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Volumn 21, Issue 3-4, 2004, Pages 125-137

Carbohydrate-to-carbohydrate interaction, through glycosynapse, as a basis of cell recognition and membrane organization

Author keywords

autoaggregation; binding protein; bivalent cation; cell adhesion; cis interaction; Gb4; Gg3; glycosphingolipid; glycosynapse; GM3; Le x; trans interaction

Indexed keywords

CARBOHYDRATE; CARBOHYDRATE BINDING PROTEIN; DIVALENT CATION; EPIDERMAL GROWTH FACTOR RECEPTOR; GANGLIOSIDE GM3; GLYCOCONJUGATE; GLYCOSPHINGOLIPID; GROWTH FACTOR RECEPTOR; INTEGRIN RECEPTOR; KALININ; LACTOSYLCERAMIDE; UVOMORULIN;

EID: 6044236885     PISSN: 02820080     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:GLYC.0000044844.95878.cf     Document Type: Review
Times cited : (142)

References (87)
  • 2
    • 0007635166 scopus 로고
    • Chain conformations in the sol-gel transitions for polysaccharide systems, and their characterisation by spectroscopic methods
    • Bryce TA, McKinnon AA, Morris ER, Rees DA, Thom D, Chain conformations in the sol-gel transitions for polysaccharide systems, and their characterisation by spectroscopic methods, Faraday Disc Chem Soc 57, 221-9 (1974).
    • (1974) Faraday Disc Chem Soc , vol.57 , pp. 221-229
    • Bryce, T.A.1    McKinnon, A.A.2    Morris, E.R.3    Rees, D.A.4    Thom, D.5
  • 3
    • 0018874090 scopus 로고
    • Interactions between the carbohydrate chains of hyaluronate and chondroitin sulphate
    • Turley EA, Roth S, Interactions between the carbohydrate chains of hyaluronate and chondroitin sulphate, Nature 283, 268-71 (1980).
    • (1980) Nature , vol.283 , pp. 268-271
    • Turley, E.A.1    Roth, S.2
  • 4
    • 0032080122 scopus 로고    scopus 로고
    • Galectin-1 is a major receptor for ganglioside GM1, a product of the growth-controlling activity of a cell surface ganglioside sialidase, on human neuroblastoma cells in culture
    • Kopitz J, von Reitzenstein C, Burchert M, Cantz M, Gabius HJ, Galectin-1 is a major receptor for ganglioside GM1, a product of the growth-controlling activity of a cell surface ganglioside sialidase, on human neuroblastoma cells in culture, J Biol Chem 273, 11205-11 (1998).
    • (1998) J Biol Chem , vol.273 , pp. 11205-11211
    • Kopitz, J.1    Von Reitzenstein, C.2    Burchert, M.3    Cantz, M.4    Gabius, H.J.5
  • 5
    • 0031959770 scopus 로고    scopus 로고
    • Galectins: Versatile modulators of cell adhesion, cell proliferation, and cell death
    • Perillo NL, Marcus ME, Baum LG, Galectins: Versatile modulators of cell adhesion, cell proliferation, and cell death, J Mol Med 76(6), 402-12 (1998).
    • (1998) J Mol Med , vol.76 , Issue.6 , pp. 402-412
    • Perillo, N.L.1    Marcus, M.E.2    Baum, L.G.3
  • 6
    • 0035929631 scopus 로고    scopus 로고
    • Negative regulation of neuroblastoma cell growth by carbohydrate- dependent surface binding of galectin-1 and functional divergence from galectin-3
    • Kopitz J, von Reitzenstein C, Andre S, Kaltner H, Uhl J, Ehemann V, Cantz M, Gabius H-J, Negative regulation of neuroblastoma cell growth by carbohydrate-dependent surface binding of galectin-1 and functional divergence from galectin-3, J Biol Chem 276(38), 35917-23 (2001).
    • (2001) J Biol Chem , vol.276 , Issue.38 , pp. 35917-35923
    • Kopitz, J.1    Von Reitzenstein, C.2    Andre, S.3    Kaltner, H.4    Uhl, J.5    Ehemann, V.6    Cantz, M.7    Gabius, H.-J.8
  • 7
    • 0037470066 scopus 로고    scopus 로고
    • The ST6Ga1 I sialyltransferase selectively modifies N-glycans on CD45 to negatively regulate galectin-1-induced CD45 clustering, phosphatase modulation, and T cell death
    • Amano M, Galvan M, He J, Baum LG, The ST6Ga1 I sialyltransferase selectively modifies N-glycans on CD45 to negatively regulate galectin-1-induced CD45 clustering, phosphatase modulation, and T cell death, J Biol Chem 278(9), 7469-75 (2003).
    • (2003) J Biol Chem , vol.278 , Issue.9 , pp. 7469-7475
    • Amano, M.1    Galvan, M.2    He, J.3    Baum, L.G.4
  • 8
    • 6044275441 scopus 로고    scopus 로고
    • Special issue on galectins
    • Leffler H, Glycoconjugate Journal, Vol. 19, No. 7/8/9, "Special issue on galectins", 2004.
