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Volumn 120, Issue 1, 2007, Pages 33-44

Glycodelin-A interacts with fucosyltransferase on human sperm plasma membrane to inhibit spermatozoa-zona pellucida binding

Author keywords

Fucosyltransferase; Glycodelin; Spermatozoa; Zona pellucida

Indexed keywords

ENZYME ANTIBODY; FUCOSYLTRANSFERASE; MEMBRANE PROTEIN; PLACENTA PROTEIN 14; RECEPTOR;

EID: 33846828527     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.03258     Document Type: Article
Times cited : (68)

References (77)
  • 1
    • 0025075878 scopus 로고
    • Identification of a ZP3-binding protein on acrosome-intact mouse sperm by photoaffinity crosslinking
    • Bleil, J. D. and Wassarman, P. M. (1990). Identification of a ZP3-binding protein on acrosome-intact mouse sperm by photoaffinity crosslinking. Proc. Natl. Acad. Sci. USA 87, 5563-5567.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5563-5567
    • Bleil, J.D.1    Wassarman, P.M.2
  • 2
    • 0020336827 scopus 로고
    • New soluble placental tissue proteins: Their isolation, characterization, localization and quantification
    • Bohn, H., Kraus, W. and Winckler, W. (1982). New soluble placental tissue proteins: their isolation, characterization, localization and quantification. Placenta Suppl. 4, 67-81.
    • (1982) Placenta Suppl. , vol.4 , pp. 67-81
    • Bohn, H.1    Kraus, W.2    Winckler, W.3
  • 3
    • 0029093994 scopus 로고
    • Expression of human chromosome 19p alpha(1,3)-fucosyltransferase genes in normal tissues. Alternative splicing, polyadenylation, and isoforms
    • Cameron, H. S., Szczepainiak, D. and Weston, B. W. (1995). Expression of human chromosome 19p alpha(1,3)-fucosyltransferase genes in normal tissues. Alternative splicing, polyadenylation, and isoforms. J. Biol. Chem. 270, 20112-20122.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20112-20122
    • Cameron, H.S.1    Szczepainiak, D.2    Weston, B.W.3
  • 4
    • 0024519272 scopus 로고
    • Characterization of fucosyltransferase activity during mouse spermatogenesis: Evidence for a cell surface fucosyltransferase
    • Cardullo, R. A., Armant, D. R. and Millette, C. F. (1989). Characterization of fucosyltransferase activity during mouse spermatogenesis: evidence for a cell surface fucosyltransferase. Biochemistry 28, 1611-1617.
    • (1989) Biochemistry , vol.28 , pp. 1611-1617
    • Cardullo, R.A.1    Armant, D.R.2    Millette, C.F.3
  • 6
    • 0030252486 scopus 로고    scopus 로고
    • The role of carbohydrate in sperm-ZP3 adhesion
    • Chapman, N. R. and Barratt, C. L. (1996). The role of carbohydrate in sperm-ZP3 adhesion. Mol. Hum. Reprod. 2, 767-774.
    • (1996) Mol. Hum. Reprod. , vol.2 , pp. 767-774
    • Chapman, N.R.1    Barratt, C.L.2
  • 7
    • 0028227343 scopus 로고
    • Sperm-egg recognition in the mouse: Characterization of sp56, a sperm protein having specific affinity for ZP3
    • Cheng, A., Le, T., Palacios, M., Bookbinder, L. H., Wassarman, P. M., Suzuki, F. and Bleil, J. D. (1994). Sperm-egg recognition in the mouse: characterization of sp56, a sperm protein having specific affinity for ZP3. J. Cell Biol. 125, 867-878.
    • (1994) J. Cell Biol. , vol.125 , pp. 867-878
    • Cheng, A.1    Le, T.2    Palacios, M.3    Bookbinder, L.H.4    Wassarman, P.M.5    Suzuki, F.6    Bleil, J.D.7
  • 8
    • 0036137510 scopus 로고    scopus 로고
    • Comparative study of the biological activity of spermatozoa-zona pellucida binding inhibitory factors from human follicular fluid on various sperm function parameters
    • Chiu, P. C., Ho. P. C., Ng, E. H. and Yeung, W. S. (2002). Comparative study of the biological activity of spermatozoa-zona pellucida binding inhibitory factors from human follicular fluid on various sperm function parameters. Mol. Reprod. Dev. 61, 205-212.
    • (2002) Mol. Reprod. Dev. , vol.61 , pp. 205-212
    • Chiu, P.C.1    Ho, P.C.2    Ng, E.H.3    Yeung, W.S.4
  • 9
    • 0038112170 scopus 로고    scopus 로고
    • Zona-binding inhibitory factor-1 from human follicular fluid is an isoform of glycodelin
    • Chiu, P. C., Koistinen, R., Koistinen, H., Seppala, M., Lee, K. F. and Yeung, W. S. (2003a). Zona-binding inhibitory factor-1 from human follicular fluid is an isoform of glycodelin. Biol. Reprod. 69, 365-372.
