메뉴 건너뛰기




Volumn 8, Issue 10 SUPPL., 2002, Pages

The state of the union: The cell biology of fertilization

Author keywords

[No Author keywords available]

Indexed keywords

ACROSOME REACTION; CELL FUNCTION; CONTRACEPTION; CYTOLOGY; FERTILIZATION; GAMETE; HUMAN; MAMMAL; NONHUMAN; PRIORITY JOURNAL; REVIEW; SPERMATOZOON CAPACITATION; ZONA PELLUCIDA; ANIMAL; BIOLOGICAL MODEL; FEMALE; FERTILITY; GENETICS; INFERTILITY; MALE; PHYSIOLOGY; REPRODUCTION;

EID: 85046913038     PISSN: 10788956     EISSN: None     Source Type: Journal    
DOI: 10.1038/nm-fertilityS57     Document Type: Review
Times cited : (118)

References (107)
  • 2
    • 0028824618 scopus 로고
    • Maturation promoting factor in the early days
    • Maller, J. L. Maturation promoting factor in the early days. Trends Biochem. Sci. 20, 524-528 (1995).
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 524-528
    • Maller, J.L.1
  • 3
    • 0028331705 scopus 로고
    • The family of guanylyl cyclase receptors and their ligands
    • Drewett, J. G. & Garbers, D. L. The family of guanylyl cyclase receptors and their ligands Endocr. Rev. 15, 135-162 (1994).
    • (1994) Endocr. Rev. , vol.15 , pp. 135-162
    • Drewett, J.G.1    Garbers, D.L.2
  • 4
    • 0034725748 scopus 로고    scopus 로고
    • Soluble adenylyl cyclase as an evolutionarily conserved bicarbonate sensor
    • Chen, Y. et al. Soluble adenylyl cyclase as an evolutionarily conserved bicarbonate sensor. Science 299, 625-628 (2000).
    • (2000) Science , vol.299 , pp. 625-628
    • Chen, Y.1
  • 5
    • 0034141195 scopus 로고    scopus 로고
    • The ADAM gene family: Surface proteins with adhesion and protease activity
    • Primakoff, P. & Myles, D. G The ADAM gene family: surface proteins with adhesion and protease activity. Trends Genet. 16, 83-87 (2000).
    • (2000) Trends Genet. , vol.16 , pp. 83-87
    • Primakoff, P.1    Myles, D.G.2
  • 6
    • 0010949457 scopus 로고    scopus 로고
    • U.S. Census Bureau World Popclock. http://www.census.gov/cgi-bin/ipc/popclockw (2002).
    • (2002)
  • 10
    • 0031049748 scopus 로고    scopus 로고
    • Why did the sperm cross the cumulus - To get to the oocyte: Functions of the sperm surface proteins PH-20 and fertilin in arriving at and fusing with the egg
    • Myles, D. G. & Primakoff, P. Why did the sperm cross the cumulus - to get to the oocyte: functions of the sperm surface proteins PH-20 and fertilin in arriving at and fusing with the egg. Biol. Reprod. 56, 320-327 (1997).
    • (1997) Biol. Reprod. , vol.56 , pp. 320-327
    • Myles, D.G.1    Primakoff, P.2
  • 11
    • 0029896017 scopus 로고    scopus 로고
    • The molecules of mammalian fertilization
    • Snell, W. J. & White, J. M. The molecules of mammalian fertilization. Cell 85, 629-637 (1996).
    • (1996) Cell , vol.85 , pp. 629-637
    • Snell, W.J.1    White, J.M.2
  • 12
    • 0032566791 scopus 로고
    • Evolution of gamete recognition proteins
    • Vacquier, V. D. Evolution of gamete recognition proteins. Science 281, 1995-1998 (1978).
    • (1978) Science , vol.281 , pp. 1995-1998
    • Vacquier, V.D.1
  • 13
    • 0031954799 scopus 로고    scopus 로고
    • The molecu]ar basis of sperm capacitation
    • Visconti, P. E. et al. The molecu]ar basis of sperm capacitation. J. Androl. 19, 242-248 (1998).
    • (1998) J. Androl. , vol.19 , pp. 242-248
    • Visconti, P.E.1
  • 14
    • 0001072026 scopus 로고    scopus 로고
    • An intimate biochemistry: Egg-regulated acrosome reactions of mammalian sperm
    • Florman, H. M., Arnoult, C., Kazam, I. G., Li, C. & O'Toole, C. M. B. An intimate biochemistry: egg-regulated acrosome reactions of mammalian sperm. Adv. Devel. Biochem. 5, 147-186 (1999).
    • (1999) Adv. Devel. Biochem. , vol.5 , pp. 147-186
    • Florman, H.M.1    Arnoult, C.2    Kazam, I.G.3    Li, C.4    O'Toole, C.M.B.5
  • 15
    • 0036271669 scopus 로고    scopus 로고
    • Novel signaling pathways involved in sperm acquisition of fertilizing capacity
    • Visconti, P. E. et al. Novel signaling pathways involved in sperm acquisition of fertilizing capacity. J. Reprod. Immunol. 53, 133-150 (2002).
    • (2002) J. Reprod. Immunol. , vol.53 , pp. 133-150
    • Visconti, P.E.1
  • 16
    • 0032572581 scopus 로고    scopus 로고
    • 2+ entry into sperm
    • 2+ entry into sperm. J. Cell Biol. 142, 473-484 (1998).
