메뉴 건너뛰기




Volumn 64, Issue 14, 2007, Pages 1805-1823

New insights into the molecular mechanisms of sperm-egg interaction

Author keywords

Capacitation; Fertilisation; Gamete; Oocyte; Spermatozoa

Indexed keywords

ADAM PROTEIN; CRISP 1 PROTEIN; EGG PROTEIN; GLYCOPROTEIN; GLYCOSYLPHOSPHATIDYLINOSITOL; IMMUNOGLOBULIN; INTEGRIN; OXIDOREDUCTASE; OXIDOREDUCTASE ERP57; PROTEIN; PROTEIN IZUMO; SECRETORY PROTEIN; SPERM LYSOZYME LIKE PROTEIN; TETRASPANIN; UNCLASSIFIED DRUG;

EID: 34447635697     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-007-6552-x     Document Type: Review
Times cited : (88)

References (195)
  • 1
    • 0021814123 scopus 로고
    • Changes in the lipid content of boar sperm plasma membranes during epididymal maturation
    • Nikolopoulou, M., Soucek, D. A. and Vary, J. C. (1985) Changes in the lipid content of boar sperm plasma membranes during epididymal maturation. Biochim. Biophys. Acta 815, 486-498.
    • (1985) Biochim. Biophys. Acta , vol.815 , pp. 486-498
    • Nikolopoulou, M.1    Soucek, D.A.2    Vary, J.C.3
  • 2
    • 0031451736 scopus 로고    scopus 로고
    • Changes in lipids and membrane anisotropy in human spermatozoa during epididymal maturation
    • Haidl, G. and Opper, C. (1997) Changes in lipids and membrane anisotropy in human spermatozoa during epididymal maturation. Hum. Reprod. 12, 2720-2723.
    • (1997) Hum. Reprod , vol.12 , pp. 2720-2723
    • Haidl, G.1    Opper, C.2
  • 3
    • 0031829606 scopus 로고    scopus 로고
    • Maturation of mammalian spermatozoa: Modifications of the acrosome and plasma membrane leading to fertilization
    • Toshimori, K. (1998) Maturation of mammalian spermatozoa: modifications of the acrosome and plasma membrane leading to fertilization. Cell Tissue Res. 293, 177-187.
    • (1998) Cell Tissue Res , vol.293 , pp. 177-187
    • Toshimori, K.1
  • 4
    • 0028535827 scopus 로고
    • Fertility of mammalian spermatozoa: Its development and relativity
    • Yanagimachi, R. (1994) Fertility of mammalian spermatozoa: its development and relativity. Zygote 2, 371-372.
    • (1994) Zygote , vol.2 , pp. 371-372
    • Yanagimachi, R.1
  • 5
    • 0028957362 scopus 로고
    • Capacitation of mouse spermatozoa. I. Correlation between the capacitation state and protein tyrosine phosphorylation
    • Visconti, P. E., Bailey, J. L., Moore, G. D., Pan, D., Olds-Clarke, P. and Kopf, G. S. (1995) Capacitation of mouse spermatozoa. I. Correlation between the capacitation state and protein tyrosine phosphorylation. Development 121, 1129-1137.
    • (1995) Development , vol.121 , pp. 1129-1137
    • Visconti, P.E.1    Bailey, J.L.2    Moore, G.D.3    Pan, D.4    Olds-Clarke, P.5    Kopf, G.S.6
  • 6
    • 0028936801 scopus 로고
    • Capacitation of mouse spermatozoa. II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway
    • Visconti, P. E., Moore, G. D., Bailey, J. L., Leclerc, P., Connors, S. A., Pan, D., Olds-Clarke, P. and Kopf, G. S. (1995) Capacitation of mouse spermatozoa. II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway. Development 121, 1139-1150.
    • (1995) Development , vol.121 , pp. 1139-1150
    • Visconti, P.E.1    Moore, G.D.2    Bailey, J.L.3    Leclerc, P.4    Connors, S.A.5    Pan, D.6    Olds-Clarke, P.7    Kopf, G.S.8
  • 7
    • 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
  • 10
    • 0035211053 scopus 로고    scopus 로고
    • Biosynthesis and expression of zona pellucida glycoproteins in mammals
    • Sinowatz, F., Kolle, S. and Topfer-Petersen, E. (2001) Biosynthesis and expression of zona pellucida glycoproteins in mammals. Cells Tissues Organs 168, 24-35.
    • (2001) Cells Tissues Organs , vol.168 , pp. 24-35
    • Sinowatz, F.1    Kolle, S.2    Topfer-Petersen, E.3
  • 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. (1980) 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
  • 13
    • 0022429080 scopus 로고
    • Mouse egg extracellular coat is a matrix of interconnected filaments possessing a structural repeat
    • Greve, J. M. and Wassarman, P. M. (1985) Mouse egg extracellular coat is a matrix of interconnected filaments possessing a structural repeat. J. Mol. Biol. 181, 253-264.
    • (1985) J. Mol. Biol , vol.181 , pp. 253-264
    • Greve, J.M.1    Wassarman, P.M.2
  • 14
    • 0026334512 scopus 로고
    • Structure of the mouse egg extracellular coat, the zona pellucida
    • Wassarman, P. M. and Mortillo, S. (1991) Structure of the mouse egg extracellular coat, the zona pellucida. Int. Rev. Cytol. 130, 85-110.
    • (1991) Int. Rev. Cytol , vol.130 , pp. 85-110
    • Wassarman, P.M.1    Mortillo, S.2
  • 15
    • 0022480709 scopus 로고
    • Oocyte-specific gene expression: Molecular characterization of a cDNA coding for ZP-3, the sperm receptor of the mouse zona pellucida
    • Ringuette, M. J., Sobieski, D. A., Chamow, S. M. and Dean, J. (1986) Oocyte-specific gene expression: molecular characterization of a cDNA coding for ZP-3, the sperm receptor of the mouse zona pellucida. Proc. Natl. Acad. Sci. USA 83, 4341-4345.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4341-4345
    • Ringuette, M.J.1    Sobieski, D.A.2    Chamow, S.M.3    Dean, J.4
  • 16
    • 0023926939 scopus 로고
    • Molecular analysis of cDNA coding for ZP3, a sperm binding protein of the mouse zona pellucida
    • Ringuette, M. J., Chamberlin, M. E., Baur, A. W., Sobieski, D. A. and Dean, J. (1988) Molecular analysis of cDNA coding for ZP3, a sperm binding protein of the mouse zona pellucida. Dev. Biol. 127, 287-295.
    • (1988) Dev. Biol , vol.127 , pp. 287-295
    • Ringuette, M.J.1    Chamberlin, M.E.2    Baur, A.W.3    Sobieski, D.A.4    Dean, J.5
  • 18
    • 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
  • 19
    • 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
  • 20
    • 0028910318 scopus 로고
    • Inhibition of zona pellucida gene expression by antisense oligonucleotides injected into mouse oocytes
    • Tong, Z. B., Nelson, L. M. and Dean, J. (1995) Inhibition of zona pellucida gene expression by antisense oligonucleotides injected into mouse oocytes. J. Biol. Chem. 270, 849-853.
    • (1995) J. Biol. Chem , vol.270 , pp. 849-853
    • Tong, Z.B.1    Nelson, L.M.2    Dean, J.3
  • 21
    • 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
  • 22
    • 0022552266 scopus 로고
    • Autoradiographic visualization of the mouse egg's sperm receptor bound to sperm
    • Bleil, J. D. and Wassarman, P. M. (1986) Autoradiographic visualization of the mouse egg's sperm receptor bound to sperm. J. Cell Biol. 102, 1363-1371.
    • (1986) J. Cell Biol , vol.102 , pp. 1363-1371
    • Bleil, J.D.1    Wassarman, P.M.2
  • 23
    • 0024642651 scopus 로고
    • Interaction of mouse sperm with purified sperm receptors covalently linked to silica beads
    • Vazquez, M. H., Phillips, D. M. and Wassarman, P. M. (1989) Interaction of mouse sperm with purified sperm receptors covalently linked to silica beads. J. Cell Sci. 92 (Pt 4), 713-722.
    • (1989) J. Cell Sci , vol.92 , Issue.PART 4 , pp. 713-722
    • Vazquez, M.H.1    Phillips, D.M.2    Wassarman, P.M.3
  • 24
    • 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
  • 25
    • 33748859212 scopus 로고    scopus 로고
    • Gamete interaction: Is it species-specific?
    • Vieira, A. and Miller, D. J. (2006) Gamete interaction: is it species-specific? Mol. Reprod. & Dev. 73, 1422-1429.
    • (2006) Mol. Reprod. & Dev , vol.73 , pp. 1422-1429
    • Vieira, A.1    Miller, D.J.2
  • 26
    • 1842843784 scopus 로고    scopus 로고
    • Insights into the molecular basis of sperm-egg recognition in mammals
    • Hoodbhoy, T. and Dean, J. (2004) Insights into the molecular basis of sperm-egg recognition in mammals. Reproduction 127, 417-422.
    • (2004) Reproduction , vol.127 , pp. 417-422
    • Hoodbhoy, T.1    Dean, J.2
  • 27
    • 0017352879 scopus 로고
    • Receptor activity of the hamster and mouse solubilized zona pellucida before and after the zona reaction
    • Gwatkin, R. B. and Williams, D. T. (1977) Receptor activity of the hamster and mouse solubilized zona pellucida before and after the zona reaction. J. Reprod. Fertil. 49, 55-59.
    • (1977) J. Reprod. Fertil , vol.49 , pp. 55-59
    • Gwatkin, R.B.1    Williams, D.T.2
  • 28
    • 0021874149 scopus 로고
    • O-linked oligosaccharides of mouse egg ZP3 account for its sperm receptor activity
    • Florman, H. M. and Wassarman, P. M. (1985) O-linked oligosaccharides of mouse egg ZP3 account for its sperm receptor activity. Cell 41, 313-324.
    • (1985) Cell , vol.41 , pp. 313-324
    • Florman, H.M.1    Wassarman, P.M.2
  • 29
    • 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
  • 30
    • 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
  • 32
    • 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
  • 34
    • 0032571326 scopus 로고    scopus 로고
    • Hetero-oligomerization-dependent binding of pig oocyte zona pellucida glycoproteins ZPB and ZPC to boar sperm membrane vesicles
    • Yurewicz, E. C., Sacco, A. G., Gupta, S. K., Xu, N. and Gage, D. A. (1998) Hetero-oligomerization-dependent binding of pig oocyte zona pellucida glycoproteins ZPB and ZPC to boar sperm membrane vesicles. J. Biol. Chem. 273, 7488-7494.