    • (2003) Biol. Reprod. , vol.69 , pp. 365-372
    • Chiu, P.C.1    Koistinen, R.2    Koistinen, H.3    Seppala, M.4    Lee, K.F.5    Yeung, W.S.6
  • 10
    • 0037494894 scopus 로고    scopus 로고
    • Binding of zona binding inhibitory factor-1 (ZIF-1) from human follicular fluid on spermatozoa
    • Chiu, P. C., Koistinen, R., Koistinen, H., Seppala, M., Lee, K. F. and Yeung, W. S. (2003b). Binding of zona binding inhibitory factor-1 (ZIF-1) from human follicular fluid on spermatozoa. J. Biol. Chem. 278, 13570-13577.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13570-13577
    • Chiu, P.C.1    Koistinen, R.2    Koistinen, H.3    Seppala, M.4    Lee, K.F.5    Yeung, W.S.6
  • 11
    • 2642581631 scopus 로고    scopus 로고
    • The contribution of D-mannose, L-fucose, N-acetylglucosamine, and selectin residues on the binding of glycodelin isoforms to human spermatozoa
    • Chiu, F. C., Tsang, H. Y., Koistinen, R., Koistinen, H., Seppala, M., Lee, K. F. and Yeung, W. S. (2004). The contribution of D-mannose, L-fucose, N-acetylglucosamine, and selectin residues on the binding of glycodelin isoforms to human spermatozoa. Biol. Reprod. 70, 1710-1719.
    • (2004) Biol. Reprod. , vol.70 , pp. 1710-1719
    • Chiu, F.C.1    Tsang, H.Y.2    Koistinen, R.3    Koistinen, H.4    Seppala, M.5    Lee, K.F.6    Yeung, W.S.7
  • 12
    • 21844454726 scopus 로고    scopus 로고
    • Glycodelin-S in human seminal plasma reduces cholesterol efflux and inhibits capacitation of spermatozoa
    • Chiu, P. C., Chung, M. K., Tsang, H. Y., Koistinen, R., Koistinen, H., Seppala, M., Lee, K. F. and Yeung, W. S. (2005). Glycodelin-S in human seminal plasma reduces cholesterol efflux and inhibits capacitation of spermatozoa. J. Biol. Chem. 280, 25580-25589.
    • (2005) J. Biol. Chem. , vol.280 , pp. 25580-25589
    • Chiu, P.C.1    Chung, M.K.2    Tsang, H.Y.3    Koistinen, R.4    Koistinen, H.5    Seppala, M.6    Lee, K.F.7    Yeung, W.S.8
  • 13
    • 0034429536 scopus 로고    scopus 로고
    • Glycosylation of the N-terminal potential N-glycosylation sites in the human alphal,3-fucosyltransferase V and -VI (hFucTV and -VI)
    • Christensen, L. L., Bross, P. and Orntoft, T. F. (2000a). Glycosylation of the N-terminal potential N-glycosylation sites in the human alphal,3-fucosyltransferase V and -VI (hFucTV and -VI). Glycoconjugate J. 17, 859-865.
    • (2000) Glycoconjugate J. , vol.17 , pp. 859-865
    • Christensen, L.L.1    Bross, P.2    Orntoft, T.F.3
  • 14
    • 0033843689 scopus 로고    scopus 로고
    • The C-terminal N-glycosylation sites of the human alpha 1,3/ 4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) are necessary for the expression of full enzyme activity
    • Christensen, L. L., Jensen, U. B., Bross, P. and Orntoft, T. F. (2000b). The C-terminal N-glycosylation sites of the human alpha 1,3/ 4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) are necessary for the expression of full enzyme activity. Glycobiology 10, 931-939.
    • (2000) Glycobiology , vol.10 , pp. 931-939
    • Christensen, L.L.1    Jensen, U.B.2    Bross, P.3    Orntoft, T.F.4
  • 15
    • 0031040995 scopus 로고    scopus 로고
    • Golgi localization of glycosyltransferases: More questions than answers
    • Colley, K. J. (1997). Golgi localization of glycosyltransferases: more questions than answers. Glycobiology 7, 1-13.
    • (1997) Glycobiology , vol.7 , pp. 1-13
    • Colley, K.J.1
  • 17
    • 33846788246 scopus 로고
    • Acceptor specificity of different length constructs of human recombinant alpha 1,3/4-fucosyltransferases. Replacement of the stem region and the transmembrane domain of fucosyltransferase V by protein A results in an enzyme with GDP-fucose hydrolyzing activity
    • de Vries, T., Srnka, C. A., Palcic, M. M., Swiedler, S. J., van den Eijnden, D. H. and Macher, B. A. (1995). Acceptor specificity of different length constructs of human recombinant alpha 1,3/ 4-fucosyltransferases. Replacement of the stem region and the transmembrane domain of fucosyltransferase V by protein A results in an enzyme with GDP-fucose hydrolyzing activity. J. Biol. Chem. 272, 29721-29728.
