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Volumn 20, Issue 1, 1996, Pages 11-20

Fucosylated glycoconjugates of the human spermatozoon. Comparison of the domains of these glycoconjugates with the α-fucosyl binding sites, and with lactosaminic glycoconjugates and β-D-galactosyl binding site domains

Author keywords

Fucose; Glycoconjugates; Human spermatozoon

Indexed keywords

AMINOSUGAR; FLUORESCEIN ISOTHIOCYANATE; FOLLITROPIN; FUCOSE; GALACTOSE; GLYCOCONJUGATE; LACTOSAMINE; LECTIN; LUTEINIZING HORMONE;

EID: 0030115910     PISSN: 03279545     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (21)

References (53)
  • 2
    • 0023645052 scopus 로고
    • The role of asparagine-linked carbohydrate in Natural Killer cell-mediated cytolysis
    • AHRENS PB, ANKEL H (1987). The role of asparagine-linked carbohydrate in Natural Killer cell-mediated cytolysis. J Biol Chem 262: 7575-7579.
    • (1987) J Biol Chem , vol.262 , pp. 7575-7579
    • Ahrens, P.B.1    Ankel, H.2
  • 3
    • 0020371271 scopus 로고
    • Fertilization studies in the hamster: The role of cell surface carbohydrates
    • AHUJA KK (1982). Fertilization studies in the hamster: The role of cell surface carbohydrates. Expl Cell Res 140: 353-362.
    • (1982) Expl Cell Res , vol.140 , pp. 353-362
    • Ahuja, K.K.1
  • 4
    • 0027498916 scopus 로고
    • Human sperm fertilizing potential in vitro is correlated with differential expression of a head-specific mannose-ligand receptor
    • BENOFF S, COOPER GW, HURLEY IH, NAPOLITANO B, ROSENFELD DL, SCHOLL GM, HERSHLANG A (1993). Human sperm fertilizing potential in vitro is correlated with differential expression of a head-specific mannose-ligand receptor. Fertil Steril 59: 854-862.
    • (1993) Fertil Steril , vol.59 , pp. 854-862
    • Benoff, S.1    Cooper, G.W.2    Hurley, I.H.3    Napolitano, B.4    Rosenfeld, D.L.5    Scholl, G.M.6    Hershlang, A.7
  • 5
    • 21344492280 scopus 로고
    • Biological functions of oligosaccharides on glycoproteins
    • a minireview
    • BLITHE DL (1993). Biological functions of oligosaccharides on glycoproteins. Trends in Glycoscience and Glycotechnology (TIGG), 5, 81-98, a minireview.
    • (1993) Trends in Glycoscience and Glycotechnology (TIGG) , vol.5 , pp. 81-98
    • Blithe, D.L.1
  • 7
    • 0023077389 scopus 로고
    • Glycoconjugates of the human sperm surface: Distribution and alterations that accompany capacitation in vitro
    • CROSS NL, AND OVERSTREET JW (1987). Glycoconjugates of the human sperm surface: distribution and alterations that accompany capacitation in vitro. Gamete Res 16: 23-35.
    • (1987) Gamete Res , vol.16 , pp. 23-35
    • Cross, N.L.1    Overstreet, J.W.2
  • 8
    • 0023096199 scopus 로고
    • Lack of a head in human spermatozoa from sterile patients; a syndrome associated with impaired fertilization
    • CHEMES HE, CARRIZA C, SCARINCI F, BRUGO S, NEUSPILLER N (1987). Lack of a head in human spermatozoa from sterile patients; a syndrome associated with impaired fertilization. Fertil Steril 47: 310-316.
    • (1987) Fertil Steril , vol.47 , pp. 310-316
    • Chemes, H.E.1    Carriza, C.2    Scarinci, F.3    Brugo, S.4    Neuspiller, N.5
  • 9
    • 0028932706 scopus 로고
    • Expression of mannose-binding sites on human spermatozoa and their role in sperm-zona pellucida binding
    • CHEN JS, DONCELL GF, ALVAREZ C, ACOSTA AA (1995). Expression of mannose-binding sites on human spermatozoa and their role in sperm-zona pellucida binding. J Androl 16: 55-63.