    • (1998) J. Biol. Chem , vol.273 , pp. 7488-7494
    • Yurewicz, E.C.1    Sacco, A.G.2    Gupta, S.K.3    Xu, N.4    Gage, D.A.5
  • 35
    • 0034819583 scopus 로고    scopus 로고
    • 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. of Biochem. 268, 3587-35 94.
    • 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. of Biochem. 268, 3587-35 94.
  • 36
    • 0035084331 scopus 로고    scopus 로고
    • Purified and refolded recombinant bonnet monkey (Macaca radiata) zona pellucida glycoprotein-B expressed in Escherichia coli binds to spermatozoa
    • Govind, C. K., Gahlay, G. K., Choudhury, S. and Gupta, S. K. (2001) Purified and refolded recombinant bonnet monkey (Macaca radiata) zona pellucida glycoprotein-B expressed in Escherichia coli binds to spermatozoa. Biol. Reprod. 64, 1147-1152.
    • (2001) Biol. Reprod , vol.64 , pp. 1147-1152
    • Govind, C.K.1    Gahlay, G.K.2    Choudhury, S.3    Gupta, S.K.4
  • 37
    • 0033970760 scopus 로고    scopus 로고
    • Delineation of a conserved B cell epitope on bonnet monkey (Macaca radiata) and human zona pellucida glycoprotein-B by monoclonal antibodies demonstrating inhibition of sperm-egg binding
    • Govind, C. K., Hasegawa, A., Koyama, K. and Gupta, S. K. (2000) Delineation of a conserved B cell epitope on bonnet monkey (Macaca radiata) and human zona pellucida glycoprotein-B by monoclonal antibodies demonstrating inhibition of sperm-egg binding. Biol. Reprod. 62, 67-75.
    • (2000) Biol. Reprod , vol.62 , pp. 67-75
    • Govind, C.K.1    Hasegawa, A.2    Koyama, K.3    Gupta, S.K.4
  • 38
    • 0034677921 scopus 로고    scopus 로고
    • Structural analysis of murine zona pellucida glycans. Evidence for the expression of core 2-type O-glycans and the Sd(a) 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 Sd(a) 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
  • 39
    • 0037301078 scopus 로고    scopus 로고
    • Glycoconjugates in sperm function and gamete interactions: How much sugar does it take to sweet-talk the egg?
    • Diekman, A. B. (2003) Glycoconjugates in sperm function and gamete interactions: how much sugar does it take to sweet-talk the egg? Cell. Mol. Life Sci. 60, 298-308.
    • (2003) Cell. Mol. Life Sci , vol.60 , pp. 298-308
    • Diekman, A.B.1
  • 40
    • 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
  • 41
    • 0028260347 scopus 로고
    • O-linked trisaccharide and N-linked poly-N- acetyllactosaminyl glycans are present on mouse ZP2 and ZP3
    • Nagdas, S. K., Araki, Y., Chayko, C. A., Orgebin-Crist, M. C. and Tulsiani, D. R. (1994) O-linked trisaccharide and N-linked poly-N- acetyllactosaminyl glycans are present on mouse ZP2 and ZP3. Biol. Reprod. 51, 262-272.
    • (1994) Biol. Reprod , vol.51 , pp. 262-272
    • Nagdas, S.K.1    Araki, Y.2    Chayko, C.A.3    Orgebin-Crist, M.C.4    Tulsiani, D.R.5
  • 42
    • 0028982258 scopus 로고
    • Oocyte Gal alpha 1,3Gal 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 Gal alpha 1,3Gal 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
  • 43
    • 0026611050 scopus 로고
    • Complementarity between sperm surface beta-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 beta-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
  • 44
    • 0031183547 scopus 로고    scopus 로고
    • Carbohydrates and fertilization: An overview
    • Benoff, S. (1997) Carbohydrates and fertilization: an overview. Mol. Hum. Reprod. 3, 599-637.
    • (1997) Mol. Hum. Reprod , vol.3 , pp. 599-637
    • Benoff, S.1
  • 45
    • 0037709377 scopus 로고    scopus 로고
    • Capacitated acrosome-intact mouse spermatozoa bind to Sepharose beads coated with functional neoglycoproteins
    • Bendahmane, M. and Tulsiani, D. R. (2003) Capacitated acrosome-intact mouse spermatozoa bind to Sepharose beads coated with functional neoglycoproteins. Arch. Biochem. Biophys. 415, 203-212.
    • (2003) Arch. Biochem. Biophys , vol.415 , pp. 203-212
    • Bendahmane, M.1    Tulsiani, D.R.2
  • 46
    • 0032428668 scopus 로고    scopus 로고
    • Core 2 oligosaccharide biosynthesis distinguishes between selectin ligands essential for leukocyte homing and inflammation
    • Ellies, L. G., Tsuboi, S., Petryniak, B., Lowe, J. B., Fukuda, M. and Marth, J. D. (1998) Core 2 oligosaccharide biosynthesis distinguishes between selectin ligands essential for leukocyte homing and inflammation. Immunity 9, 881-890.
    • (1998) Immunity , vol.9 , pp. 881-890
    • Ellies, L.G.1    Tsuboi, S.2    Petryniak, B.3    Lowe, J.B.4    Fukuda, M.5    Marth, J.D.6
  • 47
    • 7644233735 scopus 로고    scopus 로고
    • Shi, S., Williams, S. A., Seppo, A., Kurniawan, H., Chen, W., Ye, Z., Marth, J. D. and Stanley, P. (2004) Inactivation of the Mgat1 gene in oocytes impairs oogenesis, but embryos lacking complex and hybrid N-glycans develop and implant. [Erratum appears in Mol. Cell. Biol. 2005 Feb; 25(3): 1214. Mol. Cell. Biol. 24, 9920-9929.
    • Shi, S., Williams, S. A., Seppo, A., Kurniawan, H., Chen, W., Ye, Z., Marth, J. D. and Stanley, P. (2004) Inactivation of the Mgat1 gene in oocytes impairs oogenesis, but embryos lacking complex and hybrid N-glycans develop and implant. [Erratum appears in Mol. Cell. Biol. 2005 Feb; 25(3): 1214. Mol. Cell. Biol. 24, 9920-9929.
  • 48
    • 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
  • 49
    • 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
  • 50
    • 14744281877 scopus 로고    scopus 로고
    • A synthetic decapeptide from a conserved ZP3 protein domain induces the G protein-regulated acrosome reaction in bovine spermatozoa
    • Hinsch, E., Aires, V. A., Hedrich, F., Oehninger, S. and Hinsch, K. D. (2005) A synthetic decapeptide from a conserved ZP3 protein domain induces the G protein-regulated acrosome reaction in bovine spermatozoa. Theriogenology 63, 1682-1694.
    • (2005) Theriogenology , vol.63 , pp. 1682-1694
    • Hinsch, E.1    Aires, V.A.2    Hedrich, F.3    Oehninger, S.4    Hinsch, K.D.5
  • 52
    • 0347004637 scopus 로고    scopus 로고
    • Reassessing the molecular biology of sperm-egg recognition with mouse genetics
    • Dean, J. (2004) Reassessing the molecular biology of sperm-egg recognition with mouse genetics. Bioessays 26, 29-38.
    • (2004) Bioessays , vol.26 , pp. 29-38
    • Dean, J.1
  • 53
    • 33646173507 scopus 로고    scopus 로고
    • Identification of novel gamete receptors that mediate sperm adhesion to the egg coat
    • Shur, B. D., Rodeheffer, C., Ensslin, M. A., Lyng, R. and Raymond, A. (2006) Identification of novel gamete receptors that mediate sperm adhesion to the egg coat. Mol. Cell. Endocrinol. 250, 137-148.
    • (2006) Mol. Cell. Endocrinol , vol.250 , pp. 137-148
    • Shur, B.D.1    Rodeheffer, C.2    Ensslin, M.A.3    Lyng, R.4    Raymond, A.5
  • 54
    • 0026332964 scopus 로고
    • Mouse gamete adhesion molecules
    • Wassarman, P. M. (1992) Mouse gamete adhesion molecules. Biol. Reprod. 46, 186-91.
    • (1992) Biol. Reprod , vol.46 , pp. 186-191
    • Wassarman, P.M.1
  • 55
    • 2442754050 scopus 로고    scopus 로고
    • Carbohydrate-based interactions on the route of a spermatozoon to fertilization
    • Topfer-Petersen, E. (1999) Carbohydrate-based interactions on the route of a spermatozoon to fertilization. Hum. Reprod. Update 5, 314-329.
    • (1999) Hum. Reprod. Update , vol.5 , pp. 314-329
    • Topfer-Petersen, E.1
  • 56
    • 0018366421 scopus 로고
    • A specific defect in galactosyltransferase regulation on sperm bearing mutant alleles of the T/t locus
    • Shur, B. D. and Bennett, D. (1979) A specific defect in galactosyltransferase regulation on sperm bearing mutant alleles of the T/t locus. Dev. Biol. 71, 243-259.
    • (1979) Dev. Biol , vol.71 , pp. 243-259
    • Shur, B.D.1    Bennett, D.2
  • 57
    • 0020410869 scopus 로고
    • A role for mouse sperm surface galactosyltransferase in sperm binding to the egg zona pellucida
    • Shur, B. D. and Hall, N. G. (1982) A role for mouse sperm surface galactosyltransferase in sperm binding to the egg zona pellucida. J. Cell Biol. 95, 574-579.
    • (1982) J. Cell Biol , vol.95 , pp. 574-579
    • Shur, B.D.1    Hall, N.G.2
  • 58
    • 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
  • 60
    • 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
  • 61
    • 0029063226 scopus 로고
    • Tissue- and species-specific expression of sp56, a mouse sperm fertilization protein
    • Bookbinder, L. H., Cheng, A. and Bleil, J. D. (1995) Tissue- and species-specific expression of sp56, a mouse sperm fertilization protein. Science 269, 86-89.
    • (1995) Science , vol.269 , pp. 86-89
    • Bookbinder, L.H.1    Cheng, A.2    Bleil, J.D.3
  • 62
    • 0035023871 scopus 로고    scopus 로고
    • Association of egg zona pellucida glycoprotein mZP3 with sperm protein sp56 during fertilization in mice
    • Cohen, N. and Wassarman, P. M. (2001) Association of egg zona pellucida glycoprotein mZP3 with sperm protein sp56 during fertilization in mice. Int. J. Dev. Biol. 45, 569-576.
    • (2001) Int. J. Dev. Biol , vol.45 , pp. 569-576
    • Cohen, N.1    Wassarman, P.M.2
  • 63
    • 0025801542 scopus 로고
    • Inhibition of the mouse sperm surface alpha-D-mannosidase inhibits sperm-egg binding in vitro
    • Cornwall, G. A., Tulsiani, D. R. and Orgebin-Crist, M. C. (1991) Inhibition of the mouse sperm surface alpha-D-mannosidase inhibits sperm-egg binding in vitro. Biol. Reprod. 44, 913-921.
