메뉴 건너뛰기




Volumn 202, Issue 1, 1998, Pages 113-124

Voltage-dependent activation of frog eggs by a sperm surface disintegrin peptide

Author keywords

Disintegrin; Egg activation; Fertilization; Frog; Integrin

Indexed keywords

DISINTEGRIN; INTEGRIN;

EID: 0032189151     PISSN: 00121606     EISSN: None     Source Type: Journal    
DOI: 10.1006/dbio.1998.8982     Document Type: Article
Times cited : (54)

References (53)
  • 1
    • 0026350087 scopus 로고
    • Solution structure of kistrin, a potent platelet aggregation inhibitor and GP IIb-IIIa antagonist
    • Adler M., Lazarus R. A., Dennis M. S., Wagner G. Solution structure of kistrin, a potent platelet aggregation inhibitor and GP IIb-IIIa antagonist. Science. 253:1991;445-448.
    • (1991) Science , vol.253 , pp. 445-448
    • Adler, M.1    Lazarus, R.A.2    Dennis, M.S.3    Wagner, G.4
  • 2
    • 0028983956 scopus 로고
    • Integrin alpha v subunit is expressed on mesodermal cell surfaces during amphibian gastrulation
    • Alfandari D., Whittaker C. A., DeSimone D. W., Darribere T. Integrin alpha v subunit is expressed on mesodermal cell surfaces during amphibian gastrulation. Dev. Biol. 170:1995;249-261.
    • (1995) Dev. Biol. , vol.170 , pp. 249-261
    • Alfandari, D.1    Whittaker, C.A.2    DeSimone, D.W.3    Darribere, T.4
  • 5
    • 0030986652 scopus 로고    scopus 로고
    • A model for sperm-egg binding and fusion based on ADAMS and integrins
    • Bigler D., Chen M., Waters S., White J. M. A model for sperm-egg binding and fusion based on ADAMS and integrins. Trends Cell. Biol. 7:1997;220-225.
    • (1997) Trends Cell. Biol. , vol.7 , pp. 220-225
    • Bigler, D.1    Chen, M.2    Waters, S.3    White, J.M.4
  • 6
    • 0025371355 scopus 로고
    • Proteolytic processing of a protein involved in sperm-egg fusion correlates with acquisition of fertilization competence
    • Blobel C. P., Myles D. G., Primakoff P., White J. M. Proteolytic processing of a protein involved in sperm-egg fusion correlates with acquisition of fertilization competence. J. Cell Biol. 111:1990;69-78.
    • (1990) J. Cell Biol. , vol.111 , pp. 69-78
    • Blobel, C.P.1    Myles, D.G.2    Primakoff, P.3    White, J.M.4
  • 7
    • 0026510747 scopus 로고
    • A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion
    • Blobel C. P., Wolfsberg T. G., Turck C. W., Myles D. G., Primakoff P., White J. M. A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature. 356:1992;248-252.
    • (1992) Nature , vol.356 , pp. 248-252
    • Blobel, C.P.1    Wolfsberg, T.G.2    Turck, C.W.3    Myles, D.G.4    Primakoff, P.5    White, J.M.6
  • 8
    • 0030891962 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of transmembrane ligands for Eph receptors
    • Bruckner K., Pasquale E. B., Klein R. Tyrosine phosphorylation of transmembrane ligands for Eph receptors. Science. 275:1997;1640-1643.
    • (1997) Science , vol.275 , pp. 1640-1643
    • Bruckner, K.1    Pasquale, E.B.2    Klein, R.3
  • 9
    • 0018821079 scopus 로고
    • A fast block to polyspermy in frogs is mediated by changes in the membrane potential
    • Cross N. L., Elinson R. P. A fast block to polyspermy in frogs is mediated by changes in the membrane potential. Dev. Biol. 75:1980;187-198.
    • (1980) Dev. Biol. , vol.75 , pp. 187-198
    • Cross, N.L.1    Elinson, R.P.2
  • 10
    • 0027483111 scopus 로고
    • Extracellular matrix-stimulated phospholipase activation is mediated by beta 1-integrin
    • Cybulsky A. V., Carbonetto S., Cyr M. D., McTavish A. J., Huang Q. Extracellular matrix-stimulated phospholipase activation is mediated by beta 1-integrin. Am. J. Physiol. 264:1993;C323-C332.