    • (1995) J Androl , vol.16 , pp. 55-63
    • Chen, J.S.1    Doncell, G.F.2    Alvarez, C.3    Acosta, A.A.4
  • 11
    • 0024230477 scopus 로고
    • Cytochemical detection of receptors specific for N-linked oligosaccharides of glycoproteins in the membrane of the human spermatozoon and their distribution in the different zones of that membrane
    • DE CEREZO JMS, MAESTRE AJ, CEREZO AS (1988). Cytochemical detection of receptors specific for N-linked oligosaccharides of glycoproteins in the membrane of the human spermatozoon and their distribution in the different zones of that membrane. Journal of Reproductive Immunology (JRI), 14: 213-223.
    • (1988) Journal of Reproductive Immunology (JRI) , vol.14 , pp. 213-223
    • De Cerezo, J.M.S.1    Maestre, A.J.2    Cerezo, A.S.3
  • 13
    • 85081473646 scopus 로고
    • Domains of different N-linked oligosaccharides on the surface of the human spermatozoon
    • N. Alexander, D. Griffin, J.M. Spieler and G.M. Waites, Eds. (CONRAD-WHO). New York
    • DE CEREZO JMS, CEREZO AS (1990). Domains of different N-linked oligosaccharides on the surface of the human spermatozoon. In: Gamete interaction: prospects for immunocontraception. N. Alexander, D. Griffin, J.M. Spieler and G.M. Waites, Eds. (CONRAD-WHO). New York, pp. 620.
    • (1990) Gamete Interaction: Prospects for Immunocontraception , pp. 620
    • De Cerezo, J.M.S.1    Cerezo, A.S.2
  • 14
    • 85081473040 scopus 로고
    • Domains of fucosylated conjugates and their possible affinity binding sites on the human spermatozoon
    • DE CEREZO JMS, MARQUINEZ A.C., LELLI S, CEREZO AS (1992 a). domains of fucosylated conjugates and their possible affinity binding sites on the human spermatozoon. J Immunol and Immunopharmacol, XII, 136.
    • (1992) J Immunol and Immunopharmacol , vol.12 , pp. 136
    • De Cerezo, J.M.S.1    Marquinez, A.C.2    Lelli, S.3    Cerezo, A.S.4
  • 15
    • 85081463141 scopus 로고
    • Binding sites of Phaseolus vulgaris and β3-D-galactosyl-BSA neoglycoprotein on the human spermatozoon
    • DE CEREZO JMS, MARQUINEZ AC, CEREZO AS (1992 b). Binding sites of Phaseolus vulgaris and β3-D-galactosyl-BSA neoglycoprotein on the human spermatozoon. Micr Electr Biol Cel 16: 123-140.
    • (1992) Micr Electr Biol Cel , vol.16 , pp. 123-140
    • De Cerezo, J.M.S.1    Marquinez, A.C.2    Cerezo, A.S.3
  • 16
    • 85081474057 scopus 로고
    • Molecular probes for the location of human sperm α-D-mannosidases II. The FITC-α-d-mannosylated-albumin
    • DE CEREZO JMS, MARQUINEZ AC, CEREZO AS (1995). Molecular probes for the location of human sperm α-D-mannosidases II. The FITC-α-d-mannosylated-albumin. Biocell 19(1): 11-16.
    • (1995) Biocell , vol.19 , Issue.1 , pp. 11-16
    • De Cerezo, J.M.S.1    Marquinez, A.C.2    Cerezo, A.S.3
  • 17
    • 0024146885 scopus 로고
    • Role for fucosesulfate-rich carbohydrates in the penetration of zona-pellucida-free hamster eggs by hamster spermatozoa
    • DRAVLAND JE, MORTIMER D (1988). Role for fucosesulfate-rich carbohydrates in the penetration of zona-pellucida-free hamster eggs by hamster spermatozoa. Gamete Res 21: 353-358.
