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Volumn 39, Issue 1, 2011, Pages 355-359

Expression and potential biological role of α(1,2)fucosylated glycotopes on amniotic and seminal fibronectins

Author keywords

(1,2) fucose containing epitope; Amniotic fluid; Fibronectin; Glycomarker; Seminal plasma; Ulex europaeus agglutinin

Indexed keywords

FIBRONECTIN; FUCOSE; GLYCOPROTEIN;

EID: 79551493033     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST0390355     Document Type: Conference Paper
Times cited : (12)

References (49)
  • 2
    • 33748569518 scopus 로고    scopus 로고
    • Lower expression of α(2,3)- sialylated fibronectin glycoform and appearance of asialo-FN glycoform associate with high concentration of fibronectin in human seminal plasma with abnormal semen parameters
    • Ka̧tnik-Prastowska, I., Kratz, M.E., Faundez, R. and Chełmońska-Soyta, A. (2006) Lower expression of α(2,3)- sialylated fibronectin glycoform and appearance of asialo-FN glycoform associate with high concentration of fibronectin in human seminal plasma with abnormal semen parameters. Clin. Chem. Lab. Med. 44, 1119-1125
    • (2006) Clin. Chem. Lab. Med. , vol.44 , pp. 1119-1125
    • Ka̧tnik-Prastowska, I.1    Kratz, M.E.2    Faundez, R.3    Chełmoń ska-Soyta, A.4
  • 3
    • 33847136152 scopus 로고    scopus 로고
    • Amniotic fibronectin fragmentation and domain and sialyl- and fucosyl-glycotope expression associated with pregnancy complicated by intrauterine infection
    • Hirnle, L. and Ka̧tnik-Prastowska, I. (2007) Amniotic fibronectin fragmentation and domain and sialyl- and fucosyl-glycotope expression associated with pregnancy complicated by intrauterine infection. Clin. Chem. Lab. Med. 45, 208-214
    • (2007) Clin. Chem. Lab. Med. , vol.45 , pp. 208-214
    • Hirnle, L.1    Ka̧tnik-Prastowska, I.2
  • 4
    • 35648976089 scopus 로고    scopus 로고
    • Relative sialylation and fucosylation of synovial and plasma fibronectins in relation to the progression and activity of rheumatoid arthritis
    • Przybysz, M., Maszczak, D., Borysewicz, K., Szechiński, J. and Ka̧tnik-Prastowska, I. (2007) Relative sialylation and fucosylation of synovial and plasma fibronectins in relation to the progression and activity of rheumatoid arthritis. Glycoconjugate J. 24, 543-550
    • (2007) Glycoconjugate J. , vol.24 , pp. 543-550
    • Przybysz, M.1    Maszczak, D.2    Borysewicz, K.3    Szechiński, J.4    Ka̧tnik-Prastowska, I.5
  • 5
    • 28444460388 scopus 로고    scopus 로고
    • Differential analysis of site-specific glycans on plasma and cellular fibronectins: Application of a hydrophilic affinity method for glycopeptide enrichment
    • Tajiri, M., Yoshida, S. and Wada, Y. (2005) Differential analysis of site-specific glycans on plasma and cellular fibronectins: application of a hydrophilic affinity method for glycopeptide enrichment. Glycobiology 15, 1332-1340
    • (2005) Glycobiology , vol.15 , pp. 1332-1340
    • Tajiri, M.1    Yoshida, S.2    Wada, Y.3
  • 6
    • 0028816805 scopus 로고
    • Influence of carbohydrate on structure, stability and function of gelatin-binding fragments of fibronectin
    • Ingham, K.C., Brew, S.A. and Novokhatny, V.V. (1985) Influence of carbohydrate on structure, stability and function of gelatin-binding fragments of fibronectin. Arch. Biochem. Biophys. 316, 235-240
    • (1985) Arch. Biochem. Biophys. , vol.316 , pp. 235-240
    • Ingham, K.C.1    Brew, S.A.2    Novokhatny, V.V.3
