메뉴 건너뛰기




Volumn 24, Issue 1, 2009, Pages 20-27

Enhancement of sperm-zona pellucida (ZP) binding capacity by activation of protein kinase A and C pathways in certain infertile men with defective sperm-ZP binding

Author keywords

Male infertility; PKA; PKC; Sperm zona binding; Tyrosine phosphorylation

Indexed keywords

BUCLADESINE; CYCLIC AMP DEPENDENT PROTEIN KINASE; MONOCLONAL ANTIBODY; PHORBOL 13 ACETATE 12 MYRISTATE; PHOSPHOTYROSINE; PROTEIN KINASE C; PROTEIN TYROSINE KINASE;

EID: 57749198885     PISSN: 02681161     EISSN: 14602350     Source Type: Journal    
DOI: 10.1093/humrep/den334     Document Type: Article
Times cited : (11)

References (41)
  • 1
    • 4444254836 scopus 로고    scopus 로고
    • Tyrosine phosphorylation activities surface chaperones facilitating sperm-zona recognition
    • Asquith KL, Baleato RM, Mclaughlin EA, Nixon B, Aitken RJ. Tyrosine phosphorylation activities surface chaperones facilitating sperm-zona recognition. J Cell Sci 2004;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
  • 2
    • 0042025019 scopus 로고    scopus 로고
    • Involvement of tyrosine kinase and cAMP-dependent kinase cross-talk in the regulation of human sperm motility
    • . Bajpai M, Doncel GF. Involvement of tyrosine kinase and cAMP-dependent kinase cross-talk in the regulation of human sperm motility. Reproduction 2003;126:183-195.
    • (2003) Reproduction , vol.126 , pp. 183-195
    • Bajpai, M.1    Doncel, G.F.2
  • 3
    • 0035904783 scopus 로고    scopus 로고
    • Interaction between sperm and zona pellucida in male fertility
    • Barratt CL, Publicover SJ. Interaction between sperm and zona pellucida in male fertility. Lancet 2001;358:1660-1662.
    • (2001) Lancet , vol.358 , pp. 1660-1662
    • Barratt, C.L.1    Publicover, S.J.2
  • 4
    • 0018822414 scopus 로고
    • Structure and function of the zona pellucida: Identification and characterization of the proteins of the mouse oocyte's zona pellucida
    • Bleil JD, Wassarman PM. Structure and function of the zona pellucida: identification and characterization of the proteins of the mouse oocyte's zona pellucida. Dev Biol 1980;76:185-202.
    • (1980) Dev Biol , vol.76 , pp. 185-202
    • Bleil, J.D.1    Wassarman, P.M.2
  • 5
    • 0025075878 scopus 로고
    • Identification of ZP3-binding protein on acrosome-intact mouse sperm by photoaffinity crosslinking
    • Bleil JD, Wassarman PM. Identification of ZP3-binding protein on acrosome-intact mouse sperm by photoaffinity crosslinking. Proc Natl Acad Sci 1990;87:5563-5567.
    • (1990) Proc Natl Acad Sci , vol.87 , pp. 5563-5567
    • Bleil, J.D.1    Wassarman, P.M.2
  • 6
    • 21044434065 scopus 로고    scopus 로고
    • Capacitation- associated protein tyrosine phosphorylation and membrane fluidity changes are impaired in the spermatozoa of asthenozoospermic patients
    • Buffone MG, Calamera JC, Verstraeten SV, Doncel GF. Capacitation- associated protein tyrosine phosphorylation and membrane fluidity changes are impaired in the spermatozoa of asthenozoospermic patients. Reproduction 2005;129:697-705.
    • (2005) Reproduction , vol.129 , pp. 697-705
    • Buffone, M.G.1    Calamera, J.C.2    Verstraeten, S.V.3    Doncel, G.F.4
  • 7
    • 0029012301 scopus 로고
    • Normal fertilization and embryo development with an round headed acrosomeless sperm
    • Bourne H, Liu DY, Clarke GN, Baker HWG. Normal fertilization and embryo development with an round headed acrosomeless sperm. Fertil Steril 1995;63:1329-1332.
