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Volumn 56, Issue 5, 2010, Pages 349-364

The mammalian zona pellucida: A matrix that mediates both gamete binding and immune recognition?

Author keywords

Egg binding proteins; fertilization; glycosylation; immune response; oligosaccharides

Indexed keywords

GLYCOPROTEIN; GLYCOSYLTRANSFERASE; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1;

EID: 77956915396     PISSN: 19396368     EISSN: 19396368     Source Type: Journal    
DOI: 10.3109/19396360903524812     Document Type: Review
Times cited : (28)

References (133)
  • 1
    • 0035040864 scopus 로고    scopus 로고
    • Essential role of the nonreducing terminal a-mannosyl residues of the N-linked carbohydrate chain of bovine zona pellucida glyco-proteins in sperm-egg binding
    • Amari, S., Yonezawa, N., Mitsui, S., Katsumata, T., Hamano, S., Kuwayama, M., Hashimoto, Y., Suzuki, A., Takeda, Y. and Nakano, M. (2001) Essential role of the nonreducing terminal a-mannosyl residues of the N-linked carbohydrate chain of bovine zona pellucida glyco-proteins in sperm-egg binding. Mol Reprod Dev 59:221-226.
    • (2001) Mol Reprod Dev , vol.59 , pp. 221-226
    • Amari, S.1    Yonezawa, N.2    Mitsui, S.3    Katsumata, T.4    Hamano, S.5    Kuwayama, M.6    Hashimoto, Y.7    Suzuki, A.8    Takeda, Y.9    Nakano, M.10
  • 2
    • 0028229673 scopus 로고
    • An acrosomal protein, sp32, in mammalian sperm is a binding protein specific for two proacrosins and an acrosin intermediate
    • Baba, T., Niida, Y., Michikawa, Y., Kashiwabara, S., Kodaira, K., Takenaka, et al. (1994) An acrosomal protein, sp32, in mammalian sperm is a binding protein specific for two proacrosins and an acrosin intermediate. J Biol Chem 269:10133-10140.
    • (1994) J Biol Chem , vol.269 , pp. 10133-10140
    • Baba, T.1    Niida, Y.2    Michikawa, Y.3    Kashiwabara, S.4    Takenaka, K.K.5
  • 3
    • 67649639992 scopus 로고    scopus 로고
    • Functional activity of human ZP3 primary sperm receptor resides toward its C-terminus
    • Bansal, P., Chakrabarti, K. and Gupta, S. K. (2009) Functional activity of human ZP3 primary sperm receptor resides toward its C-terminus. Biol Reprod 81:7-15.
    • (2009) Biol Reprod , vol.81 , pp. 7-15
    • Bansal, P.1    Chakrabarti, K.2    Gupta, S.K.3
  • 4
    • 9244233286 scopus 로고    scopus 로고
    • Unusual uniformity of the N-linked oligosaccharides of HLA-A, -B, and -C glycoproteins
    • Barber, L. D., Patel, T. K. Percival, L., Gumperz, J. E., Lanier, L. L., Phillips, J. H., et al. (1996) Unusual uniformity of the N-linked oligosaccharides of HLA-A, -B, and -C glycoproteins. J Immunol 156:3275-3284.
    • (1996) J Immunol , vol.156 , pp. 3275-3284
    • Barber, L.D.1    Patel, T.K.2    Percival, L.3    Gumperz, J.E.4    Lanier, L.L.5    Phillips, J.H.6
  • 6
    • 0017693634 scopus 로고
    • Sperm/egg interaction: The specificity of human spermatozoa
    • Bedford, J. M. (1977) Sperm/egg interaction: the specificity of human spermatozoa. Anat Rec 188:477-487.
    • (1977) Anat Rec , vol.188 , pp. 477-487
    • Bedford, J.M.1
  • 7
    • 0024346478 scopus 로고
    • Sperm binding to the pig zona pellucida and inhibition of binding by solubilized components of the zona pellucida
    • Berger, T., Davis, A., Wardrip, N. J. and Hedrick, J. L. (1989a) Sperm binding to the pig zona pellucida and inhibition of binding by solubilized components of the zona pellucida. J Reprod Fertil 86:559-565.
    • (1989) J Reprod Fertil , vol.86 , pp. 559-565
    • Berger, T.1    Davis, A.2    Wardrip, N.J.3    Hedrick, J.L.4
  • 8
    • 0024623898 scopus 로고
    • Zona pellucida-induced acrosome reaction in boar sperm
    • Berger, T., Turner, K. O., Meizel, S. and Hedrick, J. L. (1989b) Zona pellucida-induced acrosome reaction in boar sperm. Biol Reprod 40:525-530.
    • (1989) Biol Reprod , vol.40 , pp. 525-530
    • Berger, T.1    Turner, K.O.2    Meizel, S.3    Hedrick, J.L.4
  • 9
    • 0023731968 scopus 로고
    • Identification of a secondary sperm receptor in the mouse egg zona pellucida: Role in maintenance of binding of acrosome-reacted sperm to eggs
    • Bleil, J. D., Greve, J. M. and Wassarman, P. M. (1988) Identification of a secondary sperm receptor in the mouse egg zona pellucida: role in maintenance of binding of acrosome-reacted sperm to eggs. Dev Biol 128:376-385.
    • (1988) Dev Biol , vol.128 , pp. 376-385
    • Bleil, J.D.1    Greve, J.M.2    Wassarman, P.M.3
  • 10
    • 54249155007 scopus 로고
    • Identification and characterization of proteins of zona pellucida
    • Bleil, J. D. and Wassarman, P. M. (1978) Identification and characterization of proteins of zona pellucida. J Cell Biol 79:A173.
    • (1978) J Cell Biol , vol.79
    • Bleil, J.D.1    Wassarman, P.M.2
  • 11
    • 0018822414 scopus 로고
    • Structure and function of the zona pellucida: Identification and characterization of the proteins of the mouse oocyte's zona pellucida
    • Bleil, J. D. and Wassarman, P. M. (1980a) Structure and function of the zona pellucida: identification and characterization of the proteins of the mouse oocyte's zona pellucida. Dev Biol 76:185-202.
    • (1980) Dev Biol , vol.76 , pp. 185-202
    • Bleil, J.D.1    Wassarman, P.M.2
  • 12
    • 0018831516 scopus 로고
    • Mammalian sperm-egg interaction: Identification of a glycoprotein in mouse egg zonae pellucidae possessing receptor activity for sperm
    • Bleil, J. D. and Wassarman, P. M. (1980b) Mammalian sperm-egg interaction: identification of a glycoprotein in mouse egg zonae pellucidae possessing receptor activity for sperm. Cell 20:873-882.
    • (1980) Cell , vol.20 , pp. 873-882
    • Bleil, J.D.1    Wassarman, P.M.2
  • 13
    • 0020665468 scopus 로고
    • Sperm-egg interactions in the mouse: Sequence of events and induction of the acrosome reaction by a zona pellucida glycoprotein
    • Bleil, J. D. and Wassarman, P. M. (1983) Sperm-egg interactions in the mouse: sequence of events and induction of the acrosome reaction by a zona pellucida glycoprotein. Dev Biol 95:317-324.
    • (1983) Dev Biol , vol.95 , pp. 317-324
    • Bleil, J.D.1    Wassarman, P.M.2
  • 14
    • 0343435291 scopus 로고
    • Galactose at the nonreducing terminus of O-linked oligosaccharides of mouse egg zona pellucida glycoprotein ZP3 is essential for the glycoprotein's sperm receptor activity
    • Bleil, J. D. and Wassarman, P. M. (1988) Galactose at the nonreducing terminus of O-linked oligosaccharides of mouse egg zona pellucida glycoprotein ZP3 is essential for the glycoprotein's sperm receptor activity. Proc Natl Acad Sci USA 85:6778-6782.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 6778-6782
    • Bleil, J.D.1    Wassarman, P.M.2
  • 15
    • 0141557578 scopus 로고    scopus 로고
    • Structural characterization of native mouse zona pellucida proteins using mass spectrometry
    • Boja, E. S., Hoodbhoy, T., Fales, H. M. and Dean, J. (2003) Structural characterization of native mouse zona pellucida proteins using mass spectrometry. J Biol Chem 278:34189-34202.
