메뉴 건너뛰기




Volumn 79, Issue 7, 2013, Pages 1071-1082

Boar seminal plasma exosomes: Effect on sperm function and protein identification by sequencing

Author keywords

Boar; Exosome; Prostasome; Seminal plasma; Sperm capacitation

Indexed keywords

PROTEIN;

EID: 84878014603     PISSN: 0093691X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.theriogenology.2013.01.028     Document Type: Article
Times cited : (74)

References (74)
  • 1
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • Raven Press, New York, E. Knobil, J.D. Neill (Eds.)
    • Yanagimachi R. Mammalian fertilization. The physiology of reproduction 1994, 189-317. Raven Press, New York. E. Knobil, J.D. Neill (Eds.).
    • (1994) The physiology of reproduction , pp. 189-317
    • Yanagimachi, R.1
  • 2
    • 3543144347 scopus 로고    scopus 로고
    • Bicarbonate and its role in mammalian sperm function
    • Gadella B.M., van Gestel R.A. Bicarbonate and its role in mammalian sperm function. Anim Reprod Sci 2004, 82-83:307-319.
    • (2004) Anim Reprod Sci , pp. 307-319
    • Gadella, B.M.1    van Gestel, R.A.2
  • 3
    • 0021995091 scopus 로고
    • Albumin-mediated changes in sperm sterol content during capacitation
    • Go K.J., Wolf D.P. Albumin-mediated changes in sperm sterol content during capacitation. Biol Reprod 1985, 32:145-153.
    • (1985) Biol Reprod , vol.32 , pp. 145-153
    • Go, K.J.1    Wolf, D.P.2
  • 4
    • 0031776647 scopus 로고    scopus 로고
    • Role of cholesterol in sperm capacitation
    • Cross N.L. Role of cholesterol in sperm capacitation. Biol Reprod 1998, 59:7-11.
    • (1998) Biol Reprod , vol.59 , pp. 7-11
    • Cross, N.L.1
  • 5
    • 0037962072 scopus 로고    scopus 로고
    • Decrease in order of human sperm lipids during capacitation
    • Cross N.L. Decrease in order of human sperm lipids during capacitation. Biol Reprod 2003, 69:529-534.
    • (2003) Biol Reprod , vol.69 , pp. 529-534
    • Cross, N.L.1
  • 6
    • 0034759226 scopus 로고    scopus 로고
    • Bicarbonate stimulated phospholipid scrambling induces cholesterol redistribution and enables cholesterol depletion in the sperm plasma membrane
    • Flesch F.M., Brouwers J.F., Nievelstein P.F., Verkleij A.J., van Golde L.M., Colenbrander B., et al. Bicarbonate stimulated phospholipid scrambling induces cholesterol redistribution and enables cholesterol depletion in the sperm plasma membrane. J Cell Sci 2001, 114:3543-3555.
    • (2001) J Cell Sci , vol.114 , pp. 3543-3555
    • Flesch, F.M.1    Brouwers, J.F.2    Nievelstein, P.F.3    Verkleij, A.J.4    van Golde, L.M.5    Colenbrander, B.6
  • 7
    • 0029456702 scopus 로고
    • Ionic control of sperm function
    • Fraser L.R. Ionic control of sperm function. Reprod Fertil Dev 1995, 7:905-925.
    • (1995) Reprod Fertil Dev , vol.7 , pp. 905-925
    • Fraser, L.R.1
  • 8
    • 0028957362 scopus 로고
    • Capacitation of mouse spermatozoa. I. Correlation between the capacitation state and protein tyrosine phosphorylation
    • Visconti P.E., Bailey J.L., Moore G.D., Pan D., Olds-Clarke P., Kopf G.S. Capacitation of mouse spermatozoa. I. 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
  • 9
    • 0001296109 scopus 로고
    • A detrimental effect of seminal plasma on the fertilizing capacity of sperm
    • Chang E.E. 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, E.E.1
  • 10
    • 0029656158 scopus 로고    scopus 로고
    • Human seminal plasma prevents sperm from becoming acrosomally responsive to the agonist, progesterone: cholesterol is the major inhibitor
    • Cross N.L. Human seminal plasma prevents sperm from becoming acrosomally responsive to the agonist, progesterone: cholesterol is the major inhibitor. Biol Reprod 1996, 54:138-145.