    • (1995) Fertil Steril , vol.63 , pp. 1329-1332
    • Bourne, H.1    Liu, D.Y.2    Clarke, G.N.3    Baker, H.W.G.4
  • 8
    • 1242272860 scopus 로고    scopus 로고
    • Crosstalk between protein kinase A and C regulates phopholipase D and F-actin formation during sperm capacitation
    • Cohen G, Rubinstein S, Gur Y, Breitbart H. Crosstalk between protein kinase A and C regulates phopholipase D and F-actin formation during sperm capacitation. Dev Biol 2004;267:230-241.
    • (2004) Dev Biol , vol.267 , pp. 230-241
    • Cohen, G.1    Rubinstein, S.2    Gur, Y.3    Breitbart, H.4
  • 9
    • 0025970814 scopus 로고
    • Effect of phorbol diesters, synthetic diacyl glycerols, and a protein kinase C inhibitors on the human sperm acrosome reaction
    • De Jonge CJ, Han H-L, Mack SR, Zaneveld LJD. Effect of phorbol diesters, synthetic diacyl glycerols, and a protein kinase C inhibitors on the human sperm acrosome reaction. J Androl 1991;12:62-70.
    • (1991) J Androl , vol.12 , pp. 62-70
    • De Jonge, C.J.1    Han, H.-L.2    Mack, S.R.3    Zaneveld, L.J.D.4
  • 10
    • 0027317156 scopus 로고
    • The ability of the hemizona assay to predict human fertilization in different and consecutive in-vitro fertilization cycles
    • Franken DR, Kruger TF, Oehninger S, Coddington CC, Lombard C, Smith K, Hodgen GD. The ability of the hemizona assay to predict human fertilization in different and consecutive in-vitro fertilization cycles. Hum Reprod 1993;8:1240-1244.
    • (1993) Hum Reprod , vol.8 , pp. 1240-1244
    • Franken, D.R.1    Kruger, T.F.2    Oehninger, S.3    Coddington, C.C.4    Lombard, C.5    Smith, K.6    Hodgen, G.D.7
  • 11
    • 0031049037 scopus 로고    scopus 로고
    • Regulation of protein phosphorylation during bovine sperm capacitation by a cyclin adenosine 30,50-monophophate-dependent pathway
    • Galantino-Homer HL, Visconti PE, Kopf GS. Regulation of protein phosphorylation during bovine sperm capacitation by a cyclin adenosine 30,50-monophophate-dependent pathway. Biol Reprod 1997; 56:707-719.
    • (1997) Biol Reprod , vol.56 , pp. 707-719
    • Galantino-Homer, H.L.1    Visconti, P.E.2    Kopf, G.S.3
  • 14
    • 53349143708 scopus 로고    scopus 로고
    • Increased activity of the human sperm tyrosine kinase SRC by the cAMP-dependent pathway in the presence of calcium
    • doi:10.1095/biolreprod.108.070367
    • Lawson C, Goupil S, Leclerc P. Increased activity of the human sperm tyrosine kinase SRC by the cAMP-dependent pathway in the presence of calcium. Biol Reprod 2008, doi:10.1095/biolreprod.108.070367.
    • (2008) Biol Reprod
    • Lawson, C.1    Goupil, S.2    Leclerc, P.3
  • 15
    • 0029792629 scopus 로고    scopus 로고
    • Cyclinc adenosine 3′,5′monophosphate-dependent regulation of protein tyrosine phosphorylation in relation to human sperm capacitation and motility
    • Leclerc P, de Lamirande E, Gagnon C. Cyclinc adenosine 3′,5′monophosphate-dependent regulation of protein tyrosine phosphorylation in relation to human sperm capacitation and motility. Biol Reprod 1996;55:684-892.
    • (1996) Biol Reprod , vol.55 , pp. 684-892
    • Leclerc, P.1    de Lamirande, E.2    Gagnon, C.3
  • 16
    • 0023260654 scopus 로고
    • Effects of phorbol esters and a dicylglycerol on the mouse sperm acrosome reaction induced by the zona pellucida
    • Lee MA, Kopf GS, Storey B. Effects of phorbol esters and a dicylglycerol on the mouse sperm acrosome reaction induced by the zona pellucida. Biol Reprod 1987;36:617-627.