    • (1993) Am. J. Physiol. , vol.264
    • Cybulsky, A.V.1    Carbonetto, S.2    Cyr, M.D.3    McTavish, A.J.4    Huang, Q.5
  • 11
    • 0028077510 scopus 로고
    • Ligand and cation binding are dual functions of a discrete segment of the integrin beta 3 subunit: Cation displacement is involved in ligand binding
    • D'Souza S. E., Haas T. A., Piotrowicz R. S., Byers-Ward V., McGrath D. E., Soule H. R., Cierniewski C., Plow E. F., Smith J. W. Ligand and cation binding are dual functions of a discrete segment of the integrin beta 3 subunit: Cation displacement is involved in ligand binding. Cell. 79:1994;659-667.
    • (1994) Cell , vol.79 , pp. 659-667
    • D'Souza, S.E.1    Haas, T.A.2    Piotrowicz, R.S.3    Byers-Ward, V.4    McGrath, D.E.5    Soule, H.R.6    Cierniewski, C.7    Plow, E.F.8    Smith, J.W.9
  • 12
    • 0030078904 scopus 로고    scopus 로고
    • Characterisation and role of integrins during gametic interaction and egg activation
    • de Nadai C., Fenichel P., Donzeau M., Epel D., Ciapa B. Characterisation and role of integrins during gametic interaction and egg activation. Zygote. 4:1996;31-40.
    • (1996) Zygote , vol.4 , pp. 31-40
    • De Nadai, C.1    Fenichel, P.2    Donzeau, M.3    Epel, D.4    Ciapa, B.5
  • 13
    • 0031193325 scopus 로고    scopus 로고
    • Characterization of the binding of recombinant mouse sperm fertilin beta subunit to mouse eggs: Evidence for adhesive activity via an egg beta 1 integrin-mediated interaction
    • Evans J. P., Kopf G. S., Schultz R. M. Characterization of the binding of recombinant mouse sperm fertilin beta subunit to mouse eggs: Evidence for adhesive activity via an egg beta 1 integrin-mediated interaction. Dev. Biol. 187:1997;79-93.
    • (1997) Dev. Biol. , vol.187 , pp. 79-93
    • Evans, J.P.1    Kopf, G.S.2    Schultz, R.M.3
  • 14
    • 0027185920 scopus 로고
    • The molecular basis of sea urchin gamete interactions at the egg plasma membrane
    • Foltz K. R., Lennarz W. J. The molecular basis of sea urchin gamete interactions at the egg plasma membrane. Dev. Biol. 158:1993;46-61.
    • (1993) Dev. Biol. , vol.158 , pp. 46-61
    • Foltz, K.R.1    Lennarz, W.J.2
  • 15
    • 0027416845 scopus 로고
    • Sea urchin egg receptor for sperm: Sequence similarity of binding domain and hsp70
    • Foltz K. R., Partin J. S., Lennarz W. J. Sea urchin egg receptor for sperm: Sequence similarity of binding domain and hsp70. Science. 259:1993;1421-1425.
    • (1993) Science , vol.259 , pp. 1421-1425
    • Foltz, K.R.1    Partin, J.S.2    Lennarz, W.J.3
  • 16
    • 0027691915 scopus 로고
    • Receptor-mediated signal transduction and egg activation
    • Foltz K. R., Shilling F. M. Receptor-mediated signal transduction and egg activation. Zygote. 1:1993;276-279.
    • (1993) Zygote , vol.1 , pp. 276-279
    • Foltz, K.R.1    Shilling, F.M.2
  • 17
    • 0028168553 scopus 로고
    • A beta 1-integrin associated alpha-chain is differentially expressed duringXenopus
    • Gawantka V., Joos T. O., Hausen P. A beta 1-integrin associated alpha-chain is differentially expressed duringXenopus. Mech. Dev. 47:1994;199-211.
    • (1994) Mech. Dev. , vol.47 , pp. 199-211
    • Gawantka, V.1    Joos, T.O.2    Hausen, P.3
  • 18
    • 0031127828 scopus 로고    scopus 로고
    • Surface localization of the sea urchin egg receptor for sperm
    • Giusti A. F., Hoang K. M., Foltz K. R. Surface localization of the sea urchin egg receptor for sperm. Dev. Biol. 184:1997;10-24.
    • (1997) Dev. Biol. , vol.184 , pp. 10-24
    • Giusti, A.F.1    Hoang, K.M.2    Foltz, K.R.3
  • 19
    • 0023104753 scopus 로고
    • Electrical responses of eggs to acrosomal protein similar to those induced by sperm
    • Gould M., Stephano J. L. Electrical responses of eggs to acrosomal protein similar to those induced by sperm. Science. 235:1987;1654-1656.