  • 7
    • 23644433820 scopus 로고    scopus 로고
    • 9F1 module pair of human fibronectin requires site-specific N-glycosylation
    • 9F1 module pair of human fibronectin requires site-specific N-glycosylation. FEBS Lett. 579, 4529-4534
    • (2005) FEBS Lett. , vol.579 , pp. 4529-4534
    • Millard, C.J.1    Campbell, I.D.2    Pickford, A.R.3
  • 8
    • 0032512876 scopus 로고    scopus 로고
    • Solution structure of the glycosylated second type 2 module of fibronectin
    • Sticht, H., Pickford, A.R., Potts, J.R. and Campbell, I.D. (1998) Solution structure of the glycosylated second type 2 module of fibronectin. J. Mol. Biol. 276, 177-187
    • (1998) J. Mol. Biol. , vol.276 , pp. 177-187
    • Sticht, H.1    Pickford, A.R.2    Potts, J.R.3    Campbell, I.D.4
  • 9
    • 0022979093 scopus 로고
    • Fibronectin glycosylation modulates fibroblast adhesion and spreading
    • Jones, G.E., Arumugham, R.G. and Tanzer, M.L. (1986) Fibronectin glycosylation modulates fibroblast adhesion and spreading. J. Cell. Biol. 103, 1663-1670
    • (1986) J. Cell. Biol. , vol.103 , pp. 1663-1670
    • Jones, G.E.1    Arumugham, R.G.2    Tanzer, M.L.3
  • 10
    • 0024316015 scopus 로고
    • An α-N-acetylgalactosaminylation at the threonine residue of a defined peptide sequence creates the oncofetal peptide epitope in human fibronectin
    • Matsuura, H., Greene, T. and Hakomori, S. (1989) An α-N- acetylgalactosaminylation at the threonine residue of a defined peptide sequence creates the oncofetal peptide epitope in human fibronectin. J. Biol. Chem. 264, 10472-10476
    • (1989) J. Biol. Chem. , vol.264 , pp. 10472-10476
    • Matsuura, H.1    Greene, T.2    Hakomori, S.3
  • 11
    • 0026064118 scopus 로고
    • Human plasma fibronectin: Demonstration of structural differences between the A- and B-chains in the IIICS region
    • Tressel, T., McCarthy, J.B., Calaycay, J., Le, T.D., Legesse, K., Shively, J.E. and Pande, H. (1991) Human plasma fibronectin: demonstration of structural differences between the A- and B-chains in the IIICS region. Biochem. J. 274, 731-738
    • (1991) Biochem. J. , vol.274 , pp. 731-738
    • Tressel, T.1    McCarthy, J.B.2    Calaycay, J.3    Le, T.D.4    Legesse, K.5    Shively, J.E.6    Pande, H.7
  • 12
    • 0036252587 scopus 로고    scopus 로고
    • Enhanced expression of a peanut agglutinin reactive O-linked oligosaccharide on fibronectins from the synovial fluid of patients with rheumatic disease, quantitation, domain localization, and functional significance
    • Carsons, S. (2002) Enhanced expression of a peanut agglutinin reactive O-linked oligosaccharide on fibronectins from the synovial fluid of patients with rheumatic disease, quantitation, domain localization, and functional significance. J. Rheumatol. 29, 896-902
    • (2002) J. Rheumatol. , vol.29 , pp. 896-902
    • Carsons, S.1
  • 13
    • 0024835314 scopus 로고
    • Developmental changes in the glycosylation and binding properties of human fibronectins: Characterization of glycan structures and ligand binding of human fibronectins from adult plasma, cord blood and amniotic fluid
    • Köttgen, E., Hell, B., Müller, C., Kainer, F. and Tauber, R. (1989) Developmental changes in the glycosylation and binding properties of human fibronectins: characterization of glycan structures and ligand binding of human fibronectins from adult plasma, cord blood and amniotic fluid. Biol. Chem. Hoppe-Seyler 370, 1285-1294