    • (1995) J. Biol. Chem. , vol.272 , pp. 29721-29728
    • de Vries, T.1    Srnka, C.A.2    Palcic, M.M.3    Swiedler, S.J.4    van den Eijnden, D.H.5    Macher, B.A.6
  • 19
    • 0028885690 scopus 로고
    • Structural analysis of the oligosaccharides derived from glycodelin, a human glycoprotein with potent immunosuppressive and contraceptive activities
    • Dell, A., Morris, H. R., Easton, R. L., Panico, M., Patankar, M., Oehniger, S., Koistinen, R., Koistinen, H., Seppala, M. and Clark, G. F. (1995). Structural analysis of the oligosaccharides derived from glycodelin, a human glycoprotein with potent immunosuppressive and contraceptive activities. J. Biol. Chem. 270, 24116-24126.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24116-24126
    • Dell, A.1    Morris, H.R.2    Easton, R.L.3    Panico, M.4    Patankar, M.5    Oehniger, S.6    Koistinen, R.7    Koistinen, H.8    Seppala, M.9    Clark, G.F.10
  • 21
    • 0018871935 scopus 로고
    • Isolation, physicochemical properties, and macromolecular composition of zona pellucida from porcine oocytes
    • Dunbar, B. S., Wardrip, N. J. and Hedrick, J. L. (1980). Isolation, physicochemical properties, and macromolecular composition of zona pellucida from porcine oocytes. Biochemistry 19, 356-365.
    • (1980) Biochemistry , vol.19 , pp. 356-365
    • Dunbar, B.S.1    Wardrip, N.J.2    Hedrick, J.L.3
  • 22
    • 0034759226 scopus 로고    scopus 로고
    • Bicarbonate stimulated phospholipid scrambling induces cholesterol redistribution and enables cholesterol depletion in the sperm plasma membrane
    • Flesch, F. M., Brouwers, J. F., Nievelstein, P. F., Verkleij, A. J. van Golde, L. M., Colenbrander, B. and Gadella, B. M. (2001). Bicarbonate stimulated phospholipid scrambling induces cholesterol redistribution and enables cholesterol depletion in the sperm plasma membrane. J. Cell Sci. 114, 3543-3555.
    • (2001) J. Cell Sci. , vol.114 , pp. 3543-3555
    • Flesch, F.M.1    Brouwers, J.F.2    Nievelstein, P.F.3    Verkleij, A.J.4    van Golde, L.M.5    Colenbrander, B.6    Gadella, B.M.7
  • 23
    • 0035211574 scopus 로고    scopus 로고
    • Carbohydrate-mediated sperm-egg interaction and species specificity: A clue from the Unio elongatulus model
    • Focarelli, R., La Sala, G.B., Balasini, M. and Rosati, F. (2001). Carbohydrate-mediated sperm-egg interaction and species specificity: a clue from the Unio elongatulus model. Cells Tissues Organs 168, 76-81.
    • (2001) Cells Tissues Organs , vol.168 , pp. 76-81
    • Focarelli, R.1    La Sala, G.B.2    Balasini, M.3    Rosati, F.4
  • 24
    • 0028030980 scopus 로고
    • Sperm binding capacity of human zona pellucida derived from oocytes obtained from different sources
    • Franken, D. R., Kruger, T. F., Oehninger, S. C., Kaskar, K. and Hodgen, G. D. (1994). Sperm binding capacity of human zona pellucida derived from oocytes obtained from different sources. Andrologia 26, 277-281.
    • (1994) Andrologia , vol.26 , pp. 277-281
    • Franken, D.R.1    Kruger, T.F.2    Oehninger, S.C.3    Kaskar, K.4    Hodgen, G.D.5
  • 25
    • 0026087535 scopus 로고
    • Isolation, characterization, and localization of a sperm-bound N-acetylglucosaminidase that is indispensable for fertilization in the ascidian, Phallusia mammillata
    • Godknecht, A. and Honegger, T. G. (1991). Isolation, characterization, and localization of a sperm-bound N-acetylglucosaminidase that is indispensable for fertilization in the ascidian, Phallusia mammillata. Dev. Biol. 143, 398-407.
    • (1991) Dev. Biol. , vol.143 , pp. 398-407
    • Godknecht, A.1    Honegger, T.G.2
  • 27
    • 13644260111 scopus 로고    scopus 로고
    • Mutation of amino acids in the alpha 1,3-fucosyltransferase motif affects enzyme activity and Km for donor and acceptor substrates
    • Jost, F., de Vries, T., Knegtel, R. M. and Macher, B. A. (2005). Mutation of amino acids in the alpha 1,3-fucosyltransferase motif affects enzyme activity and Km for donor and acceptor substrates. Glycobiology 15, 165-175.
    • (2005) Glycobiology , vol.15 , pp. 165-175
    • Jost, F.1    de Vries, T.2    Knegtel, R.M.3    Macher, B.A.4
  • 29
    • 0037369738 scopus 로고    scopus 로고
    • Purification and characterization of plasma membrane-associated human sperm alpha-L-fucosidase
    • Khunsook, S., Bean, B. S., McGowan, S. R. and Alhadeff, J. A. (2003). Purification and characterization of plasma membrane-associated human sperm alpha-L-fucosidase. Biol. Reprod. 68, 709-716.