    • (2003) J Biol Chem , vol.278 , pp. 34189-34202
    • Boja, E.S.1    Hoodbhoy, T.2    Fales, H.M.3    Dean, J.4
  • 16
    • 0036151697 scopus 로고    scopus 로고
    • Structural organization and evolution of the marsupial zona pellucida
    • Breed, W. G., Hope, R. M., Wiebkin, O. W., Spargo, S. C. and Chapman, J. A. (2002) Structural organization and evolution of the marsupial zona pellucida. Reproduction 123:13-21.
    • (2002) Reproduction , vol.123 , pp. 13-21
    • Breed, W.G.1    Hope, R.M.2    Wiebkin, O.W.3    Spargo, S.C.4    Chapman, J.A.5
  • 17
    • 54249097511 scopus 로고    scopus 로고
    • The role of the acrosomal matrix in fertilization
    • Buffone, M. G., Foster, J. A. and Gerton, G. L. (2008a) The role of the acrosomal matrix in fertilization. Int J Dev Biol 52:511-522.
    • (2008) Int J Dev Biol , vol.52 , pp. 511-522
    • Buffone, M.G.1    Foster, J.A.2    Gerton, G.L.3
  • 18
    • 45549097542 scopus 로고    scopus 로고
    • Recombinant mouse sperm ZP3-binding protein (ZP3R/sp56) forms a high order oligomer that binds eggs and inhibits mouse fertilization in vitro
    • Buffone, M. G., Zhuang, T., Ord, T. S., Hui, L., Moss, S. B. and Gerton, G. L. (2008b) Recombinant mouse sperm ZP3-binding protein (ZP3R/sp56) forms a high order oligomer that binds eggs and inhibits mouse fertilization in vitro. J Biol Chem 283:12438-12445.
    • (2008) J Biol Chem , vol.283 , pp. 12438-12445
    • Buffone, M.G.1    Zhuang, T.2    Ord, T.S.3    Hui, L.4    Moss, S.B.5    Gerton, G.L.6
  • 19
    • 0023942614 scopus 로고
    • The hemizona assay (HZA): Development of a diagnostic test for the binding of human spermatozoa to the human hemizona pellucida to predict fertilization potential
    • Burkman, L. J., Coddington, C. C., Franken, D. R., Krugen, T. F., Rosenwaks, Z. and Hogen, G. D. (1988) The hemizona assay (HZA): development of a diagnostic test for the binding of human spermatozoa to the human hemizona pellucida to predict fertilization potential. Fertil Steril 49:688-697.
    • (1988) Fertil Steril , vol.49 , pp. 688-697
    • Burkman, L.J.1    Coddington, C.C.2    Franken, D.R.3    Krugen, T.F.4    Rosenwaks, Z.5    Hogen, G.D.6
  • 20
    • 0029832604 scopus 로고    scopus 로고
    • Boar spermadhesins AQN-1 and AQN-3: Oligosaccharide and zona pellucida binding characteristics
    • Calvete, J. J., Carrera, E., Sanz, L. and Topfer-Petersen, E. (1996) Boar spermadhesins AQN-1 and AQN-3: oligosaccharide and zona pellucida binding characteristics. Biol Chem 377:521-527.
    • (1996) Biol Chem , vol.377 , pp. 521-527
    • Calvete, J.J.1    Carrera, E.2    Sanz, L.3    Topfer-Petersen, E.4
  • 21
    • 36849093557 scopus 로고    scopus 로고
    • Relevance of glycosylation of human zona pellucida glycoproteins for their binding to capacitated human spermatozoa and subsequent induction of acrosomal exocytosis
    • Chakravarty, S., Kadunganattil, S., Bansal, P., Sharma, R. K. and Gupta, S. K. (2008) Relevance of glycosylation of human zona pellucida glycoproteins for their binding to capacitated human spermatozoa and subsequent induction of acrosomal exocytosis. Mol Reprod Dev 75:75-88.
    • (2008) Mol Reprod Dev , vol.75 , pp. 75-88
    • Chakravarty, S.1    Kadunganattil, S.2    Bansal, P.3    Sharma, R.K.4    Gupta, S.K.5
  • 22
    • 26444579958 scopus 로고    scopus 로고
    • Baculovirus expressed recombinant human zona pellucida glycoprotein-B induces acrosomal exocytosis in capacitated spermatozoa in addition to zona pellucida glycoprotein-C
    • Chakravarty, S., Kadunganattil, S. and Gupta, S. K. (2005) Baculovirus expressed recombinant human zona pellucida glycoprotein-B induces acrosomal exocytosis in capacitated spermatozoa in addition to zona pellucida glycoprotein-C. Mol Hum Reprod 11:365-372.
    • (2005) Mol Hum Reprod , vol.11 , pp. 365-372
    • Chakravarty, S.1    Kadunganattil, S.2    Gupta, S.K.3
  • 23
    • 0024561274 scopus 로고
    • Genomic organization of a sex specific gene: The primary sperm receptor of the mouse zona pellucida
    • Chamberlin, M. E. and Dean, J. (1989) Genomic organization of a sex specific gene: the primary sperm receptor of the mouse zona pellucida. Dev Biol 131:207-214.
    • (1989) Dev Biol , vol.131 , pp. 207-214
    • Chamberlin, M.E.1    Dean, J.2
  • 24
    • 0025102002 scopus 로고
    • Human homolog of the mouse sperm receptor
    • Chamberlin, M. E. and Dean, J. (1990) Human homolog of the mouse sperm receptor. Proc Natl Acad Sci USA 87:6014-6018.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6014-6018
    • Chamberlin, M.E.1    Dean, J.2
  • 25
    • 0032030791 scopus 로고    scopus 로고
    • The polypeptide backbone of recombinant human zona pellucida glycoprotein-3 initiates acrosomal exocytosis in human spermatozoa in vitro
    • Chapman, N., Kessopoulou, E., Andrews, P., Hornby, D. and Barratt, C. R. (1998) The polypeptide backbone of recombinant human zona pellucida glycoprotein-3 initiates acrosomal exocytosis in human spermatozoa in vitro. Biochem J 330 (Pt 2):839-845.
    • (1998) Biochem J , vol.330 , Issue.PART 2 , pp. 839-845
    • Chapman, N.1    Kessopoulou, E.2    Andrews, P.3    Hornby, D.4    Barratt, C.R.5
  • 26
    • 0032568506 scopus 로고    scopus 로고
    • Inactivation of the mouse sperm receptor, mZP3, by site-directed mutagenesis of individual serine residues located at the combining site for sperm
    • Chen, J., Litscher, E. S. and Wassarman, P. M. (1998) Inactivation of the mouse sperm receptor, mZP3, by site-directed mutagenesis of individual serine residues located at the combining site for sperm. Proc Natl Acad Sci USA 95:6193-6197.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6193-6197
    • Chen, J.1    Litscher, E.S.2    Wassarman, P.M.3
  • 27
    • 33846828527 scopus 로고    scopus 로고
    • Glycodelin-A interacts with fucosyltransferase on human sperm plasma membrane to inhibit spermatozoa-zona pellucida binding
    • Chiu, P. C., Chung, M. K., Koistinen, R., Koistinen, H., Seppala, M., Ho, P. C., et al. (2007) Glycodelin-A interacts with fucosyltransferase on human sperm plasma membrane to inhibit spermatozoa-zona pellucida binding. J Cell Sci 120:33-44.
    • (2007) J Cell Sci , vol.120 , pp. 33-44
    • Chiu, P.C.1    Chung, M.K.2    Koistinen, R.3    Koistinen, H.4    Seppala, M.5    Ho, P.C.6
  • 28
    • 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., et al. (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
  • 29
    • 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
  • 30
    • 55549122993 scopus 로고    scopus 로고
    • Effects of native human zona pellucida glycoproteins 3 and 4 on acrosome reaction and zona pellucida binding of human spermatozoa
    • Chiu, P. C., Wong, B. S., Chung, M. K., Lam, K. K., Pang, R. T., Lee, K. F., et al. (2008b) Effects of native human zona pellucida glycoproteins 3 and 4 on acrosome reaction and zona pellucida binding of human spermatozoa. Biol Reprod 79:869-877.
    • (2008) Biol Reprod , vol.79 , pp. 869-877
    • Chiu, P.C.1    Wong, B.S.2    Chung, M.K.3    Lam, K.K.4    Pang, R.T.5    Lee, K.F.6
  • 32
    • 33744911153 scopus 로고    scopus 로고
    • Molecular models for murine sperm-egg binding
    • Clark, G. F. and Dell, A. (2006) Molecular models for murine sperm-egg binding. J Biol Chem 281:13853-13856.