    • (1989) Biol. Chem. Hoppe-Seyler , vol.370 , pp. 1285-1294
    • Köttgen, E.1    Hell, B.2    Müller, C.3    Kainer, F.4    Tauber, R.5
  • 16
    • 0020490791 scopus 로고
    • Carbohydrate structure of hamster plasma fibronectin: Evidence for chemical diversity between cellular and plasma fibronectins
    • Fukuda, M., Levery, S.B. and Hakomori, S. (1982) Carbohydrate structure of hamster plasma fibronectin: evidence for chemical diversity between cellular and plasma fibronectins. J. Biol. Chem. 257, 6856-6860
    • (1982) J. Biol. Chem. , vol.257 , pp. 6856-6860
    • Fukuda, M.1    Levery, S.B.2    Hakomori, S.3
  • 17
    • 0021959950 scopus 로고
    • Structure of the carbohydrate units of human amniotic fluid fibronectin
    • Krusius, T., Fukuda, M., Dell, A. and Ruoslahti, E. (1985) Structure of the carbohydrate units of human amniotic fluid fibronectin. J. Biol. Chem. 260, 4110-4116
    • (1985) J. Biol. Chem. , vol.260 , pp. 4110-4116
    • Krusius, T.1    Fukuda, M.2    Dell, A.3    Ruoslahti, E.4
  • 18
    • 0024335289 scopus 로고
    • Structure of asparagine-linked oligosaccharides of human placental fibronectin
    • Tokyo
    • Takamoto, M., Endo, T., Isemura, M., Kochibe, N. and Kobata, A. (1989) Structure of asparagine-linked oligosaccharides of human placental fibronectin. J. Biochem. (Tokyo) 105, 742-750
    • (1989) J. Biochem. , vol.105 , pp. 742-750
    • Takamoto, M.1    Endo, T.2    Isemura, M.3    Kochibe, N.4    Kobata, A.5
  • 19
    • 79551504775 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted
  • 20
    • 0034350549 scopus 로고    scopus 로고
    • The 2.2 Å resolution structure of the O(H) blood-group-specific lectin I from Ulex europaeus
    • Audette, G.F., Vandonselaar, M. and Delbaere, L.T.J. (2000) The 2.2 Å resolution structure of the O(H) blood-group-specific lectin I from Ulex europaeus. J. Mol. Biol. 304, 423-433
    • (2000) J. Mol. Biol. , vol.304 , pp. 423-433
    • Audette, G.F.1    Vandonselaar, M.2    Delbaere, L.T.J.3
  • 24
    • 0033980308 scopus 로고    scopus 로고
    • α(1,2)Fucosylation prevents sialyl Lewis X expression and E-selectin-mediated adhesion of fucosyltransferase VII-transfected cells
    • Zerfaoui, M., Fukuda, M., Sbarra, V., Lombardo, D. and El-Battari, A. (2000) α(1,2)fucosylation prevents sialyl Lewis X expression and E-selectin-mediated adhesion of fucosyltransferase VII-transfected cells Eur. J. Biochem. 267, 53-61
    • (2000) Eur. J. Biochem. , vol.267 , pp. 53-61
    • Zerfaoui, M.1    Fukuda, M.2    Sbarra, V.3    Lombardo, D.4    El-Battari, A.5
  • 25
    • 24044534176 scopus 로고    scopus 로고
    • Increased sialylation and defucosylation of plasma proteins are early events in the acute phase response
    • Chavan, M.M., Kawle, P.D. and Mehta, N.G. (2005) Increased sialylation and defucosylation of plasma proteins are early events in the acute phase response. Glycobiology 15, 838-848
    • (2005) Glycobiology , vol.15 , pp. 838-848
    • Chavan, M.M.1    Kawle, P.D.2    Mehta, N.G.3
  • 26
    • 0038495798 scopus 로고    scopus 로고
    • Fucose: Biosynthesis and biological function in mammals
    • Becker, D.J. and Lowe, J.B. (2003) Fucose: biosynthesis and biological function in mammals. Glycobiology 13, 41R-53R
    • (2003) Glycobiology , vol.13
    • Becker, D.J.1    Lowe, J.B.2
  • 29
    • 67049095491 scopus 로고    scopus 로고
    • Comprehensive clinico-glycomic study of 16 colorectal cancer specimens: Elucidation of aberrant glycosylation and its mechanistic causes in colorectal cancer cells