    • (1988) Gamete Res , vol.21 , pp. 353-358
    • Dravland, J.E.1    Mortimer, D.2
  • 18
    • 0029015255 scopus 로고
    • Purification and partial characterization of acrosome reaction inhibiting glycoprotein from human seminal plasma
    • DRISDEL RC, MACK SR, ANDERSON RA, ZANEVELD LJD (1995). Purification and partial characterization of acrosome reaction inhibiting glycoprotein from human seminal plasma. Biol Reprod 53: 201-208.
    • (1995) Biol Reprod , vol.53 , pp. 201-208
    • Drisdel, R.C.1    Mack, S.R.2    Anderson, R.A.3    Zaneveld, L.J.D.4
  • 19
    • 0026515350 scopus 로고
    • Distribution of sugar residues in the bovine testis during postnatal ontogenesis demonstrated with lectin-horseradish peroxidase conjugates
    • ERTL C, WROBEL KH (1992). Distribution of sugar residues in the bovine testis during postnatal ontogenesis demonstrated with lectin-horseradish peroxidase conjugates. Histochemistry 97: 161-171.
    • (1992) Histochemistry , vol.97 , pp. 161-171
    • Ertl, C.1    Wrobel, K.H.2
  • 20
    • 0028903966 scopus 로고
    • Fluorescein isothiocyanate conjugate-wheat germ agglutinin staining of human spermatozoa and fertilization in vitro
    • GABRIEL LK, FRANKEN DR, VAN DER HORST G, KRUGER TF (1995). Fluorescein isothiocyanate conjugate-wheat germ agglutinin staining of human spermatozoa and fertilization in vitro. Fertil Steril 63: 894-901.
    • (1995) Fertil Steril , vol.63 , pp. 894-901
    • Gabriel, L.K.1    Franken, D.R.2    Van Der Horst, G.3    Kruger, T.F.4
  • 21
    • 0020327756 scopus 로고
    • Carbohydrate specificity of sea urchin sperm binding: A cell surface lectin mediating sperm-egg adhesion
    • GLABE CG, GRABEL LB, VACQUIER VD, ROSEN SD (1982). Carbohydrate specificity of sea urchin sperm binding: a cell surface lectin mediating sperm-egg adhesion. J Cell Biol 94: 123-128.
    • (1982) J Cell Biol , vol.94 , pp. 123-128
    • Glabe, C.G.1    Grabel, L.B.2    Vacquier, V.D.3    Rosen, S.D.4
  • 22
    • 85081470999 scopus 로고
    • Oligosaccharide specificities of Phasoelus vulgaris leukoagglutinating and erithroagglutinating phytohemagglutinins
    • GREEN ED, BAEZINGER JU (1986). Oligosaccharide specificities of Phasoelus vulgaris leukoagglutinating and erithroagglutinating phytohemagglutinins. J Biol Chem 261: 12018-12029.
    • (1986) J Biol Chem , vol.261 , pp. 12018-12029
    • Green, E.D.1    Baezinger, J.U.2
  • 23
    • 0025231502 scopus 로고
    • Assessment of the human sperm acrosome reaction using Concanavalin A lectin
    • HOLDEN CA, HYNE RV, SATHANANTHAN AH, TROUNSON AO (1990). Assessment of the human sperm acrosome reaction using Concanavalin A lectin. Mol Reprod Dev 25: 247-257.
    • (1990) Mol Reprod Dev , vol.25 , pp. 247-257
    • Holden, C.A.1    Hyne, R.V.2    Sathananthan, A.H.3    Trounson, A.O.4
  • 24
    • 0022964694 scopus 로고
    • Sperm glycosidase as a plausible mediator of sperm binding to the vitelline envelope in ascidians
    • J.L. Hedrick, Ed., Plenum Press, New York
    • HOSHI M (1986). Sperm glycosidase as a plausible mediator of sperm binding to the vitelline envelope in ascidians. In: The molecular and cellular biology of fertilization. J.L. Hedrick, Ed., Plenum Press, New York, pp. 251-260.
