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Volumn 76, Issue 3, 2007, Pages 353-361

Semen-coagulating protein, SVS2, in mouse seminal plasma controls sperm fertility

Author keywords

Acrosome reaction; Decapacitation factor; Epididymal sperm; Female reproductive tract; Fertilization; Male reproductive tract; Seminal vesicles; Sperm capacitation

Indexed keywords

BASIC PROTEIN; DECAPACITATION FACTOR; SEMINAL PLASMA PROTEIN; SEMINAL VESICLE PROTEIN SECRETION 2; TYROSINE; UNCLASSIFIED DRUG;

EID: 33847223490     PISSN: 00063363     EISSN: None     Source Type: Journal    
DOI: 10.1095/biolreprod.106.056887     Document Type: Article
Times cited : (71)

References (51)
  • 1
    • 36949091315 scopus 로고
    • Fertilizing capacity of spermatozoa deposited into the fallopian tubes
    • Chang MC. Fertilizing capacity of spermatozoa deposited into the fallopian tubes. Nature 1951; 168:697-698.
    • (1951) Nature , vol.168 , pp. 697-698
    • Chang, M.C.1
  • 2
    • 76949114656 scopus 로고
    • Observations on the penetration of the sperm into the mammalian egg
    • Austin CR. Observations on the penetration of the sperm into the mammalian egg. Aust J Sci Res 1951; (6)4:581-596.
    • (1951) Aust J Sci Res , vol.4 , Issue.6 , pp. 581-596
    • Austin, C.R.1
  • 3
    • 0027373720 scopus 로고
    • Ca(2+)-related changes in the capacitation state of human spermatozoa assessed by a chlortetracycline fluorescence assay
    • DasGupta S, Mills CL, Fraser LR. Ca(2+)-related changes in the capacitation state of human spermatozoa assessed by a chlortetracycline fluorescence assay. J Reprod Fertil 1993; 99:135-143.
    • (1993) J Reprod Fertil , vol.99 , pp. 135-143
    • DasGupta, S.1    Mills, C.L.2    Fraser, L.R.3
  • 4
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • Knobil E, Neil JD eds, New York: Raven Press;
    • Yanagimachi R. Mammalian fertilization. In: Knobil E, Neil JD (eds.), The Physiology of Reproduction. New York: Raven Press; 1994:189-317.
    • (1994) The Physiology of Reproduction , pp. 189-317
    • Yanagimachi, R.1
  • 5
    • 0028957362 scopus 로고
    • Capacitation of mouse spermatozoa. II. Correlation between the capacitation state and protein tyrosine phosphorylation
    • Visconti PE, Bailey JL, Moore GD, Pan D, Olds-Clarke P, Kopf GS. Capacitation of mouse spermatozoa. II. Correlation between the capacitation state and protein tyrosine phosphorylation. Development 1995; 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
    • 1642462435 scopus 로고    scopus 로고
    • Analysis of the mechanism by which calcium negatively regulates the tyrosine phosphorylation cascade associated with sperm capacitation
    • Baker MA, Hetherington L, Ecroyd H, Roman SD, Aitken RJ. Analysis of the mechanism by which calcium negatively regulates the tyrosine phosphorylation cascade associated with sperm capacitation. J Cell Sci 2004; 117(Pt 2):211-222.
    • (2004) J Cell Sci , vol.117 , Issue.PART 2 , pp. 211-222
    • Baker, M.A.1    Hetherington, L.2    Ecroyd, H.3    Roman, S.D.4    Aitken, R.J.5
  • 7
    • 0001296109 scopus 로고
    • A detrimental effect of seminal plasma on the fertilizing capacity of sperm
    • Chang MC. A detrimental effect of seminal plasma on the fertilizing capacity of sperm. Nature 1957; 179:258-259.
    • (1957) Nature , vol.179 , pp. 258-259
    • Chang, M.C.1
  • 8
    • 0242394947 scopus 로고
    • Removal of decapacitation factor from seminal plasma by high-speed centrifugation
    • Bedford JM, Chang MC. Removal of decapacitation factor from seminal plasma by high-speed centrifugation. Am J Physiol 1962; 202:179-181.
    • (1962) Am J Physiol , vol.202 , pp. 179-181
    • Bedford, J.M.1    Chang, M.C.2
  • 9
    • 0016017003 scopus 로고
    • Biochemistry of mammalian fertilization
    • McRorie RA, Williams WL. Biochemistry of mammalian fertilization. Annu Rev Biochem 1974; 43:777-803.