    • (2004) Glycoconjugate Journal , vol.19 , Issue.7-9
    • Leffler, H.1
  • 9
    • 0028041301 scopus 로고
    • Selectin ligands
    • Varki A, Selectin ligands, Proc Natl Acad Sci USA 91, 7390-97 (1994).
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 7390-7397
    • Varki, A.1
  • 10
    • 0030854107 scopus 로고    scopus 로고
    • Cell adhesion in vascular biology: Role of PSGL-1 binding to selectins in leukocyte recruitment
    • McEver RP, Cummings RD, Cell adhesion in vascular biology: Role of PSGL-1 binding to selectins in leukocyte recruitment, J Clin Invest 100(3), 485-91 (1997).
    • (1997) J Clin Invest , vol.100 , Issue.3 , pp. 485-491
    • McEver, R.P.1    Cummings, R.D.2
  • 11
    • 0030811894 scopus 로고    scopus 로고
    • Carbohydrate-mediated cell adhesion involved in hematogenous metastasis of cancer
    • Kannagi R, Carbohydrate-mediated cell adhesion involved in hematogenous metastasis of cancer, Glycoconj J 14, 577-84 (1997).
    • (1997) Glycoconj J , vol.14 , pp. 577-584
    • Kannagi, R.1
  • 12
    • 6044227702 scopus 로고    scopus 로고
    • Sialic acid-dependent cell-cell interactions mediated by siglecs: Roles of sialoadhesin and CD22 in macrophage adhesion and B cell homing to the bone marrow
    • edited by Inoue Y, Lee YC, Troy FA. Osaka (Gakushin Publ. Co., Japan)
    • Crocker PR, Floyd H, Ferguson DJP, Nitschke L, Sialic acid-dependent cell-cell interactions mediated by siglecs: Roles of sialoadhesin and CD22 in macrophage adhesion and B cell homing to the bone marrow, In, Sialobiology and Other Novel Forms of Glycosylation, edited by Inoue Y, Lee YC, Troy FA. Osaka (Gakushin Publ. Co., Japan, 1999), pp. 111-20.
    • (1999) Sialobiology and Other Novel Forms of Glycosylation , pp. 111-120
    • Crocker, P.R.1    Floyd, H.2    Ferguson, D.J.P.3    Nitschke, L.4
  • 13
    • 0035015565 scopus 로고    scopus 로고
    • Siglecs in the immune system
    • Crocker PR, Varki A, Siglecs in the immune system, Immunology 103(2), 137-45 (2001).
    • (2001) Immunology , vol.103 , Issue.2 , pp. 137-145
    • Crocker, P.R.1    Varki, A.2
  • 14
    • 0037039367 scopus 로고    scopus 로고
    • The glycosynapse
    • Hakomori S, The glycosynapse, Proc Natl Acad Sci USA 99(1), 225-32 (2002).
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.1 , pp. 225-232
    • Hakomori, S.1
  • 15
    • 0037201965 scopus 로고    scopus 로고
    • Glycosphingolipid-dependent cross-talk between glycosynapses interfacing tumor cells with their host cells: Essential basis to define tumor malignancy
    • Hakomori S, Handa K, Glycosphingolipid-dependent cross-talk between glycosynapses interfacing tumor cells with their host cells: Essential basis to define tumor malignancy, FEBS Lett 531(1), 88-92 (2002).
    • (2002) FEBS Lett , vol.531 , Issue.1 , pp. 88-92
    • Hakomori, S.1    Handa, K.2
  • 17
    • 0036467376 scopus 로고    scopus 로고
    • Dynamics of the immunological synapse: Finding, establishing and solidifying a connection
    • Krummel MF, Davis MM, Dynamics of the immunological synapse: Finding, establishing and solidifying a connection, Curr Opin Immunol 14, 66-74 (2002).
    • (2002) Curr Opin Immunol , vol.14 , pp. 66-74
    • Krummel, M.F.1    Davis, M.M.2
  • 18
    • 2542479929 scopus 로고    scopus 로고
    • Carbohydrate-carbohydrate interaction provides adhesion force and specificity for cellular recognition
    • Bucior I, Scheuring S, Engel A, Burger MM, Carbohydrate-carbohydrate interaction provides adhesion force and specificity for cellular recognition, J Cell Biol 165(4), 529-37 (2004).
    • (2004) J Cell Biol , vol.165 , Issue.4 , pp. 529-537
    • Bucior, I.1    Scheuring, S.2    Engel, A.3    Burger, M.M.4
  • 19
    • 0001988610 scopus 로고
    • Chemical dissolution and in vitro reconstruction of sponge cell adhesions: I. Isolation and functional demonstration of the components involved
    • Humphreys T, Chemical dissolution and in vitro reconstruction of sponge cell adhesions: I. Isolation and functional demonstration of the components involved, Dev Biol 8, 27-47 (1963).
    • (1963) Dev Biol , vol.8 , pp. 27-47
    • Humphreys, T.1
  • 20
    • 0015878882 scopus 로고
    • Characterization of sponge aggregation factor: A unique proteoglycan complex
    • Henkart P, Humphreys S, Humphreys T, Characterization of sponge aggregation factor: A unique proteoglycan complex, Biochemistry 12(16), 3045-50 (1973).
