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Volumn 75, Issue 4, 2008, Pages 641-649

A novel approach to identify bovine sperm membrane proteins that interact with receptors on the vitelline membrane of bovine oocytes

Author keywords

Activation; Bovine; Integrin; Ligand; Oocyte; Receptor

Indexed keywords

MEMBRANE PROTEIN;

EID: 40049091590     PISSN: 1040452X     EISSN: 10982795     Source Type: Journal    
DOI: 10.1002/mrd.20805     Document Type: Article
Times cited : (5)

References (54)
  • 1
    • 0027937402 scopus 로고
    • Tyrosine phosphorylation of the egg receptor for sperm at fertilization
    • Abassi YA, Foltz KR. 1994. Tyrosine phosphorylation of the egg receptor for sperm at fertilization. Dev Biol 164:430-443.
    • (1994) Dev Biol , vol.164 , pp. 430-443
    • Abassi, Y.A.1    Foltz, K.R.2
  • 3
    • 0032506002 scopus 로고    scopus 로고
    • Involvement of focal adhesion kinase in invasin-mediated uptake
    • Alrutz MA, Isberg RR. 1998. Involvement of focal adhesion kinase in invasin-mediated uptake. Proc Natl Acad Sci U S A 95:13658-13663.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 13658-13663
    • Alrutz, M.A.1    Isberg, R.R.2
  • 4
    • 0024219844 scopus 로고
    • Cytosolic calcium oscillators
    • Berridge MJ, Galione A. 1988. Cytosolic calcium oscillators. Faseb J 2:3074-3082.
    • (1988) Faseb J , vol.2 , pp. 3074-3082
    • Berridge, M.J.1    Galione, A.2
  • 5
    • 0026510747 scopus 로고
    • A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion
    • Blobel CP, Wolfsberg TG, Turck CW, Myles DG, Primakoff P, White JM. 1992. A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature 356:248-252.
    • (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
  • 6
    • 0025650560 scopus 로고
    • Evidence that an Arg-Gly-Asp adhesion sequence plays a role in mammalian fertilization
    • Bronson RA, Fusi F. 1990. Evidence that an Arg-Gly-Asp adhesion sequence plays a role in mammalian fertilization. Biol Reprod 43:1019-1025.
    • (1990) Biol Reprod , vol.43 , pp. 1019-1025
    • Bronson, R.A.1    Fusi, F.2
  • 7
    • 0032956726 scopus 로고    scopus 로고
    • An investigation of the latency period between sperm oolemmal adhesion and oocyte penetration
    • Bronson RA, Bronson SK, Oula L, Fusi FM, Calzi F, Phillips DM. 1999. An investigation of the latency period between sperm oolemmal adhesion and oocyte penetration. Mol Reprod Dev 52:319-327.
    • (1999) Mol Reprod Dev , vol.52 , pp. 319-327
    • Bronson, R.A.1    Bronson, S.K.2    Oula, L.3    Fusi, F.M.4    Calzi, F.5    Phillips, D.M.6
  • 8
    • 0034072254 scopus 로고    scopus 로고
    • Ability of integrins to mediate fertilization, intracellular calcium release, and parthenogenetic development in bovine oocytes
    • Campbell KD, Reed WA, White KL. 2000. Ability of integrins to mediate fertilization, intracellular calcium release, and parthenogenetic development in bovine oocytes. Biol Reprod 62:1702-1709.
    • (2000) Biol Reprod , vol.62 , pp. 1702-1709
    • Campbell, K.D.1    Reed, W.A.2    White, K.L.3
  • 11
    • 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, 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
  • 12
    • 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 SA, Naaby-Hansen S, Shetty J, Shibahara H, Chen M, White JM, Herr JC. 1999b. 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. Dev Biol 207:334-349.
    • (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
  • 13
    • 0028578120 scopus 로고
    • Mechanism of calcium oscillations in fertilized rabbit eggs
    • Fissore RA, Robl JM. 1994. Mechanism of calcium oscillations in fertilized rabbit eggs. Dev Biol 166:634-642.