    • (2003) Biol. Reprod. , vol.68 , pp. 709-716
    • Khunsook, S.1    Bean, B.S.2    McGowan, S.R.3    Alhadeff, J.A.4
  • 30
    • 0242624744 scopus 로고    scopus 로고
    • Differential release of soluble and matrix components: Evidence for intermediate states of secretion during spontaneous acrosomal exocytosis in mouse sperm
    • Kim, K. S. and Gerton, G. L. (2003) Differential release of soluble and matrix components: evidence for intermediate states of secretion during spontaneous acrosomal exocytosis in mouse sperm. Dev. Biol. 264, 141-152.
    • (2003) Dev. Biol. , vol.264 , pp. 141-152
    • Kim, K.S.1    Gerton, G.L.2
  • 31
    • 1842477367 scopus 로고    scopus 로고
    • The embryotrophic activity of oviductal cell-derived complement C3b and iC3b, a novel function of complement protein in reproduction
    • Lee, Y. L., Lee, K. F., Xu, J. S., He, Q. Y., Chia, J. F., Lee, W. M., Luk, J. M. and Yeung, W. S. (2004). The embryotrophic activity of oviductal cell-derived complement C3b and iC3b, a novel function of complement protein in reproduction. J. Biol. Chem. 279, 12763-12768.
    • (2004) J. Biol. Chem. , vol.279 , pp. 12763-12768
    • Lee, Y.L.1    Lee, K.F.2    Xu, J.S.3    He, Q.Y.4    Chia, J.F.5    Lee, W.M.6    Luk, J.M.7    Yeung, W.S.8
  • 32
    • 0027080725 scopus 로고
    • Regulation of mouse gamete interaction by a sperm tyrosine kinase
    • Leyton, L., LeGuen, P., Bunch, D. and Saling, P. M. (1992). Regulation of mouse gamete interaction by a sperm tyrosine kinase. Proc. Natl. Acad. Sci. USA 89, 11692-11695.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11692-11695
    • Leyton, L.1    LeGuen, P.2    Bunch, D.3    Saling, P.M.4
  • 33
    • 0028902581 scopus 로고
    • Oligosaccharide constructs with defined structures that inhibit binding of mouse sperm to unfertilized eggs in vitro
    • Litscher, E. S., Juntunen, K., Seppo, A., Penttila, L., Niemela, R., Renkonen, O. and Wassarman, P. M. (1995). Oligosaccharide constructs with defined structures that inhibit binding of mouse sperm to unfertilized eggs in vitro. Biochemistry 34, 4662-4669.
    • (1995) Biochemistry , vol.34 , pp. 4662-4669
    • Litscher, E.S.1    Juntunen, K.2    Seppo, A.3    Penttila, L.4    Niemela, R.5    Renkonen, O.6    Wassarman, P.M.7
  • 34
    • 0030728461 scopus 로고    scopus 로고
    • Sperm from beta 1,4-galactosyltransferase-null mice are refractory to ZP3-induced acrosome reactions and penetrate the zona pellucida poorly
    • Lu, Q. and Shur, B. D. (1997). Sperm from beta 1,4-galactosyltransferase-null mice are refractory to ZP3-induced acrosome reactions and penetrate the zona pellucida poorly. Development 124, 4121-4131.
    • (1997) Development , vol.124 , pp. 4121-4131
    • Lu, Q.1    Shur, B.D.2
  • 35
    • 0031775962 scopus 로고    scopus 로고
    • Plasma membrane receptor for beta-lactoglobulin and retinol-binding protein in murine hybridomas
    • Mansouri, A., Gueant, J. L., Capiaumont, J., Pelosi, P., Nabet, P. and Haertle, T. (1998). Plasma membrane receptor for beta-lactoglobulin and retinol-binding protein in murine hybridomas. Biofactors 7, 287-298.
    • (1998) Biofactors , vol.7 , pp. 287-298
    • Mansouri, A.1    Gueant, J.L.2    Capiaumont, J.3    Pelosi, P.4    Nabet, P.5    Haertle, T.6
  • 36
    • 0035339119 scopus 로고    scopus 로고
    • Fucosyltransferase1 and H-type complex carbohydrates modulate epithelial cell proliferation during prostatic branching morphogenesis
    • Marker, P. C., Stephan, J. P., Lee, J., Bald, L., Mather, J. P. and Cunha, G. R. (2001). fucosyltransferase1 and H-type complex carbohydrates modulate epithelial cell proliferation during prostatic branching morphogenesis. Dev. Biol. 233, 95-108.
    • (2001) Dev. Biol. , vol.233 , pp. 95-108
    • Marker, P.C.1    Stephan, J.P.2    Lee, J.3    Bald, L.4    Mather, J.P.5    Cunha, G.R.6
  • 37
    • 0023853115 scopus 로고
    • Study of the fucosyltransferase system in intestinal microsomes
    • Martin, A., Biol, M. C., Broquet, P., Richard, M. and Louisot, P. (1988). Study of the fucosyltransferase system in intestinal microsomes. Enzyme 39, 17-27.
    • (1988) Enzyme , vol.39 , pp. 17-27
    • Martin, A.1    Biol, M.C.2    Broquet, P.3    Richard, M.4    Louisot, P.5
  • 38
    • 0022622670 scopus 로고
    • Surface glycosyltransferase activities during development of neuronal cell cultures
    • Matsui, Y., Lombard, D., Massarelli, R., Mandel, P. and Dreyfus, H. (1986). Surface glycosyltransferase activities during development of neuronal cell cultures. J. Neurochem. 46, 144-150.