    • (1973) Biochemistry , vol.12 , Issue.16 , pp. 3045-3050
    • Henkart, P.1    Humphreys, S.2    Humphreys, T.3
  • 21
    • 0019316292 scopus 로고
    • Cell-cell recognition: Specific binding of Microciona sponge aggregation factor to homotypic cells and the role of calcium ions
    • Jumblatt JE, Schlup V, Burger MM, Cell-cell recognition: Specific binding of Microciona sponge aggregation factor to homotypic cells and the role of calcium ions, Biochemistry 19(5), 1038-42 (1980).
    • (1980) Biochemistry , vol.19 , Issue.5 , pp. 1038-1042
    • Jumblatt, J.E.1    Schlup, V.2    Burger, M.M.3
  • 22
    • 0025258971 scopus 로고
    • The species-specific cell-binding site of the aggregation factor from the sponge Microciona prolifera is a highly repetitive novel glycan containing glucuronic acid, fucose, and mannose
    • Misevic GN, Burger MM, The species-specific cell-binding site of the aggregation factor from the sponge Microciona prolifera is a highly repetitive novel glycan containing glucuronic acid, fucose, and mannose, J Biol Chem 265(33), 20577-84 (1990).
    • (1990) J Biol Chem , vol.265 , Issue.33 , pp. 20577-20584
    • Misevic, G.N.1    Burger, M.M.2
  • 23
    • 0027462168 scopus 로고
    • Carbohydrate-carbohydrate interactions of a novel acidic glycan can mediate sponge cell adhesion
    • Misevic GN, Burger MM, Carbohydrate-carbohydrate interactions of a novel acidic glycan can mediate sponge cell adhesion, J Biol Chem 268, 4922-29 (1993).
    • (1993) J Biol Chem , vol.268 , pp. 4922-4929
    • Misevic, G.N.1    Burger, M.M.2
  • 24
    • 0029790807 scopus 로고    scopus 로고
    • 4-kDa aggregation factor responsible for species-specific cell adhesion in the marine sponge Microciona prolifera
    • 4-kDa aggregation factor responsible for species-specific cell adhesion in the marine sponge Microciona prolifera, J Biol Chem 271(38), 23558-65 (1996).
    • (1996) J Biol Chem , vol.271 , Issue.38 , pp. 23558-23565
    • Fernandez-Busquets, X.1    Kammerer, R.A.2    Burger, M.M.3
  • 25
    • 0027378268 scopus 로고
    • Characterization of a novel pyruvylated carbohydrate unit implicated in the cell aggregation of the marine sponge Microciona prolifera
    • Spillmann D, Hard K, Thomas-Oates J, Vliegenthart JFG, Misevic G, Burger MM, Finne J, Characterization of a novel pyruvylated carbohydrate unit implicated in the cell aggregation of the marine sponge Microciona prolifera, J Biol Chem 268(18), 13378-87 (1993).
    • (1993) J Biol Chem , vol.268 , Issue.18 , pp. 13378-13387
    • Spillmann, D.1    Hard, K.2    Thomas-Oates, J.3    Vliegenthart, J.F.G.4    Misevic, G.5    Burger, M.M.6    Finne, J.7
  • 26
    • 0028910997 scopus 로고
    • Characterization of a novel sulfated carbohydrate unit implicated in the carbohydrate-carbohydrate-mediated cell aggregation of the marine sponge Microciona prolifera
    • Spillmann D, Thomas-Oates JE, van Kuik JA, Vliegenthart JFG, Misevic G, Burger MM, Finne J, Characterization of a novel sulfated carbohydrate unit implicated in the carbohydrate-carbohydrate-mediated cell aggregation of the marine sponge Microciona prolifera, J Biol Chem 270(10), 5089-97 (1995).
    • (1995) J Biol Chem , vol.270 , Issue.10 , pp. 5089-5097
    • Spillmann, D.1    Thomas-Oates, J.E.2    Van Kuik, J.A.3    Vliegenthart, J.F.G.4    Misevic, G.5    Burger, M.M.6    Finne, J.7
  • 28
    • 0010472032 scopus 로고
    • Monoclonal antibody defining a stage-specific mouse embryonic antigen (SSEA-1)
    • Solter D, Knowles BB, Monoclonal antibody defining a stage-specific mouse embryonic antigen (SSEA-1), Proc Natl Acad Sci USA 75, 5565-69 (1978).
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 5565-5569
    • Solter, D.1    Knowles, B.B.2
  • 29
    • 0019480183 scopus 로고
    • The hapten structure of a developmentally regulated glycolipid antigen (SSEA-1) isolated from human erythrocytes and adenocarcinoma: A preliminary note
    • Hakomori S, Nudelman ED, Levery SB, Solter D, Knowles BB, The hapten structure of a developmentally regulated glycolipid antigen (SSEA-1) isolated from human erythrocytes and adenocarcinoma: A preliminary note, Biochem Biophys Res Commun 100, 1578-86 (1981).
    • (1981) Biochem Biophys Res Commun , vol.100 , pp. 1578-1586
    • Hakomori, S.1    Nudelman, E.D.2    Levery, S.B.3    Solter, D.4    Knowles, B.B.5
  • 30
    • 0020465415 scopus 로고
    • A series of human erythrocyte glycosphingolipids reacting to the monoclonal antibody directed to a developmentally regulated antigen, SSEA-1
    • Kannagi R, Nudelman ED, Levery SB, Hakomori S, A series of human erythrocyte glycosphingolipids reacting to the monoclonal antibody directed to a developmentally regulated antigen, SSEA-1, J Biol Chem 257, 14865-74 (1982).