    • (1991) Biol. Reprod , vol.44 , pp. 913-921
    • Cornwall, G.A.1    Tulsiani, D.R.2    Orgebin-Crist, M.C.3
  • 64
    • 0032489040 scopus 로고    scopus 로고
    • Species diversity in the structure of zonadhesin, a sperm-specific membrane protein containing multiple cell adhesion molecule-like domains
    • Gao, Z. and Garbers, D. L. (1998) Species diversity in the structure of zonadhesin, a sperm-specific membrane protein containing multiple cell adhesion molecule-like domains. J. Biol. Chem. 273, 3415-3421.
    • (1998) J. Biol. Chem , vol.273 , pp. 3415-3421
    • Gao, Z.1    Garbers, D.L.2
  • 66
    • 0031567823 scopus 로고    scopus 로고
    • Targeted mutation in beta1,4-galactosyltransferase leads to pituitary insufficiency and neonatal lethality
    • Lu, Q., Hasty, P. and Shur, B. D. (1997) Targeted mutation in beta1,4-galactosyltransferase leads to pituitary insufficiency and neonatal lethality. Dev. Biol. 181, 257-267.
    • (1997) Dev. Biol , vol.181 , pp. 257-267
    • Lu, Q.1    Hasty, P.2    Shur, B.D.3
  • 67
    • 32644435333 scopus 로고    scopus 로고
    • Mammalian sperm translate nuclear-encoded proteins by mitochondrial-type ribosomes
    • Gur, Y. and Breitbart, H. (2006) Mammalian sperm translate nuclear-encoded proteins by mitochondrial-type ribosomes. Genes Dev. 20, 411-416.
    • (2006) Genes Dev , vol.20 , pp. 411-416
    • Gur, Y.1    Breitbart, H.2
  • 68
    • 23844541714 scopus 로고    scopus 로고
    • The mouse epididymal transcriptome: Transcriptional profiling of segmental gene expression in the epididymis
    • Johnston, D. S., Jelinsky, S. A., Bang, H. J., DiCandeloro, P., Wilson, E., Kopf, G. S. and Turner, T. T. (2005) The mouse epididymal transcriptome: transcriptional profiling of segmental gene expression in the epididymis. Biol. of Reprod. 73, 404-413.
    • (2005) Biol. of Reprod , vol.73 , pp. 404-413
    • Johnston, D.S.1    Jelinsky, S.A.2    Bang, H.J.3    DiCandeloro, P.4    Wilson, E.5    Kopf, G.S.6    Turner, T.T.7
  • 69
    • 33646199098 scopus 로고    scopus 로고
    • Epididymal genomics and the search for amale contraceptive
    • Turner, T. T., Johnston, D. S. and Jelinsky, S. A. (2006) Epididymal genomics and the search for amale contraceptive. Mol. Cell. Endocrinol. 250, 178-183.
    • (2006) Mol. Cell. Endocrinol , vol.250 , pp. 178-183
    • Turner, T.T.1    Johnston, D.S.2    Jelinsky, S.A.3
  • 70
    • 0034893005 scopus 로고    scopus 로고
    • Dynamic changes in gene expression along the rat epididymis
    • Jervis, K. M. and Robaire, B. (2001) Dynamic changes in gene expression along the rat epididymis. Biol. Reprod. 65, 696-703.
    • (2001) Biol. Reprod , vol.65 , pp. 696-703
    • Jervis, K.M.1    Robaire, B.2
  • 73
    • 4444254836 scopus 로고    scopus 로고
    • Tyrosine phosphorylation activates surface chaperones facilitating sperm-zona recognition
    • Asquith, K. L., Baleato, R. M., McLaughlin, E. A., Nixon, B. and Aitken, R. J. (2004) Tyrosine phosphorylation activates surface chaperones facilitating sperm-zona recognition. J. Cell Sci. 117, 3645-3657.
    • (2004) J. Cell Sci , vol.117 , pp. 3645-3657
    • Asquith, K.L.1    Baleato, R.M.2    McLaughlin, E.A.3    Nixon, B.4    Aitken, R.J.5
  • 74
    • 12344309010 scopus 로고    scopus 로고
    • Localization and significance of molecular chaperones, heat shock protein 1, and tumor rejection antigen gp96 in the male reproductive tract and during capacitation and acrosome reaction
    • Asquith, K. L., Harman, A. J., McLaughlin, E. A., Nixon, B. and Aitken, R. J. (2005) Localization and significance of molecular chaperones, heat shock protein 1, and tumor rejection antigen gp96 in the male reproductive tract and during capacitation and acrosome reaction. Biol. Reprod. 72, 328-337.
    • (2005) Biol. Reprod , vol.72 , pp. 328-337
    • Asquith, K.L.1    Harman, A.J.2    McLaughlin, E.A.3    Nixon, B.4    Aitken, R.J.5
  • 75
    • 0029046131 scopus 로고
    • Redox regulation of tyrosine phosphorylation in human spermatozoa and its role in the control of human sperm function
    • Aitken, R. J., Paterson, M., Fisher, H., Buckingham, D. W. and van Duin, M. (1995) Redox regulation of tyrosine phosphorylation in human spermatozoa and its role in the control of human sperm function. J. Cell Sci. 108 (Pt 5), 2017-2025.
    • (1995) J. Cell Sci , vol.108 , Issue.PART 5 , pp. 2017-2025
    • Aitken, R.J.1    Paterson, M.2    Fisher, H.3    Buckingham, D.W.4    van Duin, M.5
  • 76
    • 0031049037 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphorylation during bovine sperm capacitation by a cyclic adenosine 3′5′-monophosphate-dependent pathway
    • Galantino-Homer, H. L., Visconti, P. E. and Kopf, G. S. (1997) Regulation of protein tyrosine phosphorylation during bovine sperm capacitation by a cyclic adenosine 3′5′-monophosphate-dependent pathway. Biol. Reprod. 56, 707-719.
    • (1997) Biol. Reprod , vol.56 , pp. 707-719
    • Galantino-Homer, H.L.1    Visconti, P.E.2    Kopf, G.S.3
  • 77
    • 0032438668 scopus 로고    scopus 로고
    • Regulation of sperm function by protein tyrosine phosphorylation in diverse wild felid species
    • Pukazhenthi, B. S., Long, J. A., Wildt, D. E., Ottinger, M. A., Armstrong, D. L. and Howard, J. (1998) Regulation of sperm function by protein tyrosine phosphorylation in diverse wild felid species. J. Androl. 19, 675-685.
    • (1998) J. Androl , vol.19 , pp. 675-685
    • Pukazhenthi, B.S.1    Long, J.A.2    Wildt, D.E.3    Ottinger, M.A.4    Armstrong, D.L.5    Howard, J.6
  • 78
    • 0031687185 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphorylation in boar sperm through a cAMP-dependent pathway
    • Kalab, P., Peknicova, J., Geussova, G. and Moos, J. (1998) Regulation of protein tyrosine phosphorylation in boar sperm through a cAMP-dependent pathway. Mol. Reprod. Dev. 51, 304-314.
    • (1998) Mol. Reprod. Dev , vol.51 , pp. 304-314
    • Kalab, P.1    Peknicova, J.2    Geussova, G.3    Moos, J.4
  • 79
    • 0032891280 scopus 로고    scopus 로고
    • Protein tyrosine phosphorylation during hyperactivated motility of cynomolgus monkey (Macaca fascicularis) spermatozoa
    • Mahony, M. C. and Gwathmey, T. (1999) Protein tyrosine phosphorylation during hyperactivated motility of cynomolgus monkey (Macaca fascicularis) spermatozoa. Biol. Reprod. 60, 1239-1243.
    • (1999) Biol. Reprod , vol.60 , pp. 1239-1243
    • Mahony, M.C.1    Gwathmey, T.2
  • 80
    • 0034947017 scopus 로고    scopus 로고
    • A redox-regulated tyrosine phosphorylation cascade in rat spermatozoa
    • Lewis, B. and Aitken, R. J. (2001) A redox-regulated tyrosine phosphorylation cascade in rat spermatozoa. J. Androl. 22, 611-622.
    • (2001) J. Androl , vol.22 , pp. 611-622
    • Lewis, B.1    Aitken, R.J.2
  • 81
    • 0037379268 scopus 로고    scopus 로고
    • Phosphorylation of protein tyrosine residues in fresh and cryopre-served stallion spermatozoa under capacitating conditions
    • Pommer, A. C., Rutllant, J. and Meyers, S. A. (2003) Phosphorylation of protein tyrosine residues in fresh and cryopre-served stallion spermatozoa under capacitating conditions. Biol. Reprod. 68, 1208-1214.
    • (2003) Biol. Reprod , vol.68 , pp. 1208-1214
    • Pommer, A.C.1    Rutllant, J.2    Meyers, S.A.3
  • 82
    • 33645300734 scopus 로고    scopus 로고
    • Tyrosine phosphorylation on capacitated human sperm tail detected by immunofluorescence correlates strongly with sperm-zona pellucida (ZP) binding but not with the ZP-induced acrosome reaction
    • Liu, D. Y., Clarke, G. N. and Baker, H. W. (2006) Tyrosine phosphorylation on capacitated human sperm tail detected by immunofluorescence correlates strongly with sperm-zona pellucida (ZP) binding but not with the ZP-induced acrosome reaction. Hum. Reprod. 21, 1002-1008.
    • (2006) Hum. Reprod , vol.21 , pp. 1002-1008
    • Liu, D.Y.1    Clarke, G.N.2    Baker, H.W.3
  • 83
    • 33750019007 scopus 로고    scopus 로고
    • Dynamic quantification of the tyrosine phosphorylation of the sperm surface proteins during capacitation
    • Piehler, E., Petrunkina, A. M., Ekhlasi-Hundrieser, M. and Topfer-Petersen, E. (2006) Dynamic quantification of the tyrosine phosphorylation of the sperm surface proteins during capacitation. Cytometry 69A, 1062-1070.
    • (2006) Cytometry , vol.69 A , pp. 1062-1070
    • Piehler, E.1    Petrunkina, A.M.2    Ekhlasi-Hundrieser, M.3    Topfer-Petersen, E.4
  • 84
    • 0033533489 scopus 로고    scopus 로고
    • Capacitation induces tyrosine phosphorylation of proteins in the boar sperm plasma membrane
    • Flesch, F. M., Colenbrander, B., van Golde, L. M. and Gadella, B. M. (1999) Capacitation induces tyrosine phosphorylation of proteins in the boar sperm plasma membrane. Biochem. Biophys. Res. Commun. 262, 787-792.