    • (1974) Annu Rev Biochem , vol.43 , pp. 777-803
    • McRorie, R.A.1    Williams, W.L.2
  • 10
    • 0001385492 scopus 로고
    • Inhibition of fertilizing capacity in mammalian spermatozoa by natural and synthetic vesicles
    • Kabara JJ ed, Champaign, Illinois: The American Oil Chemists Society;
    • Davis BK. Inhibition of fertilizing capacity in mammalian spermatozoa by natural and synthetic vesicles. In: Kabara JJ (ed.), Symposium on the Pharmacological Effect of Lipids. Champaign, Illinois: The American Oil Chemists Society; 1978:145-157.
    • (1978) Symposium on the Pharmacological Effect of Lipids , pp. 145-157
    • Davis, B.K.1
  • 11
    • 0022350183 scopus 로고
    • Sperm surface components involved in the control of the acrosome reaction
    • Oliphant G, Reynolds AB, Thomas TS. Sperm surface components involved in the control of the acrosome reaction. Am J Anat 1985; 174:269-284.
    • (1985) Am J Anat , vol.174 , pp. 269-284
    • Oliphant, G.1    Reynolds, A.B.2    Thomas, T.S.3
  • 12
    • 0031692764 scopus 로고    scopus 로고
    • Interactions between a decapacitation factor and mouse spermatozoa appear to involve fucose residues and a GPI-anchored receptor
    • Fraser LR. Interactions between a decapacitation factor and mouse spermatozoa appear to involve fucose residues and a GPI-anchored receptor. Mol Reprod Dev 1998; 51:193-202.
    • (1998) Mol Reprod Dev , vol.51 , pp. 193-202
    • Fraser, L.R.1
  • 14
    • 31044442157 scopus 로고    scopus 로고
    • The identification of mouse sperm-surface-associated proteins and characterization of their ability to act as decapacitation factors
    • Nixon B, MacIntyre DA, Mitchell LA, Gibbs GM, O'Bryan M, Aitken RJ. The identification of mouse sperm-surface-associated proteins and characterization of their ability to act as decapacitation factors. Biol Reprod 2006; 74:275-287.
    • (2006) Biol Reprod , vol.74 , pp. 275-287
    • Nixon, B.1    MacIntyre, D.A.2    Mitchell, L.A.3    Gibbs, G.M.4    O'Bryan, M.5    Aitken, R.J.6
  • 15
    • 0021339950 scopus 로고
    • Transglutaminases and the clotting of mammalian seminal fluids
    • Williams-Ashman HG. Transglutaminases and the clotting of mammalian seminal fluids. Mol Cell Biochem 1984; 58:51-61.
    • (1984) Mol Cell Biochem , vol.58 , pp. 51-61
    • Williams-Ashman, H.G.1
  • 16
    • 0024562089 scopus 로고
    • Semenogelin, the predominant protein in human semen. Primary structure and identification of closely related proteins in the male accessory sex glands and on the spermatozoa
    • Lilja H, Abrahamsson PA, Lundwall A. Semenogelin, the predominant protein in human semen. Primary structure and identification of closely related proteins in the male accessory sex glands and on the spermatozoa. J Biol Chem 1989; 264:1894-1900.
    • (1989) J Biol Chem , vol.264 , pp. 1894-1900
    • Lilja, H.1    Abrahamsson, P.A.2    Lundwall, A.3
  • 17
    • 9644287861 scopus 로고    scopus 로고
    • Rate of molecular evolution of the seminal protein gene SEMG2 correlates with levels of female promiscuity
    • Dorus S, Evans PD, Wyckoff GJ, Choi SS, Lahn BT. Rate of molecular evolution of the seminal protein gene SEMG2 correlates with levels of female promiscuity. Nat Genet 2004; 36:1326-1329.
    • (2004) Nat Genet , vol.36 , pp. 1326-1329
    • Dorus, S.1    Evans, P.D.2    Wyckoff, G.J.3    Choi, S.S.4    Lahn, B.T.5
  • 18
    • 0030060587 scopus 로고    scopus 로고
    • The cloning of a rapidly evolving seminal-vesicle-transcribed gene encoding the major clot-forming protein of mouse semen
    • Lundwall A. The cloning of a rapidly evolving seminal-vesicle-transcribed gene encoding the major clot-forming protein of mouse semen. Eur J Biochem 1996; 235:424-430.
    • (1996) Eur J Biochem , vol.235 , pp. 424-430
    • Lundwall, A.1
  • 21
    • 0029101861 scopus 로고
    • Cloning of boar SPMI gene which is expressed specifically in seminal vesicle and codes for a sperm motility inhibitor protein
    • Iwamoto T, Hiroaki H, Furuichi Y, Wada K, Satoh M, Osada T. Cloning of boar SPMI gene which is expressed specifically in seminal vesicle and codes for a sperm motility inhibitor protein. FEBS Lett 1995; 368:420-424.