    • (1994) Dev Biol , vol.166 , pp. 634-642
    • Fissore, R.A.1    Robl, J.M.2
  • 15
  • 16
    • 0037053319 scopus 로고    scopus 로고
    • A mouse serine protease TESP5 is selectively included into lipid rafts of sperm membrane presumably as a glycosylphosphatidylinositol-anchored protein
    • Honda A, Yamagata K, Sugiura S, Watanabe K, Baba T. 2002. A mouse serine protease TESP5 is selectively included into lipid rafts of sperm membrane presumably as a glycosylphosphatidylinositol-anchored protein. J Biol Chem 277:16976-16984.
    • (2002) J Biol Chem , vol.277 , pp. 16976-16984
    • Honda, A.1    Yamagata, K.2    Sugiura, S.3    Watanabe, K.4    Baba, T.5
  • 17
    • 0031814234 scopus 로고    scopus 로고
    • What have snakes taught us about integrins?
    • Huang TF. 1998. What have snakes taught us about integrins? Cell Mol Life Sci 54:527-540.
    • (1998) Cell Mol Life Sci , vol.54 , pp. 527-540
    • Huang, T.F.1
  • 18
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes RO. 1992. Integrins: Versatility, modulation, and signaling in cell adhesion. Cell 69:11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 19
    • 0032217313 scopus 로고    scopus 로고
    • 2+ and fluorescent markers between the sperm and egg after fusion in the mouse
    • 2+ and fluorescent markers between the sperm and egg after fusion in the mouse. Development 125:4627-4635.
    • (1998) Development , vol.125 , pp. 4627-4635
    • Jones, K.T.1    Soeller, C.2    Cannell, M.B.3
  • 21
    • 0028859194 scopus 로고
    • Dibromobimane as a fluorescent crosslinking reagent
    • Kim JS, Raines RT. 1995. Dibromobimane as a fluorescent crosslinking reagent. Anal Biochem 225:174-176.
    • (1995) Anal Biochem , vol.225 , pp. 174-176
    • Kim, J.S.1    Raines, R.T.2
  • 23
    • 0032881430 scopus 로고    scopus 로고
    • A protein tyrosine phosphatase inhibitor, sodium orthovanadate, causes parthenogenetic activation of pig oocytes via an increase in protein tyrosine kinase activity
    • Kim JH, Do HJ, Wang WH, Machaty Z, Han YM, Day BN, Prather RS. 1999. A protein tyrosine phosphatase inhibitor, sodium orthovanadate, causes parthenogenetic activation of pig oocytes via an increase in protein tyrosine kinase activity. Biol Reprod 61:900-905.
    • (1999) Biol Reprod , vol.61 , pp. 900-905
    • Kim, J.H.1    Do, H.J.2    Wang, W.H.3    Machaty, Z.4    Han, Y.M.5    Day, B.N.6    Prather, R.S.7
  • 24
    • 0028928533 scopus 로고
    • A positive correlation between expression of beta 1-integrin cell adhesion molecules and fertilizing ability of human spermatozoa in vitro
    • Klentzeris LD, Fishel S, McDermott H, Dowell K, Hall J, Green S. 1995. A positive correlation between expression of beta 1-integrin cell adhesion molecules and fertilizing ability of human spermatozoa in vitro. Hum Reprod 10:728-733.
    • (1995) Hum Reprod , vol.10 , pp. 728-733
    • Klentzeris, L.D.1    Fishel, S.2    McDermott, H.3    Dowell, K.4    Hall, J.5    Green, S.6
  • 25
    • 0026551829 scopus 로고
    • Repetitive calcium transients and the role of calcium in exocytosis and cell cycle activation in the mouse egg
    • Kline D, Kline JT. 1992. Repetitive calcium transients and the role of calcium in exocytosis and cell cycle activation in the mouse egg. Dev Biol 149:80-89.