    • (2006) J Biol Chem , vol.281 , pp. 13853-13856
    • Clark, G.F.1    Dell, A.2
  • 33
    • 33744926287 scopus 로고    scopus 로고
    • The eutherian fetoembryonic defense system hypothesis: An update
    • ed. Mor, G. Landes Bioscience/Springer Science Business Media New York, NY
    • Clark, G. F., Dell, A., Morris, H. R. and Patankar, M. S. (2006) The eutherian fetoembryonic defense system hypothesis: an update. In Immunology of Pregnancy ed. Mor, G. Landes Bioscience/Springer Science Business Media New York, NY pp. 179-194.
    • (2006) Immunology of Pregnancy , pp. 179-194
    • Clark, G.F.1    Dell, A.2    Morris, H.R.3    Patankar, M.S.4
  • 34
    • 0035211941 scopus 로고    scopus 로고
    • The species recognition system: A new corrolary for the human fetoembryonic defense system hypothesis
    • Clark, G. F., Dell, A., Morris, H. R., Patankar, M. S. and Easton, R. L. (2001) The species recognition system: a new corrolary for the human fetoembryonic defense system hypothesis. Cells Tissue Organs 168:113-121.
    • (2001) Cells Tissue Organs , vol.168 , pp. 113-121
    • Clark, G.F.1    Dell, A.2    Morris, H.R.3    Patankar, M.S.4    Easton, R.L.5
  • 35
    • 0030177992 scopus 로고    scopus 로고
    • Role for glyco-conjugates in cellular communication in the human reproductive system
    • Clark, G. F., Oehninger, S. and Seppala, M. (1996) Role for glyco-conjugates in cellular communication in the human reproductive system. Mol Hum Reprod 2:513-517.
    • (1996) Mol Hum Reprod , vol.2 , pp. 513-517
    • Clark, G.F.1    Oehninger, S.2    Seppala, M.3
  • 36
    • 77956903405 scopus 로고    scopus 로고
    • Carbohydrate-mediated binding and induction of acrosomal exocytosis in a sperm-somatic cell adhesion model
    • (abstr.)
    • Clark, G. F., Sutovsky, P., Zimmerman, S., and Lafrenz, D. E. (2009) Carbohydrate-mediated binding and induction of acrosomal exocytosis in a sperm-somatic cell adhesion model. Biol Reprod 81: 328 (abstr.).
    • (2009) Biol Reprod , vol.81 , pp. 328
    • Clark, G.F.1    Sutovsky, P.2    Zimmerman, S.3    Lafrenz, D.E.4
  • 38
    • 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., et al. (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
  • 39
    • 0035825644 scopus 로고    scopus 로고
    • Negative regulation of T-cell activation and autoimmunity by Mgat5 N-glycosylation
    • Demetriou, M., Granovsky, M., Quaggin, S. and Dennis, J. W. (2001) Negative regulation of T-cell activation and autoimmunity by Mgat5 N-glycosylation. Nature 409:733-739.
    • (2001) Nature , vol.409 , pp. 733-739
    • Demetriou, M.1    Granovsky, M.2    Quaggin, S.3    Dennis, J.W.4
  • 40
    • 54249114380 scopus 로고
    • Isolation and physico-chemical properties of porcine zona pellucida
    • Dunbar, B. S., Wardrip, N. J. and Hedrick, J. L. (1978) Isolation and physico-chemical properties of porcine zona pellucida. J Cell Biol 79:A163.
    • (1978) J Cell Biol , vol.79
    • Dunbar, B.S.1    Wardrip, N.J.2    Hedrick, J.L.3
  • 41
    • 0034677921 scopus 로고    scopus 로고
    • Structural analysis of murine zona pellucida glycans. Evidence for the expression of core 2-type O-glycans and the Sda antigen
    • Easton, R. L., Patankar, M. S., Lattanzio, F. A., Leaven, T. H., Morris, H. R., Clark, G. F. and Dell, A. (2000) Structural analysis of murine zona pellucida glycans. Evidence for the expression of core 2-type O-glycans and the Sda antigen. J Biol Chem 275:7731-7742.
    • (2000) J Biol Chem , vol.275 , pp. 7731-7742
    • Easton, R.L.1    Patankar, M.S.2    Lattanzio, F.A.3    Leaven, T.H.4    Morris, H.R.5    Clark, G.F.6    Dell, A.7
  • 42
    • 0028972248 scopus 로고
    • Glycophorin A protects K562 cells from natural killer cell attack. Role of oligosaccharides
    • el Ouagari, K., Teissie, J. and Benoist, H. (1995) Glycophorin A protects K562 cells from natural killer cell attack. Role of oligosaccharides. J Biol Chem 270:26970-26975.
    • (1995) J Biol Chem , vol.270 , pp. 26970-26975
    • El Ouagari, K.1    Teissie, J.2    Benoist, H.3
  • 43
    • 0029583780 scopus 로고
    • Identification by affinity chromatography of boar sperm membrane-associated proteins bound to immobilized porcine zona pellucida. Mapping of the phosphorylethanolamine-binding region of spermadhesin AWN
    • Ensslin, M., Calvete, J. J., Thole, H. H., Sierralta, W. D., Adermann, K., Sanz, L. and Topfer-Petersen, E. (1995) Identification by affinity chromatography of boar sperm membrane-associated proteins bound to immobilized porcine zona pellucida. Mapping of the phosphorylethanolamine-binding region of spermadhesin AWN. Biol Chem Hoppe Seyler 376:733-738.
    • (1995) Biol Chem Hoppe Seyler , vol.376 , pp. 733-738
    • Ensslin, M.1    Calvete, J.J.2    Thole, H.H.3    Sierralta, W.D.4    Adermann, K.5    Sanz, L.6    Topfer-Petersen, E.7
  • 44
    • 0043029287 scopus 로고    scopus 로고
    • Identification of mouse sperm SED1, a bimotif EGF repeat and discoidin-domain protein involved in sperm-egg binding
    • Ensslin, M. A. and Shur, B. D. (2003) Identification of mouse sperm SED1, a bimotif EGF repeat and discoidin-domain protein involved in sperm-egg binding. Cell 114:405-417.
    • (2003) Cell , vol.114 , pp. 405-417
    • Ensslin, M.A.1    Shur, B.D.2
  • 45
    • 0028818844 scopus 로고
    • Mouse Zp1 encodes a zona pellucida protein homologous to egg envelope proteins in mammals and fish
    • Epifano, O., Liang, L. F. and Dean, J. (1995) Mouse Zp1 encodes a zona pellucida protein homologous to egg envelope proteins in mammals and fish. J Biol Chem 270:27254-27258.
    • (1995) J Biol Chem , vol.270 , pp. 27254-27258
    • Epifano, O.1    Liang, L.F.2    Dean, J.3
  • 46
    • 0021710179 scopus 로고
    • Enzymatic dissection of the functions of the mouse egg's receptor for sperm
    • Florman, H. M., Bechtol, K. B. and Wassarman, P. M. (1984) Enzymatic dissection of the functions of the mouse egg's receptor for sperm. Dev Biol 106:243-255.
    • (1984) Dev Biol , vol.106 , pp. 243-255
    • Florman, H.M.1    Bechtol, K.B.2    Wassarman, P.M.3
  • 47
    • 0023715942 scopus 로고
    • The regulation of acrosomal exocytosis I. Sperm capacitation is required for the induction of acrosome reactions by the bovine zona pellucida in vitro
    • Florman, H. M. and First, N. L. (1988) The regulation of acrosomal exocytosis. I. Sperm capacitation is required for the induction of acrosome reactions by the bovine zona pellucida in vitro. Dev Biol 128:453-463.
    • (1988) Dev Biol , vol.128 , pp. 453-463
    • Florman, H.M.1    First, N.L.2
  • 49
    • 0030974131 scopus 로고    scopus 로고
    • AM67, a secretory component of the guinea pig sperm acrosomal matrix, is related to mouse sperm protein sp56 and the complement component 4-binding proteins
    • Foster, J. A., Friday, B. B., Maulit, M. T., Blobel, C., Winfrey, V. P., Olson, G. E., et al. (1997) AM67, a secretory component of the guinea pig sperm acrosomal matrix, is related to mouse sperm protein sp56 and the complement component 4-binding proteins. J Biol Chem 272:12714-12722.