    • (1995) FEBS Lett , vol.368 , pp. 420-424
    • Iwamoto, T.1    Hiroaki, H.2    Furuichi, Y.3    Wada, K.4    Satoh, M.5    Osada, T.6
  • 22
    • 0029285612 scopus 로고
    • Interaction of non-aggregated boar AWN-1 and AQN-3 with phospholipid matrices. A model for coating of sperm adhesins to the sperm surface
    • Dostalova Z, Calvete JJ, Topfer-Petersen E. Interaction of non-aggregated boar AWN-1 and AQN-3 with phospholipid matrices. A model for coating of sperm adhesins to the sperm surface. Biol Chem Hoppe Seyler 1995; 376:237-242.
    • (1995) Biol Chem Hoppe Seyler , vol.376 , pp. 237-242
    • Dostalova, Z.1    Calvete, J.J.2    Topfer-Petersen, E.3
  • 23
    • 0034940268 scopus 로고    scopus 로고
    • Semenogelin, the main protein of semen coagulum, inhibits human sperm capacitation by interfering with the Superoxide anion generated during this process
    • de Lamirande E, Yoshida K, Yoshiike TM, Iwamoto T, Gagnon C. Semenogelin, the main protein of semen coagulum, inhibits human sperm capacitation by interfering with the Superoxide anion generated during this process. J Androl 2001; 22:672-679.
    • (2001) J Androl , vol.22 , pp. 672-679
    • de Lamirande, E.1    Yoshida, K.2    Yoshiike, T.M.3    Iwamoto, T.4    Gagnon, C.5
  • 24
    • 0242541030 scopus 로고    scopus 로고
    • Quantification of seminal plasma motility inhibitor/semenogelin in human seminal plasma
    • Yoshida K, Yamasaki T, Yoshiike M, Takano S, Sato I, Iwamoto T. Quantification of seminal plasma motility inhibitor/semenogelin in human seminal plasma. J Androl 2003; 24:878-884.
    • (2003) J Androl , vol.24 , pp. 878-884
    • Yoshida, K.1    Yamasaki, T.2    Yoshiike, M.3    Takano, S.4    Sato, I.5    Iwamoto, T.6
  • 27
    • 0347026693 scopus 로고    scopus 로고
    • Motility and penetration competence of frozen-thawed miniature pig spermatozoa are substantially altered by exposure to seminal plasma before freezing
    • Kawano N, Shimada M, Terada T. Motility and penetration competence of frozen-thawed miniature pig spermatozoa are substantially altered by exposure to seminal plasma before freezing. Theriogenology 2003; 61:351-364.
    • (2003) Theriogenology , vol.61 , pp. 351-364
    • Kawano, N.1    Shimada, M.2    Terada, T.3
  • 28
    • 0013594914 scopus 로고
    • Coagulation, liquefaction and viscosity of human semen
    • Amelar RD. Coagulation, liquefaction and viscosity of human semen. J Urol 1962; 87:187-190.
    • (1962) J Urol , vol.87 , pp. 187-190
    • Amelar, R.D.1
  • 29
    • 0029800159 scopus 로고    scopus 로고
    • Classification of male factor infertility relevant to in vitro fertilization insemination strategies using mannose ligands, acrosome status and anti-cytoskeletal antibodies
    • Benoff S, Barcia M, Hurley IR, Cooper GW, Mandel FS, Heyner S, Garside WT, Gilbert BR, Hershlag A. Classification of male factor infertility relevant to in vitro fertilization insemination strategies using mannose ligands, acrosome status and anti-cytoskeletal antibodies. Hum Reprod 1996; 11:1905-1918.
    • (1996) Hum Reprod , vol.11 , pp. 1905-1918
    • Benoff, S.1    Barcia, M.2    Hurley, I.R.3    Cooper, G.W.4    Mandel, F.S.5    Heyner, S.6    Garside, W.T.7    Gilbert, B.R.8    Hershlag, A.9
  • 30
    • 0031091041 scopus 로고    scopus 로고
    • Isolation and characterization of the primary structure of testis-specific L-type calcium channel: Implications for contraception
    • Goodwin LO, Leeds NB, Hurley I, Mandel FS, Pergolizzi RG, Benoff S. Isolation and characterization of the primary structure of testis-specific L-type calcium channel: implications for contraception. Mol Hum Reprod 1997; 3:255-268.