    • (1986) The Molecular and Cellular Biology of Fertilization , pp. 251-260
    • Hoshi, M.1
  • 25
    • 0019969344 scopus 로고
    • Evidence suggesting that L-fucose is part of a recognition signal for sperm-zona pellucida attachment in mammals
    • HUANG TTF, OHZU E, YANAGIMACHI R (1982). Evidence suggesting that L-fucose is part of a recognition signal for sperm-zona pellucida attachment in mammals. Gamete Res 5: 355-361.
    • (1982) Gamete Res , vol.5 , pp. 355-361
    • Huang, T.T.F.1    Ohzu, E.2    Yanagimachi, R.3
  • 26
    • 0021244589 scopus 로고
    • Fucoidin inhibits attachment of guinea pig spermatozoa to the zona pellucida through binding to the inner acrosomal membrane and equatorial domains
    • HUANG TTF, YANAGIMACHI R (1984). Fucoidin inhibits attachment of guinea pig spermatozoa to the zona pellucida through binding to the inner acrosomal membrane and equatorial domains. Expl Cell Res 153: 363-373.
    • (1984) Expl Cell Res , vol.153 , pp. 363-373
    • Huang, T.T.F.1    Yanagimachi, R.2
  • 27
    • 0023885039 scopus 로고
    • Carbohydrate-binding properties of boar sperm proacrosin and assessment of its role in sperm-egg recognition and adhesion during fertilization
    • JONES R, BROWN CR, LANCASTER RT (1988). Carbohydrate-binding properties of boar sperm proacrosin and assessment of its role in sperm-egg recognition and adhesion during fertilization. Development 102: 781-792.
    • (1988) Development , vol.102 , pp. 781-792
    • Jones, R.1    Brown, C.R.2    Lancaster, R.T.3
  • 28
    • 0024374545 scopus 로고
    • 125I] neoglycoprotein probes
    • 125I] neoglycoprotein probes. Human Reproduction 4: 550-557.
    • (1989) Human Reproduction , vol.4 , pp. 550-557
    • Jones, R.1
  • 29
    • 0025801953 scopus 로고
    • Interaction of zona pellucida glycoproteins, sulphated carbohydrates and synthetic polymers with proacrosin, the putative egg-binding protein from mammalian spermatozoa
    • JONES R (1991). Interaction of zona pellucida glycoproteins, sulphated carbohydrates and synthetic polymers with proacrosin, the putative egg-binding protein from mammalian spermatozoa. Development 111: 1155-1163.
    • (1991) Development , vol.111 , pp. 1155-1163
    • Jones, R.1
  • 30
    • 0028891816 scopus 로고
    • Carbohydrate moieties on sperm surface: Physiological relevance
    • KURPISZ M, ALEXANDER NJ (1995). Carbohydrate moieties on sperm surface: physiological relevance. Fertil Steril 63: 158-165.
    • (1995) Fertil Steril , vol.63 , pp. 158-165
    • Kurpisz, M.1    Alexander, N.J.2
  • 31
    • 0024412454 scopus 로고
    • Human sperm-zona pellucida binding, sperm characteristics and in-vitro fertilization
    • LIU DY, LOPATA A, JOHNSTON WIH, BAKER HWC (1989). Human sperm-zona pellucida binding, sperm characteristics and in-vitro fertilization. Human Reproduction 4: 696-701.
    • (1989) Human Reproduction , vol.4 , pp. 696-701
    • Liu, D.Y.1    Lopata, A.2    Johnston, W.I.H.3    Baker, H.W.C.4
  • 32
    • 0028003677 scopus 로고
    • A fucose-containing epitope potentially involved in gamete interaction on the human zona pellucida
    • LUCAS H, BERCAGEAY S, LE PENDU J, JEAN M, MIRALLIE S, BARRIERE P (1994). A fucose-containing epitope potentially involved in gamete interaction on the human zona pellucida. Hum Reprod 9: 1532-1538.