    • (1998) J. Cell Biol. , vol.142 , pp. 473-484
    • Wiesner, B.1
  • 17
    • 0034769287 scopus 로고    scopus 로고
    • Hyperactivation of mammalian spermatozoa: Function and regulation
    • Ho, H. C. & Suarez, S. S. Hyperactivation of mammalian spermatozoa: function and regulation. Reproduction 122, 519-526 (2001).
    • (2001) Reproduction , vol.122 , pp. 519-526
    • Ho, H.C.1    Suarez, S.S.2
  • 18
    • 0033535956 scopus 로고    scopus 로고
    • Control of the low voltage-activated calcium channel of mouse sperm by egg ZP3 and by membrane hyperpolarization during capacitation
    • Arnoult, C. et al. Control of the low voltage-activated calcium channel of mouse sperm by egg ZP3 and by membrane hyperpolarization during capacitation. Proc. Natl Acad. Sci. USA 96, 6757-6762 (1999)
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6757-6762
    • Arnoult, C.1
  • 19
    • 0033570112 scopus 로고    scopus 로고
    • Cholesterol efflux-mediated signal transduction in mammalian sperm: Cholesterol release signals an increase in protein tyrosine phosphorylation during mouse sperm capacitation
    • Visconti, P. E. et al. Cholesterol efflux-mediated signal transduction in mammalian sperm: cholesterol release signals an increase in protein tyrosine phosphorylation during mouse sperm capacitation. Dev. Biol. 214, 429-443 (1999).
    • (1999) Dev. Biol. , vol.214 , pp. 429-443
    • Visconti, P.E.1
  • 20
    • 0034913241 scopus 로고    scopus 로고
    • Detection of progesterone receptors in human spermatozoa and their correlation with morphological and functional properties
    • Contreras, H. R. & Llanos, M. N. Detection of progesterone receptors in human spermatozoa and their correlation with morphological and functional properties. Int. J. Androl. 24, 246-252 (2001).
    • (2001) Int. J. Androl. , vol.24 , pp. 246-252
    • Contreras, H.R.1    Llanos, M.N.2
  • 21
    • 0022552266 scopus 로고
    • Autoradiographic visualization of the mouse egg's sperm receptor bound to sperm
    • Bleil, J. D. & Wassarman, P. M. Autoradiographic visualization of the mouse egg's sperm receptor bound to sperm. J. Cell Biol. 102, 1363-1371 (1986).
    • (1986) J. Cell Biol. , vol.102 , pp. 1363-1371
    • Bleil, J.D.1    Wassarman, P.M.2
  • 22
    • 0018831516 scopus 로고
    • Mammalian sperm-egg interaction: Identification of a glycoprotein in mouse egg zonae cellucidae possessing receptor activity for sperm
    • Bleil, J. D. & Wassarman, P. M. Mammalian sperm-egg interaction: identification of a glycoprotein in mouse egg zonae cellucidae possessing receptor activity for sperm. Cell 20, 873-882 (1980).
    • (1980) Cell , vol.20 , pp. 873-882
    • Bleil, J.D.1    Wassarman, P.M.2
  • 23
    • 0021874149 scopus 로고
    • O-linked oligosaccharides of mouse egg ZP3 account for its sperm receptor activity
    • Florman, H. M. & Wassarman, P. M. O-linked oligosaccharides of mouse egg ZP3 account for its sperm receptor activity. Cell 41, 313-324 (1985).
    • (1985) Cell , vol.41 , pp. 313-324
    • Florman, H.M.1    Wassarman, P.M.2
  • 24
    • 0035211076 scopus 로고    scopus 로고
    • Towards the molecular basis of sperm and egg interaction during mammalian fertilization
    • Wassarman, P. M. & Litscher, E. S. Towards the molecular basis of sperm and egg interaction during mammalian fertilization. Cells Tissues Organs 168, 36-45 (2001).
    • (2001) Cells Tissues Organs , vol.168 , pp. 36-45
    • Wassarman, P.M.1    Litscher, E.S.2
  • 26
    • 0028846510 scopus 로고
    • A sperm membrane protein that binds in a species-specific manner to the egg extracellular matrix is homologous to von Willebrand factor
    • Hardy, D. M. & Garbers, D. L. A sperm membrane protein that binds in a species-specific manner to the egg extracellular matrix is homologous to von Willebrand factor. J. Biol. Chem. 270, 26025-26028 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 26025-26028
    • Hardy, D.M.1    Garbers, D.L.2
  • 27
    • 0028342441 scopus 로고
    • Species-specific binding of sperm proteins to the extracellular matrix (zona pellucida) of the egg
    • Hardy, D. M. & Garbers, D. L. Species-specific binding of sperm proteins to the extracellular matrix (zona pellucida) of the egg. J. Biol. Chem. 269, 19000-19004 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 19000-19004
    • Hardy, D.M.1    Garbers, D.L.2
  • 28
    • 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. & Wassarman, P. M. Inactivation of the mouse sperm receptor, mZP3, by site-directed mutagenesis of individual serine residues located at the combining site for sperm. Proc. Nati Acad. Sci. USA 95, 6193-6197 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6193-6197
    • Chen, J.1    Litscher, E.S.2    Wassarman, P.M.3
  • 29
    • 0026052068 scopus 로고
    • Aggregation of α-1.4-galactosyltransferase on mouse sperm induces the acrosome reaction
    • Macek, M. B., Lopez, L. C. & Shur, B. D. Aggregation of α-1.4-galactosyltransferase on mouse sperm induces the acrosome reaction. Dev. Biol. 147, 440-444 (1991).