    • (1986) J. Neurochem. , vol.46 , pp. 144-150
    • Matsui, Y.1    Lombard, D.2    Massarelli, R.3    Mandel, P.4    Dreyfus, H.5
  • 40
    • 0034142329 scopus 로고    scopus 로고
    • Calcium ion-independent recognition of sialyl and nonsialyl N-acetyllactosamme and Le(x) structures by boar sperm
    • Mori, E., Yoshitani, N., Mori, T. and Takasaki, S. (2000) Calcium ion-independent recognition of sialyl and nonsialyl N-acetyllactosamme and Le(x) structures by boar sperm. Arch. Biochem. Biophys. 374, 86-92.
    • (2000) Arch. Biochem. Biophys. , vol.374 , pp. 86-92
    • Mori, E.1    Yoshitani, N.2    Mori, T.3    Takasaki, S.4
  • 42
    • 0022470810 scopus 로고
    • Purification and properties of N-acetylglucosaminide alpha 1-3-fucosyltransferase from embryonal carcinoma cells
    • Muramatsu, H., Kamada, Y. and Muramatsu, T. (1986). Purification and properties of N-acetylglucosaminide alpha 1-3-fucosyltransferase from embryonal carcinoma cells. Eur. J. Biochem. 157, 71-75.
    • (1986) Eur. J. Biochem. , vol.157 , pp. 71-75
    • Muramatsu, H.1    Kamada, Y.2    Muramatsu, T.3
  • 44
    • 0035208161 scopus 로고    scopus 로고
    • Molecular basis of human sperm-zona pellucida interaction
    • Oehninger, S. (2001). Molecular basis of human sperm-zona pellucida interaction. Cells Tissues Organs 168, 58-64.
    • (2001) Cells Tissues Organs , vol.168 , pp. 58-64
    • Oehninger, S.1
  • 45
    • 0027255818 scopus 로고
    • The specificity of human spermatozoa/zona pellucida interaction under hemizona assay conditions
    • Oehninger, S., Mahony, M. C., Swanson, J. R. and Hodgen, G. D. (1993). The specificity of human spermatozoa/zona pellucida interaction under hemizona assay conditions. Mol. Reprod. Dev. 35, 57-61.
    • (1993) Mol. Reprod. Dev. , vol.35 , pp. 57-61
    • Oehninger, S.1    Mahony, M.C.2    Swanson, J.R.3    Hodgen, G.D.4
  • 46
    • 0028854639 scopus 로고
    • Factors affecting fertilization: Endometrial placental protein 14 reduces the capacity of human spermatozoa to bind to the human zona pellucida
    • Oehninger, S., Coddington, C. C., Hodgen, G. D. and Seppala, M. (1995). Factors affecting fertilization: endometrial placental protein 14 reduces the capacity of human spermatozoa to bind to the human zona pellucida. Fertil. Steril. 63, 377-383.
    • (1995) Fertil. Steril. , vol.63 , pp. 377-383
    • Oehninger, S.1    Coddington, C.C.2    Hodgen, G.D.3    Seppala, M.4
  • 47
    • 0031982107 scopus 로고    scopus 로고
    • Direct evidence for the involvement of carbohydrate sequences in human sperm-zona pellucida binding
    • Ozgur, K., Patankar, M. S., Oehninger, S. and Clark, G. F. (1998). Direct evidence for the involvement of carbohydrate sequences in human sperm-zona pellucida binding. Mol. Hum. Reprod. 4, 318-324.
    • (1998) Mol. Hum. Reprod. , vol.4 , pp. 318-324
    • Ozgur, K.1    Patankar, M.S.2    Oehninger, S.3    Clark, G.F.4
  • 48
    • 0028920010 scopus 로고
    • The interaction in vitro of human spermatozoa with epithelial cells from the human uterine (fallopian) tube
    • Pacey, A. A., Hill, C. J., Scudamore, I. W., Warren, M. A., Barratt, C. L. and Cooke, I. D. (1995). The interaction in vitro of human spermatozoa with epithelial cells from the human uterine (fallopian) tube. Hum. Reprod. 10, 360-366.
    • (1995) Hum. Reprod. , vol.10 , pp. 360-366
    • Pacey, A.A.1    Hill, C.J.2    Scudamore, I.W.3    Warren, M.A.4    Barratt, C.L.5    Cooke, I.D.6
  • 49
    • 0019840759 scopus 로고
    • Co-purification of the Lewis blood group N-acetylglucosaminide alpha 1 goes to 4 fucosyltransferase and an N-acetylglucosammide alpha 1 goes to 3 fucosyltransferase from human milk
    • Prieels, J. P., Monnom, D., Dolmans, M., Beyer, T. A. and Hill, R. L. (1981). Co-purification of the Lewis blood group N-acetylglucosaminide alpha 1 goes to 4 fucosyltransferase and an N-acetylglucosammide alpha 1 goes to 3 fucosyltransferase from human milk. J. Biol. Chem. 256, 10456-10463.