    • (1997) J Biol Chem , vol.272 , pp. 12714-12722
    • Foster, J.A.1    Friday, B.B.2    Maulit, M.T.3    Blobel, C.4    Winfrey, V.P.5    Olson, G.E.6
  • 50
    • 0029864670 scopus 로고    scopus 로고
    • Defining bioassay conditions to evaluate sperm/zona interaction: Inhibition of zona binding mediated by solubilized human zona pellucida
    • Franken, D. R., Henkel, R., Kaskar, K. and Habenicht, U. F. (1996) Defining bioassay conditions to evaluate sperm/zona interaction: inhibition of zona binding mediated by solubilized human zona pellucida. J Assist Reprod Genet 13:329-332.
    • (1996) J Assist Reprod Genet , vol.13 , pp. 329-332
    • Franken, D.R.1    Henkel, R.2    Kaskar, K.3    Habenicht, U.F.4
  • 52
    • 0024288350 scopus 로고
    • Structure elucidation of blood group B-like and I-active ceramide eicosa- and pentacosasaccharides from rabbit erythrocyte membranes by combined gas chromatography-mass spectrometry; Electron-impact and fast-atom-bombardment mass spectrometry; And two-dimensional correlated, relayed-coherence transfer, and nuclear Overhauser effect 500-MHz 1H-n.m.r. spectroscopy
    • Hanfland, P., Kordowicz, M., Peter-Katalinic, J., Egge, H., Dabrowski, J. and Dabrowski, U. (1988) Structure elucidation of blood group B-like and I-active ceramide eicosa- and pentacosasaccharides from rabbit erythrocyte membranes by combined gas chromatography-mass spectrometry; electron-impact and fast-atom-bombardment mass spectrometry; and two-dimensional correlated, relayed-coherence transfer, and nuclear Overhauser effect 500-MHz 1H-n.m.r. spectroscopy. Carbohydr Res 178:1-21.
    • (1988) Carbohydr Res , vol.178 , pp. 1-21
    • Hanfland, P.1    Kordowicz, M.2    Peter-Katalinic, J.3    Egge, H.4    Dabrowski, J.5    Dabrowski, U.6
  • 53
    • 0028045713 scopus 로고
    • Cloning and characterization of zona pellucida genes and cDNAs from a variety of mammalian species: The ZPA, ZPB and ZPC gene families
    • Harris, J. D., Hibler, D. W., Fontenot, G. K., Hsu, K. T., Yurewicz, E. C. and Sacco, A. G. (1994) Cloning and characterization of zona pellucida genes and cDNAs from a variety of mammalian species: the ZPA, ZPB and ZPC gene families. DNA Seq 4:361-393.
    • (1994) DNA Seq , vol.4 , pp. 361-393
    • Harris, J.D.1    Hibler, D.W.2    Fontenot, G.K.3    Hsu, K.T.4    Yurewicz, E.C.5    Sacco, A.G.6
  • 54
    • 54249091677 scopus 로고    scopus 로고
    • Anuran and pig egg zona pellucida glycoproteins in fertilization and early development
    • Hedrick, J. L. (2008) Anuran and pig egg zona pellucida glycoproteins in fertilization and early development. Int J Dev Biol 52:683-701.
    • (2008) Int J Dev Biol , vol.52 , pp. 683-701
    • Hedrick, J.L.1
  • 56
    • 0027183480 scopus 로고
    • Structure of three acidic O-linked carbohydrate chains of porcine zona pellucida glycoproteins
    • Hokke, C. H., Damm, J. B., Kamerling, J. P. and Vliegenthart, J. F. (1993) Structure of three acidic O-linked carbohydrate chains of porcine zona pellucida glycoproteins. FEBS Lett 329:29-34.
    • (1993) FEBS Lett , vol.329 , pp. 29-34
    • Hokke, C.H.1    Damm, J.B.2    Kamerling, J.P.3    Vliegenthart, J.F.4
  • 58
    • 16844387092 scopus 로고    scopus 로고
    • Human sperm do not bind to rat zonae pellucidae despite the presence of four homologous glycoproteins
    • Hoodbhoy, T., Joshi, S., Boja, E. S., Williams, S. A., Stanley, P. and Dean, J. (2005) Human sperm do not bind to rat zonae pellucidae despite the presence of four homologous glycoproteins. J Biol Chem 280:12721-12731.
    • (2005) J Biol Chem , vol.280 , pp. 12721-12731
    • Hoodbhoy, T.1    Joshi, S.2    Boja, E.S.3    Williams, S.A.4    Stanley, P.5    Dean, J.6
  • 59
    • 0032719660 scopus 로고    scopus 로고
    • Identification of the true human orthologue of the mouse Zp1 gene: Evidence for greater complexity in the mammalian zona pellucida?
    • Hughes, D. C. and Barratt, C. L. (1999) Identification of the true human orthologue of the mouse Zp1 gene: evidence for greater complexity in the mammalian zona pellucida? Biochim Biophys Acta 1447:303-306.
    • (1999) Biochim Biophys Acta , vol.1447 , pp. 303-306
    • Hughes, D.C.1    Barratt, C.L.2
  • 60
    • 0031915969 scopus 로고    scopus 로고
    • Murine sperm-zona binding, a fucosyl residue is required for a high affinity sperm-binding ligand. A second site on sperm binds a nonfucosylated, b-galactosyl-capped oligosaccharide
    • Johnston, D. S., Wright, W. W., Shaper, J. H., Hokke, C. H., Van den Eijnden, D. H. and Joziasse, D. H. (1998) Murine sperm-zona binding, a fucosyl residue is required for a high affinity sperm-binding ligand. A second site on sperm binds a nonfucosylated, b-galactosyl-capped oligosaccharide. J Biol Chem 273:1888-1895.
    • (1998) J Biol Chem , vol.273 , pp. 1888-1895
    • Johnston, D.S.1    Wright, W.W.2    Shaper, J.H.3    Hokke, C.H.4    Van Den Eijnden, D.H.5    Joziasse, D.H.6
  • 61
    • 34848826611 scopus 로고    scopus 로고
    • Recombinant bovine zona pellucida glycoproteins ZP3 and ZP4 coexpressed in Sf9 cells form a sperm-binding active hetero-complex
    • Kanai, S., Yonezawa, N., Ishii, Y., Tanokura, M. and Nakano, M. (2007) Recombinant bovine zona pellucida glycoproteins ZP3 and ZP4 coexpressed in Sf9 cells form a sperm-binding active hetero-complex. Febs J 274:5390-5405.
    • (2007) Febs J , vol.274 , pp. 5390-5405
    • Kanai, S.1    Yonezawa, N.2    Ishii, Y.3    Tanokura, M.4    Nakano, M.5
  • 62
    • 0036229771 scopus 로고    scopus 로고
    • NK cells, MHC class i molecules and the missing self
    • Karre, K. (2002) NK cells, MHC class I molecules and the missing self. Scand J Immunol 55:221-228.
    • (2002) Scand J Immunol , vol.55 , pp. 221-228
    • Karre, K.1
  • 63
    • 0029830057 scopus 로고    scopus 로고
    • Structural characterization of the N-linked carbohydrate chains of the zona pellucida glycoproteins from bovine ovarian and fertilized eggs
    • Katsumata, T., Noguchi, S., Yonezawa, N., Tanokura, M. and Nakano, M. (1996) Structural characterization of the N-linked carbohydrate chains of the zona pellucida glycoproteins from bovine ovarian and fertilized eggs. Eur J Biochem 240:448-453.
    • (1996) Eur J Biochem , vol.240 , pp. 448-453
    • Katsumata, T.1    Noguchi, S.2    Yonezawa, N.3    Tanokura, M.4    Nakano, M.5
  • 64
    • 4243068580 scopus 로고    scopus 로고
    • Lewis X-containing glycans are specific and potent competitive inhibitors of the binding of ZP3 to complementary sites on capacitated, acrosome-intact mouse sperm
    • Kerr, C. L., Hanna, W. F., Shaper, J. H. and Wright, W. W. (2004) Lewis X-containing glycans are specific and potent competitive inhibitors of the binding of ZP3 to complementary sites on capacitated, acrosome-intact mouse sperm. Biol Reprod 71:770-777.
    • (2004) Biol Reprod , vol.71 , pp. 770-777
    • Kerr, C.L.1    Hanna, W.F.2    Shaper, J.H.3    Wright, W.W.4
  • 65
    • 0026086535 scopus 로고
    • Embryonal carcinoma cells transfected with ZP3 genes differentially glycosylate similar polypeptides and secrete active mouse sperm receptor
    • Kinloch, R. A., Mortillo, S., Stewart, C. L. and Wassarman, P. M. (1991) Embryonal carcinoma cells transfected with ZP3 genes differentially glycosylate similar polypeptides and secrete active mouse sperm receptor. J Cell Biol 115:655-664.