    • (1996) Biol Reprod , vol.54 , pp. 138-145
    • Cross, N.L.1
  • 11
    • 0018340741 scopus 로고
    • Effects of human seminal plasma on fertilizing capacity of human spermatozoa
    • Kanwar K.C., Yanagimachi R., Lopata A. Effects of human seminal plasma on fertilizing capacity of human spermatozoa. Fertil Steril 1979, 31:321-327.
    • (1979) Fertil Steril , vol.31 , pp. 321-327
    • Kanwar, K.C.1    Yanagimachi, R.2    Lopata, A.3
  • 12
    • 0031934887 scopus 로고    scopus 로고
    • Treatment of human spermatozoa with seminal plasma inhibits protein tyrosine phosphorylation
    • Tomes C.N., Carballada R., Moses D.F., Katz D.F., Saling P.M. Treatment of human spermatozoa with seminal plasma inhibits protein tyrosine phosphorylation. Mol Hum Reprod 1998, 4:17-25.
    • (1998) Mol Hum Reprod , vol.4 , pp. 17-25
    • Tomes, C.N.1    Carballada, R.2    Moses, D.F.3    Katz, D.F.4    Saling, P.M.5
  • 13
    • 0017154197 scopus 로고
    • Inhibitory effect of synthetic phospholipid vesicles containing cholesterol on the fertilizing ability of rabbit spermatozoa
    • Davis B.K. Inhibitory effect of synthetic phospholipid vesicles containing cholesterol on the fertilizing ability of rabbit spermatozoa. Proc Soc Exp Biol Med 1976, 152:257-261.
    • (1976) Proc Soc Exp Biol Med , vol.152 , pp. 257-261
    • Davis, B.K.1
  • 14
    • 47649108885 scopus 로고    scopus 로고
    • Protein composition of human epididymosomes collected during surgical vasectomy reversal: a proteomic and genomic approach
    • Thimon V., Frenette G., Saez F., Thabet M., Sullivan R. Protein composition of human epididymosomes collected during surgical vasectomy reversal: a proteomic and genomic approach. Hum Reprod 2008, 23:1698-1707.
    • (2008) Hum Reprod , vol.23 , pp. 1698-1707
    • Thimon, V.1    Frenette, G.2    Saez, F.3    Thabet, M.4    Sullivan, R.5
  • 15
    • 58849151841 scopus 로고    scopus 로고
    • Structural heterogeneity and protein composition of exosome-like vesicles (prostasomes) in human semen
    • Poliakov A., Spilman M., Dokland T., Amling C.L., Mobley J.A. Structural heterogeneity and protein composition of exosome-like vesicles (prostasomes) in human semen. Prostate 2009, 69:159-167.
    • (2009) Prostate , vol.69 , pp. 159-167
    • Poliakov, A.1    Spilman, M.2    Dokland, T.3    Amling, C.L.4    Mobley, J.A.5
  • 16
    • 33645876205 scopus 로고    scopus 로고
    • Biochemical characterization and membrane fluidity of membranous vesicles isolated from boar seminal plasma
    • Piehl L.L., Cisale H., Torres N., Capani F., Sterin-Speziale N., Hager A. Biochemical characterization and membrane fluidity of membranous vesicles isolated from boar seminal plasma. Anim Reprod Sci 2006, 92:401-410.
    • (2006) Anim Reprod Sci , vol.92 , pp. 401-410
    • Piehl, L.L.1    Cisale, H.2    Torres, N.3    Capani, F.4    Sterin-Speziale, N.5    Hager, A.6
  • 17
    • 0024460831 scopus 로고
    • Human prostasome membranes exhibit very high cholesterol/phospholipid ratios yielding high molecular ordering
    • Arvidson G., Ronquist G., Wikander G., Ojteg A.C. Human prostasome membranes exhibit very high cholesterol/phospholipid ratios yielding high molecular ordering. Biochim Biophys Acta 1989, 984:167-173.
    • (1989) Biochim Biophys Acta , vol.984 , pp. 167-173
    • Arvidson, G.1    Ronquist, G.2    Wikander, G.3    Ojteg, A.C.4
  • 19
    • 0042744813 scopus 로고    scopus 로고
    • Epididymosomes and prostasomes: their roles in posttesticular maturation of the sperm cells