    • (1999) Biochem. Biophys. Res. Commun , vol.262 , pp. 787-792
    • Flesch, F.M.1    Colenbrander, B.2    van Golde, L.M.3    Gadella, B.M.4
  • 85
    • 0034902491 scopus 로고    scopus 로고
    • Capacitation dependent activation of tyrosine phosphorylation generates two sperm head plasma membrane proteins with high primary binding affinity for the zona pellucida
    • Flesch, F. M., Wijnand, E., van de Lest, C. H., Colenbrander, B., van Golde, L. M. and Gadella, B. M. (2001) Capacitation dependent activation of tyrosine phosphorylation generates two sperm head plasma membrane proteins with high primary binding affinity for the zona pellucida. Mol. Reprod. Dev. 60, 107-115.
    • (2001) Mol. Reprod. Dev , vol.60 , pp. 107-115
    • Flesch, F.M.1    Wijnand, E.2    van de Lest, C.H.3    Colenbrander, B.4    van Golde, L.M.5    Gadella, B.M.6
  • 86
    • 0345169713 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of HSP-90 during mammalian sperm capacitation
    • Ecroyd, H., Jones, R. C. and Aitken, R. J. (2003) Tyrosine phosphorylation of HSP-90 during mammalian sperm capacitation. Biol. Reprod. 69, 1801-1807.
    • (2003) Biol. Reprod , vol.69 , pp. 1801-1807
    • Ecroyd, H.1    Jones, R.C.2    Aitken, R.J.3
  • 87
    • 33646863600 scopus 로고    scopus 로고
    • Proteomic analysis of sperm regions that mediate sperm-egg interactions
    • Stein, K. K., Go, J. C., Lane, W. S., Primakoff, P. and Myles, D. G. (2006) Proteomic analysis of sperm regions that mediate sperm-egg interactions. Proteomics 6, 3533-3543.
    • (2006) Proteomics , vol.6 , pp. 3533-3543
    • Stein, K.K.1    Go, J.C.2    Lane, W.S.3    Primakoff, P.4    Myles, D.G.5
  • 96
    • 0033898407 scopus 로고    scopus 로고
    • A Fourier-transform infrared study of the interaction between germ-cell specific sulfogalactosylglycerolipid and dimyristoylglycerophosphocholine
    • Attar, M., Kates, M., Bou Khalil, M., Carrier, D., Wong, P. T. and Tanphaichitr, N. (2000) A Fourier-transform infrared study of the interaction between germ-cell specific sulfogalactosylglycerolipid and dimyristoylglycerophosphocholine. Chem. Phys. Lipids 106, 101-114.
    • (2000) Chem. Phys. Lipids , vol.106 , pp. 101-114
    • Attar, M.1    Kates, M.2    Bou Khalil, M.3    Carrier, D.4    Wong, P.T.5    Tanphaichitr, N.6
  • 97
    • 33846379145 scopus 로고    scopus 로고
    • Visualizing the localization of sulfoglycolipids in lipid raft domains in model membranes and sperm membrane extracts
    • Weerachatyanukul, W., Probodh, I., Kongmanas, K., Tanphaichitr, N. and Johnston, L. J. (2007) Visualizing the localization of sulfoglycolipids in lipid raft domains in model membranes and sperm membrane extracts. Biochim. Biophys. Acta. 1768, 299-310.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 299-310
    • Weerachatyanukul, W.1    Probodh, I.2    Kongmanas, K.3    Tanphaichitr, N.4    Johnston, L.J.5
  • 98
    • 0026628742 scopus 로고
    • Role of a germ cell-specific sulfolipid-immobilizing protein (SLIP1) in mouse in vivo fertilization
    • Tanphaichitr, N., Tayabali, A., Gradil, C., Juneja, S., Leveille, M. C. and Lingwood, C. A. (1992) Role of a germ cell-specific sulfolipid-immobilizing protein (SLIP1) in mouse in vivo fertilization. Mol. Reprod. Dev. 32, 17-22.
    • (1992) Mol. Reprod. Dev , vol.32 , pp. 17-22
    • Tanphaichitr, N.1    Tayabali, A.2    Gradil, C.3    Juneja, S.4    Leveille, M.C.5    Lingwood, C.A.6
  • 99
    • 0027476856 scopus 로고
    • Role of a gamete-specific sulfoglycolipid immobilizing protein on mouse sperm-egg binding
    • Tanphaichitr, N., Smith, J., Mongkolsirikieart, S., Gradil, C. and Lingwood, C. A. (1993) Role of a gamete-specific sulfoglycolipid immobilizing protein on mouse sperm-egg binding. Dev. Biol. 156, 164-175.
    • (1993) Dev. Biol , vol.156 , pp. 164-175
    • Tanphaichitr, N.1    Smith, J.2    Mongkolsirikieart, S.3    Gradil, C.4    Lingwood, C.A.5
  • 102
    • 0019846906 scopus 로고
    • The appearance of an extracellular arylsulfatase during morphogenesis of the sea urchin Strongylocentrotus purpuratus
    • Rapraeger, A. C. and Epel, D. (1981) The appearance of an extracellular arylsulfatase during morphogenesis of the sea urchin Strongylocentrotus purpuratus. Dev. Biol. 88, 269-278.
    • (1981) Dev. Biol , vol.88 , pp. 269-278
    • Rapraeger, A.C.1    Epel, D.2
  • 103
    • 0002178898 scopus 로고
    • Galactoglycerolipids of mammalian testis, spermatozoa, and nervous tissue
    • Sweeley, C. C, Ed, American Chemical Society, Washington, D. C
    • Murray, R. K., Narsimhan, R., Levine, M. and Pinteric, L. (1980) Galactoglycerolipids of mammalian testis, spermatozoa, and nervous tissue. In: Cell Surface Glycolipids, pp. 105-125, Sweeley, C. C. (Ed.), American Chemical Society, Washington, D. C.
    • (1980) Cell Surface Glycolipids , pp. 105-125
    • Murray, R.K.1    Narsimhan, R.2    Levine, M.3    Pinteric, L.4
  • 104
    • 0022272133 scopus 로고
    • Involvement of sperm sulphatases in early sperm-zona interactions in the hamster
    • Ahuja, K. K. and Gilburt, D. J. (1985) Involvement of sperm sulphatases in early sperm-zona interactions in the hamster. J. Cell Sci. 78, 247-261.
    • (1985) J. Cell Sci , vol.78 , pp. 247-261
    • Ahuja, K.K.1    Gilburt, D.J.2
  • 105
    • 33646914190 scopus 로고    scopus 로고
    • Targeted disruption of tyrosylprotein sulfotransferase-2, an enzyme that catalyzes post-translational protein tyrosine Osulfation, causes male infertility
    • Borghei, A., Ouyang, Y. B., Westmuckett, A. D., Marcello, M. R., Landel, C. P., Evans, J. P. and Moore, K. L. (2006) Targeted disruption of tyrosylprotein sulfotransferase-2, an enzyme that catalyzes post-translational protein tyrosine Osulfation, causes male infertility. J. Biol. Chem. 281, 9423-9431.
    • (2006) J. Biol. Chem , vol.281 , pp. 9423-9431
    • Borghei, A.1    Ouyang, Y.B.2    Westmuckett, A.D.3    Marcello, M.R.4    Landel, C.P.5    Evans, J.P.6    Moore, K.L.7
  • 107
    • 16844366282 scopus 로고    scopus 로고
    • The sulfogalactose moiety of sulfoglycosphingolipids serves as a mimic of tyrosine phosphate in many recognition processes. Prediction and demonstration of Src homology 2 domain/sulfogalactose binding
    • Lingwood, C., Mylvaganam, M., Minhas, F., Binnington, B., Branch, D. R. and Pomes, R. (2005)The sulfogalactose moiety of sulfoglycosphingolipids serves as a mimic of tyrosine phosphate in many recognition processes. Prediction and demonstration of Src homology 2 domain/sulfogalactose binding. J. Biol. Chem. 280, 12542-12547.
    • (2005) J. Biol. Chem , vol.280 , pp. 12542-12547
    • Lingwood, C.1    Mylvaganam, M.2    Minhas, F.3    Binnington, B.4    Branch, D.R.5    Pomes, R.6
  • 108
    • 17244370591 scopus 로고    scopus 로고
    • Unveiling the mechanisms of cell-cell fusion
    • Chen, E. H. and Olson, E. N. (2005) Unveiling the mechanisms of cell-cell fusion. Science 308, 369-373.
    • (2005) Science , vol.308 , pp. 369-373
    • Chen, E.H.1    Olson, E.N.2
  • 109
    • 0037484291 scopus 로고    scopus 로고
    • Expression of the molecular chaperone Hsp70 in detergent-resistant microdomains correlates with its membrane delivery and release
    • Broquet, A. H., Thomas, G., Masliah, J., Trugnan, G. and Bachelet, M. (2003) Expression of the molecular chaperone Hsp70 in detergent-resistant microdomains correlates with its membrane delivery and release. J. Biol. Chem. 278, 21601-21606.
    • (2003) J. Biol. Chem , vol.278 , pp. 21601-21606
    • Broquet, A.H.1    Thomas, G.2    Masliah, J.3    Trugnan, G.4    Bachelet, M.5
  • 110
    • 0037160084 scopus 로고    scopus 로고
    • Interactions of STAT3 with caveolin-1 and heat shock protein 90 in plasma membrane raft and cytosolic complexes. Preservation of cytokine signaling during fever
    • Shah, M., Patel, K., Fried, V. A. and Sehgal, P. B. (2002) Interactions of STAT3 with caveolin-1 and heat shock protein 90 in plasma membrane raft and cytosolic complexes. Preservation of cytokine signaling during fever. J. Biol. Chem. 277, 45662-45669.
    • (2002) J. Biol. Chem , vol.277 , pp. 45662-45669
    • Shah, M.1    Patel, K.2    Fried, V.A.3    Sehgal, P.B.4
  • 111
    • 8744294003 scopus 로고    scopus 로고
    • The integrity of cholesterol-enriched microdomains is essential for the constitutive high activity of protein kinase B in tumour cells
    • Elhyany, S., Assa-Kunik, E., Tsory, S., Muller, T., Fedida, S., Segal, S. and Fishman, D. (2004) The integrity of cholesterol-enriched microdomains is essential for the constitutive high activity of protein kinase B in tumour cells. Biochem. Soc. Trans. 32, 837-839.