    • (1981) J. Biol. Chem. , vol.256 , pp. 10456-10463
    • Prieels, J.P.1    Monnom, D.2    Dolmans, M.3    Beyer, T.A.4    Hill, R.L.5
  • 50
    • 0034704176 scopus 로고    scopus 로고
    • The acceptor and site specificity of alpha 3-fucosyltransferase V. High reactivity of the proximal and low of the distal galbeta 1-4GlcNAc unit in i-type polylactosamines
    • Pykari, M., Toivonen, S., Natunen, J., Niemela, R., Salminen, H., Aitio, O., Ekstrom, M., Parmanne, P., Valimaki, M., Alais, J. et al. (2000). The acceptor and site specificity of alpha 3-fucosyltransferase V. High reactivity of the proximal and low of the distal galbeta 1-4GlcNAc unit in i-type polylactosamines. J. Biol. Chem. 275, 40057-40063.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40057-40063
    • Pykari, M.1    Toivonen, S.2    Natunen, J.3    Niemela, R.4    Salminen, H.5    Aitio, O.6    Ekstrom, M.7    Parmanne, P.8    Valimaki, M.9    Alais, J.10
  • 51
    • 13744265847 scopus 로고    scopus 로고
    • A time-resolved immunofluorometric method for the measurement of sialyl Lewis x-synthesizing alpha 1,3-fucosyltransferase activity
    • Rabina, J., Smithers, N., Britten, C. J. and Renkonen, R. (1997). A time-resolved immunofluorometric method for the measurement of sialyl Lewis x-synthesizing alpha 1,3-fucosyltransferase activity. Anal. Biochem. 246, 71-78.
    • (1997) Anal. Biochem. , vol.246 , pp. 71-78
    • Rabina, J.1    Smithers, N.2    Britten, C.J.3    Renkonen, R.4
  • 52
    • 0038190995 scopus 로고    scopus 로고
    • Negative regulation of T cell activation by placental protein 14 is mediated by the tyrosine phosphatase receptor CD45
    • Rachmilewitz, J., Borovsky, Z., Riely, G. J., Miller, R. and Tykocinski, M. L. (2003). Negative regulation of T cell activation by placental protein 14 is mediated by the tyrosine phosphatase receptor CD45. J Biol. Chem. 278, 14059-14065.
    • (2003) J Biol. Chem. , vol.278 , pp. 14059-14065
    • Rachmilewitz, J.1    Borovsky, Z.2    Riely, G.J.3    Miller, R.4    Tykocinski, M.L.5
  • 53
    • 0024632478 scopus 로고
    • Expression and topographical localization of cell surface fucosyltransferase activity during epididymal sperm maturation in the mouse
    • Ram, P. A., Cardullo, R. A. and Millette, C. F. (1989). Expression and topographical localization of cell surface fucosyltransferase activity during epididymal sperm maturation in the mouse. Gamete Res. 22, 321-332.
    • (1989) Gamete Res. , vol.22 , pp. 321-332
    • Ram, P.A.1    Cardullo, R.A.2    Millette, C.F.3
  • 54
    • 0028785759 scopus 로고
    • Glycosidic specificity of fucosyltransferases present in rat epididymal spermatozoa
    • Raychoudhury, S. S. and Millette, C. F. (1995). Glycosidic specificity of fucosyltransferases present in rat epididymal spermatozoa. J Androl. 16, 448-456.
    • (1995) J Androl. , vol.16 , pp. 448-456
    • Raychoudhury, S.S.1    Millette, C.F.2
  • 55
    • 0030935579 scopus 로고    scopus 로고
    • Multiple fucosyltransferases and their carbohydrate ligands are involved in spermatogenic cell-Sertoli cell adhesion in vitro in rats
    • Raychoudhury, S. S. and Millette, C. F. (1997). Multiple fucosyltransferases and their carbohydrate ligands are involved in spermatogenic cell-Sertoli cell adhesion in vitro in rats. Biol. Reprod. 56, 1268-1273.
    • (1997) Biol. Reprod. , vol.56 , pp. 1268-1273
    • Raychoudhury, S.S.1    Millette, C.F.2
  • 56
    • 0029095778 scopus 로고
    • Relative positions of two clusters of human alpha-L-fucosyltransferases in 19q (FUT1-FUT2) and 19p (FUT6-FUT3-FUT5) within the microsatellite genetic map of chromosome 19
    • Reguigne-Arnould, I, Couillin, P., Mollicone, R., Faure, S., Fletcher, A., Kelly, R. J., Lowe, J. B. and Oriol, R. (1995). Relative positions of two clusters of human alpha-L-fucosyltransferases in 19q (FUT1-FUT2) and 19p (FUT6-FUT3-FUT5) within the microsatellite genetic map of chromosome 19. Cytogenet. Cell Genet. 71, 158-162.