    • (1991) J Cell Biol , vol.115 , pp. 655-664
    • Kinloch, R.A.1    Mortillo, S.2    Stewart, C.L.3    Wassarman, P.M.4
  • 67
    • 0032521660 scopus 로고    scopus 로고
    • Localization of carbohydrate chains of pig sperm ligand in the glycoprotein ZPB of egg zona pellucida
    • Kudo, K., Yonezawa, N., Katsumata, T., Aoki, H. and Nakano, M. (1998) Localization of carbohydrate chains of pig sperm ligand in the glycoprotein ZPB of egg zona pellucida. Eur J Biochem 252:492-499.
    • (1998) Eur J Biochem , vol.252 , pp. 492-499
    • Kudo, K.1    Yonezawa, N.2    Katsumata, T.3    Aoki, H.4    Nakano, M.5
  • 69
    • 35848965902 scopus 로고    scopus 로고
    • Polypeptide backbone derived from carboxyl terminal of mouse ZP3 inhibits sperm-zona binding
    • Li, D., Cao, S. and Xu, C. (2007) Polypeptide backbone derived from carboxyl terminal of mouse ZP3 inhibits sperm-zona binding. Mol Reprod Dev 74:1327-1336.
    • (2007) Mol Reprod Dev , vol.74 , pp. 1327-1336
    • Li, D.1    Cao, S.2    Xu, C.3
  • 70
    • 0025255277 scopus 로고
    • Oocyte-specific expression of mouse Zp-2: Developmental regulation of the zona pellucida genes
    • Liang, L. F., Chamow, S. M. and Dean, J. (1990) Oocyte-specific expression of mouse Zp-2: developmental regulation of the zona pellucida genes. Mol Cell Biol 10:1507-1515.
    • (1990) Mol Cell Biol , vol.10 , pp. 1507-1515
    • Liang, L.F.1    Chamow, S.M.2    Dean, J.3
  • 71
    • 0027416199 scopus 로고
    • Conservation of mammalian secondary sperm receptor genes enables the promoter of the human gene to function in mouse oocytes
    • Liang, L. F. and Dean, J. (1993) Conservation of mammalian secondary sperm receptor genes enables the promoter of the human gene to function in mouse oocytes. Dev Biol 156:399-408.
    • (1993) Dev Biol , vol.156 , pp. 399-408
    • Liang, L.F.1    Dean, J.2
  • 72
    • 34748822250 scopus 로고    scopus 로고
    • Loss of zona pellucida binding proteins in the acrosomal matrix disrupts acrosome biogenesis and sperm morphogenesis
    • Lin, Y. N., Roy, A., Yan, W., Burns, K. H. and Matzuk, M. M. (2007) Loss of zona pellucida binding proteins in the acrosomal matrix disrupts acrosome biogenesis and sperm morphogenesis. Mol Cell Biol 27:6794-6805.
    • (2007) Mol Cell Biol , vol.27 , pp. 6794-6805
    • Lin, Y.N.1    Roy, A.2    Yan, W.3    Burns, K.H.4    Matzuk, M.M.5
  • 73
    • 33751155433 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
  • 74
    • 0029946034 scopus 로고    scopus 로고
    • Characterization of mouse ZP3-derived glycopeptide, gp55, that exhibits sperm receptor and acrosome reaction-inducing activity in vitro
    • Litscher, E. S. and Wassarman, P. M. (1996) Characterization of mouse ZP3-derived glycopeptide, gp55, that exhibits sperm receptor and acrosome reaction-inducing activity in vitro. Biochemistry 35:3980-3985.
    • (1996) Biochemistry , vol.35 , pp. 3980-3985
    • Litscher, E.S.1    Wassarman, P.M.2
  • 75
    • 9344231925 scopus 로고    scopus 로고
    • Targeted disruption of the mZP3 gene results in production of eggs lacking a zona pellucida and infertility in female mice
    • Liu, C., Litscher, E. S., Mortillo, S., Sakai, Y., Kinloch, R. A., Stewart, C. L. and Wassarman, P.M. (1996) Targeted disruption of the mZP3 gene results in production of eggs lacking a zona pellucida and infertility in female mice. Proc Natl Acad Sci USA 93:5431-5436.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5431-5436
    • Liu, C.1    Litscher, E.S.2    Mortillo, S.3    Sakai, Y.4    Kinloch, R.A.5    Stewart, C.L.6    Wassarman, P.M.7
  • 76
    • 0031265217 scopus 로고    scopus 로고
    • Normal sperm-zona pellucida interaction and fertilization in vitro in a1-3-galactosyltransferase gene knockout mice
    • Liu, D. Y., Baker, H. W., Pearse, M. J. and d'Apice, A. J. (1997) Normal sperm-zona pellucida interaction and fertilization in vitro in a1-3-galactosyltransferase gene knockout mice. Mol Hum Reprod 3:1015-1016.
    • (1997) Mol Hum Reprod , vol.3 , pp. 1015-1016
    • Liu, D.Y.1    Baker, H.W.2    Pearse, M.J.3    D'Apice, A.J.4
  • 77
    • 0022351299 scopus 로고
    • Receptor function of mouse sperm surface galactosyltransferase during fertilization
    • Lopez, L. C., Bayna, E. M., Litoff, D., Shaper, N. L., Shaper, J. H. and Shur, B. D. (1985) Receptor function of mouse sperm surface galactosyltransferase during fertilization. J Cell Biol 101:1501-1510.
    • (1985) J Cell Biol , vol.101 , pp. 1501-1510
    • Lopez, L.C.1    Bayna, E.M.2    Litoff, D.3    Shaper, N.L.4    Shaper, J.H.5    Shur, B.D.6
  • 78
    • 0030728461 scopus 로고    scopus 로고
    • Sperm from b1,4-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 b1,4-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
  • 79
    • 0034954813 scopus 로고    scopus 로고
    • Glycobiology of sperm-egg interactions in deuterostomes
    • Mengerink, K. J. and Vacquier, V. D. (2001) Glycobiology of sperm-egg interactions in deuterostomes. Glycobiology 11:37R-43R.
    • (2001) Glycobiology , vol.11
    • Mengerink, K.J.1    Vacquier, V.D.2
  • 80
    • 0026611050 scopus 로고
    • Complementarity between sperm surface b-1,4-galactosyltransferase and egg-coat ZP3 mediates sperm-egg binding
    • Miller, D. J., Macek, M. B. and Shur, B. D. (1992) Complementarity between sperm surface b-1,4-galactosyltransferase and egg-coat ZP3 mediates sperm-egg binding. Nature 357:589-593.
    • (1992) Nature , vol.357 , pp. 589-593
    • Miller, D.J.1    MacEk, M.B.2    Shur, B.D.3
  • 81
    • 57349125672 scopus 로고    scopus 로고
    • Crystal structure of the ZP-N domain of ZP3 reveals the core fold of animal egg coats
    • Monne, M., Han, L., Schwend, T., Burendahl, S. and Jovine, L. (2008) Crystal structure of the ZP-N domain of ZP3 reveals the core fold of animal egg coats. Nature 456:653-657.
    • (2008) Nature , vol.456 , pp. 653-657
    • Monne, M.1    Han, L.2    Schwend, T.3    Burendahl, S.4    Jovine, L.5
  • 82
    • 0031860314 scopus 로고    scopus 로고
    • Occurrence of reducing terminal N-acetylglucosamine 3-sulfate and fucosylated outer chains in acidic N-glycans of porcine zona pellucida glycoproteins
    • Mori, E., Hedrick, J. L., Wardrip, N. J., Mori, T. and Takasaki, S. (1998) Occurrence of reducing terminal N-acetylglucosamine 3-sulfate and fucosylated outer chains in acidic N-glycans of porcine zona pellucida glycoproteins. Glycoconj J 15:447-456.
    • (1998) Glycoconj J , vol.15 , pp. 447-456
    • Mori, E.1    Hedrick, J.L.2    Wardrip, N.J.3    Mori, T.4    Takasaki, S.5
  • 83
    • 0031559852 scopus 로고    scopus 로고
    • Binding of mouse sperm to b-galactose residues on egg zona pellucida and asialofetuin-coupled beads
    • Mori, E., Mori, T. and Takasaki, S. (1997) Binding of mouse sperm to b-galactose residues on egg zona pellucida and asialofetuin-coupled beads. Biochem Biophys Res Commun 238:95-99.