    • (2004) Biochem. Soc. Trans , vol.32 , pp. 837-839
    • Elhyany, S.1    Assa-Kunik, E.2    Tsory, S.3    Muller, T.4    Fedida, S.5    Segal, S.6    Fishman, D.7
  • 112
    • 33750287154 scopus 로고    scopus 로고
    • Reorganization of mouse sperm lipid rafts by capacitation
    • Thaler, C. D., Thomas, M. and Ramalie, J. R. (2006 ) Reorganization of mouse sperm lipid rafts by capacitation. Mol. Reprod. Dev. 73, 1541-1549.
    • (2006) Mol. Reprod. Dev , vol.73 , pp. 1541-1549
    • Thaler, C.D.1    Thomas, M.2    Ramalie, J.R.3
  • 113
    • 25144513384 scopus 로고    scopus 로고
    • Isolation and proteomic analysis of mouse sperm detergent-resistant membrane fractions: Evidence for dissociation of lipid rafts during capacitation
    • Sleight, S. B., Miranda, P. V., Plaskett, N. W., Maier, B., Lysiak, J., Scrable, H., Herr, J. C. and Visconti, P. E. (2005) Isolation and proteomic analysis of mouse sperm detergent-resistant membrane fractions: evidence for dissociation of lipid rafts during capacitation. Biol. Reprod. 73, 721-729.
    • (2005) Biol. Reprod , vol.73 , pp. 721-729
    • Sleight, S.B.1    Miranda, P.V.2    Plaskett, N.W.3    Maier, B.4    Lysiak, J.5    Scrable, H.6    Herr, J.C.7    Visconti, P.E.8
  • 114
    • 0034141195 scopus 로고    scopus 로고
    • The ADAM gene family: Surface proteins with adhesion and protease activity
    • Primakoff, P. and Myles, D. G. (2000) The ADAM gene family: surface proteins with adhesion and protease activity. Trends Genet. 16, 83-87.
    • (2000) Trends Genet , vol.16 , pp. 83-87
    • Primakoff, P.1    Myles, D.G.2
  • 115
    • 0034729369 scopus 로고    scopus 로고
    • The cysteine-rich domain of human ADAM 12 supports cell adhesion through syndecans and triggers signaling events that lead to beta1 integrin-dependent cell spreading
    • Iba, K., Albrechtsen, R., Gilpin, B., Frohlich, C., Loechel, F., Zolkiewska, A., Ishiguro, K., Kojima, T., Liu, W., Langford, J. K. et al. (2000) The cysteine-rich domain of human ADAM 12 supports cell adhesion through syndecans and triggers signaling events that lead to beta1 integrin-dependent cell spreading. J. Cell Biol. 149, 1143-1156.
    • (2000) J. Cell Biol , vol.149 , pp. 1143-1156
    • Iba, K.1    Albrechtsen, R.2    Gilpin, B.3    Frohlich, C.4    Loechel, F.5    Zolkiewska, A.6    Ishiguro, K.7    Kojima, T.8    Liu, W.9    Langford, J.K.10
  • 116
    • 0023100910 scopus 로고
    • Identification and purification of a sperm surface protein with a potential role in sperm-egg membrane fusion
    • Primakoff, P., Hyatt, H. and Tredick-Kline, J. (1987) Identification and purification of a sperm surface protein with a potential role in sperm-egg membrane fusion. J. Cell Biol. 104, 141-149.
    • (1987) J. Cell Biol , vol.104 , pp. 141-149
    • Primakoff, P.1    Hyatt, H.2    Tredick-Kline, J.3
  • 117
    • 0030940446 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of bovine fertilin alpha and beta (ADAM 1 and ADAM 2): A candidate sperm-egg binding/fusion complex
    • Waters, S. I. and White, J. M. (1997) Biochemical and molecular characterization of bovine fertilin alpha and beta (ADAM 1 and ADAM 2): a candidate sperm-egg binding/fusion complex. Biol. Reprod. 56, 1245-1254.
    • (1997) Biol. Reprod , vol.56 , pp. 1245-1254
    • Waters, S.I.1    White, J.M.2
  • 118
    • 0034660644 scopus 로고    scopus 로고
    • Analysis of mouse fertilin in wild-type and fertilin beta(-/-) sperm: Evidence for C-terminal modification, alpha/beta dimerization, and lack of essential role of fertilin alpha in sperm-egg fusion
    • Cho, C., Ge, H., Branciforte, D., Primakoff, P. and Myles, D. G. (2000) Analysis of mouse fertilin in wild-type and fertilin beta(-/-) sperm: evidence for C-terminal modification, alpha/beta dimerization, and lack of essential role of fertilin alpha in sperm-egg fusion. Dev. Biol. 222, 289-295.
    • (2000) Dev. Biol , vol.222 , pp. 289-295
    • Cho, C.1    Ge, H.2    Branciforte, D.3    Primakoff, P.4    Myles, D.G.5
  • 119
    • 0027930754 scopus 로고
    • Sequence and expression of a monkey testicular transcript encoding tMDC I, a novel member of the metalloproteinase-like, disintegrin-like, cysteine-rich (MDC) protein family
    • Barker, H. L., Perry, A. C., Jones, R. and Hall, L. (1994) Sequence and expression of a monkey testicular transcript encoding tMDC I, a novel member of the metalloproteinase-like, disintegrin-like, cysteine-rich (MDC) protein family. Biochim. Biophys. Acta. 1218, 429-431.
    • (1994) Biochim. Biophys. Acta , vol.1218 , pp. 429-431
    • Barker, H.L.1    Perry, A.C.2    Jones, R.3    Hall, L.4
  • 120
    • 0029045064 scopus 로고
    • ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain
    • Wolfsberg, T. G., Straight, P. D., Gerena, R. L., Huovila, A. P., Primakoff, P., Myles, D. G. and White, J. M. (1995) ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain. Dev. Biol. 169, 378-383.
    • (1995) Dev. Biol , vol.169 , pp. 378-383
    • Wolfsberg, T.G.1    Straight, P.D.2    Gerena, R.L.3    Huovila, A.P.4    Primakoff, P.5    Myles, D.G.6    White, J.M.7
  • 121
    • 0028276534 scopus 로고    scopus 로고
    • Male germ cell-expressed mouse gene TAZ83 encodes a putative, cysteine rich transmembrane protein (cyritestin) sharing homologies with snake toxins and sperm-egg fusion proteins
    • Heinlein, U. A.O., Wallat, S., Senftleben, A. and Lemaire, L (1996) Male germ cell-expressed mouse gene TAZ83 encodes a putative, cysteine rich transmembrane protein (cyritestin) sharing homologies with snake toxins and sperm-egg fusion proteins. Dev. Growth Differ. 36, 49-58.
    • (1996) Dev. Growth Differ , vol.36 , pp. 49-58
    • Heinlein, U.A.O.1    Wallat, S.2    Senftleben, A.3    Lemaire, L.4
  • 122
    • 0035070684 scopus 로고    scopus 로고
    • Do fertilin beta and cyritestin play a major role in mammalian sperm-oolemma interactions? A critical reevaluation of the use of peptide mimics in identifying specific oocyte recognition protiens
    • McLaughlin, E. A., Frayne, J. , Bloomerg, G. and Hall, L. (2001) Do fertilin beta and cyritestin play a major role in mammalian sperm-oolemma interactions? A critical reevaluation of the use of peptide mimics in identifying specific oocyte recognition protiens. Mol. Hum. Reprod. 7, 313-317.
    • (2001) Mol. Hum. Reprod , vol.7 , pp. 313-317
    • McLaughlin, E.A.1    Frayne, J.2    Bloomerg, G.3    Hall, L.4
  • 123
    • 0030951614 scopus 로고    scopus 로고
    • A role for the disintegrin domain of cyritestin, a sperm surface protein belonging to the ADAM family, in mouse sperm-egg plasma membrane adhesion and fusion
    • Yuan, R., Primakoff, P. and Myles, D. G. (1997)A role for the disintegrin domain of cyritestin, a sperm surface protein belonging to the ADAM family, in mouse sperm-egg plasma membrane adhesion and fusion. J. Cell Biol. 137, 105-112.
    • (1997) J. Cell Biol , vol.137 , pp. 105-112
    • Yuan, R.1    Primakoff, P.2    Myles, D.G.3
  • 125
    • 0035337709 scopus 로고    scopus 로고
    • Analysis of loss of adhesive function in sperm lacking cyritestin or fertilin beta
    • Nishimura, H., Cho, C., Branciforte, D. R., Myles, D. G. and Primakoff, P. (2001) Analysis of loss of adhesive function in sperm lacking cyritestin or fertilin beta. Dev. Biol. 233, 204-213.
    • (2001) Dev. Biol , vol.233 , pp. 204-213
    • Nishimura, H.1    Cho, C.2    Branciforte, D.R.3    Myles, D.G.4    Primakoff, P.5
  • 127
    • 0031877099 scopus 로고    scopus 로고
    • Sequence analysis of a variety of primate fertilin alpha genes: Evidence for nonfunctional genes in the gorilla and man
    • Jury, J. A., Frayne, J. and Hall, L. (1998) Sequence analysis of a variety of primate fertilin alpha genes: evidence for nonfunctional genes in the gorilla and man. Mol. Reprod. Dev. 51, 92-97.
    • (1998) Mol. Reprod. Dev , vol.51 , pp. 92-97
    • Jury, J.A.1    Frayne, J.2    Hall, L.3
  • 128
    • 0032528978 scopus 로고    scopus 로고
    • The gene for the human tMDC I sperm surface protein is non-functional: Implications for its proposed role in mammalian sperm-egg recognition
    • Frayne, J. and Hall, L. (1998) The gene for the human tMDC I sperm surface protein is non-functional: implications for its proposed role in mammalian sperm-egg recognition. Biochem. J. 334 (Pt 1), 171-176.
    • (1998) Biochem. J , vol.334 , Issue.PART 1 , pp. 171-176
    • Frayne, J.1    Hall, L.2
  • 129
    • 0033303122 scopus 로고    scopus 로고
    • Hall, L. and Frayne, J. (1999) Non-functional fertility genes in humans: contributory factors in reduced male fertility? Hum. Fertil. (Camb) 2, 36-41.
    • Hall, L. and Frayne, J. (1999) Non-functional fertility genes in humans: contributory factors in reduced male fertility? Hum. Fertil. (Camb) 2, 36-41.
  • 130
    • 0033178820 scopus 로고    scopus 로고
    • Transcripts encoding the sperm surface protein tMDC II are non-functional in the human
    • Frayne, J., Dimsey, E. A., Jury, J. A. and Hall, L. (1999) Transcripts encoding the sperm surface protein tMDC II are non-functional in the human. Biochem. J. 341 (Pt 3), 771-775.