    • (1995) Cytogenet. Cell Genet. , vol.71 , pp. 158-162
    • Reguigne-Arnould, I.1    Couillin, P.2    Mollicone, R.3    Faure, S.4    Fletcher, A.5    Kelly, R.J.6    Lowe, J.B.7    Oriol, R.8
  • 57
    • 0025968785 scopus 로고
    • Monoclonal antibodies against endometrial protein PP14 and their use for purification and radioimmunoassay of PP14
    • Riittinen, L., Narvanen, O., Virtanen, I. and Seppala, M. (1991). Monoclonal antibodies against endometrial protein PP14 and their use for purification and radioimmunoassay of PP14. J. Immunol. Methods 136, 85-90.
    • (1991) J. Immunol. Methods , vol.136 , pp. 85-90
    • Riittinen, L.1    Narvanen, O.2    Virtanen, I.3    Seppala, M.4
  • 58
    • 0019433474 scopus 로고
    • Glycosyltransferases of the human cervical epithelium. I. Characterization of a beta-galactoside alpha-2-L-fucosyltransferase and the identification of a beta-N-acetylglucosaminide alpha-3-L-fucosyltransferase
    • Scudder, P. R. and Chantler, E. N. (1981). Glycosyltransferases of the human cervical epithelium. I. Characterization of a beta-galactoside alpha-2-L-fucosyltransferase and the identification of a beta-N-acetylglucosaminide alpha-3-L-fucosyltransferase. Biochim. Biophys. Acta 660, 128-135.
    • (1981) Biochim. Biophys. Acta , vol.660 , pp. 128-135
    • Scudder, P.R.1    Chantler, E.N.2
  • 59
    • 0036668182 scopus 로고    scopus 로고
    • Glycodelin: A major lipocalin protein of the reproductive axis with diverse actions in cell recognition and differentiation
    • Seppala, M., Taylor, R. N., Koistinen, H., Koistinen, R. and Milgrom, E. (2002). Glycodelin: a major lipocalin protein of the reproductive axis with diverse actions in cell recognition and differentiation. Endocr. Rev. 23, 401-430.
    • (2002) Endocr. Rev. , vol.23 , pp. 401-430
    • Seppala, M.1    Taylor, R.N.2    Koistinen, H.3    Koistinen, R.4    Milgrom, E.5
  • 60
    • 0024297290 scopus 로고
    • Plasma membrane association, purification, and partial characterization of mouse sperm beta 1,4-galactosyltransferase
    • Shur, B. D. and Neely, C. A. (1988). Plasma membrane association, purification, and partial characterization of mouse sperm beta 1,4-galactosyltransferase. J. Biol. Chem. 263, 17706-17714.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17706-17714
    • Shur, B.D.1    Neely, C.A.2
  • 61
    • 29544450106 scopus 로고    scopus 로고
    • Sperm transport in the female reproductive tract
    • Suarez, S. S. and Pacey, A. A. (2006). Sperm transport in the female reproductive tract. Hum. Reprod. Update 12, 23-37.
    • (2006) Hum. Reprod. Update , vol.12 , pp. 23-37
    • Suarez, S.S.1    Pacey, A.A.2
  • 62
    • 0032488909 scopus 로고    scopus 로고
    • The transfer of retinol from serum retinol-binding protein to cellular retinol-binding protein is mediated by a membrane receptor
    • Sundaram, M., Sivaprasadarao, A., DeSousa, M. M. and Findlay, J. B. (1998). The transfer of retinol from serum retinol-binding protein to cellular retinol-binding protein is mediated by a membrane receptor. J. Biol. Chem. 273, 3336-3342.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3336-3342
    • Sundaram, M.1    Sivaprasadarao, A.2    DeSousa, M.M.3    Findlay, J.B.4
  • 63
    • 0029836135 scopus 로고    scopus 로고
    • The initial molecular interaction between mouse sperm and the zona pellucida is a complex binding event
    • Thaler, C. D. and Cardullo, R. A. (1996). The initial molecular interaction between mouse sperm and the zona pellucida is a complex binding event. J. Biol. Chem. 271, 23289-23297.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23289-23297
    • Thaler, C.D.1    Cardullo, R.A.2
  • 64
    • 0344199907 scopus 로고    scopus 로고
    • Molecules on the sperm's route to fertilization
    • Topfer-Petersen, E. (1999). Molecules on the sperm's route to fertilization. J. Exp. Zool. 285, 259-266.
    • (1999) J. Exp. Zool. , vol.285 , pp. 259-266
    • Topfer-Petersen, E.1
  • 66
    • 0024439966 scopus 로고
    • Novel alpha-D-mannosidase of rat sperm plasma membranes: Characterization and potential role in sperm-egg interactions
    • Tulsiani, D. R., Skudlarek, M. D. and Orgebin-Crist, M. C. (1989). Novel alpha-D-mannosidase of rat sperm plasma membranes: characterization and potential role in sperm-egg interactions. J. Cell Biol. 109, 1257-1267.
    • (1989) J. Cell Biol. , vol.109 , pp. 1257-1267
    • Tulsiani, D.R.1    Skudlarek, M.D.2    Orgebin-Crist, M.C.3
  • 67
    • 0025327871 scopus 로고
    • Human sperm plasma membranes possess alpha-D-mannosidase activity but no galactosyltransferase activity
    • Tulsiani, D. R., Skudlarek, M. D. and Orgebin-Crist, M. C. (1990). Human sperm plasma membranes possess alpha-D-mannosidase activity but no galactosyltransferase activity. Biol. Reprod. 42, 843-858.