    • (1987) Biol Reprod , vol.36 , pp. 617-627
    • Lee, M.A.1    Kopf, G.S.2    Storey, B.3
  • 18
    • 0026662025 scopus 로고
    • Tests of human sperm function and fertilization in vitro
    • Liu DY, Baker HWG. Tests of human sperm function and fertilization in vitro. Fertil Steril 1992;58:465-483.
    • (1992) Fertil Steril , vol.58 , pp. 465-483
    • Liu, D.Y.1    Baker, H.W.G.2
  • 19
    • 0031297295 scopus 로고    scopus 로고
    • Protein kinase C plays an important role in the human zona pellucida-induced acrosome reaction
    • Liu DY, Baker HWG. Protein kinase C plays an important role in the human zona pellucida-induced acrosome reaction. Mol Hum Reprod 1997;3:1037-1043.
    • (1997) Mol Hum Reprod , vol.3 , pp. 1037-1043
    • Liu, D.Y.1    Baker, H.W.G.2
  • 20
    • 0034104557 scopus 로고    scopus 로고
    • Defective sperm-zona pellucida interaction: A major cause of failure of fertilization in clinical in-vitro fertilization
    • Liu DY, Baker HWG. Defective sperm-zona pellucida interaction: a major cause of failure of fertilization in clinical in-vitro fertilization. Hum Reprod 2000;15:702-708.
    • (2000) Hum Reprod , vol.15 , pp. 702-708
    • Liu, D.Y.1    Baker, H.W.G.2
  • 21
    • 0036150326 scopus 로고    scopus 로고
    • An anti-actin monoclonal antibody inhibits the zona pellucida induced acrosome reaction and hyperactivated motility of human sperm
    • Liu DY, Martic M, Clarke GN, Grkovic I, Garrett C, Dunlop ME, Baker HWG. An anti-actin monoclonal antibody inhibits the zona pellucida induced acrosome reaction and hyperactivated motility of human sperm. Mol Hum Reprod 2002a;8:37-47.
    • (2002) Mol Hum Reprod , vol.8 , pp. 37-47
    • Liu, D.Y.1    Martic, M.2    Clarke, G.N.3    Grkovic, I.4    Garrett, C.5    Dunlop, M.E.6    Baker, H.W.G.7
  • 22
    • 0036297398 scopus 로고    scopus 로고
    • Phorbol myristate acetate induces ruffling of the acrosome of human spermatozoa
    • Liu DY, Martic M, Garrett C, Dunlop ME, Baker HWG. Phorbol myristate acetate induces ruffling of the acrosome of human spermatozoa. Fertil Steril 2002b;78:128-136.
    • (2002) Fertil Steril , vol.78 , pp. 128-136
    • Liu, D.Y.1    Martic, M.2    Garrett, C.3    Dunlop, M.E.4    Baker, H.W.G.5
  • 23
    • 0242522127 scopus 로고    scopus 로고
    • Low proportions of spermatozoa can bind to the zona pellucida of human oocytes
    • Liu DY, Garrett C, Baker HWG. Low proportions of spermatozoa can bind to the zona pellucida of human oocytes. Hum Reprod 2003;18: 2382-2389.
    • (2003) Hum Reprod , vol.18 , pp. 2382-2389
    • Liu, D.Y.1    Garrett, C.2    Baker, H.W.G.3
  • 24
    • 7944224759 scopus 로고    scopus 로고
    • Clinical application of sperm-oocyte interaction tests in in vitro fertilization-embryo transfer and intracytoplasmic sperm injection programs
    • Liu DY, Garrett C, Baker HWG. Clinical application of sperm-oocyte interaction tests in in vitro fertilization-embryo transfer and intracytoplasmic sperm injection programs. Fertil Steril 2004;82: 1251-1263.
    • (2004) Fertil Steril , vol.82 , pp. 1251-1263
    • Liu, D.Y.1    Garrett, C.2    Baker, H.W.G.3
  • 25
    • 33645300734 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of capacitated human sperm tail detected by immunofluorescence correlates with sperm-zona pellucida (ZP) binding and not the ZP-induced acrosome reaction
    • Liu DY, Clarke GN, Baker HWG. Tyrosine phosphorylation of capacitated human sperm tail detected by immunofluorescence correlates with sperm-zona pellucida (ZP) binding and not the ZP-induced acrosome reaction. Hum Reprod 2006;21:1002-1008.