    • (1997) Biochem Biophys Res Commun , vol.238 , pp. 95-99
    • Mori, E.1    Mori, T.2    Takasaki, S.3
  • 84
    • 0025975588 scopus 로고
    • Neutral oligosaccharide structures linked to asparagines of porcine zona pellucida glycoproteins
    • Mori, E., Takasaki, S., Hedrick, J. L., Wardrip, N. J., Mori, T. and Kobata, A. (1991) Neutral oligosaccharide structures linked to asparagines of porcine zona pellucida glycoproteins. Biochemistry 30:2078-2087.
    • (1991) Biochemistry , vol.30 , pp. 2078-2087
    • Mori, E.1    Takasaki, S.2    Hedrick, J.L.3    Wardrip, N.J.4    Mori, T.5    Kobata, A.6
  • 85
    • 10544251443 scopus 로고    scopus 로고
    • Gender-specific glycosylation of human glycodelin affects its contraceptive activity
    • Morris, H. R., Dell, A., Easton, R. L., Panico, M., Koistinen, H., Koistinen, R., et al. (1996) Gender-specific glycosylation of human glycodelin affects its contraceptive activity. J Biol Chem 271:32159-32167.
    • (1996) J Biol Chem , vol.271 , pp. 32159-32167
    • Morris, H.R.1    Dell, A.2    Easton, R.L.3    Panico, M.4    Koistinen, H.5    Koistinen, R.6
  • 86
    • 0030333226 scopus 로고    scopus 로고
    • Structure and function of the N-linked carbohydrate chains of pig zona pellucida glycoproteins
    • Nakano, M., Yonezawa, N., Hatanaka, Y. and Noguchi, S. (1996) Structure and function of the N-linked carbohydrate chains of pig zona pellucida glycoproteins. J Reprod Fertil Suppl 50:25-34.
    • (1996) J Reprod Fertil Suppl , vol.50 , pp. 25-34
    • Nakano, M.1    Yonezawa, N.2    Hatanaka, Y.3    Noguchi, S.4
  • 87
    • 23644440524 scopus 로고    scopus 로고
    • The role of molecular chaperones in mouse sperm-egg interactions
    • Nixon, B., Asquith, K. L. and Aitken, R. J. (2005) The role of molecular chaperones in mouse sperm-egg interactions. Mol Cell Endocrinol 240:1-10.
    • (2005) Mol Cell Endocrinol , vol.240 , pp. 1-10
    • Nixon, B.1    Asquith, K.L.2    Aitken, R.J.3
  • 89
    • 0026658978 scopus 로고
    • Structural analysis of the N-linked carbohydrate chains of the 55-kDa glycoprotein family (pZP3) from porcine zona pellucida
    • Noguchi, S., Hatanaka, Y., Tobita, T. and Nakano, M. (1992) Structural analysis of the N-linked carbohydrate chains of the 55-kDa glycoprotein family (pZP3) from porcine zona pellucida. Eur J Biochem 207:1130.
    • (1992) Eur J Biochem , vol.207 , pp. 1130
    • Noguchi, S.1    Hatanaka, Y.2    Tobita, T.3    Nakano, M.4
  • 90
    • 0026441404 scopus 로고
    • Structure of the acidic N-linked carbohydrate chains of the 55-kDa glycoprotein family (PZP3) from porcine zona pellucida
    • Noguchi, S. and Nakano, M. (1992) Structure of the acidic N-linked carbohydrate chains of the 55-kDa glycoprotein family (PZP3) from porcine zona pellucida. Eur J Biochem 209:883-894.
    • (1992) Eur J Biochem , vol.209 , pp. 883-894
    • Noguchi, S.1    Nakano, M.2
  • 91
    • 0027421777 scopus 로고
    • Structural characterization of the N-linked carbohydrate chains from mouse zona pellucida glycoproteins ZP2 and ZP3
    • Noguchi, S. and Nakano, M. (1993) Structural characterization of the N-linked carbohydrate chains from mouse zona pellucida glycoproteins ZP2 and ZP3. Biochim Biophys Acta 1158:217-226.
    • (1993) Biochim Biophys Acta , vol.1158 , pp. 217-226
    • Noguchi, S.1    Nakano, M.2
  • 93
    • 0025190765 scopus 로고
    • Antagonistic and agonistic properties of saccharide moieties in the hemizona assay
    • Oehninger, S., Acosta, A. and Hodgen, G. D. (1990) 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
  • 94
    • 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
  • 95
    • 0017066575 scopus 로고
    • Penetration of the zona pellucida of nonliving human oocytes by human spermatozoa in vitro
    • Overstreet, J. W. and Hembree, W. C. (1976) Penetration of the zona pellucida of nonliving human oocytes by human spermatozoa in vitro. Fertil Steril 27:815-831.
    • (1976) Fertil Steril , vol.27 , pp. 815-831
    • Overstreet, J.W.1    Hembree, W.C.2
  • 96
    • 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
  • 97
    • 37549046431 scopus 로고    scopus 로고
    • Expression of bisecting type and Lewisx/Lewisy terminated N-glycans on human sperm
    • Pang, P. C., Tissot, B., Drobnis, E. Z., Sutovsky, P., Morris, H. R., Clark, G. F. and Dell, A. (2007) Expression of bisecting type and Lewisx/Lewisy terminated N-glycans on human sperm. J Biol Chem 282:36593-36602.
    • (2007) J Biol Chem , vol.282 , pp. 36593-36602
    • Pang, P.C.1    Tissot, B.2    Drobnis, E.Z.3    Sutovsky, P.4    Morris, H.R.5    Clark, G.F.6    Dell, A.7
  • 98
    • 0027494436 scopus 로고
    • A revised structure for fucoidan may explain some of its biological activities
    • Patankar, M. S., Oehninger, S., Barnett, T., Williams, R. L. and Clark, G. F. (1993) A revised structure for fucoidan may explain some of its biological activities. J Biol Chem 268:21770-21776.
    • (1993) J Biol Chem , vol.268 , pp. 21770-21776
    • Patankar, M.S.1    Oehninger, S.2    Barnett, T.3    Williams, R.L.4    Clark, G.F.5
  • 99
  • 100
    • 0029818998 scopus 로고    scopus 로고
    • Mice homozygous for an insertional mutation in the ZP3 gene lack a zona pellucida and are infertile
    • Rankin, T., Familari, M., Lee, E., Ginsberg, A., Dwyer, N., Blanchette-Mackie, J., et al. (1996) Mice homozygous for an insertional mutation in the ZP3 gene lack a zona pellucida and are infertile. Development 122:2903-2910.
    • (1996) Development , vol.122 , pp. 2903-2910
    • Rankin, T.1    Familari, M.2    Lee, E.3    Ginsberg, A.4    Dwyer, N.5    Blanchette-Mackie, J.6
  • 101
    • 0032821285 scopus 로고    scopus 로고
    • Abnormal zonae pellucidae in mice lacking ZP1 result in early embryonic loss
    • Rankin, T., Talbot, P., Lee, E. and Dean, J. (1999) Abnormal zonae pellucidae in mice lacking ZP1 result in early embryonic loss. Development 126:3847-3855.
    • (1999) Development , vol.126 , pp. 3847-3855
    • Rankin, T.1    Talbot, P.2    Lee, E.3    Dean, J.4
  • 102
    • 0037672205 scopus 로고    scopus 로고
    • Fertility and taxon-specific sperm binding persist after replacement of mouse sperm receptors with human homologs
    • Rankin, T. L., Coleman, J. S., Epifano, O., Hoodbhoy, T., Turner, S. G., Castle, P. E., et al. (2003) Fertility and taxon-specific sperm binding persist after replacement of mouse sperm receptors with human homologs. Dev Cell 5:33-43.
    • (2003) Dev Cell , vol.5 , pp. 33-43
    • Rankin, T.L.1    Coleman, J.S.2    Epifano, O.3    Hoodbhoy, T.4    Turner, S.G.5    Castle, P.E.6
  • 103
    • 0031927829 scopus 로고    scopus 로고
    • Human ZP3 restores fertility in ZP3 null mice without affecting order-specific sperm binding
    • Rankin, T. L., Tong, Z. B., Castle, P. E., Lee, E., Gore-Langton, R., Nelson, L. M. and Dean, J. (1998) Human ZP3 restores fertility in ZP3 null mice without affecting order-specific sperm binding. Development 125:2415-2424.