    • (1982) J Biol Chem , vol.257 , pp. 14865-14874
    • Kannagi, R.1    Nudelman, E.D.2    Levery, S.B.3    Hakomori, S.4
  • 31
    • 0019860424 scopus 로고
    • Stage-specific embryonic antigen involves a1-3 fucosylated type 2 blood group chains
    • Gooi HC, Feizi T, Kapadia A, Knowles BB, Solter D, Evans MJ, Stage-specific embryonic antigen involves a1-3 fucosylated type 2 blood group chains, Nature 292, 156-8 (1981).
    • (1981) Nature , vol.292 , pp. 156-158
    • Gooi, H.C.1    Feizi, T.2    Kapadia, A.3    Knowles, B.B.4    Solter, D.5    Evans, M.J.6
  • 32
    • 0021710314 scopus 로고
    • A multivalent lacto-N-fucopentaose III-lysyllysine conjugate decompacts preimplantation mouse embryos, while the free oligosaccharide is ineffective
    • Fenderson BA, Zehavi U, Hakomori S, A multivalent lacto-N-fucopentaose III-lysyllysine conjugate decompacts preimplantation mouse embryos, while the free oligosaccharide is ineffective, J Exp Med 160, 1591-6 (1984).
    • (1984) J Exp Med , vol.160 , pp. 1591-1596
    • Fenderson, B.A.1    Zehavi, U.2    Hakomori, S.3
  • 33
    • 0001881463 scopus 로고
    • The role of glycoconjugates in embryogenesis
    • edited by Ohyama M, Muramatsu T (Professional Postgraduate Services, Japan)
    • Rosenman SJ, Fenderson BA, Hakomori S, The role of glycoconjugates in embryogenesis, In Glycoconjugates in Medicine, edited by Ohyama M, Muramatsu T (Professional Postgraduate Services, Japan, 1988, pp. 43-50).
    • (1988) Glycoconjugates in Medicine , pp. 43-50
    • Rosenman, S.J.1    Fenderson, B.A.2    Hakomori, S.3
  • 36
    • 0018722341 scopus 로고
    • Cell surface carbohydrates of embryonal carcinoma cells: Polysaccharidic side chains of F9 antigens and of receptors to two lectins, FBP and PNA
    • Muramatsu T, Gachelin G, Damonneville M, Delarbre C, Jacob F, Cell surface carbohydrates of embryonal carcinoma cells: Polysaccharidic side chains of F9 antigens and of receptors to two lectins, FBP and PNA, Cell 18, 183-91 (1979).
    • (1979) Cell , vol.18 , pp. 183-191
    • Muramatsu, T.1    Gachelin, G.2    Damonneville, M.3    Delarbre, C.4    Jacob, F.5
  • 37
    • 84867743573 scopus 로고
    • High molecular weight carbohydrates on embryonal carcinoma cells
    • edited by Muramatsu T, Gachelin G, Moscona AA, Ikawa Y, Japan Scientific Societies Press (Tokyo)
    • Muramatsu T, Muramatsu H, Gachelin G, Jacob F, High molecular weight carbohydrates on embryonal carcinoma cells, In Teratocarcinoma and embryonic cell interactions, edited by Muramatsu T, Gachelin G, Moscona AA, Ikawa Y, Japan Scientific Societies Press (Tokyo, p. 143-56), 1982.
    • (1982) Teratocarcinoma and Embryonic Cell Interactions , pp. 143-156
    • Muramatsu, T.1    Muramatsu, H.2    Gachelin, G.3    Jacob, F.4
  • 39
    • 0037012739 scopus 로고    scopus 로고
    • A model system mimicking glycosphingolipid clusters to quantify carbohydrate self-interactions by surface plasmon resonance
    • Hernaiz MJ, de la Fuente JM, Barrientos AG, Penades S, A model system mimicking glycosphingolipid clusters to quantify carbohydrate self-interactions by surface plasmon resonance, Angew Chem Intl Ed 41(9), 1554-7 (2002).
    • (2002) Angew Chem Intl Ed , vol.41 , Issue.9 , pp. 1554-1557
    • Hernaiz, M.J.1    De La Fuente, J.M.2    Barrientos, A.G.3    Penades, S.4
  • 41
    • 0025894092 scopus 로고
    • Cadherin cell adhesion receptors as a morphogenetic regulator
    • Takeichi M, Cadherin cell adhesion receptors as a morphogenetic regulator, Science 251, 1451-5 (1991).
    • (1991) Science , vol.251 , pp. 1451-1455
    • Takeichi, M.1
  • 42
    • 0028059290 scopus 로고
    • E-cadherin null mutant embryos fail to form a trophectoderm epithelium
    • Larue L, Ohsugi M, Hirchenhain J, Kemler R, E-cadherin null mutant embryos fail to form a trophectoderm epithelium, Proc Natl Acad Sci USA 91, 8263-7 (1994).