    • (1999) Biochem. J , vol.341 , Issue.PART 3 , pp. 771-775
    • Frayne, J.1    Dimsey, E.A.2    Jury, J.A.3    Hall, L.4
  • 131
    • 0037472673 scopus 로고    scopus 로고
    • Identification and characterization of ADAM32 with testis-predominant gene expression
    • Choi, I., Woo, J. M., Hong, S., Jung, Y. K., Kim, D., H. and Cho, C. (2003) Identification and characterization of ADAM32 with testis-predominant gene expression. Gene 304, 151-162.
    • (2003) Gene , vol.304 , pp. 151-162
    • Choi, I.1    Woo, J.M.2    Hong, S.3    Jung, Y.K.4    Kim, D.H.5    Cho, C.6
  • 132
    • 0037123373 scopus 로고    scopus 로고
    • Molecular cloning and expression analysis of a novel member of the Disintegrin and Metalloprotease-Domain (ADAM) family
    • Brachvogel, B., Reichenberg, D., Beyer, S., Jehn, B., von der Mark, K. and Bielke, W. (2002) Molecular cloning and expression analysis of a novel member of the Disintegrin and Metalloprotease-Domain (ADAM) family. Gene 288, 203-210.
    • (2002) Gene , vol.288 , pp. 203-210
    • Brachvogel, B.1    Reichenberg, D.2    Beyer, S.3    Jehn, B.4    von der Mark, K.5    Bielke, W.6
  • 133
    • 0035005450 scopus 로고    scopus 로고
    • Testase 1 (ADAM 24) a plasma membrane-anchored sperm protease implicated in sperm function during epididymal maturation or fertilization
    • Zhu, G. Z., Myles, D. G. and Primakoff, P. (2001) Testase 1 (ADAM 24) a plasma membrane-anchored sperm protease implicated in sperm function during epididymal maturation or fertilization. J. Cell Sci. 114, 1787-1794.
    • (2001) J. Cell Sci , vol.114 , pp. 1787-1794
    • Zhu, G.Z.1    Myles, D.G.2    Primakoff, P.3
  • 134
    • 0036713392 scopus 로고    scopus 로고
    • Human tMDC III: A sperm protein with a potential role in oocyte recognition
    • Frayne, J., Hurd, E. A. and Hall, L. (2002) Human tMDC III: a sperm protein with a potential role in oocyte recognition. Mol. Hum. Reprod. 8, 817-822.
    • (2002) Mol. Hum. Reprod , vol.8 , pp. 817-822
    • Frayne, J.1    Hurd, E.A.2    Hall, L.3
  • 135
    • 0017067054 scopus 로고
    • Androgen-controlled specific proteins in rat epididymis
    • Cameo, M. S. and Blaquier, J. A. (1976) Androgen-controlled specific proteins in rat epididymis. J. Endocrinol. 69, 47-55.
    • (1976) J. Endocrinol , vol.69 , pp. 47-55
    • Cameo, M.S.1    Blaquier, J.A.2
  • 136
    • 0024742682 scopus 로고
    • Cloning and mapping of a testis-specific gene with sequence similarity to a sperm-coating glycoprotein gene
    • Kasahara, M., Gutknecht, J., Brew, K., Spurr, N. and Goodfellow, P. N. (1989) Cloning and mapping of a testis-specific gene with sequence similarity to a sperm-coating glycoprotein gene. Genomics 5, 527-534.
    • (1989) Genomics , vol.5 , pp. 527-534
    • Kasahara, M.1    Gutknecht, J.2    Brew, K.3    Spurr, N.4    Goodfellow, P.N.5
  • 137
    • 0026788322 scopus 로고
    • Mouse submandibular glands express an androgen-regulated transcript encoding an acidic epididymal glycoprotein-like molecule
    • Mizuki, N. and Kasahara, M. (1992) Mouse submandibular glands express an androgen-regulated transcript encoding an acidic epididymal glycoprotein-like molecule. Mol. Cell. Endocrinol. 89, 25-32.
    • (1992) Mol. Cell. Endocrinol , vol.89 , pp. 25-32
    • Mizuki, N.1    Kasahara, M.2
  • 138
    • 0027321118 scopus 로고
    • Transcripts for cysteine-rich secretory protein-1 (CRISP-1; DE/AEG) and the novel related CRISP-3 are expressed under androgen control in the mouse salivary gland
    • Haendler, B., Kratzschmar, J., Theuring, F. and Schleuning, W. D. (1993) Transcripts for cysteine-rich secretory protein-1 (CRISP-1; DE/AEG) and the novel related CRISP-3 are expressed under androgen control in the mouse salivary gland. Endocrinology 133, 192-198.
    • (1993) Endocrinology , vol.133 , pp. 192-198
    • Haendler, B.1    Kratzschmar, J.2    Theuring, F.3    Schleuning, W.D.4
  • 139
    • 0029925313 scopus 로고    scopus 로고
    • The human cysteine-rich secretory protein (CRISP) family. Primary structure and tissue distribution of CRISP-1, CRISP-2 and CRISP-3
    • Kratzschmar, J., Haendler, B., Eberspaecher, U., Roosterman, D., Donner, P. and Schleuning, W. D. (1996) The human cysteine-rich secretory protein (CRISP) family. Primary structure and tissue distribution of CRISP-1, CRISP-2 and CRISP-3. Eur. J. Biochem. 236, 827-836.
    • (1996) Eur. J. Biochem , vol.236 , pp. 827-836
    • Kratzschmar, J.1    Haendler, B.2    Eberspaecher, U.3    Roosterman, D.4    Donner, P.5    Schleuning, W.D.6
  • 142
    • 34447650185 scopus 로고    scopus 로고
    • Cuasnicu, P. S., Conesa, D. and Rockwerger, L (1990) Potential contraceptive use of an epididymal protein that particpates in fertilsation. In: A. N. J., Griffin, D., Speiler, J. M., and Waites, G. M. H. (eds.), Gamete Interactions: Prospects for Immunocontraception, Wiley-Liss, New York. pp. 143-153.
    • Cuasnicu, P. S., Conesa, D. and Rockwerger, L (1990) Potential contraceptive use of an epididymal protein that particpates in fertilsation. In: A. N. J., Griffin, D., Speiler, J. M., and Waites, G. M. H. (eds.), Gamete Interactions: Prospects for Immunocontraception, Wiley-Liss, New York. pp. 143-153.
  • 143
    • 0026670417 scopus 로고
    • Mammalian sperm-egg fusion: The rat egg has complementary sites for a sperm protein that mediates gamete fusion
    • Rochwerger, L., Cohen, D. J. and Cuasnicu, P. S. (1992) Mammalian sperm-egg fusion: the rat egg has complementary sites for a sperm protein that mediates gamete fusion. Dev. Biol. 153, 83-90.
    • (1992) Dev. Biol , vol.153 , pp. 83-90
    • Rochwerger, L.1    Cohen, D.J.2    Cuasnicu, P.S.3
  • 144
    • 0033870427 scopus 로고    scopus 로고
    • Mammalian sperm-egg fusion: Evidence that epididymal protein DE plays a role in mouse gamete fusion
    • Cohen, D. J., Ellerman, D. A. and Cuasnicu, P. S. (2000) Mammalian sperm-egg fusion: evidence that epididymal protein DE plays a role in mouse gamete fusion. Biol. Reprod. 63, 462-468.
    • (2000) Biol. Reprod , vol.63 , pp. 462-468
    • Cohen, D.J.1    Ellerman, D.A.2    Cuasnicu, P.S.3
  • 145
    • 0031738499 scopus 로고    scopus 로고
    • Potential contraceptive use of epididymal proteins: Immunization of male rats with epididymal protein DE inhibits sperm fusion ability
    • Ellerman, D. A., Brantua, V. S., Martinez, S. P., Cohen, D. J., Conesa, D. and Cuasnicu, P. S. (1998) Potential contraceptive use of epididymal proteins: immunization of male rats with epididymal protein DE inhibits sperm fusion ability. Biol. Reprod. 59, 1029-1036.
    • (1998) Biol. Reprod , vol.59 , pp. 1029-1036
    • Ellerman, D.A.1    Brantua, V.S.2    Martinez, S.P.3    Cohen, D.J.4    Conesa, D.5    Cuasnicu, P.S.6
  • 146
    • 33748061640 scopus 로고    scopus 로고
    • Sperm protein 'DE' mediates gamete fusion through an evolutionarily conserved site of the CRISP family
    • Ellerman, D. A., Cohen, D. J., Da Ros, V. G., Morgenfeld, M. M., Busso, D. and Cuasnicu, P. S. (2006) Sperm protein 'DE' mediates gamete fusion through an evolutionarily conserved site of the CRISP family. Dev. Biol. 297, 228-237.
    • (2006) Dev. Biol , vol.297 , pp. 228-237
    • Ellerman, D.A.1    Cohen, D.J.2    Da Ros, V.G.3    Morgenfeld, M.M.4    Busso, D.5    Cuasnicu, P.S.6
  • 147
    • 23244434065 scopus 로고    scopus 로고
    • Mouse SLLP1, a sperm lysozyme-like protein involved in sperm-egg binding and fertilization
    • Herrero, M. B., Mandal, A., Digilio, L. C., Coonrod, S. A., Maier, B. and Herr, J. C. (2005) Mouse SLLP1, a sperm lysozyme-like protein involved in sperm-egg binding and fertilization. Dev. Biol. 284, 126-142.
    • (2005) Dev. Biol , vol.284 , pp. 126-142
    • Herrero, M.B.1    Mandal, A.2    Digilio, L.C.3    Coonrod, S.A.4    Maier, B.5    Herr, J.C.6
  • 148
    • 0036836665 scopus 로고    scopus 로고
    • Proteins of the PDI family: Unpredicted non-ER locations and functions
    • Turano, C., Coppari, S., Altieri, F. and Ferraro, A. (2002) Proteins of the PDI family: unpredicted non-ER locations and functions. J. Cell Physiol. 193, 154-163.
    • (2002) J. Cell Physiol , vol.193 , pp. 154-163
    • Turano, C.1    Coppari, S.2    Altieri, F.3    Ferraro, A.4
  • 149
    • 33646882179 scopus 로고    scopus 로고
    • A role for sperm surface protein disulfide isomerase activity in gamete fusion: Evidence for the participation of ERp57
    • Ellerman, D. A., Myles, D. G. and Primakoff, P. (2006)A role for sperm surface protein disulfide isomerase activity in gamete fusion: evidence for the participation of ERp57. Dev. Cell 10, 831-837.
    • (2006) Dev. Cell , vol.10 , pp. 831-837
    • Ellerman, D.A.1    Myles, D.G.2    Primakoff, P.3
  • 150
    • 15044362481 scopus 로고    scopus 로고
    • The immunoglobulin superfamily protein Izumo is required for sperm to fuse with eggs
    • Inoue, N., Ikawa, M., Isotani, A. and Okabe, M. (2005) The immunoglobulin superfamily protein Izumo is required for sperm to fuse with eggs. Nature 434, 234-238.