    • (1987) Science , vol.235 , pp. 1654-1656
    • Gould, M.1    Stephano, J.L.2
  • 20
    • 0025833241 scopus 로고
    • Peptides from sperm acrosomal protein that initiate egg development
    • Gould M. C., Stephano J. L. Peptides from sperm acrosomal protein that initiate egg development. Dev. Biol. 146:1991;509-518.
    • (1991) Dev. Biol. , vol.146 , pp. 509-518
    • Gould, M.C.1    Stephano, J.L.2
  • 21
    • 0031282203 scopus 로고    scopus 로고
    • Analysis of the process of localization of fertilin to the sperm posterior head plasma membrane domain during sperm maturation in the epididymis
    • Hunnicutt G. R., Koppel D. E., Myles D. G. Analysis of the process of localization of fertilin to the sperm posterior head plasma membrane domain during sperm maturation in the epididymis. Dev. Biol. 191:1997;146-159.
    • (1997) Dev. Biol. , vol.191 , pp. 146-159
    • Hunnicutt, G.R.1    Koppel, D.E.2    Myles, D.G.3
  • 23
    • 0024720301 scopus 로고
    • Evidence that the voltage-dependent component in the fertilization process is contributed by the sperm
    • Iwao Y., Jaffe L. A. Evidence that the voltage-dependent component in the fertilization process is contributed by the sperm. Dev. Biol. 134:1989;446-451.
    • (1989) Dev. Biol. , vol.134 , pp. 446-451
    • Iwao, Y.1    Jaffe, L.A.2
  • 24
    • 0025582545 scopus 로고
    • First messengers at fertilization
    • Jaffe L. A. First messengers at fertilization. J. Reprod. Fertil. 42:1990;107-116.
    • (1990) J. Reprod. Fertil. , vol.42 , pp. 107-116
    • Jaffe, L.A.1
  • 25
    • 0020807717 scopus 로고
    • Studies of the voltage-dependent polyspermy block using cross-species fertilization of amphibians
    • Jaffe L. A., Cross N. S., Picheral B. Studies of the voltage-dependent polyspermy block using cross-species fertilization of amphibians. Dev. Biol. 98:1983;319-326.
    • (1983) Dev. Biol. , vol.98 , pp. 319-326
    • Jaffe, L.A.1    Cross, N.S.2    Picheral, B.3
  • 26
    • 0020105712 scopus 로고
    • Studies of the mechanism of the electrical polyspermy block using voltage clamp during cross-species fertilization
    • Jaffe L. A., Gould-Somero M., Holland L. Z. Studies of the mechanism of the electrical polyspermy block using voltage clamp during cross-species fertilization. J. Cell Biol. 92:1982;616-621.
    • (1982) J. Cell Biol. , vol.92 , pp. 616-621
    • Jaffe, L.A.1    Gould-Somero, M.2    Holland, L.Z.3
  • 28
    • 0024294553 scopus 로고
    • Fertilization events induced by neurotransmitters after injection of mRNA inXenopus
    • Kline D., Simoncini L., Mandel G., Maue R. A., Kado R. T., Jaffe L. A. Fertilization events induced by neurotransmitters after injection of mRNA inXenopus. Science. 241:1988;464-467.
    • (1988) Science , vol.241 , pp. 464-467
    • Kline, D.1    Simoncini, L.2    Mandel, G.3    Maue, R.A.4    Kado, R.T.5    Jaffe, L.A.6
  • 30
    • 0031127431 scopus 로고    scopus 로고
    • Identification of a 97-kDa heat shock protein from S. franciscanusS. purpuratus
    • Mauk R., Jaworski D., Kamei N., Glabe C. G. Identification of a 97-kDa heat shock protein fromS. franciscanusS. purpuratus. Dev. Biol. 184:1997;31-37.
    • (1997) Dev. Biol. , vol.184 , pp. 31-37
    • Mauk, R.1    Jaworski, D.2    Kamei, N.3    Glabe, C.G.4
  • 31
    • 0027516985 scopus 로고
    • Species-specific inhibition of fertilization by a peptide derived from the sperm protein bindin
    • Minor J. E., Britten R. J., Davidson E. H. Species-specific inhibition of fertilization by a peptide derived from the sperm protein bindin. Mol. Biol. Cell. 4:1993;375-387.