    • (1997) Mol Hum Reprod , vol.3 , pp. 255-268
    • Goodwin, L.O.1    Leeds, N.B.2    Hurley, I.3    Mandel, F.S.4    Pergolizzi, R.G.5    Benoff, S.6
  • 31
    • 0024274138 scopus 로고
    • An influx of extracellular calcium is required for initiation of the human sperm acrosome reaction induced by human follicular fluid
    • Thomas P, Meizel S. An influx of extracellular calcium is required for initiation of the human sperm acrosome reaction induced by human follicular fluid. Gamete Res 1988; 20:397-411.
    • (1988) Gamete Res , vol.20 , pp. 397-411
    • Thomas, P.1    Meizel, S.2
  • 32
    • 0031878297 scopus 로고    scopus 로고
    • Live mice from cryopreserved embryos derived in vitro with cryopreserved ejaculated spermatozoa
    • Songsasen N, Leibo SP. Live mice from cryopreserved embryos derived in vitro with cryopreserved ejaculated spermatozoa. Lab Anim Sci 1998; 48:275-281.
    • (1998) Lab Anim Sci , vol.48 , pp. 275-281
    • Songsasen, N.1    Leibo, S.P.2
  • 33
    • 0033213945 scopus 로고    scopus 로고
    • Seminal vesicle autoantigen, a novel phospholipid-binding protein secreted from luminal epithelium of mouse seminal vesicle, exhibits the ability to suppress mouse sperm motility
    • Huang YH, Chu ST, Chen YH. Seminal vesicle autoantigen, a novel phospholipid-binding protein secreted from luminal epithelium of mouse seminal vesicle, exhibits the ability to suppress mouse sperm motility. Biochem J 1999; 343(Pt 1):241-248.
    • (1999) Biochem J , vol.343 , Issue.PART 1 , pp. 241-248
    • Huang, Y.H.1    Chu, S.T.2    Chen, Y.H.3
  • 34
    • 0033761216 scopus 로고    scopus 로고
    • A seminal vesicle autoantigen of mouse is able to suppress sperm capacitation-related events stimulated by serum albumin
    • Huang YH, Chu ST, Chen YH. A seminal vesicle autoantigen of mouse is able to suppress sperm capacitation-related events stimulated by serum albumin. Biol Reprod 2000; 63:1562-1566.
    • (2000) Biol Reprod , vol.63 , pp. 1562-1566
    • Huang, Y.H.1    Chu, S.T.2    Chen, Y.H.3
  • 35
    • 78651001534 scopus 로고
    • Effects of heterologous seminal plasma and sperm cells on fertilizing capacity of rabbit spermatozoa
    • Chang MC. Effects of heterologous seminal plasma and sperm cells on fertilizing capacity of rabbit spermatozoa. Proc Exp Biol Med 1949; 70:32.
    • (1949) Proc Exp Biol Med , vol.70 , pp. 32
    • Chang, M.C.1
  • 36
    • 0019177482 scopus 로고
    • Taurine and hypotaurine: Their effects on motility, capacitation and the acrosome reaction of hamster sperm in vitro and their presence in sperm and reproductive tract fluids of several mammals
    • Meizel S, Lui WC, Working KP, Mrsny JR. Taurine and hypotaurine: their effects on motility, capacitation and the acrosome reaction of hamster sperm in vitro and their presence in sperm and reproductive tract fluids of several mammals. Dev Growth Differ 1980; 22:483-494.
    • (1980) Dev Growth Differ , vol.22 , pp. 483-494
    • Meizel, S.1    Lui, W.C.2    Working, K.P.3    Mrsny, J.R.4
  • 37
    • 0018775847 scopus 로고
    • Fertilization: A uterine glycosaminoglycan stimulates the conversion of sperm proacrosin to acrosin
    • Wincek TJ, Parrish RF, Polakoski KL. Fertilization: a uterine glycosaminoglycan stimulates the conversion of sperm proacrosin to acrosin. Science 1979; 203:553-554.
    • (1979) Science , vol.203 , pp. 553-554
    • Wincek, T.J.1    Parrish, R.F.2    Polakoski, K.L.3
  • 38
    • 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 PE, Ning X, Fornes MW, Alvarez JG, Stein P, Connors SA, Kopf GS. Cholesterol efflux-mediated signal transduction in mammalian sperm: cholesterol release signals an increase in protein tyrosine phosphorylation during mouse sperm capacitation. Dev Biol 1999; 214:429-443.