    • (1991) Dev. Biol. , vol.147 , pp. 440-444
    • Macek, M.B.1    Lopez, L.C.2    Shur, B.D.3
  • 30
    • 0029094342 scopus 로고
    • Activation of a G protein complex by aggregation of β-1,4-galactosyltransferase on the surfacce of sperm
    • Gong, X., Dubois, D. H., Miller, D. J. & Shur, B. D. Activation of a G protein complex by aggregation of β-1,4-galactosyltransferase on the surfacce of sperm. Science 269, 1718-1721 (1995).
    • (1995) Science , vol.269 , pp. 1718-1721
    • Gong, X.1    Dubois, D.H.2    Miller, D.J.3    Shur, B.D.4
  • 31
    • 0030888059 scopus 로고    scopus 로고
    • Structure of the main saccharide chain in the acrosome reaction-inducing substance of the starfish, Asterias amurensis
    • Koyota, S., Wimalasiri, K. M. & Hoshi, M. Structure of the main saccharide chain in the acrosome reaction-inducing substance of the starfish, Asterias amurensis. J. Biol. Chem. 272, 10372-10376 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 10372-10376
    • Koyota, S.1    Wimalasiri, K.M.2    Hoshi, M.3
  • 32
    • 0037059738 scopus 로고    scopus 로고
    • 2+ channels involved in triggering the sea urchin sperm acrosome reaction
    • 2+ channels involved in triggering the sea urchin sperm acrosome reaction. J. Biol. Chem. 277, 1182-1189 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 1182-1189
    • Hirohashi, N.1    Vacquier, V.D.2
  • 34
    • 0028181719 scopus 로고
    • 12 mouse sperm by the zona pellucida, the eggs extracellular matrix
    • 12 mouse sperm by the zona pellucida, the eggs extracellular matrix. J. Biol. Chem. 269, 13254-13258 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 13254-13258
    • Ward, C.R.1    Storey, B.T.2    Kopf, G.S.3
  • 35
    • 0030025691 scopus 로고    scopus 로고
    • Activation of mouse sperm phosphatidylinositol-4,5 bisphosphate-phospholipase C by zona pellucida is modulated by tyrosine phosphorylation
    • Tomes, C. N., McMaster, C. R. & Saling, P. M. Activation of mouse sperm phosphatidylinositol-4,5 bisphosphate-phospholipase C by zona pellucida is modulated by tyrosine phosphorylation. Mol. Reprod. Dev. 43, 196-204 (1996).
    • (1996) Mol. Reprod. Dev. , vol.43 , pp. 196-204
    • Tomes, C.N.1    McMaster, C.R.2    Saling, P.M.3
  • 36
    • 0035804913 scopus 로고    scopus 로고
    • Requirement of phospholipase Cδ4 for the zona pellucida-induced acrosome reaction
    • Fukami, K. et al. Requirement of phospholipase Cδ4 for the zona pellucida-induced acrosome reaction. Science 292, 920-923 (2001).
    • (2001) Science , vol.292 , pp. 920-923
    • Fukami, K.1
  • 37
    • 0028650360 scopus 로고
    • Exocytosis in spermatozoa in response to progesterone and zona pellucida
    • Roldan, E. R. S., Murase, T. & Shi, Q.-X. Exocytosis in spermatozoa in response to progesterone and zona pellucida. Science 266, 1578-1581 (1994).
    • (1994) Science , vol.266 , pp. 1578-1581
    • Roldan, E.R.S.1    Murase, T.2    Shi, Q.-X.3
  • 38
    • 0024366051 scopus 로고
    • An adhesion-associated agonist from the zona pellucida activates G protein-promoted elevations of internal Ca and pH that mediate mammalian sperm acrosomal exocytosis
    • Florman, H. M., Tombes, R. M., First, N. L. & Babcock, D. F. An adhesion-associated agonist from the zona pellucida activates G protein-promoted elevations of internal Ca and pH that mediate mammalian sperm acrosomal exocytosis. Dev. Biol. 135, 133-146 (1989).
    • (1989) Dev. Biol. , vol.135 , pp. 133-146
    • Florman, H.M.1    Tombes, R.M.2    First, N.L.3    Babcock, D.F.4
  • 39
    • 0029775791 scopus 로고    scopus 로고
    • ZP3-dependent activation of sperm cation channels regulates acrosomal secretion during mammalian fertilization
    • Arnoult, C., Zeng, Y., & Florman, H. M. ZP3-dependent activation of sperm cation channels regulates acrosomal secretion during mammalian fertilization. J. Cell Biol. 134, 637-645 (1996).
    • (1996) J. Cell Biol. , vol.134 , pp. 637-645
    • Arnoult, C.1    Zeng, Y.2    Florman, H.M.3
  • 40
    • 0028136068 scopus 로고
    • 2+ are initiated by the zona pellucida during acrosomal exocytosis
    • 2+ are initiated by the zona pellucida during acrosomal exocytosis. Dev. Biol. 165, 152-164 (1994).