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8263-8267
    • Larue, L.1    Ohsugi, M.2    Hirchenhain, J.3    Kemler, R.4
  • 43
    • 0023392668 scopus 로고
    • Mutants of embryonal carcinoma cells defective in the expression of embryoglycan
    • Draber P, Maly P, Mutants of embryonal carcinoma cells defective in the expression of embryoglycan, Proc Natl Acad Sci USA 84, 5798-802 (1987).
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5798-5802
    • Draber, P.1    Maly, P.2
  • 46
    • 0015747788 scopus 로고
    • Altered growth behavior of malignant cells associated with changes in externally labeled glycoprotein and glycolipids
    • Gahmberg CG, Hakomori S, Altered growth behavior of malignant cells associated with changes in externally labeled glycoprotein and glycolipids, Proc Natl Acad Sci USA 70, 3329-33 (1973).
    • (1973) Proc Natl Acad Sci USA , vol.70 , pp. 3329-3333
    • Gahmberg, C.G.1    Hakomori, S.2
  • 47
    • 0345164291 scopus 로고
    • Alteration of cell surface proteins by viral transformation and proteolysis
    • Hynes RO, Alteration of cell surface proteins by viral transformation and proteolysis, Proc Natl Acad Sci USA 70, 3170-4 (1973).
    • (1973) Proc Natl Acad Sci USA , vol.70 , pp. 3170-3174
    • Hynes, R.O.1
  • 49
    • 0242535062 scopus 로고
    • Ganglioside inhibition of fibronectin-mediated cell adhesion to collagen
    • Kleinman HK, Martin GR, Fishman PH, Ganglioside inhibition of fibronectin-mediated cell adhesion to collagen, Proc Natl Acad Sci USA 76, 3367-71 (1979).
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 3367-3371
    • Kleinman, H.K.1    Martin, G.R.2    Fishman, P.H.3
  • 51
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes RO, Integrins: Versatility, modulation, and signaling in cell adhesion, Cell 69, 11-25 (1992).
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 52
    • 0023601045 scopus 로고
    • An Arg-Gly-Asp-directed receptor on the surface of human melanoma cells exists in a divalent cation-dependent functional complex with the disialoganglioside GD2
    • Cheresh DA, Pytela R, Pierschbacher MD, Klier FG, Ruoslahti E, Reisfeld RA, An Arg-Gly-Asp-directed receptor on the surface of human melanoma cells exists in a divalent cation-dependent functional complex with the disialoganglioside GD2, J Cell Biol 105, 1163-73 (1987).
    • (1987) J Cell Biol , vol.105 , pp. 1163-1173
    • Cheresh, D.A.1    Pytela, R.2    Pierschbacher, M.D.3    Klier, F.G.4    Ruoslahti, E.5    Reisfeld, R.A.6
  • 54
    • 0024378959 scopus 로고
    • Specific interaction between gangliotriaosylceramide (Gg3) and sialosyllactosylceramide (GM3) as a basis for specific cellular recognition between lymphoma and melanoma cells
    • Kojima N, Hakomori S. Specific interaction between gangliotriaosylceramide (Gg3) and sialosyllactosylceramide (GM3) as a basis for specific cellular recognition between lymphoma and melanoma cells, J Biol Chem 264, 20159-62 (1989).
    • (1989) J Biol Chem , vol.264 , pp. 20159-20162
    • Kojima, N.1    Hakomori, S.2
  • 55
    • 0025945830 scopus 로고
    • M3-expressing cells based on glycolipid-glycolipid interaction
    • M3-expressing cells based on glycolipid-glycolipid interaction, J Biol Chem 266, 17552-58 (1991).
    • (1991) J Biol Chem , vol.266 , pp. 17552-17558
    • Kojima, N.1    Hakomori, S.2
  • 56
    • 0034596320 scopus 로고    scopus 로고
    • A quantitative estimation of carbohydrate-carbohydrate interaction using clustered oligosaccharides of glycolipid monolayers and of artificial glycoconjugate polymers by surface plasmon resonance
    • Matsuura K, Kitakouji H, Sawada N, Ishida H, Kiso M, Kitajima K, Kobayashi K, A quantitative estimation of carbohydrate-carbohydrate interaction using clustered oligosaccharides of glycolipid monolayers and of artificial glycoconjugate polymers by surface plasmon resonance, J Am Chem Soc 122(30), 7406-7 (2000).
    • (2000) J Am Chem Soc , vol.122 , Issue.30 , pp. 7406-7407
    • Matsuura, K.1    Kitakouji, H.2    Sawada, N.3    Ishida, H.4    Kiso, M.5    Kitajima, K.6    Kobayashi, K.7
  • 57
    • 0016207440 scopus 로고
    • Glycosphingolipids covalently linked to agarose gel or glass beads
    • Laine RA, Yogeeswaran G, Hakomori S, Glycosphingolipids covalently linked to agarose gel or glass beads, J Biol Chem 249, 4460-6 (1974).
    • (1974) J Biol Chem , vol.249 , pp. 4460-4466
    • Laine, R.A.1    Yogeeswaran, G.2    Hakomori, S.3
  • 58
    • 0017904894 scopus 로고
    • Chemical composition, gross structure, and organization of transformation-sensitive glycoproteins
    • Carter WG, Fukuda M, Lingwood C, Hakomori S, Chemical composition, gross structure, and organization of transformation-sensitive glycoproteins, Ann NY Acad Sci 312, 160-77 (1978).
