J. Biol. Chem. 1984, 259, 10925-10935.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10925-10935
    • Fukuda, M.1    Spooncer, E.2    Oates, J.E.3    Dell, A.4    Klock, J.C.5
  • 52
    • 0021342469 scopus 로고
    • Isolation and characterization of polyfucosylated lactosaminoglycan from human granulocytes
    • Spooncer, E., Fukuda, M., Klock, J. C., Oates, J. E., Dell, A., Isolation and characterization of polyfucosylated lactosaminoglycan from human granulocytes. J. Biol. Chem. 1984, 259, 4792-4801.
    • (1984) J. Biol. Chem. , vol.259 , pp. 4792-4801
    • Spooncer, E.1    Fukuda, M.2    Klock, J.C.3    Oates, J.E.4    Dell, A.5
  • 53
    • 0022369777 scopus 로고
    • Structures of sialylated fucosyl polylactosaminoglycans isolated from chronic myelogenous leukemia cells
    • Fukuda, M., Bothner, B., Ramsamooj, P., Dell, A. et al., Structures of sialylated fucosyl polylactosaminoglycans isolated from chronic myelogenous leukemia cells. J. Biol. Chem. 1985, 260, 12957-12967.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12957-12967
    • Fukuda, M.1    Bothner, B.2    Ramsamooj, P.3    Dell, A.4
  • 54
    • 0023895599 scopus 로고
    • A membrane-anchored form but not the secretory form of human chorionic gonadotropin-alpha chain acquires polylactosaminoglycan
    • Fukuda, M., Guan, J. L., Rose, J. K., A membrane-anchored form but not the secretory form of human chorionic gonadotropin-alpha chain acquires polylactosaminoglycan. J. Biol. Chem. 1988, 263, 5314-5318.
    • (1988) J. Biol. Chem. , vol.263 , pp. 5314-5318
    • Fukuda, M.1    Guan, J.L.2    Rose, J.K.3
  • 55
    • 0025222845 scopus 로고
    • The polylactosaminoglycans of human lysosomal membrane glycoproteins lamp-1 and lamp-2. Localization on the peptide backbones
    • Carlsson, S. R., Fukuda, M., The polylactosaminoglycans of human lysosomal membrane glycoproteins lamp-1 and lamp-2. Localization on the peptide backbones. J. Biol. Chem. 1990, 265, 20488-20495.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20488-20495
    • Carlsson, S.R.1    Fukuda, M.2
  • 56
    • 0024497455 scopus 로고
    • Survival of recombinant erythropoietin in the circulation: the role of carbohydrates
    • Fukuda, M. N., Sasaki, H., Lopez, L., Fukuda, M., Survival of recombinant erythropoietin in the circulation: the role of carbohydrates. Blood 1989, 73, 84-89.
    • (1989) Blood , vol.73 , pp. 84-89
    • Fukuda, M.N.1    Sasaki, H.2    Lopez, L.3    Fukuda, M.4
  • 57
    • 0025317594 scopus 로고
    • Poly-N-acetyllactosamine-specific tomato lectin interacts with gastric parietal cellsDD Identification of a tomato-lectin binding 60-90 X 10(3) Mr membrane glycoprotein of tubulovesicles
    • Callaghan, J. M., Toh, B. H., Pettitt, J. M., Humphris, D. C., Gleeson, P. A., Poly-N-acetyllactosamine-specific tomato lectin interacts with gastric parietal cellsDD Identification of a tomato-lectin binding 60-90 X 10(3) Mr membrane glycoprotein of tubulovesicles. J. Cell. Sci. 1990, 95, 563-576.
    • (1990) J. Cell. Sci. , vol.95 , pp. 563-576
    • Callaghan, J.M.1    Toh, B.H.2    Pettitt, J.M.3    Humphris, D.C.4    Gleeson, P.A.5
  • 58
    • 0026522794 scopus 로고
    • Rapid purification of the gastric H+/K(+)-ATPase complex by tomato-lectin affinity chromatography
    • Callaghan, J. M., Toh, B. H., Simpson, R. J., Baldwin, G. S., Gleeson, P. A., Rapid purification of the gastric H+/K(+)-ATPase complex by tomato-lectin affinity chromatography. Biochem. J. 1992, 283, 63-68.