    • (2006) Hum Reprod , vol.21 , pp. 1002-1008
    • Liu, D.Y.1    Clarke, G.N.2    Baker, H.W.G.3
  • 26
    • 34447332515 scopus 로고    scopus 로고
    • Comparison of the frequency of defective sperm-zona pellucida (ZP) binding and the ZP-induced acrosome reaction between subfertile men with normal and abnormal semen
    • Liu DY, Liu ML, Garrett C, Baker HWG. Comparison of the frequency of defective sperm-zona pellucida (ZP) binding and the ZP-induced acrosome reaction between subfertile men with normal and abnormal semen. Hum Reprod 2007;22:1878-1884.
    • (2007) Hum Reprod , vol.22 , pp. 1878-1884
    • Liu, D.Y.1    Liu, M.L.2    Garrett, C.3    Baker, H.W.G.4
  • 27
    • 43049102422 scopus 로고    scopus 로고
    • Investigation of the role of SRC in capacitation-associated tyrosine phosphorylation of human spermatozoa
    • Mitchell LA, Nixon B, Baker MA, Aitken RJ. Investigation of the role of SRC in capacitation-associated tyrosine phosphorylation of human spermatozoa. Mol Hum Reprod 2008;14:235-243.
    • (2008) Mol Hum Reprod , vol.14 , pp. 235-243
    • Mitchell, L.A.1    Nixon, B.2    Baker, M.A.3    Aitken, R.J.4
  • 28
    • 0033045786 scopus 로고    scopus 로고
    • Modulation of sperm tail protein tyrosine phosphorylation by pentoxifylline and its correlation with hyperactivated motility
    • Nassar A, Mathony M, Morshedi M, Lin MH, Srisombut C, Oehninger S. Modulation of sperm tail protein tyrosine phosphorylation by pentoxifylline and its correlation with hyperactivated motility. Fertil Steril 1999;71:919-923.
    • (1999) Fertil Steril , vol.71 , pp. 919-923
    • Nassar, A.1    Mathony, M.2    Morshedi, M.3    Lin, M.H.4    Srisombut, C.5    Oehninger, S.6
  • 30
    • 0037378683 scopus 로고    scopus 로고
    • Localization of tyrosine phosphorylated proteins in human sperm and relation to capacitation and zona pellucida binding
    • Sakkas D, Leppens-Luisier G, Lucas H, Chardonnens A, Campana A, Franken DR, Urner F. Localization of tyrosine phosphorylated proteins in human sperm and relation to capacitation and zona pellucida binding. Biol Reprod 2003;68:1463-1469.
    • (2003) Biol Reprod , vol.68 , pp. 1463-1469
    • Sakkas, D.1    Leppens-Luisier, G.2    Lucas, H.3    Chardonnens, A.4    Campana, A.5    Franken, D.R.6    Urner, F.7
  • 31
    • 0029836135 scopus 로고    scopus 로고
    • The initial molecular interaction between mouse sperm and the zona pellucida is a complex binding events
    • Thaler CD, Cardullo RA. The initial molecular interaction between mouse sperm and the zona pellucida is a complex binding events. J Biol Chem 1996;271:23289-23297.
    • (1996) J Biol Chem , vol.271 , pp. 23289-23297
    • Thaler, C.D.1    Cardullo, R.A.2
  • 32
    • 0029002541 scopus 로고
    • Effect of protein kinase C stimulators on zona pellucida binding and the acrosome reaction of macaque sperm
    • Tollner TL, Overstreet JW, Vandevoort CA. Effect of protein kinase C stimulators on zona pellucida binding and the acrosome reaction of macaque sperm. Biol Reprod 1995;52:1418-1425.