    • (2005) Nature , vol.434 , pp. 234-238
    • Inoue, N.1    Ikawa, M.2    Isotani, A.3    Okabe, M.4
  • 152
    • 33644977667 scopus 로고    scopus 로고
    • CD9 controls the formation of clusters that contain tetraspanins and the integrin alpha 6 beta 1, which are involved in human and mouse gamete fusion
    • Ziyyat, A., Rubinstein, E., Monier-Gavelle, F., Barraud, V., Kulski, O., Prenant, M., Boucheix, C., Bomsel, M. and Wolf, J. P. (2006) CD9 controls the formation of clusters that contain tetraspanins and the integrin alpha 6 beta 1, which are involved in human and mouse gamete fusion. J. Cell Sci. 119, 416-424.
    • (2006) J. Cell Sci , vol.119 , pp. 416-424
    • Ziyyat, A.1    Rubinstein, E.2    Monier-Gavelle, F.3    Barraud, V.4    Kulski, O.5    Prenant, M.6    Boucheix, C.7    Bomsel, M.8    Wolf, J.P.9
  • 153
    • 0023801763 scopus 로고
    • Effect of a monoclonal anti-mouse sperm antibody (OBF13) on the interaction of mouse sperm with zona-free mouse and hamster eggs
    • Okabe, M., Yagasaki, M., Oda, H., Matzno, S., Kohama, Y. and Mimura, T. (1988) Effect of a monoclonal anti-mouse sperm antibody (OBF13) on the interaction of mouse sperm with zona-free mouse and hamster eggs. J. Reprod. Immunol. 13, 211-219.
    • (1988) J. Reprod. Immunol , vol.13 , pp. 211-219
    • Okabe, M.1    Yagasaki, M.2    Oda, H.3    Matzno, S.4    Kohama, Y.5    Mimura, T.6
  • 154
    • 0036629075 scopus 로고    scopus 로고
    • The molecular basis of sperm-oocyte membrane interactions during mammalian fertilization
    • Evans, J. P. (2002) The molecular basis of sperm-oocyte membrane interactions during mammalian fertilization. Hum. Reprod. Update 8, 297-311.
    • (2002) Hum. Reprod. Update , vol.8 , pp. 297-311
    • Evans, J.P.1
  • 155
    • 0037124066 scopus 로고    scopus 로고
    • Functional classification of ADAMs based on a conserved motif for binding to integrin alpha 9beta 1: Implications for sperm-egg binding and other cell interactions
    • Eto, K., Huet, C., Tarui, T., Kupriyanov, S., Liu, H. Z., Puzon-McLaughlin, W., Zhang, X. P., Sheppard, D., Engvall, E. and Takada, Y. (2002) Functional classification of ADAMs based on a conserved motif for binding to integrin alpha 9beta 1: implications for sperm-egg binding and other cell interactions. J. Biol. Chem. 277, 17804-17810.
    • (2002) J. Biol. Chem , vol.277 , pp. 17804-17810
    • Eto, K.1    Huet, C.2    Tarui, T.3    Kupriyanov, S.4    Liu, H.Z.5    Puzon-McLaughlin, W.6    Zhang, X.P.7    Sheppard, D.8    Engvall, E.9    Takada, Y.10
  • 156
    • 0033559614 scopus 로고    scopus 로고
    • Treatment of mouse oocytes with PI-PLC releases 70-kDa (pI 5) and 35- to 45-kDa (pI 5.5) protein clusters from the egg surface and inhibits sperm-oolemma binding and fusion
    • Coonrod, S. A., Naaby-Hansen, S., Shetty, J., Shibahara, H., Chen, M., White, J. M. and Herr, J. C. (1999b) Treatment of mouse oocytes with PI-PLC
    • (1999) Dev. Biol , vol.207 , pp. 334-349
    • Coonrod, S.A.1    Naaby-Hansen, S.2    Shetty, J.3    Shibahara, H.4    Chen, M.5    White, J.M.6    Herr, J.C.7
  • 157
    • 0034697006 scopus 로고    scopus 로고
    • Sequence-specific interaction between the disintegrin domain of mouse ADAM 2 (fertilin beta) and murine eggs. Role of the alpha(6) integrin subunit
    • Bigler, D., Takahashi, Y., Chen, M. S., Almeida, E. A., Osbourne, L. and White, J. M. (2000) Sequence-specific interaction between the disintegrin domain of mouse ADAM 2 (fertilin beta) and murine eggs. Role of the alpha(6) integrin subunit. J. Biol. Chem. 275, 11576-11584.
    • (2000) J. Biol. Chem , vol.275 , pp. 11576-11584
    • Bigler, D.1    Takahashi, Y.2    Chen, M.S.3    Almeida, E.A.4    Osbourne, L.5    White, J.M.6
  • 158
    • 0035163797 scopus 로고    scopus 로고
    • Sequence-specific interaction between the disintegrin domain of mouse ADAM 3 and murine eggs: Role of beta1 integrin-associated proteins CD9, CD81, and CD98
    • Takahashi, Y., Bigler, D., Ito, Y. and White, J. M. (2001) Sequence-specific interaction between the disintegrin domain of mouse ADAM 3 and murine eggs: role of beta1 integrin-associated proteins CD9, CD81, and CD98. Mol. Biol. Cell 12, 809-820.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 809-820
    • Takahashi, Y.1    Bigler, D.2    Ito, Y.3    White, J.M.4
  • 159
    • 0033933982 scopus 로고    scopus 로고
    • Meltrin gamma(ADAM-9) mediates cellular adhesion through alpha(6)beta(1)integrin, leading to a marked induction of fibroblast cell motility
    • Nath, D., Slocombe, P. M., Webster, A., Stephens, P. E., Docherty, A. J. and Murphy, G. (2000) Meltrin gamma(ADAM-9) mediates cellular adhesion through alpha(6)beta(1)integrin, leading to a marked induction of fibroblast cell motility. J. Cell Sci. 113 (Pt 12), 2319-2328.
    • (2000) J. Cell Sci , vol.113 , Issue.PART 12 , pp. 2319-2328
    • Nath, D.1    Slocombe, P.M.2    Webster, A.3    Stephens, P.E.4    Docherty, A.J.5    Murphy, G.6
  • 160
    • 0032969233 scopus 로고    scopus 로고
    • Interaction of metargidin (ADAM-15) with alphavbeta3 and alpha5beta1 integrins on different haemopoietic cells
    • Nath, D. , Slocombe, P. M. , Stephens, P. E. , Warn, A., Hutchinson, G. R. , Yamada, K. M. , Docherty, A. J. and Murphy, G. (1999) Interaction of metargidin (ADAM-15) with alphavbeta3 and alpha5beta1 integrins on different haemopoietic cells. J. Cell Sci. 112 (Pt 4), 579-587.
    • (1999) J. Cell Sci , vol.112 , Issue.PART 4 , pp. 579-587
    • Nath, D.1    Slocombe, P.M.2    Stephens, P.E.3    Warn, A.4    Hutchinson, G.R.5    Yamada, K.M.6    Docherty, A.J.7    Murphy, G.8
  • 161
    • 0032571315 scopus 로고    scopus 로고
    • Specific interaction of the recombinant disintegrin-like domain of MDC-15 (metargidin, ADAM-15) with integrin alphavbeta3
    • Zhang, X. P., Kamata, T., Yokoyama, K., Puzon-McLaughlin, W. and Takada, Y. (1998) Specific interaction of the recombinant disintegrin-like domain of MDC-15 (metargidin, ADAM-15) with integrin alphavbeta3. J. Biol. Chem. 273, 7345-7350.
    • (1998) J. Biol. Chem , vol.273 , pp. 7345-7350
    • Zhang, X.P.1    Kamata, T.2    Yokoyama, K.3    Puzon-McLaughlin, W.4    Takada, Y.5
  • 162
    • 0034074860 scopus 로고    scopus 로고
    • ADAM 23/MDC3, a human disintegrin that promotes cell adhesion via interaction with the alphavbeta3 integrin through an RGD-independent mechanism
    • Cal, S., Freije, J. M., Lopez, J. M., Takada, Y. and Lopez-Otin, C. (2000) ADAM 23/MDC3, a human disintegrin that promotes cell adhesion via interaction with the alphavbeta3 integrin through an RGD-independent mechanism. Mol. Biol. Cell 11, 1457-1469.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1457-1469
    • Cal, S.1    Freije, J.M.2    Lopez, J.M.3    Takada, Y.4    Lopez-Otin, C.5
  • 163
    • 0034811643 scopus 로고    scopus 로고
    • MDC-9 (ADAM-9/Meltrin gamma) functions as an adhesion molecule by binding the alpha(v)beta(5) integrin
    • Zhou, M., Graham, R., Russell, G. and Croucher, P. I. (2001) MDC-9 (ADAM-9/Meltrin gamma) functions as an adhesion molecule by binding the alpha(v)beta(5) integrin. Biochem Biophys. Res. Commun. 280, 574-580.
    • (2001) Biochem Biophys. Res. Commun , vol.280 , pp. 574-580
    • Zhou, M.1    Graham, R.2    Russell, G.3    Croucher, P.I.4
  • 164
    • 0036479289 scopus 로고    scopus 로고
    • The lymphocyte metalloprotease MDC-L (ADAM 28) is a ligand for the integrin alpha4beta1
    • Bridges, L. C., Tani, P. H., Hanson, K. R., Roberts, C. M., Judkins, M. B. and Bowditch, R. D. (2002) The lymphocyte metalloprotease MDC-L (ADAM 28) is a ligand for the integrin alpha4beta1. J. Biol. Chem. 277, 3784-3792.
    • (2002) J. Biol. Chem , vol.277 , pp. 3784-3792
    • Bridges, L.C.1    Tani, P.H.2    Hanson, K.R.3    Roberts, C.M.4    Judkins, M.B.5    Bowditch, R.D.6
  • 166
    • 0037442567 scopus 로고    scopus 로고
    • None of the integrins known to be present on the mouse egg or to be ADAM receptors are essential for sperm-egg binding and fusion
    • He, Z. Y., Brakebusch, C., Fassler, R., Kreidberg, J. A., Primakoff, P. and Myles, D. G. (2003) None of the integrins known to be present on the mouse egg or to be ADAM receptors are essential for sperm-egg binding and fusion. Dev. Biol. 254, 226-237.