    • (1994) Dev. Biol. , vol.165 , pp. 152-164
    • Florman, H.M.1
  • 41
    • 0036080482 scopus 로고    scopus 로고
    • TRP channel proteins and signal transduction
    • Minke, B. & Cook, B. TRP Channel Proteins and Signal Transduction. Physiol. Rev. 82, 429-472 (2002).
    • (2002) Physiol. Rev. , vol.82 , pp. 429-472
    • Minke, B.1    Cook, B.2
  • 42
    • 0032486352 scopus 로고    scopus 로고
    • Structure and mRNA expression of a bovine trp homologue related to mammalian trp2 transcripts
    • Wissenbach, U., Schroth, G., Phillipp, S. & Flockerzi, V. Structure and mRNA expression of a bovine trp homologue related to mammalian trp2 transcripts. FEBS Lett. 429, 61-66 (1998).
    • (1998) FEBS Lett. , vol.429 , pp. 61-66
    • Wissenbach, U.1    Schroth, G.2    Phillipp, S.3    Flockerzi, V.4
  • 44
    • 0035976822 scopus 로고    scopus 로고
    • Identification of mouse trp homologs and lipid rafts from spermatogenic cells and sperm
    • Trevino, C. L., Serrano, C. J., Beltran, C., Felix, R. & Darszon, A. Identification of mouse trp homologs and lipid rafts from spermatogenic cells and sperm. FEBS Lett. 509, 119-125 (2001).
    • (2001) FEBS Lett. , vol.509 , pp. 119-125
    • Trevino, C.L.1    Serrano, C.J.2    Beltran, C.3    Felix, R.4    Darszon, A.5
  • 45
    • 0029125139 scopus 로고
    • Inositol 1,4,5-trisphosphate receptors selectively localized to the acrosomes of mammalian sperm
    • Walensky, L. D. & Snyder, S. H. Inositol 1,4,5-trisphosphate receptors selectively localized to the acrosomes of mammalian sperm. J. Cell Biol. 130, 857-869 (1995).
    • (1995) J. Cell Biol. , vol.130 , pp. 857-869
    • Walensky, L.D.1    Snyder, S.H.2
  • 46
    • 0028865529 scopus 로고
    • TRPC1, a human homolog of a Drosophila store-operated channel
    • Wes, P. D. et al. TRPC1, a human homolog of a Drosophila store-operated channel. Proc. Natl Acad. Sci. USA 92, 9652-9656 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9652-9656
    • Wes, P.D.1
  • 48
    • 0036136446 scopus 로고    scopus 로고
    • Synaptotagmin VIII Is localized to the mouse sperm head and may function in acrosomal exocytosis
    • Hutt, D. M., Cardullo, R. A., Baltz, I. M. & Kgsee, J. K. Synaptotagmin VIII Is localized to the mouse sperm head and may function in acrosomal exocytosis. Biol. Reprod. 66, 50-56 (2002).
    • (2002) Biol. Reprod. , vol.66 , pp. 50-56
    • Hutt, D.M.1    Cardullo, R.A.2    Baltz, I.M.3    Kgsee, J.K.4
  • 49
    • 0031281655 scopus 로고    scopus 로고
    • The exocytosis regulatory proteins syntaxin and VAMP are shed from sea urchin sperm during the acrosome reaction
    • Schulz, J. R., Wessel, G. M. & Vacquier, V. D. The exocytosis regulatory proteins syntaxin and VAMP are shed from sea urchin sperm during the acrosome reaction. Dev. Biol. 191, 80-87 (1997).
    • (1997) Dev. Biol. , vol.191 , pp. 80-87
    • Schulz, J.R.1    Wessel, G.M.2    Vacquier, V.D.3
  • 50
    • 0034730154 scopus 로고    scopus 로고
    • Calcium-triggered acrosomal exocytosis in human spermatozoa requires the coordinated activation of Rab3A and N-ethylmaleimide-sensitive factor
    • Michaut, M., Tomes. C. N., De Blas, G., Yunes, R. & Mayorga, L. S. Calcium-triggered acrosomal exocytosis in human spermatozoa requires the coordinated activation of Rab3A and N-ethylmaleimide-sensitive factor. Proc. Natl Acad. Sci. USA 97, 9996-10001 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9996-10001
    • Michaut, M.1    Tomes, C.N.2    De Blas, G.3    Yunes, R.4    Mayorga, L.S.5
  • 51
    • 0023026714 scopus 로고
    • Development of ability to penetrate the cumulus oophorus by hamster spermatozoa capacitated in vitro, in relation to the timing of the acrosome reaction
    • Cummins, J. M. & Yanagimachi, R. Development of ability to penetrate the cumulus oophorus by hamster spermatozoa capacitated in vitro, in relation to the timing of the acrosome reaction. Gamete Res. 15, 187-212 (1986).
    • (1986) Gamete Res. , vol.15 , pp. 187-212
    • Cummins, J.M.1    Yanagimachi, R.2
  • 52
    • 0033555056 scopus 로고    scopus 로고
    • Sperm disintegrins, egg integrins, and other cell adhesion molecules of mammalian gamete plasma membrane interactions
    • Evans, J. P. Sperm disintegrins, egg integrins, and other cell adhesion molecules of mammalian gamete plasma membrane interactions. Front. Biosci. 4, D114-D131 (1999).