    • (1990) Biol. Reprod. , vol.42 , pp. 843-858
    • Tulsiani, D.R.1    Skudlarek, M.D.2    Orgebin-Crist, M.C.3
  • 68
    • 0027531069 scopus 로고
    • Glycosylation of rat sperm plasma membrane during epididymal maturation
    • Tulsiani, D. R., Skudlarek, M. D., Holland, M. K. and Orgebin-Crist, M. C. (1993). Glycosylation of rat sperm plasma membrane during epididymal maturation. Biol. Reprod. 48, 417-428.
    • (1993) Biol. Reprod. , vol.48 , pp. 417-428
    • Tulsiani, D.R.1    Skudlarek, M.D.2    Holland, M.K.3    Orgebin-Crist, M.C.4
  • 69
    • 0032566436 scopus 로고    scopus 로고
    • Human alpha 1,3/4-fucosyltransferases. II. A single amino acid at the COOH terminus of FucT III and V alters their kinetic properties
    • Vo, L., Lee, S., Marcinko, M. C., Holmes, E. H. and Macher, B. A. (1998). Human alpha 1,3/4-fucosyltransferases. II. A single amino acid at the COOH terminus of FucT III and V alters their kinetic properties. J. Biol. Chem. 273, 25250-25255.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25250-25255
    • Vo, L.1    Lee, S.2    Marcinko, M.C.3    Holmes, E.H.4    Macher, B.A.5
  • 70
    • 0033593530 scopus 로고    scopus 로고
    • Mammalian fertilization: Molecular aspects of gamete adhesion, exocytosis, and fusion
    • Wassarman, P. M. (1999). Mammalian fertilization: molecular aspects of gamete adhesion, exocytosis, and fusion. Cell 96, 175-183.
    • (1999) Cell , vol.96 , pp. 175-183
    • Wassarman, P.M.1
  • 72
    • 0034705389 scopus 로고    scopus 로고
    • Binding and cross-linking studies show that scavenger receptor BI interacts with multiple sites in apolipoprotein A-I and identify the class A amphipatbic alpha-helix as a recognition motif
    • Williams, D. L., de La Llera-Moya, M., Thuahnai, S. T., Lund-Katz, S., Connelly, M. A., Azhar, S., Anantharamaiah, G. M. and Phillips, M. C. (2000). Binding and cross-linking studies show that scavenger receptor BI interacts with multiple sites in apolipoprotein A-I and identify the class A amphipatbic alpha-helix as a recognition motif. J. Biol. Chem. 275, 18897-18904.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18897-18904
    • Williams, D.L.1    de La Llera-Moya, M.2    Thuahnai, S.T.3    Lund-Katz, S.4    Connelly, M.A.5    Azhar, S.6    Anantharamaiah, G.M.7    Phillips, M.C.8
  • 73
    • 3242877152 scopus 로고
    • Mammalian fertilization
    • In 2nd edn (ed. E. Knobil and J. D. Neill), New York: Raven Press Ltd
    • Yanagimachi, R. (1994). Mammalian fertilization. In The Physiology of Mamalian Reproduction, 2nd edn (ed. E. Knobil and J. D. Neill), New York: Raven Press Ltd.
    • (1994) The Physiology of Mamalian Reproduction
    • Yanagimachi, R.1
  • 74
    • 0029810035 scopus 로고    scopus 로고
    • The factors affecting sperm binding to the zona pellucida in the hemizona binding assay
    • Yao, Y. Q., Yeung, W. S. and Ho, P. C. (1996). The factors affecting sperm binding to the zona pellucida in the hemizona binding assay. Hum. Reprod. 11, 1516-1519.
    • (1996) Hum. Reprod. , vol.11 , pp. 1516-1519
    • Yao, Y.Q.1    Yeung, W.S.2    Ho, P.C.3
  • 75
    • 0031689675 scopus 로고    scopus 로고
    • Glycoproteins present in human follicular fluid that inhibit the zona-binding capacity of spermatozoa
    • Yao, Y. Q., Chiu, C. N., Ip, S. M., Ho, P. C. and Yeung, W. S. (1998). Glycoproteins present in human follicular fluid that inhibit the zona-binding capacity of spermatozoa. Hum. Reprod. 13, 2541-2547.
    • (1998) Hum. Reprod. , vol.13 , pp. 2541-2547
    • Yao, Y.Q.1    Chiu, C.N.2    Ip, S.M.3    Ho, P.C.4    Yeung, W.S.5
  • 77
    • 0039107603 scopus 로고    scopus 로고
    • Localization of neutral N-linked carbohydrate chains in pig zona pellucida glycoprotein ZPC
    • Yonezawa, N., Fukui, N., Kudo, K. and Nakano, M. (1999). Localization of neutral N-linked carbohydrate chains in pig zona pellucida glycoprotein ZPC. Eur. J. Biochem. 260, 57-63.
    • (1999) Eur. J. Biochem. , vol.260 , pp. 57-63
    • Yonezawa, N.1    Fukui, N.2    Kudo, K.3    Nakano, M.4


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