    • (1978) Ann NY Acad Sci , vol.312 , pp. 160-177
    • Carter, W.G.1    Fukuda, M.2    Lingwood, C.3    Hakomori, S.4
  • 59
    • 0020036796 scopus 로고
    • Cell surface antigens of a clonal human embryonal carcinoma cell line: Morphological and antigenic differentiation in culture
    • Andrews PW, Goodfellow PN, Shevinsky LH, Bronson DL, Knowles BB, Cell surface antigens of a clonal human embryonal carcinoma cell line: Morphological and antigenic differentiation in culture, Int J Cancer 29, 523-31 (1982).
    • (1982) Int J Cancer , vol.29 , pp. 523-531
    • Andrews, P.W.1    Goodfellow, P.N.2    Shevinsky, L.H.3    Bronson, D.L.4    Knowles, B.B.5
  • 60
    • 0021321996 scopus 로고
    • Pluripotent embryonal carcinoma clones derived from the human teratocarcinoma cell line TERA-2: Differentiation in vivo and in vitro
    • Andrews PW, Damjanov I, Simon D, Banting G, Carlin C, Dracopoli NC, Fogh J, Pluripotent embryonal carcinoma clones derived from the human teratocarcinoma cell line TERA-2: Differentiation in vivo and in vitro. Lab Invest 50, 147-62 (1984).
    • (1984) Lab Invest , vol.50 , pp. 147-162
    • Andrews, P.W.1    Damjanov, I.2    Simon, D.3    Banting, G.4    Carlin, C.5    Dracopoli, N.C.6    Fogh, J.7
  • 61
    • 0023219544 scopus 로고
    • Human embryonal carcinoma cells and their differentiation in culture
    • Andrews PW, Fenderson BA, Hakomori S, Human embryonal carcinoma cells and their differentiation in culture, Int J Androl 10, 95-104 (1987).
    • (1987) Int J Androl , vol.10 , pp. 95-104
    • Andrews, P.W.1    Fenderson, B.A.2    Hakomori, S.3
  • 62
    • 0020957226 scopus 로고
    • New globoseries glycosphingolipids in human teratocarcinoma reactive with the monoclonal antibody directed to a developmentally regulated antigen, stage-specific embryonic antigen 3
    • Kannagi R, Levery SB, Ishigami F, Hakomori S, Shevinsky LH, Knowles BB, Solter D, New globoseries glycosphingolipids in human teratocarcinoma reactive with the monoclonal antibody directed to a developmentally regulated antigen, stage-specific embryonic antigen 3, J Biol Chem 258, 8934-42 (1983).
    • (1983) J Biol Chem , vol.258 , pp. 8934-8942
    • Kannagi, R.1    Levery, S.B.2    Ishigami, F.3    Hakomori, S.4    Shevinsky, L.H.5    Knowles, B.B.6    Solter, D.7
  • 63
    • 0020997754 scopus 로고
    • Stage-specific embryonic antigens (SSEA-3 and -4) are epitopes of a unique globo-series ganglioside isolated from human teratocarcinoma cells
    • Kannagi R, Cochran NA, Ishigami F, Hakomori S, Andrews PW, Knowles BB, Solter D, Stage-specific embryonic antigens (SSEA-3 and -4) are epitopes of a unique globo-series ganglioside isolated from human teratocarcinoma cells, EMBO J 2, 2355-61 (1983).
    • (1983) EMBO J , vol.2 , pp. 2355-2361
    • Kannagi, R.1    Cochran, N.A.2    Ishigami, F.3    Hakomori, S.4    Andrews, P.W.5    Knowles, B.B.6    Solter, D.7
  • 64
    • 0032579279 scopus 로고    scopus 로고
    • Globoside-dependent adhesion of human embryonal carcinoma cells, based on carbohydrate-carbohydrate interaction, initiates signal transduction and induces enhanced activity of transcription factors AP1 and CREB
    • Yu S, Withers DA, Hakomori S, Globoside-dependent adhesion of human embryonal carcinoma cells, based on carbohydrate-carbohydrate interaction, initiates signal transduction and induces enhanced activity of transcription factors AP1 and CREB, J Biol Chem 273, 2517-25 (1998).
    • (1998) J Biol Chem , vol.273 , pp. 2517-2525
    • Yu, S.1    Withers, D.A.2    Hakomori, S.3
  • 66
    • 0000988187 scopus 로고
    • Measurement of forces between two mica surfaces in aqueous electrolyte solutions in the range 0-100 nm
    • Israelachvili JN, Adams GE, Measurement of forces between two mica surfaces in aqueous electrolyte solutions in the range 0-100 nm, J Chem Soc Faraday Trans 74, 975-1001 (1978).
    • (1978) J Chem Soc Faraday Trans , vol.74 , pp. 975-1001
    • Israelachvili, J.N.1    Adams, G.E.2
  • 68
    • 0028949325 scopus 로고
    • Binding strength between cell adhesion proteoglycans measured by atomic force microscopy
    • Dammer U, Popescu O, Wagner P, Anselmetti D, Guntherodt H-J, Misevic GN, Binding strength between cell adhesion proteoglycans measured by atomic force microscopy, Science 267, 1173-75 (1995).