    • (1999) Front. Biosci. , vol.4
    • Evans, J.P.1
  • 53
    • 0035673219 scopus 로고    scopus 로고
    • Molecular mechanisms involved in mammalian gamete fusion
    • Cuasnicu, P. S. et al. Molecular mechanisms involved in mammalian gamete fusion. Arch. Med. Res. 32, 634-618 (2001).
    • (2001) Arch. Med. Res. , vol.32 , pp. 614-618
    • Cuasnicu, P.S.1
  • 54
    • 0032544623 scopus 로고    scopus 로고
    • Fertilization defects in sperm from mice lacking fertilin β
    • Cho, C. et al. Fertilization defects in sperm from mice lacking fertilin β. Science 281, 1857-1859 (1998).
    • (1998) Science , vol.281 , pp. 1857-1859
    • Cho, C.1
  • 55
    • 0035337709 scopus 로고    scopus 로고
    • Analysis of loss of adhesive function in sperm lacking cyritestin or fertilin β
    • Nishimura, H., Cho, C., Branciforte, D. R., Myles, D. G. & Primakoff, P. Analysis of loss of adhesive function in sperm lacking cyritestin or fertilin β. Dev. Biol. 233, 204-213 (2001).
    • (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
  • 56
    • 0034677883 scopus 로고    scopus 로고
    • Identification of key functional amino acids of the mouse fertilin β (ADAM2) disintegrin loop for cell-cell adhesion during fertilization
    • Zhu, X., Bansal, N. P. & Evans, J. P. Identification of key functional amino acids of the mouse fertilin β (ADAM2) disintegrin loop for cell-cell adhesion during fertilization. J. Biol. Chem. 275, 7677-7683 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 7677-7683
    • Zhu, X.1    Bansal, N.P.2    Evans, J.P.3
  • 57
    • 0034697006 scopus 로고    scopus 로고
    • κ integrin subunit
    • κ integrin subunit. J. Biol. Chem. 275, 11576-11584 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 11576-11584
    • Bigler, D.1
  • 59
    • 13044252869 scopus 로고    scopus 로고
    • 1: Implications for murine fertilization
    • 1: implications for murine fertilization. Proc. Natl Acad. Sci. USA 96, 11830-11835 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11830-11835
    • Chen, M.S.1
  • 60
    • 0029047919 scopus 로고
    • 1 functions as a sperm receptor
    • 1 functions as a sperm receptor. Cell 81, 1095-1104 (1995).
    • (1995) Cell , vol.81 , pp. 1095-1104
    • Almeida, E.A.1
  • 61
    • 0032782655 scopus 로고    scopus 로고
    • 1 integrin is the receptor for sperm fertilin β
    • 1 integrin is the receptor for sperm fertilin β. Chem. Biol. 6, 1-10 (1999).
    • (1999) Chem. Biol. , vol.6 , pp. 1-10
    • Chen, H.1    Sampson, N.S.2
  • 63
    • 0034914182 scopus 로고    scopus 로고
    • Fertilin β other ADAMs as integrin ligands: Insights into cell adhesion and fertilization
    • Evans, J. P. Fertilin β and other ADAMs as integrin ligands: insights into cell adhesion and fertilization. BioEssays 23, 628-639 (2001).
    • (2001) BioEssays , vol.23 , pp. 628-639
    • Evans, J.P.1
  • 64
    • 0036197618 scopus 로고    scopus 로고
    • 9 integrins, and CD9 in the interaction of the fertilin β (ADAM2) disintegrin domain with the mouse egg membrane
    • 9 integrins, and CD9 in the interaction of the fertilin β (ADAM2) disintegrin domain with the mouse egg membrane. Biol. Reprod. 66, 1193-1202 (2002).
    • (2002) Biol. Reprod. , vol.66 , pp. 1193-1202
    • Zhu, X.1    Evans, J.P.2
  • 65
    • 0037124066 scopus 로고    scopus 로고
    • 1. Implications for sperm-egg binding and other cell interactions
    • 1. Implications for sperm-egg binding and other cell interactions. J. Biol. Chem. 277, 17804-17810 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 17804-17810
    • Eto, K.1
  • 67
    • 0033958932 scopus 로고    scopus 로고
    • Requirement of CD9 on the egg plasma membrane for fertilization
    • Miyado, K. et al. Requirement of CD9 on the egg plasma membrane for fertilization. Science 287, 321-324 (2000).
    • (2000) Science , vol.287 , pp. 321-324
    • Miyado, K.1
  • 68
    • 0034091646 scopus 로고    scopus 로고
    • The gamete fusion process is defective in eggs of CD9-defective mice
    • Kaji, K. et al. The gamete fusion process is defective in eggs of CD9-defective mice. Nature Genet. 24, 279-282 (2000).
    • (2000) Nature Genet. , vol.24 , pp. 279-282
    • Kaji, K.1
  • 69
    • 0036333987 scopus 로고    scopus 로고
    • Residues SFQ (173-175) in the large extracellular loop of CD 9 are required for gamete fusion
    • Zhu, G. Z. et al. Residues SFQ (173-175) in the large extracellular loop of CD9 are required for gamete fusion. Development 129, 1995-2002 (2002).