    • Misonou, Y., Shida, K., Korekane, H., Seki, Y., Noura, S., Ohue, M. and Miyamoto, Y. (2009) Comprehensive clinico-glycomic study of 16 colorectal cancer specimens: elucidation of aberrant glycosylation and its mechanistic causes in colorectal cancer cells. J. Proteome Res. 8, 2990-3005
    • (2009) J. Proteome Res. , vol.8 , pp. 2990-3005
    • Misonou, Y.1    Shida, K.2    Korekane, H.3    Seki, Y.4    Noura, S.5    Ohue, M.6    Miyamoto, Y.7
  • 30
    • 77954520377 scopus 로고    scopus 로고
    • O-linked oligosaccharides from salivary agglutinin: Helicobacter pylori binding sialyl-Lewis X and Lewis B are terminating moieties on hyperfucosylated oligo-N-acetyllactosamine
    • Issa, S., Moran, A.P., Ustinov, S.N., Lin, J.H.-H., Ligtenberg, A.J. and Karlsson, N.G. (2010) O-linked oligosaccharides from salivary agglutinin: Helicobacter pylori binding sialyl-Lewis X and Lewis B are terminating moieties on hyperfucosylated oligo-N-acetyllactosamine. Glycobiology 20, 1046-1057
    • (2010) Glycobiology , vol.20 , pp. 1046-1057
    • Issa, S.1    Moran, A.P.2    Ustinov, S.N.3    Lin, J.H.-H.4    Ligtenberg, A.J.5    Karlsson, N.G.6
  • 31
    • 28344433526 scopus 로고    scopus 로고
    • Relative amounts of sialic acid and fucose of amniotic fluid glycoconjugates in relation to pregnancy age
    • Orczyk-Pawiłowicz, M., Floriański, J., Zalewski, J. and Ka̧tnik-Prastowska, I. (2005) Relative amounts of sialic acid and fucose of amniotic fluid glycoconjugates in relation to pregnancy age. Glycoconjugate J. 22, 433-442
    • (2005) Glycoconjugate J. , vol.22 , pp. 433-442
    • Orczyk-Pawiłowicz, M.1    Floriański, J.2    Zalewski, J.3    Ka̧tnik-Prastowska, I.4
  • 32
    • 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., Dell, A. and Clark, G.F. (2009) Analysis of the human seminal plasma glycome reveals the presence of immunomodulatory carbohydrate functional groups. J. Proteome Res. 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    Dell, A.5    Clark, G.F.6
  • 33
    • 0036591696 scopus 로고    scopus 로고
    • High level of α1-acid glycoprotein in human seminal plasma is associated with high branching and expression of Lewis A groups on its glycans: Supporting evidence for a prostatic origin
    • Poland, D.C., Kratz, E., Vermeiden, J.P., de Groot, S.M., Bruyneel, B., de Vries, T. and van Dijk, W. (2002) High level of α1-acid glycoprotein in human seminal plasma is associated with high branching and expression of Lewis A groups on its glycans: supporting evidence for a prostatic origin. Prostate 52, 34-42
    • (2002) Prostate , vol.52 , pp. 34-42
    • Poland, D.C.1    Kratz, E.2    Vermeiden, J.P.3    De Groot, S.M.4    Bruyneel, B.5    De Vries, T.6    Van Dijk, W.7
  • 34
    • 33144460070 scopus 로고    scopus 로고
    • Meet the multifunctional and sexy glycoforms of glycodelin
    • Lapid, K. and Sharon, N. (2006) Meet the multifunctional and sexy glycoforms of glycodelin. Glycobiology 16, 39R-45R
    • (2006) Glycobiology , vol.16
    • Lapid, K.1    Sharon, N.2
  • 37
    • 13444257534 scopus 로고    scopus 로고
    • A role for fucose α(1-2) galactose carbohydrates in neuronal growth
    • Kulovidouris, S.A., Gama, C.I., Lee, L.W. and Hsieh-Wilson, L.C. (2005) A role for fucose α(1-2) galactose carbohydrates in neuronal growth. J. Am. Chem. Soc. 127, 1340-1341
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 1340-1341