    • (1998) Development , vol.125 , pp. 2415-2424
    • Rankin, T.L.1    Tong, Z.B.2    Castle, P.E.3    Lee, E.4    Gore-Langton, R.5    Nelson, L.M.6    Dean, J.7
  • 104
    • 0024442504 scopus 로고
    • Porcine zona pellucida: Association of sperm receptor activity with the a-glycoprotein component of the Mr = 55,000 family
    • Sacco, A. G., Yurewicz, E. C., Subramanian, M. G. and Matzat, P. D. (1989) Porcine zona pellucida: association of sperm receptor activity with the a-glycoprotein component of the Mr = 55,000 family. Biol Reprod 41:523-532.
    • (1989) Biol Reprod , vol.41 , pp. 523-532
    • Sacco, A.G.1    Yurewicz, E.C.2    Subramanian, M.G.3    Matzat, P.D.4
  • 105
    • 0006979554 scopus 로고
    • Terminal a-galactose sequences contribute to mouse sperm binding in a cell adhesion model
    • Sandow, B. A. and Clark, G. F. (1993) Terminal a-galactose sequences contribute to mouse sperm binding in a cell adhesion model. Biol. Reprod 48:A166.
    • (1993) Biol. Reprod , vol.48
    • Sandow, B.A.1    Clark, G.F.2
  • 106
    • 7644233735 scopus 로고    scopus 로고
    • Inactivation of the Mgat1 gene in oocytes impairs oogenesis, but embryos lacking complex and hybrid N-glycans develop and implant
    • Shi, S., Williams, S. A., Seppo, A., Kurniawan, H., Chen, W., Ye, Z., et al. (2004) Inactivation of the Mgat1 gene in oocytes impairs oogenesis, but embryos lacking complex and hybrid N-glycans develop and implant. Mol Cell Biol 24:9920-9929.
    • (2004) Mol Cell Biol , vol.24 , pp. 9920-9929
    • Shi, S.1    Williams, S.A.2    Seppo, A.3    Kurniawan, H.4    Chen, W.5    Ye, Z.6
  • 107
    • 54249094735 scopus 로고    scopus 로고
    • Reassessing the role of protein-carbohydrate complementarity during sperm-egg interactions in the mouse
    • Shur, B. D. (2008) Reassessing the role of protein-carbohydrate complementarity during sperm-egg interactions in the mouse. Int J Dev Biol 52:703-715.
    • (2008) Int J Dev Biol , vol.52 , pp. 703-715
    • Shur, B.D.1
  • 108
    • 34447527604 scopus 로고    scopus 로고
    • Analysis of protein-linked glycosylation in a sperm-somatic cell adhesion system
    • Sutton-Smith, M., Wong, N. K., Khoo, K. H., Wu, S. W., Yu, S. Y., Patankar, M. S., et al. (2007) Analysis of protein-linked glycosylation in a sperm-somatic cell adhesion system. Glycobiology 17:553-567.
    • (2007) Glycobiology , vol.17 , pp. 553-567
    • Sutton-Smith, M.1    Wong, N.K.2    Khoo, K.H.3    Wu, S.W.4    Yu, S.Y.5    Patankar, M.S.6
  • 109
    • 0028985303 scopus 로고
    • Cloning of a cDNA coding for porcine zona pellucida glycoprotein ZP1 and its genomic organization
    • Taya, T., Yamasaki, N., Tsubamoto, H., Hasegawa, A. and Koyama, K. (1995) Cloning of a cDNA coding for porcine zona pellucida glycoprotein ZP1 and its genomic organization. Biochem Biophys Res Commun 207:790-799.
    • (1995) Biochem Biophys Res Commun , vol.207 , pp. 790-799
    • Taya, T.1    Yamasaki, N.2    Tsubamoto, H.3    Hasegawa, A.4    Koyama, K.5
  • 110
    • 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
  • 111
    • 0028982258 scopus 로고
    • Oocyte Gala1-3Gal epitopes implicated in sperm adhesion to the zona pellucida glycoprotein ZP3 are not required for fertilization in the mouse
    • Thall, A. D., Maly, P. and Lowe, J. B. (1995) Oocyte Gala1-3Gal epitopes implicated in sperm adhesion to the zona pellucida glycoprotein ZP3 are not required for fertilization in the mouse. J Biol Chem 270:21437-21440.
    • (1995) J Biol Chem , vol.270 , pp. 21437-21440
    • Thall, A.D.1    Maly, P.2    Lowe, J.B.3
  • 113
    • 0028048726 scopus 로고
    • Recombinant human zona pellucida protein ZP3 produced by Chinese hamster ovary cells induces the human sperm acrosome reaction and promotes sperm-egg interaction
    • van Duin, M., Polman, J., De Breet, I. T., van Ginneken, K., Bunschoten, H., Grootenhuis, A., et al. (1994) Recombinant human zona pellucida protein ZP3 produced by Chinese hamster ovary cells induces the human sperm acrosome reaction and promotes sperm-egg interaction. Biol Reprod 51:607-617.
    • (1994) Biol Reprod , vol.51 , pp. 607-617
    • Van Duin, M.1    Polman, J.2    De Breet, I.T.3    Van Ginneken, K.4    Bunschoten, H.5    Grootenhuis, A.6
  • 114
    • 34447312189 scopus 로고    scopus 로고
    • Multiple proteins present in purified porcine sperm apical plasma membranes interact with the zona pellucida of the oocyte
    • van Gestel, R. A., Brewis, I. A., Ashton, P. R., Brouwers, J. F. and Gadella, B. M. (2007) Multiple proteins present in purified porcine sperm apical plasma membranes interact with the zona pellucida of the oocyte. Mol Hum Reprod 13:445-454.
    • (2007) Mol Hum Reprod , vol.13 , pp. 445-454
    • Van Gestel, R.A.1    Brewis, I.A.2    Ashton, P.R.3    Brouwers, J.F.4    Gadella, B.M.5
  • 115
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • Varki, A. (1993) Biological roles of oligosaccharides: all of the theories are correct. Glycobiology 3:97-130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 116
    • 24044514682 scopus 로고    scopus 로고
    • Analysis of N-linked glycans of porcine zona pellucida glycoprotein ZPA by MALDI-TOF MS: A contribution to understanding zona pellucida structure
    • von Witzendorff, D., Ekhlasi-Hundrieser, M., Dostalova, Z., Resch, M., Rath, D., Michelmann, H. W. and Topfer-Petersen, E. (2005) Analysis of N-linked glycans of porcine zona pellucida glycoprotein ZPA by MALDI-TOF MS: a contribution to understanding zona pellucida structure. Glycobiology 15:475-488.
    • (2005) Glycobiology , vol.15 , pp. 475-488
    • Von Witzendorff, D.1    Ekhlasi-Hundrieser, M.2    Dostalova, Z.3    Resch, M.4    Rath, D.5    Michelmann, H.W.6    Topfer-Petersen, E.7
  • 117
    • 0025044472 scopus 로고
    • Profile of a mammalian sperm receptor
    • Wassarman, P. M. (1990) Profile of a mammalian sperm receptor. Development 108:1-17.
    • (1990) Development , vol.108 , pp. 1-17
    • Wassarman, P.M.1
  • 118
    • 54249138250 scopus 로고    scopus 로고
    • Mammalian fertilization: The egg's multifunctional zona pellucida
    • Wassarman, P. M. and Litscher, E. S. (2008) Mammalian fertilization: the egg's multifunctional zona pellucida. Int J Dev Biol 52:665-676.
    • (2008) Int J Dev Biol , vol.52 , pp. 665-676
    • Wassarman, P.M.1    Litscher, E.S.2
  • 119
    • 0030902194 scopus 로고    scopus 로고
    • Mutant female mice carrying a single mZP3 allele produce eggs with a thin zona pellucida, but reproduce normally
    • Wassarman, P. M., Qi, H. and Litscher, E. S. (1997) Mutant female mice carrying a single mZP3 allele produce eggs with a thin zona pellucida, but reproduce normally. Proc Roy Soc London B 264:323-328.