    • (2002) Development , vol.129 , pp. 1995-2002
    • Zhu, G.Z.1
  • 70
    • 0035816640 scopus 로고    scopus 로고
    • Analysis of fertilin α (ADAM1)-mediated sperm-egg cell adhesion during fertilization and identification of an adhesion-mediating sequence in the disintegrin-like domain
    • Wong, G. E., Zhu, X., Prater, C. E., Oh, E. & Evans, J. P. Analysis of fertilin α (ADAM1)-mediated sperm-egg cell adhesion during fertilization and identification of an adhesion-mediating sequence in the disintegrin-like domain. J. Biol. Chem. 276, 24937-24945 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 24937-24945
    • Wong, G.E.1    Zhu, X.2    Prater, C.E.3    Oh, E.4    Evans, J.P.5
  • 71
    • 0035945363 scopus 로고    scopus 로고
    • Specific tetraspanin functions
    • Hemler, M. E. Specific tetraspanin functions. J. Cell Biol. 155, 1103-1107 (2001).
    • (2001) J. Cell Biol. , vol.155 , pp. 1103-1107
    • Hemler, M.E.1
  • 73
    • 0026510747 scopus 로고
    • A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion
    • Blobel, C. P. et al. A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature 356, 248-252 (1992).
    • (1992) Nature , vol.356 , pp. 248-252
    • Blobel, C.P.1
  • 74
    • 0032710099 scopus 로고    scopus 로고
    • Male mice deficient for germ-cell cyritestin are infertile
    • Shamsadin, R. et al. Male mice deficient for germ-cell cyritestin are infertile. Biol. Reprod. 61, 1445-1451 (1999).
    • (1999) Biol. Reprod. , vol.61 , pp. 1445-1451
    • Shamsadin, R.1
  • 75
    • 0032479148 scopus 로고    scopus 로고
    • Membrane fusion is induced by a distinct peptide sequence of the sea urchin fertilization protein binding
    • Ulrich, A. S., Otter, M., Glabe, C. G. & Hoekstra, D. Membrane fusion is induced by a distinct peptide sequence of the sea urchin fertilization pmtein bindin. J. Biol. Chem. 273, 16748-16755 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 16748-16755
    • Ulrich, A.S.1    Otter, M.2    Glabe, C.G.3    Hoekstra, D.4
  • 76
    • 0035826618 scopus 로고    scopus 로고
    • The crystal structure of a fusagenic sperm protein reveals extreme surface properties
    • Kresge, N., Vacquier, V. D. & Stout, C. D. The crystal structure of a fusagenic sperm protein reveals extreme surface properties. Biochemistry 40, 3407-5413 (2001).
    • (2001) Biochemistry , vol.40 , pp. 3407-5413
    • Kresge, N.1    Vacquier, V.D.2    Stout, C.D.3
  • 77
    • 0037092883 scopus 로고    scopus 로고
    • Egg activation at fertilization: Where it all begins
    • Runft, L. L., Jaffe, L. A. & Mehlmann, L. M. Egg activation at fertilization: where it all begins. Dev. Biol. 245, 237-254 (2002).
    • (2002) Dev. Biol. , vol.245 , pp. 237-254
    • Runft, L.L.1    Jaffe, L.A.2    Mehlmann, L.M.3
  • 78
    • 0033566185 scopus 로고    scopus 로고
    • Comparative biology of calcium signaling during fertilization and egg activation in animals
    • Stricker, S. A. Comparative biology of calcium signaling during fertilization and egg activation in animals. Dev. Biol. 211, 157-176 (1999).
    • (1999) Dev. Biol. , vol.211 , pp. 157-176
    • Stricker, S.A.1
  • 80
    • 0028795988 scopus 로고
    • Molecular basis of mammalian egg activation
    • Schultz, R. M. & Kopf, G. S. Molecular basis of mammalian egg activation. Curr. Top. Dev. Biol. 30, 21-62 (1995).
    • (1995) Curr. Top. Dev. Biol. , vol.30 , pp. 21-62
    • Schultz, R.M.1    Kopf, G.S.2
  • 81
    • 0026551829 scopus 로고
    • Repetitive calcium transients and the role of calcium in exocytosis and cell cycle activation in the mouse egg
    • Kline, D. & Kline, J. T. Repetitive calcium transients and the role of calcium in exocytosis and cell cycle activation in the mouse egg. Dev. Biol. 145, 80-89 (1992).
    • (1992) Dev. Biol. , vol.145 , pp. 80-89
    • Kline, D.1    Kline, J.T.2
  • 82
    • 0033120172 scopus 로고    scopus 로고
    • Evidence that a starfish egg Src family tyrosine kinase associates with PLC-γ 1 SH2 domains at fertilization
    • Giusti, A. F., Carroll, D. J., Abassi, Y. A. & Foltz, K. R. Evidence that a starfish egg Src family tyrosine kinase associates with PLC-γ1 SH2 domains at fertilization. Dev. Biol. 208, 189-199 (1999).