    • Kulovidouris, S.A.1    Gama, C.I.2    Lee, L.W.3    Hsieh-Wilson, L.C.4
  • 38
    • 68049114414 scopus 로고    scopus 로고
    • Identification of the plasticity-relevant fucose-α(1-2) galactose proteome from the mouse olfactory bulb
    • Murrey, H.E., Ficarro, S.B., Krishnamurthy, C., Domino, S.E., Peters, E.C. and Hsieh-Wilson, L.C. (2009) Identification of the plasticity-relevant fucose-α(1-2) galactose proteome from the mouse olfactory bulb. Biochemistry 48, 7261-7270
    • (2009) Biochemistry , vol.48 , pp. 7261-7270
    • Murrey, H.E.1    Ficarro, S.B.2    Krishnamurthy, C.3    Domino, S.E.4    Peters, E.C.5    Hsieh-Wilson, L.C.6
  • 39
    • 0035054508 scopus 로고    scopus 로고
    • Glycans as legislators of host-microbial interactions: Spanning the spectrum from symbiosis to pathogenicity
    • Hooper, L.V. and Gordon, J.I. (2001) Glycans as legislators of host-microbial interactions: spanning the spectrum from symbiosis to pathogenicity. Glycobiology 11, 1R-10R
    • (2001) Glycobiology , vol.11
    • Hooper, L.V.1    Gordon, J.I.2
  • 41
    • 23944482922 scopus 로고    scopus 로고
    • Human-milk glycans protect infants against enteric pathogens
    • Newburg, D.S., Ruiz-Palacios, G.M. and Morrow, A.L. (2005) Human-milk glycans protect infants against enteric pathogens. Annu. Rev. Nutr. 25, 37-58
    • (2005) Annu. Rev. Nutr. , vol.25 , pp. 37-58
    • Newburg, D.S.1    Ruiz-Palacios, G.M.2    Morrow, A.L.3
  • 42
    • 28844459379 scopus 로고    scopus 로고
    • Fibronectin fibrillogenesis, a cell-mediated matrix assembly process
    • Mao, Y. and Schwarzbauer, J.E. (2005) Fibronectin fibrillogenesis, a cell-mediated matrix assembly process. Matrix Biol. 24, 389-399
    • (2005) Matrix Biol. , vol.24 , pp. 389-399
    • Mao, Y.1    Schwarzbauer, J.E.2
  • 44
    • 0037107551 scopus 로고    scopus 로고
    • Fibronectin at a glance
    • Pankov, R. and Yamada, K.M. (2002) Fibronectin at a glance. J. Cell Sci. 115, 3861-3863
    • (2002) J. Cell Sci. , vol.115 , pp. 3861-3863
    • Pankov, R.1    Yamada, K.M.2
  • 46
    • 0034142123 scopus 로고    scopus 로고
    • Soluble fibronectin interaction with cell surface and extracellular matrix is mediated by carbohydrate-to-carbohydrate interaction
    • Zheng, M. and Hakomori, S.I. (2000) Soluble fibronectin interaction with cell surface and extracellular matrix is mediated by carbohydrate-to- carbohydrate interaction. Arch. Biochem. Biophys. 374, 93-99
    • (2000) Arch. Biochem. Biophys. , vol.374 , pp. 93-99
    • Zheng, M.1    Hakomori, S.I.2
  • 47
    • 73849129236 scopus 로고    scopus 로고
    • Campylobacter jeluni FlpA binds fibronectin and is required for maximal host cell adherence
    • Konkel, M.E., Larson, C.L. and Flanagan, R.C. (2010) Campylobacter jeluni FlpA binds fibronectin and is required for maximal host cell adherence. J. Bacteriol. 192, 68-76
    • (2010) J. Bacteriol. , vol.192 , pp. 68-76
    • Konkel, M.E.1    Larson, C.L.2    Flanagan, R.C.3
  • 48
    • 39749123209 scopus 로고    scopus 로고
    • Fibronectin enhances Campylobacter fetus interaction with extracellular matrix components and INT 407 cells
    • Graham, L.L., Friel, T. and Woodman, R.L. (2008) Fibronectin enhances Campylobacter fetus interaction with extracellular matrix components and INT 407 cells. Can J. Microbiol. 54, 37-47
    • (2008) Can J. Microbiol. , vol.54 , pp. 37-47
    • Graham, L.L.1    Friel, T.2    Woodman, R.L.3


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