    • (1994) Hum Reprod , vol.9 , pp. 1532-1538
    • Lucas, H.1    Bercageay, S.2    Le Pendu, J.3    Jean, M.4    Mirallie, S.5    Barriere, P.6
  • 33
    • 0023933830 scopus 로고
    • Protein-carbohydrate complementarity in mammalian gamete recognition
    • a review
    • MACEK MB, SHUR BD (1988). Protein-carbohydrate complementarity in mammalian gamete recognition. Gamete Res 20: 93-109, a review.
    • (1988) Gamete Res , vol.20 , pp. 93-109
    • Macek, M.B.1    Shur, B.D.2
  • 35
    • 0018853556 scopus 로고
    • Primary structure of glycoproteins: Basis for the molecular biology of glycoproteins
    • MONTRIEUL (1980). Primary structure of glycoproteins: Basis for the molecular biology of glycoproteins. Adv Carbohyd Chem and Biochem 37:_ 157.
    • (1980) Adv Carbohyd Chem and Biochem , vol.37 , pp. 157
    • Montrieul1
  • 36
    • 0023232821 scopus 로고
    • Specific labelling by peanut agglutinin of the outer acrosomal membrane of the human spermatozoon
    • MORTIMER D, CURTIS EF, MILLER RG (1987). Specific labelling by peanut agglutinin of the outer acrosomal membrane of the human spermatozoon. J Reprod Fert 81: 127-135.
    • (1987) J Reprod Fert , vol.81 , pp. 127-135
    • Mortimer, D.1    Curtis, E.F.2    Miller, R.G.3
  • 37
    • 0025306071 scopus 로고
    • Combined use of fluorescent peanut agglutinin lectin and Hoechst 33258 to monitor the acrosomal status and vitality of human spermatozoa
    • MORTIMER D, CURTIS EF, CAMENZIND AR (1990). Combined use of fluorescent peanut agglutinin lectin and Hoechst 33258 to monitor the acrosomal status and vitality of human spermatozoa. Human Reproduction 5: 99-103.
    • (1990) Human Reproduction , vol.5 , pp. 99-103
    • Mortimer, D.1    Curtis, E.F.2    Camenzind, A.R.3
  • 38
    • 0025190765 scopus 로고
    • Antagonistic and agonistic properties of saccharide moieties in the hemizona assay
    • OEHNINGER S, ACOSTA A, HODGEN GD (1990 a). Antagonistic and agonistic properties of saccharide moieties in the hemizona assay. Fertil Steril 53: 143-149.
    • (1990) Fertil Steril , vol.53 , pp. 143-149
    • Oehninger, S.1    Acosta, A.2    Hodgen, G.D.3
  • 39
    • 0025967952 scopus 로고
    • Nature of the inhibitory effect of complex saccharide moieties on the tight binding of human spermatozoa to the human zona pellucida
    • OEHNINGER S, CLARK GF, ACOSTA AA, HODGEN GD (1990 b). Nature of the inhibitory effect of complex saccharide moieties on the tight binding of human spermatozoa to the human zona pellucida. Fertil Steril 55: 165-169.
    • (1990) Fertil Steril , vol.55 , pp. 165-169
    • Oehninger, S.1    Clark, G.F.2    Acosta, A.A.3    Hodgen, G.D.4
  • 41
    • 0026705799 scopus 로고
    • Characterization of low Mr zona pellucida binding proteins from boar spermatozoa and seminal plasma
    • PARRY RV, BARKER PJ, JONES R (1992). Characterization of low Mr zona pellucida binding proteins from boar spermatozoa and seminal plasma. Mol Reprod Dev 33: 108-115.
    • (1992) Mol Reprod Dev , vol.33 , pp. 108-115
    • Parry, R.V.1    Barker, P.J.2    Jones, R.3
  • 42
    • 0016257442 scopus 로고
    • Discussion paper: Blood group specificity of the lectin from Lotus tetragonolobus
    • PEREIRA MEA, KABAT EA (1974). Discussion paper: Blood group specificity of the lectin from Lotus tetragonolobus. Ann New York Acad Sci 234: 301-305.