    • (1992) Dev Biol , vol.149 , pp. 80-89
    • Kline, D.1    Kline, J.T.2
  • 27
    • 0028855422 scopus 로고
    • An aspartate residue of the Yersinia pseudotuberculosis invasin protein that is critical for integrin binding
    • Leong JM, Morrissey PE, Marra A, Isberg RR. 1995. An aspartate residue of the Yersinia pseudotuberculosis invasin protein that is critical for integrin binding. Embo J 14:422-431.
    • (1995) Embo J , vol.14 , pp. 422-431
    • Leong, J.M.1    Morrissey, P.E.2    Marra, A.3    Isberg, R.R.4
  • 29
    • 0028945927 scopus 로고
    • Effects of protein tyrosine kinase inhibitors on egg activation and fertilization-dependent protein tyrosine kinase activity
    • Moore KL, Kinsey WH. 1995. Effects of protein tyrosine kinase inhibitors on egg activation and fertilization-dependent protein tyrosine kinase activity. Dev Biol 168:1-10.
    • (1995) Dev Biol , vol.168 , pp. 1-10
    • Moore, K.L.1    Kinsey, W.H.2
  • 30
    • 0026564762 scopus 로고
    • Expression of the signal transducing regions of CD4-like and lck genes in murine egg
    • Mori T, Gou MW, Yoshida H, Saito S, Mori E. 1992. Expression of the signal transducing regions of CD4-like and lck genes in murine egg. Biochem Biophys Res Commun 182:527-533.
    • (1992) Biochem Biophys Res Commun , vol.182 , pp. 527-533
    • Mori, T.1    Gou, M.W.2    Yoshida, H.3    Saito, S.4    Mori, E.5
  • 32
    • 0024843557 scopus 로고    scopus 로고
    • Parrish JJ, Susko-Parrish JL, Handrow RR, Ax RL, First NL. 1989. Effect of sulfated glycoconjugates on capacitation and the acrosome reaction of bovine and hamster spermatozoa. Gamete Res 24:403-413.
    • Parrish JJ, Susko-Parrish JL, Handrow RR, Ax RL, First NL. 1989. Effect of sulfated glycoconjugates on capacitation and the acrosome reaction of bovine and hamster spermatozoa. Gamete Res 24:403-413.
  • 33
    • 0034693854 scopus 로고    scopus 로고
    • Focal adhesion kinase: A regulator of focal adhesion dynamics and cell movement
    • Parsons JT, Martin KH, Slack JK, Taylor JM, Weed SA. 2000. Focal adhesion kinase: A regulator of focal adhesion dynamics and cell movement. Oncogene 19:5606-5613.
    • (2000) Oncogene , vol.19 , pp. 5606-5613
    • Parsons, J.T.1    Martin, K.H.2    Slack, J.K.3    Taylor, J.M.4    Weed, S.A.5
  • 36
    • 0000940473 scopus 로고    scopus 로고
    • Culture of in vitro fertilized bovine embryos with bovine oviductal epithelial cells, buffalo rat liver (BRL) cells or BRL-cell-conditioned medium
    • Reed WA, Suh T, Bunch TD, White KL. 1996. Culture of in vitro fertilized bovine embryos with bovine oviductal epithelial cells, buffalo rat liver (BRL) cells or BRL-cell-conditioned medium. Theriogenology 45:439-449.
    • (1996) Theriogenology , vol.45 , pp. 439-449
    • Reed, W.A.1    Suh, T.2    Bunch, T.D.3    White, K.L.4
  • 37
    • 0023637601 scopus 로고
    • New perspectives in cell adhesion: RGD and integrins
    • Ruoslahti E, Pierschbacher MD. 1987. New perspectives in cell adhesion: RGD and integrins. Science 238:491-497.