    • (1993) Mol. Biol. Cell. , vol.4 , pp. 375-387
    • Minor, J.E.1    Britten, R.J.2    Davidson, E.H.3
  • 33
    • 0027360934 scopus 로고
    • Complete mouse egg activation in the absence of sperm by stimulation of an exogenous G protein-coupled receptor
    • Moore G. D., Kopf G. S., Schultz R. M. Complete mouse egg activation in the absence of sperm by stimulation of an exogenous G protein-coupled receptor. Dev. Biol. 159:1993;669-678.
    • (1993) Dev. Biol. , vol.159 , pp. 669-678
    • Moore, G.D.1    Kopf, G.S.2    Schultz, R.M.3
  • 34
    • 0028325475 scopus 로고
    • Identification of a binding site in the disintegrin domain of fertilin required for sperm-egg fusion
    • Myles D. G., Kimmel L. H., Blobel C. P., White J. M., Primakoff P. Identification of a binding site in the disintegrin domain of fertilin required for sperm-egg fusion. Proc. Natl. Acad. Sci. USA. 91:1994;4195-4198.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4195-4198
    • Myles, D.G.1    Kimmel, L.H.2    Blobel, C.P.3    White, J.M.4    Primakoff, P.5
  • 35
    • 0025741870 scopus 로고
    • Calcium signaling capacity of the CD11b/CD18 integrin on human neutrophils
    • Ng-Sikorski J., Andersson R., Patarroyo M., Andersson T. Calcium signaling capacity of the CD11b/CD18 integrin on human neutrophils. Exp. Cell Res. 195:1991;504-508.
    • (1991) Exp. Cell Res. , vol.195 , pp. 504-508
    • Ng-Sikorski, J.1    Andersson, R.2    Patarroyo, M.3    Andersson, T.4
  • 36
    • 0029314309 scopus 로고
    • The temperature dependence in the hydraulic conductivity, Lp, of the mouse sperm plasma membrane shows a discontinuity between 4 and 0 degrees C
    • Noiles E. E., Bailey J. L., Storey B. T. The temperature dependence in the hydraulic conductivity, Lp, of the mouse sperm plasma membrane shows a discontinuity between 4 and 0 degrees C. Cryobiology. 32:1995;220-238.
    • (1995) Cryobiology , vol.32 , pp. 220-238
    • Noiles, E.E.1    Bailey, J.L.2    Storey, B.T.3
  • 38
    • 0030035074 scopus 로고    scopus 로고
    • Calcium oscillations in mammalian eggs triggered by a soluble sperm protein
    • Parrington J., Swann K., Shevchenko V. I., Sesay A. K., Lai F. A. Calcium oscillations in mammalian eggs triggered by a soluble sperm protein. Nature. 379:1996;364-368.
    • (1996) Nature , vol.379 , pp. 364-368
    • Parrington, J.1    Swann, K.2    Shevchenko, V.I.3    Sesay, A.K.4    Lai, F.A.5
  • 39
    • 0029120428 scopus 로고
    • A peptide isolated from phage display libraries is a structural and functional mimic of an RGD-binding site on integrins
    • Pasqualini R., Koivunen E., Ruoslahti E. A peptide isolated from phage display libraries is a structural and functional mimic of an RGD-binding site on integrins. J. Cell Biol. 130:1995;1189-1196.
    • (1995) J. Cell Biol. , vol.130 , pp. 1189-1196
    • Pasqualini, R.1    Koivunen, E.2    Ruoslahti, E.3
  • 40
    • 0023100910 scopus 로고
    • Identification and purification of a sperm surface protein with a potential role in sperm-egg membrane fusion
    • Primakoff P., Hyatt H., Tredick-Kline J. Identification and purification of a sperm surface protein with a potential role in sperm-egg membrane fusion. J. Cell Biol. 104:1987;141-149.
    • (1987) J. Cell Biol. , vol.104 , pp. 141-149
    • Primakoff, P.1    Hyatt, H.2    Tredick-Kline, J.3
  • 41
    • 0015423506 scopus 로고
    • Fine structure of spermatogenesis in the South African clawed toadXenopus laevis
    • Reed S. C., Stanley H. P. Fine structure of spermatogenesis in the South African clawed toadXenopus laevis. J. Ultrastruct. Res. 41:1972;277-295.
    • (1972) J. Ultrastruct. Res. , vol.41 , pp. 277-295
    • Reed, S.C.1    Stanley, H.P.2
  • 42
    • 0029257377 scopus 로고
    • Signal transduction through integrins: A central role for focal adhesion kinase?