    • (1997) Proc Roy Soc London B , vol.264 , pp. 323-328
    • Wassarman, P.M.1    Qi, H.2    Litscher, E.S.3
  • 120
    • 46749142054 scopus 로고    scopus 로고
    • Mouse fertility is enhanced by oocyte-specific loss of core 1-derived O-glycans
    • Williams, S. A. and Stanley, P. (2008) Mouse fertility is enhanced by oocyte-specific loss of core 1-derived O-glycans. Faseb J 22:2273-2284.
    • (2008) Faseb J , vol.22 , pp. 2273-2284
    • Williams, S.A.1    Stanley, P.2
  • 121
    • 34249103694 scopus 로고    scopus 로고
    • Fertilization in mouse does not require terminal galactose or N-acetyl-glucosamine on the zona pellucida glycans
    • Williams, S. A., Xia, L., Cummings, R. D., McEver, R. P. and Stanley, P. (2007) Fertilization in mouse does not require terminal galactose or N-acetyl-glucosamine on the zona pellucida glycans. J Cell Sci 120:1341-1349.
    • (2007) J Cell Sci , vol.120 , pp. 1341-1349
    • Williams, S.A.1    Xia, L.2    Cummings, R.D.3    McEver, R.P.4    Stanley, P.5
  • 122
    • 0001231958 scopus 로고
    • The role of saccharides in fertilization in the mouse
    • Yamagata, T. (1985) The role of saccharides in fertilization in the mouse. Dev Growth Differ 27:176-177.
    • (1985) Dev Growth Differ , vol.27 , pp. 176-177
    • Yamagata, T.1
  • 123
    • 0039699798 scopus 로고
    • The involvement of a saccharide-mediated recognition mechanism in the interactions between sperm and the zona pellucida of the egg cells of the mouse
    • eds Chester, M. A., Heinegard, A., Svensson, S., Rhams, New York, NY
    • Yamagata, T., Ito, M. and Takahashi, K. (1983) The involvement of a saccharide-mediated recognition mechanism in the interactions between sperm and the zona pellucida of the egg cells of the mouse. In Glycoconjugates. eds Chester, M. A., Heinegard, A., Svensson, S., Rhams, New York, NY pp. 623-624.
    • (1983) Glycoconjugates , pp. 623-624
    • Yamagata, T.1    Ito, M.2    Takahashi, K.3
  • 124
    • 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
  • 125
    • 11244311568 scopus 로고    scopus 로고
    • Participation of the nonreducing terminal b-galactosyl residues of the neutral N-linked carbohydrate chains of porcine zona pellucida glycoproteins in sperm-egg binding
    • Yonezawa, N., Amari, S., Takahashi, K., Ikeda, K., Imai, F.L., Kanai, S., et al. (2005) Participation of the nonreducing terminal b-galactosyl residues of the neutral N-linked carbohydrate chains of porcine zona pellucida glycoproteins in sperm-egg binding. Mol Reprod Dev 70:222-227.
    • (2005) Mol Reprod Dev , vol.70 , pp. 222-227
    • Yonezawa, N.1    Amari, S.2    Takahashi, K.3    Ikeda, K.4    Imai, F.L.5    Kanai, S.6
  • 126
    • 0034819583 scopus 로고    scopus 로고
    • Molecular cloning of bovine zona pellucida glycoproteins ZPA and ZPB and analysis for sperm-binding component of the zona
    • Yonezawa, N., Fukui, N., Kuno, M., Shinoda, M., Goko, S., Mitsui, S. and Nakano, M. (2001) Molecular cloning of bovine zona pellucida glycoproteins ZPA and ZPB and analysis for sperm-binding component of the zona. Eur J Biochem 268:3587-3594.
    • (2001) Eur J Biochem , vol.268 , pp. 3587-3594
    • Yonezawa, N.1    Fukui, N.2    Kuno, M.3    Shinoda, M.4    Goko, S.5    Mitsui, S.6    Nakano, M.7
  • 127
    • 34547829494 scopus 로고    scopus 로고
    • Structural significance of N-glycans of the zona pellucida on species-selective recognition of spermatozoa between pig and cattle
    • Yonezawa, N., Kanai, S. and Nakano, M. (2007) Structural significance of N-glycans of the zona pellucida on species-selective recognition of spermatozoa between pig and cattle. Soc Reprod Fertil Suppl 63:217-228.
    • (2007) Soc Reprod Fertil Suppl , vol.63 , pp. 217-228
    • Yonezawa, N.1    Kanai, S.2    Nakano, M.3
  • 128
    • 20144380361 scopus 로고    scopus 로고
    • Recombinant porcine zona pellucida glycoproteins expressed in Sf9 cells bind to bovine sperm but not to porcine sperm
    • Yonezawa, N., Kudo, K., Terauchi, H., Kanai, S., Yoda, N., Tanokura, M., et al. (2005) Recombinant porcine zona pellucida glycoproteins expressed in Sf9 cells bind to bovine sperm but not to porcine sperm. J Biol Chem 280:20189-20196.
    • (2005) J Biol Chem , vol.280 , pp. 20189-20196
    • Yonezawa, N.1    Kudo, K.2    Terauchi, H.3    Kanai, S.4    Yoda, N.5    Tanokura, M.6
  • 129
    • 0030068748 scopus 로고    scopus 로고
    • Bisecting N-acetylglucosamine on K562 cells suppresses natural killer cytotoxicity and promotes spleen colonization
    • Yoshimura, M., Ihara, Y., Ohnishi, A., Ijuhin, N., Nishiura, T., Kanakura, Y., et al. (1996) Bisecting N-acetylglucosamine on K562 cells suppresses natural killer cytotoxicity and promotes spleen colonization. Cancer Res 56:412-418.
    • (1996) Cancer Res , vol.56 , pp. 412-418
    • Yoshimura, M.1    Ihara, Y.2    Ohnishi, A.3    Ijuhin, N.4    Nishiura, T.5    Kanakura, Y.6
  • 130
    • 30544449581 scopus 로고    scopus 로고
    • The extracellular protein coat of the inner acrosomal membrane is involved in zona pellucida binding and penetration during fertilization: Characterization of its most prominent polypeptide (IAM38)
    • Yu, Y., Xu, W., Yi, Y. J., Sutovsky, P. and Oko, R. (2006) The extracellular protein coat of the inner acrosomal membrane is involved in zona pellucida binding and penetration during fertilization: characterization of its most prominent polypeptide (IAM38). Dev Biol 290: 32-43.
    • (2006) Dev Biol , vol.290 , pp. 32-43
    • Yu, Y.1    Xu, W.2    Yi, Y.J.3    Sutovsky, P.4    Oko, R.5
  • 131
    • 0027171178 scopus 로고
    • Nucleotide sequence of cDNA encoding ZP3a, a sperm-binding glycoprotein from zona pellucida of pig oocyte
    • Yurewicz, E. C., Hibler, D., Fontenot, G. K., Sacco, A. G. and Harris, J. (1993) Nucleotide sequence of cDNA encoding ZP3a, a sperm-binding glycoprotein from zona pellucida of pig oocyte. Biochim Biophys Acta 1174:211-214.
    • (1993) Biochim Biophys Acta , vol.1174 , pp. 211-214
    • Yurewicz, E.C.1    Hibler, D.2    Fontenot, G.K.3    Sacco, A.G.4    Harris, J.5
  • 132
    • 0025984497 scopus 로고
    • Isolation, composition, and biological activity of sugar chains of porcine oocyte zona pellucida 55K glycoproteins
    • Yurewicz, E. C., Pack, B. A. and Sacco, A. G. (1991) Isolation, composition, and biological activity of sugar chains of porcine oocyte zona pellucida 55K glycoproteins. Mol Reprod Dev 30:126-134.
    • (1991) Mol Reprod Dev , vol.30 , pp. 126-134
    • Yurewicz, E.C.1    Pack, B.A.2    Sacco, A.G.3
  • 133
    • 0023164968 scopus 로고
    • Structural characterization of the Mr = 55,000 antigen (ZP3) of porcine oocyte zona pellucida. Purification and characterization of a- and b-glycoproteins following digestion of lactosaminoglycan with endo-b-galactosidase
    • Yurewicz, E. C., Sacco, A. G. and Subramanian, M. G. (1987) Structural characterization of the Mr = 55,000 antigen (ZP3) of porcine oocyte zona pellucida. Purification and characterization of a- and b-glycoproteins following digestion of lactosaminoglycan with endo-b-galactosidase. J Biol Chem 262:564-571.
    • (1987) J Biol Chem , vol.262 , pp. 564-571
    • Yurewicz, E.C.1    Sacco, A.G.2    Subramanian, M.G.3


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