    • (1999) Dev. Biol. , vol.208 , pp. 189-199
    • Giusti, A.F.1    Carroll, D.J.2    Abassi, Y.A.3    Foltz, K.R.4
  • 83
    • 0032828091 scopus 로고    scopus 로고
    • Requirement of a Src family kinase for initiating calcium release at fertilization in starfish eggs
    • Giusti, A. F. et al. Requirement of a Src family kinase for initiating calcium release at fertilization in starfish eggs. J. Biol. Chem. 274, 29318-29322 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 29318-29322
    • Giusti, A.F.1
  • 84
    • 0034595629 scopus 로고    scopus 로고
    • Evidence that fertilization activates starfish eggs by sequential activation of a Src-like kinase and phospholipase Gγ
    • Giusti, A. F., Xu, W., Hinkle, B., Terasaki, M. & Jaffe, L. A. Evidence that fertilization activates starfish eggs by sequential activation of a Src-like kinase and phospholipase Gγ. J. Biol. Chem. 275, 16788-16794 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 16788-16794
    • Giusti, A.F.1    Xu, W.2    Hinkle, B.3    Terasaki, M.4    Jaffe, L.A.5
  • 85
    • 0034284547 scopus 로고    scopus 로고
    • Role of the Fyn kinase in calcium release during fertilization of the sea urchin egg
    • Kinsey, W. H. & Shen, S. S. Role of the Fyn kinase in calcium release during fertilization of the sea urchin egg. Dev. Biol. 225, 253-264 (2000).
    • (2000) Dev. Biol. , vol.225 , pp. 253-264
    • Kinsey, W.H.1    Shen, S.S.2
  • 86
    • 0033845362 scopus 로고    scopus 로고
    • 2+ release by the same pathway as fertilization
    • 2+ release by the same pathway as fertilization. Development 127, 3227-3236 (2000).
    • (2000) Development , vol.127 , pp. 3227-3236
    • Runft, L.L.1    Jaffe, L.A.2
  • 87
    • 0030881256 scopus 로고    scopus 로고
    • Calcium release at fertilization in starfish eggs is mediated by phospholipase Cγ
    • Carroll, D. J. et al. Calcium release at fertilization in starfish eggs is mediated by phospholipase Cγ. J. Cell Biol. 138, 1303-1311 (1.997).
    • (1997) J. Cell Biol. , vol.138 , pp. 1303-1311
    • Carroll, D.J.1
  • 88
    • 0033556702 scopus 로고    scopus 로고
    • Identification of PLCγ-dependent and -independent events during fertilization of sea urchin eggs
    • Carroll, D. J., Albay, D. T., Terasaki, M., Jaffe, L. A. & Foltz, K. R. Identification of PLCγ-dependent and -independent events during fertilization of sea urchin eggs. Dev. Biol. 206, 232-247 (1999).
    • (1999) Dev. Biol. , vol.206 , pp. 232-247
    • Carroll, D.J.1    Albay, D.T.2    Terasaki, M.3    Jaffe, L.A.4    Foltz, K.R.5
  • 91
    • 0028138752 scopus 로고
    • Roles of heterotrimeric and monomeric G proteins in sperm-induced activation of mouse eggs
    • L. Moore, G. D., Ayabe, T., Visconti, P. E., Schultz, R. M. & Kopf, G. S. Roles of heterotrimeric and monomeric G proteins in sperm-induced activation of mouse eggs. Development 120, 3313-3323 (1994).
    • (1994) Development , vol.120 , pp. 3313-3323
    • Moore, G.D.1    Ayabe, T.2    Visconti, P.E.3    Schultz, R.M.4    Kopf, G.S.5
  • 93
    • 0034072254 scopus 로고    scopus 로고
    • Ability of integrins to mediate fertilization, intracellular calcium release, and parthenogenetic development in bovine oocytes
    • Campbell, K. D., Reed, W. A. & White, K. L. Ability of integrins to mediate fertilization, intracellular calcium release, and parthenogenetic development in bovine oocytes. Biol. Reprod. 62, 1702-1709 (2000).
    • (2000) Biol. Reprod. , vol.62 , pp. 1702-1709
    • Campbell, K.D.1    Reed, W.A.2    White, K.L.3
  • 95
    • 0032189151 scopus 로고    scopus 로고
    • Voltage-dependent activation of frog eggs by a sperm surface disintegrin peptide
    • Shilling, F. M., Magie, C. R. & Nuccitelli, R. Voltage-dependent activation of frog eggs by a sperm surface disintegrin peptide. Dev. Biol. 202, 113-124 (1998).
    • (1998) Dev. Biol. , vol.202 , pp. 113-124
    • Shilling, F.M.1    Magie, C.R.2    Nuccitelli, R.3
  • 96
    • 0033200368 scopus 로고    scopus 로고
    • In vitro fertilization by intracytoplasmic sperm injection
    • Tesarik, J. & Mendoza, C. In vitro fertilization by intracytoplasmic sperm injection. BioEssay 21, 791-801 (1999).
    • (1999) BioEssay , vol.21 , pp. 791-801
    • Tesarik, J.1    Mendoza, C.2
  • 97
    • 0029787662 scopus 로고    scopus 로고
    • Fertilization and development of mouse oocytes injected with isolated sperm heads
    • Kuretake, S., Kimura, Y., Hoshi, K. & Yanagimachi, R. Fertilization and development of mouse oocytes injected with isolated sperm heads. Biol. Reprod. 55, 789-795 (1996).