    • (1999) Dev Biol , vol.214 , pp. 429-443
    • Visconti, P.E.1    Ning, X.2    Fornes, M.W.3    Alvarez, J.G.4    Stein, P.5    Connors, S.A.6    Kopf, G.S.7
  • 39
    • 4544342119 scopus 로고    scopus 로고
    • Reorganization of lipid rafts during capacitation of human sperm
    • Cross NL. Reorganization of lipid rafts during capacitation of human sperm. Biol Reprod 2004; 71:1367-1373.
    • (2004) Biol Reprod , vol.71 , pp. 1367-1373
    • Cross, N.L.1
  • 40
    • 0037959071 scopus 로고    scopus 로고
    • The state of lipid rafts: From model membranes to cells
    • Edidin M. The state of lipid rafts: from model membranes to cells. Annu Rev Biophys Biomol Struct 2003; 32:257-283.
    • (2003) Annu Rev Biophys Biomol Struct , vol.32 , pp. 257-283
    • Edidin, M.1
  • 41
    • 0037947831 scopus 로고    scopus 로고
    • Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors
    • Foster LJ, De Hoog CL, Mann M. Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors. Proc Natl Acad Sci USA 2003; 100:5813-5818.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 5813-5818
    • Foster, L.J.1    De Hoog, C.L.2    Mann, M.3
  • 42
    • 0033993454 scopus 로고    scopus 로고
    • Cholesterol depletion disrupts lipid rafts and modulates the activity of multiple signaling pathways in T lymphocytes
    • Kabouridis PS, Janzen J, Magee AL, Ley SC. Cholesterol depletion disrupts lipid rafts and modulates the activity of multiple signaling pathways in T lymphocytes. Eur J Immunol 2000; 30:954-963.
    • (2000) Eur J Immunol , vol.30 , pp. 954-963
    • Kabouridis, P.S.1    Janzen, J.2    Magee, A.L.3    Ley, S.C.4
  • 43
    • 4143144331 scopus 로고    scopus 로고
    • Sperm membrane dynamics assessed by changes in lectin fluorescence before and after capacitation
    • Baker SS, Thomas M, Thaler CD. Sperm membrane dynamics assessed by changes in lectin fluorescence before and after capacitation. J Androl 2004; 25:744-751.
    • (2004) J Androl , vol.25 , pp. 744-751
    • Baker, S.S.1    Thomas, M.2    Thaler, C.D.3
  • 44
    • 3142724785 scopus 로고    scopus 로고
    • Cholesterol efflux alters lipid raft stability and distribution during capacitation of boar spermatozoa
    • Shadan S, James PS, Howes EA, Jones R. Cholesterol efflux alters lipid raft stability and distribution during capacitation of boar spermatozoa. Biol Reprod 2004; 71:253-265.
    • (2004) Biol Reprod , vol.71 , pp. 253-265
    • Shadan, S.1    James, P.S.2    Howes, E.A.3    Jones, R.4
  • 45
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown DA, London E. Functions of lipid rafts in biological membranes. Annu Rev Cell Dev Biol 1998; 14:111-136.
    • (1998) Annu Rev Cell Dev Biol , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 46
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid- and cholesterol-rich membrane rafts
    • Brown DA, London E. Structure and function of sphingolipid- and cholesterol-rich membrane rafts. J Biol Chem 2000; 275:17221-17224.
    • (2000) J Biol Chem , vol.275 , pp. 17221-17224
    • Brown, D.A.1    London, E.2
  • 47
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K, Ikonen E. Functional rafts in cell membranes. Nature 1997; 387:569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 48
    • 0034304851 scopus 로고    scopus 로고
    • Lipid rafts and signal transduction
    • Simons K, Toomre D. Lipid rafts and signal transduction. Nat Rev Mol Cell Biol 2000; 1:31-39.
    • (2000) Nat Rev Mol Cell Biol , vol.1 , pp. 31-39
    • Simons, K.1    Toomre, D.2
  • 50
    • 0024241559 scopus 로고
    • Purification and characterization of a sperm motility inhibitor in human seminal plasma
    • Iwamoto T, Gagnon C. Purification and characterization of a sperm motility inhibitor in human seminal plasma. J Androl 1988; 9:377-383.
    • (1988) J Androl , vol.9 , pp. 377-383
    • Iwamoto, T.1    Gagnon, C.2
  • 51
    • 0033016106 scopus 로고    scopus 로고
    • Robert M, Gagnon C. Semenogelin I: a coagulum forming, multifunctional seminal vesicle protein. Cell Mol Life Sci 1999; 55:944-960.
    • Robert M, Gagnon C. Semenogelin I: a coagulum forming, multifunctional seminal vesicle protein. Cell Mol Life Sci 1999; 55:944-960.


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