    • (1995) Biol Reprod , vol.52 , pp. 1418-1425
    • Tollner, T.L.1    Overstreet, J.W.2    Vandevoort, C.A.3
  • 33
    • 0032817012 scopus 로고    scopus 로고
    • Relationship between sperm motility and the processing and tyrosine phosphorylation of two human sperm fibrous sheath proteins, pro-hAKA82 and hAKA82
    • Turner RMO, Eriksson ELM, Gerton GL, Moss SB. Relationship between sperm motility and the processing and tyrosine phosphorylation of two human sperm fibrous sheath proteins, pro-hAKA82 and hAKA82. Mol Hum Reprod 1999;5:816-824.
    • (1999) Mol Hum Reprod , vol.5 , pp. 816-824
    • Turner, R.M.O.1    Eriksson, E.L.M.2    Gerton, G.L.3    Moss, S.B.4
  • 34
    • 0037285863 scopus 로고    scopus 로고
    • Protein phosphorylation in mammalian spermatozoa
    • Urner F, Sakkas D. Protein phosphorylation in mammalian spermatozoa. Reproduction 2003;125:17-26.
    • (2003) Reproduction , vol.125 , pp. 17-26
    • Urner, F.1    Sakkas, D.2
  • 35
    • 34447312189 scopus 로고    scopus 로고
    • Multiple proteins present in purified porcine sperm apical plasma membranes interact with the zona pellucida of the oocytes
    • van Gestel RA, Brewis IA, Ashton PA, Brouwers JF, Gadella BM. Multiple proteins present in purified porcine sperm apical plasma membranes interact with the zona pellucida of the oocytes. Mol Hum Reprod 2007;13:445- 454.
    • (2007) Mol Hum Reprod , vol.13 , pp. 445-454
    • van Gestel, R.A.1    Brewis, I.A.2    Ashton, P.A.3    Brouwers, J.F.4    Gadella, B.M.5
  • 36
    • 0024614764 scopus 로고
    • Phorbol esters stimulate cyclic adenosine 30, 50-monophosphate accumulation in hamster spermatozoa during in vitro capacitation
    • Visconti PE, Tezon JG. Phorbol esters stimulate cyclic adenosine 30, 50-monophosphate accumulation in hamster spermatozoa during in vitro capacitation. Biol Reprod 1989;40:223-231.
    • (1989) Biol Reprod , vol.40 , pp. 223-231
    • Visconti, P.E.1    Tezon, J.G.2
  • 37
    • 0031778295 scopus 로고    scopus 로고
    • Regulation of protein phosphorylation during sperm capacitation
    • Visconti PE, Kopf GS. Regulation of protein phosphorylation during sperm capacitation. Biol Reprod 1998;59:1-6.
    • (1998) Biol Reprod , vol.59 , pp. 1-6
    • Visconti, P.E.1    Kopf, G.S.2
  • 38
    • 44349152970 scopus 로고    scopus 로고
    • Identification of rhe molecular chaperone, heat shock protein 1(chaperonin 10), in the reproductive tract and in capacitating spermatozoa in themalemouse
    • Walsh A, Whelan D, Bielanowicz A, Skinner B, Aitken RJ, O'Bryan MK, Nixon B. Identification of rhe molecular chaperone, heat shock protein 1(chaperonin 10), in the reproductive tract and in capacitating spermatozoa in themalemouse. Biol Reprod 2008;79:983-993.
    • (2008) Biol Reprod , vol.79 , pp. 983-993
    • Walsh, A.1    Whelan, D.2    Bielanowicz, A.3    Skinner, B.4    Aitken, R.J.5    O'Bryan, M.K.6    Nixon, B.7
  • 39
    • 0033593530 scopus 로고    scopus 로고
    • Mammalian fertilization: Molecular aspects of gamete adhesion, exocytosis, and fusion
    • Wassarman PM. Mammalian fertilization: molecular aspects of gamete adhesion, exocytosis, and fusion. Cell 1999;96:175-183.
    • (1999) Cell , vol.96 , pp. 175-183
    • Wassarman, P.M.1
  • 41
    • 0002302562 scopus 로고
    • Mammalian fertilisation
    • Knobil E, Neill J eds, 2nd edn. New York: Raven Press
    • Yanagimachi R. Mammalian fertilisation. In: Knobil E, Neill J (eds). The Physiology of Reproduction, 2nd edn. New York: Raven Press, 1994, 189-317.
    • (1994) The Physiology of Reproduction , pp. 189-317
    • Yanagimachi, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.