    • Richardson A., Parsons J. T. Signal transduction through integrins: A central role for focal adhesion kinase? BioEssays. 17:1995;229-236.
    • (1995) BioEssays , vol.17 , pp. 229-236
    • Richardson, A.1    Parsons, J.T.2
  • 43
    • 0032489348 scopus 로고    scopus 로고
    • Involvement of protein-tyrosine phosphorylation and dephosphorylation in sperm-inducedXenopus
    • Sato K., Iwasaki T., Tamaki I., Aoto M., Tokmakov A. A., Fukami Y. Involvement of protein-tyrosine phosphorylation and dephosphorylation in sperm-inducedXenopus. FEBS Lett. 424:1998;113-118.
    • (1998) FEBS Lett. , vol.424 , pp. 113-118
    • Sato, K.1    Iwasaki, T.2    Tamaki, I.3    Aoto, M.4    Tokmakov, A.A.5    Fukami, Y.6
  • 44
    • 0025786742 scopus 로고
    • Three-dimensional structure of echistatin, the smallest active RGD protein
    • Saudek V., Atkinson R. A., Pelton J. T. Three-dimensional structure of echistatin, the smallest active RGD protein. Biochemistry. 30:1991;7369-7372.
    • (1991) Biochemistry , vol.30 , pp. 7369-7372
    • Saudek, V.1    Atkinson, R.A.2    Pelton, J.T.3
  • 45
    • 0028176083 scopus 로고
    • Tyrosine phosphorylation of pp125FAK in platelets requires coordinated signaling through integrin and agonist receptors
    • Shattil S. J., Haimovich B., Cunningham M., Lipfert L., Parsons J. T., Ginsberg M. H., Brugge J. S. Tyrosine phosphorylation of pp125FAK in platelets requires coordinated signaling through integrin and agonist receptors. J. Biol. Chem. 269:1994;14738-14745.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14738-14745
    • Shattil, S.J.1    Haimovich, B.2    Cunningham, M.3    Lipfert, L.4    Parsons, J.T.5    Ginsberg, M.H.6    Brugge, J.S.7
  • 46
    • 0028212732 scopus 로고
    • Evidence for both tyrosine kinase and G-protein-coupled pathways leading to starfish egg activation
    • Shilling F. M., Carroll D. J., Muslin A. J., Escobedo J. A., Williams L. T., Jaffe L. A. Evidence for both tyrosine kinase and G-protein-coupled pathways leading to starfish egg activation. Dev. Biol. 162:1994;590-599.
    • (1994) Dev. Biol. , vol.162 , pp. 590-599
    • Shilling, F.M.1    Carroll, D.J.2    Muslin, A.J.3    Escobedo, J.A.4    Williams, L.T.5    Jaffe, L.A.6
  • 49
    • 0027373782 scopus 로고
    • Activation of protein kinase C precedes alpha 5 beta 1 integrin-mediated cell spreading on fibronectin
    • Vuori K., Ruoslahti E. Activation of protein kinase C precedes alpha 5 beta 1 integrin-mediated cell spreading on fibronectin. J. Biol. Chem. 268:1993;21459-21462.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21459-21462
    • Vuori, K.1    Ruoslahti, E.2
  • 50
    • 0028355410 scopus 로고
    • A family of cellular proteins related to snake venom disintegrins
    • Weskamp G., Blobel C. P. A family of cellular proteins related to snake venom disintegrins. Proc. Natl. Acad. Sci. USA. 91:1994;2748-2751.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2748-2751
    • Weskamp, G.1    Blobel, C.P.2
  • 51
    • 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., White J. M. ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain. Dev. Biol. 169:1995;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
  • 52
    • 0030589505 scopus 로고    scopus 로고
    • ADAMs in fertilization and development
    • Wolfsberg T. G., White J. M. ADAMs in fertilization and development. Dev. Biol. 180:1996;389-401.
    • (1996) Dev. Biol. , vol.180 , pp. 389-401
    • Wolfsberg, T.G.1    White, J.M.2
  • 53
    • 0028297766 scopus 로고
    • Highly polarized EGF receptor tyrosine kinase activity initiates egg activation inXenopus
    • Yim D. L., Opresko L. K., Wiley H. S., Nuccitelli R. Highly polarized EGF receptor tyrosine kinase activity initiates egg activation inXenopus. Dev. Biol. 162:1994;41-55.
    • (1994) Dev. Biol. , vol.162 , pp. 41-55
    • Yim, D.L.1    Opresko, L.K.2    Wiley, H.S.3    Nuccitelli, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.