    • (1992) Biochem. J. , vol.283 , pp. 63-68
    • Callaghan, J.M.1    Toh, B.H.2    Simpson, R.J.3    Baldwin, G.S.4    Gleeson, P.A.5
  • 59
    • 12544251963 scopus 로고    scopus 로고
    • Trypanosoma brucei glycoproteins contain novel giant poly-N-acetyllactosamine carbohydrate chains
    • Atrih, A., Richardson, J. M., Prescott, A. R., Ferguson, M. A., Trypanosoma brucei glycoproteins contain novel giant poly-N-acetyllactosamine carbohydrate chains. J. Biol. Chem. 2005, 280, 865-871.
    • (2005) J. Biol. Chem. , vol.280 , pp. 865-871
    • Atrih, A.1    Richardson, J.M.2    Prescott, A.R.3    Ferguson, M.A.4
  • 60
    • 61849161703 scopus 로고    scopus 로고
    • Glycoproteomics of plasma based on narrow selectivity lectin affinity chromatography
    • Jung, K., Cho, W., Regnier, F. E., Glycoproteomics of plasma based on narrow selectivity lectin affinity chromatography. J. Proteome Res. 2009, 8, 643-650.
    • (2009) J. Proteome Res. , vol.8 , pp. 643-650
    • Jung, K.1    Cho, W.2    Regnier, F.E.3
  • 61
    • 4344668062 scopus 로고    scopus 로고
    • Links between CD147 function, glycosylation, and caveolin-1
    • Tang, W., Chang, S. B., Hemler, M. E., Links between CD147 function, glycosylation, and caveolin-1. Mol. Biol. Cell 2004, 15, 4043-4050.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4043-4050
    • Tang, W.1    Chang, S.B.2    Hemler, M.E.3
  • 62
    • 24044511771 scopus 로고    scopus 로고
    • Metabolic activation-related CD147-CD98 complex
    • Xu, D., Hemler, M. E., Metabolic activation-related CD147-CD98 complex. Mol. Cell. Proteomics 2005, 4, 1061-1071.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1061-1071
    • Xu, D.1    Hemler, M.E.2
  • 63
    • 23844470552 scopus 로고    scopus 로고
    • Epithelial membrane protein-1 is a biomarker of gefitinib resistance
    • Jain, A., Tindell, C. A., Laux, I., Hunter, J. B. et al., Epithelial membrane protein-1 is a biomarker of gefitinib resistance. Proc. Natl. Acad. Sci. USA 2005, 102, 11858-11863.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 11858-11863
    • Jain, A.1    Tindell, C.A.2    Laux, I.3    Hunter, J.B.4
  • 64
    • 23944515786 scopus 로고    scopus 로고
    • Endothelial intercellular adhesion molecule (ICAM)-2 regulates angiogenesis
    • Huang, M. T., Mason, J. C., Birdsey, G. M., Amsellem, V. et al., Endothelial intercellular adhesion molecule (ICAM)-2 regulates angiogenesis. Blood 2005, 106, 1636-1643.
    • (2005) Blood , vol.106 , pp. 1636-1643
    • Huang, M.T.1    Mason, J.C.2    Birdsey, G.M.3    Amsellem, V.4
  • 65
    • 0036816147 scopus 로고    scopus 로고
    • Clusters, bundles, arrays and lattices: novel mechanisms for lectin-saccharide-mediated cellular interactions
    • Brewer, C. F., Miceli, M. C., Baum, L. G., Clusters, bundles, arrays and lattices: novel mechanisms for lectin-saccharide-mediated cellular interactions. Curr. Opin. Struct. Biol. 2002, 12, 616-623.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 616-623
    • Brewer, C.F.1    Miceli, M.C.2    Baum, L.G.3
  • 66
    • 59149097542 scopus 로고    scopus 로고
    • Galectin-glycan lattices regulate cell-surface glycoprotein organization and signalling
    • Garner, O. B., Baum, L. G., Galectin-glycan lattices regulate cell-surface glycoprotein organization and signalling. Biochem. Soc. Trans. 2008, 36, 1472-1477.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 1472-1477
    • Garner, O.B.1    Baum, L.G.2
  • 67
    • 47749108740 scopus 로고    scopus 로고
    • Identification of further elongation and branching of dimeric type 1 chain on lactosylceramides from colonic adenocarcinoma by tandem mass spectrometry sequencing analyses
    • Fan, Y. Y., Yu, S. Y., Ito, H., Kameyama, A. et al., Identification of further elongation and branching of dimeric type 1 chain on lactosylceramides from colonic adenocarcinoma by tandem mass spectrometry sequencing analyses. J. Biol. Chem. 2008, 283, 16455-16468.
    • (2008) J. Biol. Chem. , vol.283 , pp. 16455-16468
    • Fan, Y.Y.1    Yu, S.Y.2    Ito, H.3    Kameyama, A.4


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