    • (1996) Biol. Reprod. , vol.55 , pp. 789-795
    • Kuretake, S.1    Kimura, Y.2    Hoshi, K.3    Yanagimachi, R.4
  • 98
    • 0031811231 scopus 로고    scopus 로고
    • Analysis of mouse oocyte activation suggests the involvement of sperm perinuclear material
    • Kimura, Y. et al. Analysis of mouse oocyte activation suggests the involvement of sperm perinuclear material. Biol. Reprod. 58, 1407-1415 (1998).
    • (1998) Biol. Reprod. , vol.58 , pp. 1407-1415
    • Kimura, Y.1
  • 99
    • 0030035074 scopus 로고    scopus 로고
    • Calcium oscillations in mammalian eggs triggered by a soluble sperm protein
    • Parrington, J., Swann, K., Sheychenko, V. I., Sesay, A. K. & Lai, F. A. Calcium oscillations in mammalian eggs triggered by a soluble sperm protein. Nature 379, 364-368 (1996).
    • (1996) Nature , vol.379 , pp. 364-368
    • Parrington, J.1    Swann, K.2    Sheychenko, V.I.3    Sesay, A.K.4    Lai, F.A.5
  • 100
    • 0032563387 scopus 로고    scopus 로고
    • Involvement of phospholipase Cγ1 in mouse egg activation induced by a truncated form of the C-kit tyrosine kinase present in spermatozoa
    • Sette, C., Bevilacqua, A., Geremia, R., & Rossi, P. Involvement of phospholipase Cγ1 in mouse egg activation induced by a truncated form of the C-kit tyrosine kinase present in spermatozoa. J. Cell Biol. 142, 1063-1074 (1998).
    • (1998) J. Cell Biol. , vol.142 , pp. 1063-1074
    • Sette, C.1    Bevilacqua, A.2    Geremia, R.3    Rossi, P.4
  • 101
    • 0031965267 scopus 로고    scopus 로고
    • Molecularly cloned mammalian glucosamine-6-phosphate deaminase localizes to transporting epithelium and lacks oscillin activity
    • Wolosker, H. et al. Molecularly cloned mammalian glucosamine-6-phosphate deaminase localizes to transporting epithelium and lacks oscillin activity. FASEB J. 12, 91-99 (1998).
    • (1998) FASEB J. , vol.12 , pp. 91-99
    • Wolosker, H.1
  • 102
    • 0032930398 scopus 로고    scopus 로고
    • Human glucosamine-6-phosphate isomerase, a homologue of hamster oscillin, does not appear to be involved in Ca2+ release in mammalian oocytes
    • Wolny, Y. M. et al. Human glucosamine-6-phosphate isomerase, a homologue of hamster oscillin, does not appear to be involved in Ca2+ release in mammalian oocytes. Mol. Reprod. Dev. 52, 277-287 (1999).
    • (1999) Mol. Reprod. Dev. , vol.52 , pp. 277-287
    • Wolny, Y.M.1
  • 103
    • 0034632895 scopus 로고    scopus 로고
    • NO is necessary and sufficient for egg activation at fertilization
    • Kuo, R. C. et al. NO is necessary and sufficient for egg activation at fertilization. Nature 406, 633-636 (2000).
    • (2000) Nature , vol.406 , pp. 633-636
    • Kuo, R.C.1
  • 104
    • 0035371449 scopus 로고    scopus 로고
    • Simultaneous measurement of intracellular nitric oxide and free calcium levels in chordate eggs demonstrates that nitric oxide has no role at fertilization
    • Hyslop, L. A., Carroll, M., Nixon, V. L., McDougall, A. & Jones, K. T. Simultaneous measurement of intracellular nitric oxide and free calcium levels in chordate eggs demonstrates that nitric oxide has no role at fertilization. Dev. Biol. 234, 216-230 (2001).
    • (2001) Dev. Biol. , vol.234 , pp. 216-230
    • Hyslop, L.A.1    Carroll, M.2    Nixon, V.L.3    McDougall, A.4    Jones, K.T.5
  • 105
    • 0034554750 scopus 로고    scopus 로고
    • 2+-sensitive phospholipase C activity that can generate InsP(3) from PIP(2) associated with intracellular organelles
    • 2+-sensitive phospholipase C activity that can generate InsP(3) from PIP(2) associated with intracellular organelles. Dev. Biol. 228, 125-135 (2000).
    • (2000) Dev. Biol. , vol.228 , pp. 125-135
    • Rice, A.1    Parrington, J.2    Jones, K.T.3    Swann, K.4
  • 106
    • 0034662838 scopus 로고    scopus 로고
    • Activation of mouse oocytes requires multiple sperm factors but not sperm PLCγ 1
    • Heyers, S. et al. Activation of mouse oocytes requires multiple sperm factors but not sperm PLCγ1. Mol. Cell Endocrinol. 166, 51-57 (2000).
    • (2000) Mol. Cell Endocrinol. , vol.166 , pp. 51-57
    • Heyers, S.1
  • 107
    • 0035041688 scopus 로고    scopus 로고
    • Sperm factor induces intracellular free calcium oscillations by stimulating the phosphoinositide pathway
    • Wu, H. et al. Sperm factor induces intracellular free calcium oscillations by stimulating the phosphoinositide pathway. Biol. Reprod. 64, 1338-1349 (2001).
    • (2001) Biol. Reprod. , vol.64 , pp. 1338-1349
    • Wu, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.