    • (2003) Dev. Biol , vol.254 , pp. 226-237
    • He, Z.Y.1    Brakebusch, C.2    Fassler, R.3    Kreidberg, J.A.4    Primakoff, P.5    Myles, D.G.6
  • 167
    • 1542397146 scopus 로고    scopus 로고
    • Integrins are not involved in the process of human sperm-oolemmal fusion
    • Sengoku, K., Takuma, N., Miyamoto, T., Horikawa, M. and Ishikawa, M. (2004) Integrins are not involved in the process of human sperm-oolemmal fusion. Hum. Reprod. 19, 639-644.
    • (2004) Hum. Reprod , vol.19 , pp. 639-644
    • Sengoku, K.1    Takuma, N.2    Miyamoto, T.3    Horikawa, M.4    Ishikawa, M.5
  • 168
    • 0032732660 scopus 로고    scopus 로고
    • PI-PLC releases a 25-40 kDa protein cluster from the hamster oolemma and affects the sperm penetration assay
    • Coonrod, S., Naaby-Hansen, S., Shetty, J. and Herr, J. (1999a) PI-PLC releases a 25-40 kDa protein cluster from the hamster oolemma and affects the sperm penetration assay. Mol. Hum. Reprod. 5, 1027-1033.
    • (1999) Mol. Hum. Reprod , vol.5 , pp. 1027-1033
    • Coonrod, S.1    Naaby-Hansen, S.2    Shetty, J.3    Herr, J.4
  • 169
    • 0038687068 scopus 로고    scopus 로고
    • Infertility in female mice with an oocyte-specific knockout of GPI-anchored proteins
    • Alfieri, J. A., Martin, A. D., Takeda, J., Kondoh, G., Myles, D. G. and Primakoff, P. (2003) Infertility in female mice with an oocyte-specific knockout of GPI-anchored proteins. J. Cell Sci. 116, 2149-2155.
    • (2003) J. Cell Sci , vol.116 , pp. 2149-2155
    • Alfieri, J.A.1    Martin, A.D.2    Takeda, J.3    Kondoh, G.4    Myles, D.G.5    Primakoff, P.6
  • 170
    • 0033582228 scopus 로고    scopus 로고
    • Role of decay-accelerating factor in regulating complement activation on the erythrocyte surface as revealed by gene targeting
    • Sun, X., Funk, C. D., Deng, C., Sahu, A., Lambris, J. D. and Song, W. C. (1999) Role of decay-accelerating factor in regulating complement activation on the erythrocyte surface as revealed by gene targeting. Proc. Natl. Acad. Sci. USA 96, 628-633.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 628-633
    • Sun, X.1    Funk, C.D.2    Deng, C.3    Sahu, A.4    Lambris, J.D.5    Song, W.C.6
  • 171
    • 0037108924 scopus 로고    scopus 로고
    • Genome wide analysis of the Drosophila tetraspanins reveals a subset with similar function in the formation of the embryonic synapse
    • Fradkin, L. G., Kamphorst, J. T., DiAntonio, A., Goodman, C. S. and Noordermeer, J. N. (2002) Genome wide analysis of the Drosophila tetraspanins reveals a subset with similar function in the formation of the embryonic synapse. Proc. Natl. Acad. Sci. USA 99, 13663-13668.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13663-13668
    • Fradkin, L.G.1    Kamphorst, J.T.2    DiAntonio, A.3    Goodman, C.S.4    Noordermeer, J.N.5
  • 175
    • 0035955657 scopus 로고    scopus 로고
    • Structure of the tetraspanin main extracellular domain. A partially conserved fold with a structurally variable domain insertion
    • Seigneuret, M., Delaguillaumie, A., Lagaudriere-Gesbert, C. and Conjeaud, H. (2001) Structure of the tetraspanin main extracellular domain. A partially conserved fold with a structurally variable domain insertion. J. Biol. Chem. 276, 40055-40064.
    • (2001) J. Biol. Chem , vol.276 , pp. 40055-40064
    • Seigneuret, M.1    Delaguillaumie, A.2    Lagaudriere-Gesbert, C.3    Conjeaud, H.4
  • 176
    • 0344708475 scopus 로고    scopus 로고
    • Tetraspanin proteins mediate cellular penetration, invasion, and fusion events and define a novel type of membrane microdomain
    • Hemler, M. E. (2003) Tetraspanin proteins mediate cellular penetration, invasion, and fusion events and define a novel type of membrane microdomain. Annu. Rev. Cell Dev. Biol. 19, 397-422.
    • (2003) Annu. Rev. Cell Dev. Biol , vol.19 , pp. 397-422
    • Hemler, M.E.1
  • 177
    • 28444441957 scopus 로고    scopus 로고
    • Tetraspanin functions and associated microdomains
    • Hemler, M. E. (2005) Tetraspanin functions and associated microdomains. Nat. Rev. Mol. Cell Biol. 6, 801-811.
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 801-811
    • Hemler, M.E.1
  • 180
    • 0034849902 scopus 로고    scopus 로고
    • Boucheix, C. and Rubinstein, E. (2001) Tetraspanins. Cell. Mol. Life Sci. 58, 1189-1205.
    • Boucheix, C. and Rubinstein, E. (2001) Tetraspanins. Cell. Mol. Life Sci. 58, 1189-1205.
  • 181
    • 13444282238 scopus 로고    scopus 로고
    • Sperm-egg fusion: Events at the plasma membrane
    • Stein, K. K., Primakoff, P. and Myles, D. (2004) Sperm-egg fusion: events at the plasma membrane. J. Cell Sci. 117, 6269-6274.
    • (2004) J. Cell Sci , vol.117 , pp. 6269-6274
    • Stein, K.K.1    Primakoff, P.2    Myles, D.3
  • 182
    • 0032782655 scopus 로고    scopus 로고
    • Mediation of sperm-egg fusion: Evidence that mouse egg alpha6beta1 integrin is the receptor for sperm fertilinbeta
    • Chen, H. and Sampson, N. S. (1999) Mediation of sperm-egg fusion: evidence that mouse egg alpha6beta1 integrin is the receptor for sperm fertilinbeta. Chem. Biol. 6, 1-10.
    • (1999) Chem. Biol , vol.6 , pp. 1-10
    • Chen, H.1    Sampson, N.S.2
  • 183
    • 1842843786 scopus 로고    scopus 로고
    • Themechanism of sperm-oocyte fusion in mammals
    • Kaji, K. and Kudo, A. (2004) Themechanism of sperm-oocyte fusion in mammals. Reproduction 127, 423-429.
    • (2004) Reproduction , vol.127 , pp. 423-429
    • Kaji, K.1    Kudo, A.2
  • 185
    • 0034640885 scopus 로고    scopus 로고
    • Normal fertilization occurs with eggs lacking the integrin alpha6beta1 and is CD9-dependent
    • Miller, B. J., Georges-Labouesse, E., Primakoff, P. and Myles, D. G. (2000) Normal fertilization occurs with eggs lacking the integrin alpha6beta1 and is CD9-dependent. J. Cell Biol. 149, 1289-1296.
    • (2000) J. Cell Biol , vol.149 , pp. 1289-1296
    • Miller, B.J.1    Georges-Labouesse, E.2    Primakoff, P.3    Myles, D.G.4
  • 188
    • 0037148519 scopus 로고    scopus 로고
    • Murine CD9 is the receptor for pregnancy-specific glycoprotein 17
    • Waterhouse, R., Ha, C. and Dveksler, G. S. (2002) Murine CD9 is the receptor for pregnancy-specific glycoprotein 17. J. Exp. Med. 195, 277-282.
    • (2002) J. Exp. Med , vol.195 , pp. 277-282
    • Waterhouse, R.1    Ha, C.2    Dveksler, G.S.3
  • 189
    • 0344875471 scopus 로고    scopus 로고
    • Direct binding of the ligand PSG17 to CD9 requires a CD9 site essential for sperm-egg fusion
    • Ellerman, D. A., Ha, C., Primakoff, P., Myles, D. G. and Dveksler, G. S. (2003) Direct binding of the ligand PSG17 to CD9 requires a CD9 site essential for sperm-egg fusion. Mol. Biol. Cell 14, 5098-5103.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 5098-5103
    • Ellerman, D.A.1    Ha, C.2    Primakoff, P.3    Myles, D.G.4    Dveksler, G.S.5
  • 190
    • 0036302083 scopus 로고    scopus 로고
    • Infertility of CD9-deficient mouse eggs is reversed by mouse CD9, human CD9, or mouse CD81; polyadenylated mRNA injection developed for molecular analysis of sperm-egg fusion
    • Kaji, K., Oda, S., Miyazaki, S. and Kudo, A. (2002) Infertility of CD9-deficient mouse eggs is reversed by mouse CD9, human CD9, or mouse CD81; polyadenylated mRNA injection developed for molecular analysis of sperm-egg fusion. Dev. Biol. 247, 327-334.
    • (2002) Dev. Biol , vol.247 , pp. 327-334
    • Kaji, K.1    Oda, S.2    Miyazaki, S.3    Kudo, A.4
  • 193
    • 0026659250 scopus 로고
    • Evidence for the presence of an integrin cell adhesion receptor on the oolemma of unfertilized human oocytes
    • Fusi, F. M., Vignali, M., Busacca, M. and Bronson, R. A. (1992) Evidence for the presence of an integrin cell adhesion receptor on the oolemma of unfertilized human oocytes. Mol. Reprod. Dev. 31, 215-222.
    • (1992) Mol. Reprod. Dev , vol.31 , pp. 215-222
    • Fusi, F.M.1    Vignali, M.2    Busacca, M.3    Bronson, R.A.4
  • 194
    • 0031920649 scopus 로고    scopus 로고
    • Human gamete fusion can bypass beta1 integrin requirement
    • Ji, Y. Z., Wolf, J. P., Jouannet, P. and Bomsel, M. (1998) Human gamete fusion can bypass beta1 integrin requirement. Hum. Reprod. 13, 682-689.
    • (1998) Hum. Reprod , vol.13 , pp. 682-689
    • Ji, Y.Z.1    Wolf, J.P.2    Jouannet, P.3    Bomsel, M.4
  • 195
    • 33947108870 scopus 로고    scopus 로고
    • Oocyte CD9 is enriched on the microvillar membrane and required for normal microvillar shape and distribution
    • Runge, K. E., Evans, J. E., He, Z. Y., Gupta, S., McDonald, K. L., Stahlberg, H., Primakoff, P. and Myles, D. G. (2007) Oocyte CD9 is enriched on the microvillar membrane and required for normal microvillar shape and distribution. Dev. Biol. 304, 317-325.
    • (2007) Dev. Biol , vol.304 , pp. 317-325
    • Runge, K.E.1    Evans, J.E.2    He, Z.Y.3    Gupta, S.4    McDonald, K.L.5    Stahlberg, H.6    Primakoff, P.7    Myles, D.G.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.