    • (1995) Science , vol.267 , pp. 1173-1175
    • Dammer, U.1    Popescu, O.2    Wagner, P.3    Anselmetti, D.4    Guntherodt, H.-J.5    Misevic, G.N.6
  • 69
    • 0032262087 scopus 로고    scopus 로고
    • Carbohydrate-carbohydrate interaction between glycolipids and glycoconjugate polystyrenes at the air-water interface
    • Matsuura K, Kitakouji H, Tsuchida A, Sawada N, Ishida H, Kiso M, Kobayashi K, Carbohydrate-carbohydrate interaction between glycolipids and glycoconjugate polystyrenes at the air-water interface, Chem Letters 1998, 1293-4 (1998).
    • (1998) Chem Letters , vol.1998 , pp. 1293-1294
    • Matsuura, K.1    Kitakouji, H.2    Tsuchida, A.3    Sawada, N.4    Ishida, H.5    Kiso, M.6    Kobayashi, K.7
  • 70
    • 0037414924 scopus 로고    scopus 로고
    • Probing specificity in carbohydrate-carbohydrate interactions with micelles and Langmuir monolayers
    • Santacroce PV, Basu A, Probing specificity in carbohydrate-carbohydrate interactions with micelles and Langmuir monolayers, Angew Chem Intl Ed 42(1), 95-8 (2003).
    • (2003) Angew Chem Intl Ed , vol.42 , Issue.1 , pp. 95-98
    • Santacroce, P.V.1    Basu, A.2
  • 71
    • 0035896632 scopus 로고    scopus 로고
    • Carbohydrate-carbohydrate binding of ganglioside to integrin a5 modulates a5b1 function
    • Wang X, Sun P, Al-Qamari A, Tai T, Kawashima I, Paller AS, Carbohydrate-carbohydrate binding of ganglioside to integrin a5 modulates a5b1 function, J Biol Chem 276(11), 8436-44 (2001).
    • (2001) J Biol Chem , vol.276 , Issue.11 , pp. 8436-8444
    • Wang, X.1    Sun, P.2    Al-Qamari, A.3    Tai, T.4    Kawashima, I.5    Paller, A.S.6
  • 72
    • 0037072814 scopus 로고    scopus 로고
    • Tetraspanin CD9 is a "proteolipid", and its interaction with a3 integrin in microdomain is promoted by GM3 ganglioside, leading to inhibition of laminin-5-dependent cell motility
    • Kawakami Y, Kawakami K, Steelant WFA, Ono M, Baek RC, Handa K, Withers DA, Hakomori S, Tetraspanin CD9 is a "proteolipid", and its interaction with a3 integrin in microdomain is promoted by GM3 ganglioside, leading to inhibition of laminin-5-dependent cell motility, J Biol Chem 277(37), 34349-58 (2002).
    • (2002) J Biol Chem , vol.277 , Issue.37 , pp. 34349-34358
    • Kawakami, Y.1    Kawakami, K.2    Wfa, S.3    Ono, M.4    Baek, R.C.5    Handa, K.6    Withers, D.A.7    Hakomori, S.8
  • 73
    • 0034922456 scopus 로고    scopus 로고
    • Epidermal growth factor receptor glycosylation is required for ganglioside GM3 binding and GM3-mediated suppression of activation
    • Wang X-Q, Sun P, O'Gorman M, Tai T, Paller AS, Epidermal growth factor receptor glycosylation is required for ganglioside GM3 binding and GM3-mediated suppression of activation, Glycobiology 11(7), 515-22 (2001).
    • (2001) Glycobiology , vol.11 , Issue.7 , pp. 515-522
    • Wang, X.-Q.1    Sun, P.2    O'Gorman, M.3    Tai, T.4    Paller, A.S.5
  • 74
    • 0035895916 scopus 로고    scopus 로고
    • Glycosylation-induced conformational modification positively regulates receptor-receptor association: A study with an aberrant epidermal growth factor receptor (EGFRvIII/DEGFR) expressed in cancer cells
    • Fernandes H, Cohen S, Bishayee S, Glycosylation-induced conformational modification positively regulates receptor-receptor association: A study with an aberrant epidermal growth factor receptor (EGFRvIII/DEGFR) expressed in cancer cells, J Biol Chem 276(7), 5375-83 (2001).
    • (2001) J Biol Chem , vol.276 , Issue.7 , pp. 5375-5383
    • Fernandes, H.1    Cohen, S.2    Bishayee, S.3
  • 75
    • 0034698077 scopus 로고    scopus 로고
    • The Asn-420-linked sugar chain in human epidermal growth factor receptor suppresses ligand-independent spontaneous oligomerization
    • Tsuda T, Ikeda Y, Taniguchi N, The Asn-420-linked sugar chain in human epidermal growth factor receptor suppresses ligand-independent spontaneous oligomerization, J Biol Chem 275, 21988-94 (2000).
    • (2000) J Biol Chem , vol.275 , pp. 21988-21994
    • Tsuda, T.1    Ikeda, Y.2    Taniguchi, N.3
  • 76
    • 0023025941 scopus 로고
    • 3 on tyrosine phosphorylation of the epidermal growth factor receptor
    • 3 on tyrosine phosphorylation of the epidermal growth factor receptor, J Biol Chem 261, 2434-40 (1986).