    • (1974) Ann New York Acad Sci , vol.234 , pp. 301-305
    • Pereira, M.E.A.1    Kabat, E.A.2
  • 43
    • 0022618897 scopus 로고
    • The role of carbohydrates in sperm-egg interaction in rats
    • SHALGI R, MATITYAHU A, NEBEL L (1986). The role of carbohydrates in sperm-egg interaction in rats. Biology of Reproduction 34: 446-452.
    • (1986) Biology of Reproduction , vol.34 , pp. 446-452
    • Shalgi, R.1    Matityahu, A.2    Nebel, L.3
  • 44
    • 0018886932 scopus 로고
    • Neoglycoproteins: The preparation and application of synthetic glycoproteins
    • STOWEL CP, LEE YC (1980). Neoglycoproteins: the preparation and application of synthetic glycoproteins. Adv Carb Chem Biochem 37: 225-281.
    • (1980) Adv Carb Chem Biochem , vol.37 , pp. 225-281
    • Stowel, C.P.1    Lee, Y.C.2
  • 45
    • 0027321676 scopus 로고
    • Solubilized human zona pellucida competes with a fucosylated noeglycoprotein for binding sites on the human sperm surface
    • TESARIK J, MENDOZA C, RAMIREZ JP, MOOS J (1993). Solubilized human zona pellucida competes with a fucosylated noeglycoprotein for binding sites on the human sperm surface. Fertil Steril 60: 344-350.
    • (1993) Fertil Steril , vol.60 , pp. 344-350
    • Tesarik, J.1    Mendoza, C.2    Ramirez, J.P.3    Moos, J.4
  • 47
    • 0023662092 scopus 로고
    • Acrosin shows zona and fucose binding, novel properties for a serine proteinase
    • TÖPFER-PETERSEN E, HENSCHEN A (1987). Acrosin shows zona and fucose binding, novel properties for a serine proteinase. FEBS Lett 226: 38-42.
    • (1987) FEBS Lett , vol.226 , pp. 38-42
    • Töpfer-Petersen, E.1    Henschen, A.2
  • 48
    • 0023873193 scopus 로고
    • Zona pellucida-binding and fucose-binding of boar sperm acrosin is not correlated with proteolytic activity
    • TÖPFER-PETERSEN E, HENSCHEN A (1988). Zona pellucida-binding and fucose-binding of boar sperm acrosin is not correlated with proteolytic activity. Biol Chem Hoppe-Seyler 369: 69-76.
    • (1988) Biol Chem Hoppe-Seyler , vol.369 , pp. 69-76
    • Töpfer-Petersen, E.1    Henschen, A.2
  • 49
    • 0028972709 scopus 로고
    • Carbohydrate-and heparin-binding proteins in mammalian fertilization
    • TÖPFER-PETERSEN E, CALVETE JJ, SANZ L, SINOWATZ F (1995). Carbohydrate-and heparin-binding proteins in mammalian fertilization. Andrologia 27: 303-324.
    • (1995) Andrologia , vol.27 , pp. 303-324
    • Töpfer-Petersen, E.1    Calvete, J.J.2    Sanz, L.3    Sinowatz, F.4
  • 50
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • a review
    • VARKI A (1993). Biological roles of oligosaccharides: all of the theories are correct. Glycobiology 3: 97-130, a review.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 52
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • G. Knobil and J. Neill et al., Eds., Raven Press Ltd. New York
    • YANAGIMACHI R (1988). Mammalian fertilization. In: The physiology of reproduction. G. Knobil and J. Neill et al., Eds., Raven Press Ltd. New York, pp. 135-185.
    • (1988) The Physiology of Reproduction , pp. 135-185
    • Yanagimachi, R.1
  • 53
    • 0028877229 scopus 로고
    • Involvement of N-linked carbohydrate chains of pig zona pellucida in sperm-egg binding
    • YONEZAWA N, AOKI H, HATANAKA Y, NAKANO M (1995). Involvement of N-linked carbohydrate chains of pig zona pellucida in sperm-egg binding. Eur J Biochem 233: 35-41.
    • (1995) Eur J Biochem , vol.233 , pp. 35-41
    • Yonezawa, N.1    Aoki, H.2    Hatanaka, Y.3    Nakano, M.4


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