    • (1987) Science , vol.238 , pp. 491-497
    • Ruoslahti, E.1    Pierschbacher, M.D.2
  • 38
    • 0034096347 scopus 로고    scopus 로고
    • Role of angiotensin-converting enzyme inhibitor, lisinopril, on spermatozoal functions in rats
    • Saha L, Garg SK, Bhargava VK, Mazumdar S. 2000. Role of angiotensin-converting enzyme inhibitor, lisinopril, on spermatozoal functions in rats. Methods Find Exp Clin Pharmacol 22:159-162.
    • (2000) Methods Find Exp Clin Pharmacol , vol.22 , pp. 159-162
    • Saha, L.1    Garg, S.K.2    Bhargava, V.K.3    Mazumdar, S.4
  • 40
    • 3342910234 scopus 로고    scopus 로고
    • FAK and paxillin: Regulators of N-cadherin adhesion and inhibitors of cell migration?
    • Schaller MD. 2004. FAK and paxillin: Regulators of N-cadherin adhesion and inhibitors of cell migration? J Cell Biol 166:157-159.
    • (2004) J Cell Biol , vol.166 , pp. 157-159
    • Schaller, M.D.1
  • 41
    • 0034076116 scopus 로고    scopus 로고
    • Rat sperm 2B17 glycoprotein (PH20) contains a C-terminal sequence motif for attachment of a glycosyl phosphatidylinositol anchor. Effects of endoproteolytic cleavage on hyaluronidase activity
    • Seaton GJ, Hall L, Jones R. 2000. Rat sperm 2B17 glycoprotein (PH20) contains a C-terminal sequence motif for attachment of a glycosyl phosphatidylinositol anchor. Effects of endoproteolytic cleavage on hyaluronidase activity. Biol Reprod 62:1667-1676.
    • (2000) Biol Reprod , vol.62 , pp. 1667-1676
    • Seaton, G.J.1    Hall, L.2    Jones, R.3
  • 42
    • 33645459777 scopus 로고    scopus 로고
    • Effects of amino acid substitutions in and around the arginine-glycine-aspartic acid (RGD) sequence on fertilization and parthenogenetic development in mature bovine oocytes
    • Sessions BR, Aston KI, Davis AP, Pate BJ, White KL. 2006. Effects of amino acid substitutions in and around the arginine-glycine-aspartic acid (RGD) sequence on fertilization and parthenogenetic development in mature bovine oocytes. Mol Reprod Dev 73:651-657.
    • (2006) Mol Reprod Dev , vol.73 , pp. 651-657
    • Sessions, B.R.1    Aston, K.I.2    Davis, A.P.3    Pate, B.J.4    White, K.L.5
  • 43
    • 0031025120 scopus 로고    scopus 로고
    • Integrin-mediated calcium signaling and regulation of cell adhesion by intracellular calcium
    • Sjaastad MD, Nelson WJ. 1997. Integrin-mediated calcium signaling and regulation of cell adhesion by intracellular calcium. Bioessays 19:47-55.
    • (1997) Bioessays , vol.19 , pp. 47-55
    • Sjaastad, M.D.1    Nelson, W.J.2
  • 44
    • 27144432810 scopus 로고    scopus 로고
    • Immunolocalization of heat shock protein 70 (Hsp 70) in boar spermatozoa and its role during fertilization
    • Spinaci M, Volpe S, Bernardini C, De Ambrogi M, Tamanini C, Seren E, Galeati G. 2005. Immunolocalization of heat shock protein 70 (Hsp 70) in boar spermatozoa and its role during fertilization. Mol Reprod Dev 72:534-541.
    • (2005) Mol Reprod Dev , vol.72 , pp. 534-541
    • Spinaci, M.1    Volpe, S.2    Bernardini, C.3    De Ambrogi, M.4    Tamanini, C.5    Seren, E.6    Galeati, G.7
  • 45
    • 0028177777 scopus 로고
    • 2+ release in unfertilized mouse eggs injected with a sperm factor
    • 2+ release in unfertilized mouse eggs injected with a sperm factor. Cell Calcium 15:331-339.