    • (1986) J Biol Chem , vol.261 , pp. 2434-2440
    • Bremer, E.G.1    Schlessinger, J.2    Hakomori, S.3
  • 79
    • 0026788506 scopus 로고
    • Cell adhesion in a dynamic flow system as compared to static system: Glycosphingolipid-glycosphingolipid interaction in the dynamic system predominates over lectin- Or integrin-based mechanisms in adhesion of B16 melanoma cells to non-activated endothelial cells
    • Kojima N, Shiota M, Sadahira Y, Handa K, Hakomori S, Cell adhesion in a dynamic flow system as compared to static system: Glycosphingolipid- glycosphingolipid interaction in the dynamic system predominates over lectin- or integrin-based mechanisms in adhesion of B16 melanoma cells to non-activated endothelial cells, J Biol Chem 267, 17264-70 (1992).
    • (1992) J Biol Chem , vol.267 , pp. 17264-17270
    • Kojima, N.1    Shiota, M.2    Sadahira, Y.3    Handa, K.4    Hakomori, S.5
  • 80
    • 0030610238 scopus 로고    scopus 로고
    • 2+ with hydroxy and non-hydroxy fatty acid species of cerebroside sulfate by Fourier transform infrared spectroscopy and molecular modeling
    • 2+ with hydroxy and non-hydroxy fatty acid species of cerebroside sulfate by Fourier transform infrared spectroscopy and molecular modeling, Biochemistry 36, 3438-47 (1997).
    • (1997) Biochemistry , vol.36 , pp. 3438-3447
    • Menikh, A.1    Nyholm, P.-G.2    Boggs, J.M.3
  • 81
    • 0037022620 scopus 로고    scopus 로고
    • Binding of rainbow trout sperm to egg is mediated by strong carbohydrate-to-carbohydrate interaction between (KDN)GM3 (deaminated neuraminyl ganglioside) and Gg3-like epitope
    • Yu S, Kojima N, Hakomori S, Kudo S, Inoue S, Inoue Y, Binding of rainbow trout sperm to egg is mediated by strong carbohydrate-to-carbohydrate interaction between (KDN)GM3 (deaminated neuraminyl ganglioside) and Gg3-like epitope, Proc Natl Acad Sci USA 99(5), 2854-59 (2002).
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.5 , pp. 2854-2859
    • Yu, S.1    Kojima, N.2    Hakomori, S.3    Kudo, S.4    Inoue, S.5    Inoue, Y.6
  • 82
    • 0030590091 scopus 로고    scopus 로고
    • Carbohydrate-mediated sorting in aggregating embryonal carcinoma cells
    • Boubelik M, Dráberova L, Draber P, Carbohydrate-mediated sorting in aggregating embryonal carcinoma cells, Biochem Biophys Res Commun 224, 283-88 (1996).
    • (1996) Biochem Biophys Res Commun , vol.224 , pp. 283-288
    • Boubelik, M.1    Dráberová, L.2    Draber, P.3
  • 83
    • 0026336463 scopus 로고
    • Synergistic effect of two cell recognition systems: Glycosphingolipid- glycosphingolipid interaction and integrin receptor interaction with pericellular matrix protein
    • Kojima N, Hakomori S, Synergistic effect of two cell recognition systems: Glycosphingolipid-glycosphingolipid interaction and integrin receptor interaction with pericellular matrix protein, Glycobiology 1, 623-30 (1991).
    • (1991) Glycobiology , vol.1 , pp. 623-630
    • Kojima, N.1    Hakomori, S.2
  • 84
    • 0025817934 scopus 로고
    • Cell adhesion molecules: Implications for a molecular histology
    • Edelman GM, Crossin KL, Cell adhesion molecules: Implications for a molecular histology, Annu Rev Biochem 60, 155-90 (1991).
    • (1991) Annu Rev Biochem , vol.60 , pp. 155-190
    • Edelman, G.M.1    Crossin, K.L.2
  • 86
    • 4544250815 scopus 로고    scopus 로고
    • Cell growth regulation through GM3-enriched microdomain in human lung embryonal fibroblast WI38 and its oncogenic transformant VA13
    • in press
    • Toledo MS, Suzuki E, Handa K, Hakomori S, Cell growth regulation through GM3-enriched microdomain in human lung embryonal fibroblast WI38 and its oncogenic transformant VA13, J Biol Chem (in press) (2004).
    • (2004) J Biol Chem
    • Toledo, M.S.1    Suzuki, E.2    Handa, K.3    Hakomori, S.4
  • 87
    • 0034804399 scopus 로고    scopus 로고
    • Association of MUC-1 and PSGL-1 with low-density microdomain in T-lymphocytes: A preliminary note
    • Handa K, Jacobs F, Longenecker BM, Hakomori S, Association of MUC-1 and PSGL-1 with low-density microdomain in T-lymphocytes: A preliminary note, Biochem Biophys Res Commun 285, 788-94 (2001).
    • (2001) Biochem Biophys Res Commun , vol.285 , pp. 788-794
    • Handa, K.1    Jacobs, F.2    Longenecker, B.M.3    Hakomori, S.4


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