    • (1994) Cell Calcium , vol.15 , pp. 331-339
    • Swann, K.1
  • 46
    • 0028267269 scopus 로고
    • Human oocyte activation after intracytoplasmic sperm injection
    • Tesarik J, Sousa M, Testart J. 1994. Human oocyte activation after intracytoplasmic sperm injection. Hum Reprod 9:511-518.
    • (1994) Hum Reprod , vol.9 , pp. 511-518
    • Tesarik, J.1    Sousa, M.2    Testart, J.3
  • 47
    • 0037353383 scopus 로고    scopus 로고
    • Mapping the proteome of barrel medic (Medicago truncatula)
    • Watson BS, Asirvatham VS, Wang L, Sumner LW. 2003. Mapping the proteome of barrel medic (Medicago truncatula). Plant Physiol 131: 1104-1123.
    • (2003) Plant Physiol , vol.131 , pp. 1104-1123
    • Watson, B.S.1    Asirvatham, V.S.2    Wang, L.3    Sumner, L.W.4
  • 48
    • 33751555589 scopus 로고    scopus 로고
    • Effects of arginine-glycine-aspartic acid (RGD) containing snake venom peptides on parthenogenetic development and in vitro fertilization of bovine oocytes
    • White KL, Passipieri M, Bunch TD, Campbell KD, Pate BJ. 2006. Effects of arginine-glycine-aspartic acid (RGD) containing snake venom peptides on parthenogenetic development and in vitro fertilization of bovine oocytes. Mol Reprod Dev 74:88-96.
    • (2006) Mol Reprod Dev , vol.74 , pp. 88-96
    • White, K.L.1    Passipieri, M.2    Bunch, T.D.3    Campbell, K.D.4    Pate, B.J.5
  • 49
    • 0026562632 scopus 로고
    • Role of G proteins in mouse egg activation: Stimulatory effects of acetylcholine on the ZP2 to ZP2f conversion and pronuclear formation in eggs expressing a functional ml muscarinic receptor
    • Williams CJ, Schultz RM, Kopf GS. 1992. Role of G proteins in mouse egg activation: Stimulatory effects of acetylcholine on the ZP2 to ZP2f conversion and pronuclear formation in eggs expressing a functional ml muscarinic receptor. Dev Biol 151:288-296.
    • (1992) Dev Biol , vol.151 , pp. 288-296
    • Williams, C.J.1    Schultz, R.M.2    Kopf, G.S.3
  • 50
    • 0030589505 scopus 로고    scopus 로고
    • ADAMs in fertilization and development
    • Wolfsberg TG, White JM. 1996. ADAMs in fertilization and development. Dev Biol 180:389-401.
    • (1996) Dev Biol , vol.180 , pp. 389-401
    • Wolfsberg, T.G.1    White, J.M.2
  • 51
    • 0028820623 scopus 로고
    • ADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: Multipotential functions in cell-cell and cell-matrix interactions
    • Wolfsberg TG, Primakoff P, Myles DG, White JM. 1995a. ADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: Multipotential functions in cell-cell and cell-matrix interactions. J Cell Biol 131:275-278.
    • (1995) J Cell Biol , vol.131 , pp. 275-278
    • Wolfsberg, T.G.1    Primakoff, P.2    Myles, D.G.3    White, J.M.4
  • 52
    • 0029045064 scopus 로고
    • ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain
    • Wolfsberg TG, Straight PD, Gerena RL, Huovila AP, Primakoff P, Myles DG, White JM. 1995b. 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
  • 53
    • 3342896372 scopus 로고    scopus 로고
    • Roles played by a subset of integrin signaling molecules in cadherin-based cell-cell adhesion
    • Yano H, Mazaki Y, Kurokawa K, Hanks SK, Matsuda M, Sabe H. 2004. Roles played by a subset of integrin signaling molecules in cadherin-based cell-cell adhesion. J Cell Biol 166:283-295.
    • (2004) J Cell Biol , vol.166 , pp. 283-295
    • Yano, H.1    Mazaki, Y.2    Kurokawa, K.3    Hanks, S.K.4    Matsuda, M.5    Sabe, H.6


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