    • Saez F., Frenette G., Sullivan R. Epididymosomes and prostasomes: their roles in posttesticular maturation of the sperm cells. J Androl 2003, 24:149-154.
    • (2003) J Androl , vol.24 , pp. 149-154
    • Saez, F.1    Frenette, G.2    Sullivan, R.3
  • 20
    • 84858864047 scopus 로고    scopus 로고
    • Prostasomes are mediators of intercellular communication: from basic research to clinical implications
    • Ronquist G. Prostasomes are mediators of intercellular communication: from basic research to clinical implications. J Intern Med 2012, 271:400-413.
    • (2012) J Intern Med , vol.271 , pp. 400-413
    • Ronquist, G.1
  • 21
    • 0026329279 scopus 로고
    • First observations on enzymatic activity and protein content of vesicles separated from rat epididymal fluid
    • Fornés M.W., Barbieri A., Sosa M.A., Bertini F. First observations on enzymatic activity and protein content of vesicles separated from rat epididymal fluid. Andrologia 1991, 23:347-351.
    • (1991) Andrologia , vol.23 , pp. 347-351
    • Fornés, M.W.1    Barbieri, A.2    Sosa, M.A.3    Bertini, F.4
  • 22
    • 0016296440 scopus 로고
    • Decapacitation and recapacitation of rabbit spermatozoa treated with membrane vesicles from seminal plasma
    • Davis B.K. Decapacitation and recapacitation of rabbit spermatozoa treated with membrane vesicles from seminal plasma. J Reprod Fertil 1974, 41:241-244.
    • (1974) J Reprod Fertil , vol.41 , pp. 241-244
    • Davis, B.K.1
  • 23
    • 0020000457 scopus 로고
    • Characterization of Mg2+- and Ca2+-ATPase activity in membrane vesicles from ejaculated ram seminal plasma
    • Breitbart H., Rubinstein S. Characterization of Mg2+- and Ca2+-ATPase activity in membrane vesicles from ejaculated ram seminal plasma. Arch Androl 1982, 9:147-157.
    • (1982) Arch Androl , vol.9 , pp. 147-157
    • Breitbart, H.1    Rubinstein, S.2
  • 24
    • 0023137588 scopus 로고
    • Effect of secretory particles in bovine seminal vesicle secretion on sperm motility and acrosome reaction
    • Agrawal Y., Vanha-Perttula T. Effect of secretory particles in bovine seminal vesicle secretion on sperm motility and acrosome reaction. J Reprod Fertil 1987, 79:409-419.
    • (1987) J Reprod Fertil , vol.79 , pp. 409-419
    • Agrawal, Y.1    Vanha-Perttula, T.2
  • 25
  • 26
    • 0028096591 scopus 로고
    • Enhanced recruitment of motile spermatozoa by prostasome inclusion in swim-up medium
    • Fabiani R., Johansson L., Lundkvist O., Ronquist G. Enhanced recruitment of motile spermatozoa by prostasome inclusion in swim-up medium. Hum Reprod 1994, 9:1485-1489.
    • (1994) Hum Reprod , vol.9 , pp. 1485-1489
    • Fabiani, R.1    Johansson, L.2    Lundkvist, O.3    Ronquist, G.4
  • 27
    • 0030610318 scopus 로고    scopus 로고
    • Prostasome fraction of human seminal plasma prevents sperm from becoming acrosomally responsive to the agonist progesterone
    • Cross N.L., Mahasreshti P. Prostasome fraction of human seminal plasma prevents sperm from becoming acrosomally responsive to the agonist progesterone. Arch Androl 1997, 39:39-44.
    • (1997) Arch Androl , vol.39 , pp. 39-44
    • Cross, N.L.1    Mahasreshti, P.2
  • 28
    • 0242493102 scopus 로고    scopus 로고
    • Fusion of prostasomes to human spermatozoa stimulates the acrosome reaction
    • Palmerini C.A., Saccardi C., Carlini E., Fabiani R., Arienti G. Fusion of prostasomes to human spermatozoa stimulates the acrosome reaction. Fertil Steril 2003, 80:1181-1184.
    • (2003) Fertil Steril , vol.80 , pp. 1181-1184
    • Palmerini, C.A.1    Saccardi, C.2    Carlini, E.3    Fabiani, R.4    Arienti, G.5
  • 29
    • 81455142498 scopus 로고    scopus 로고
    • Prostasomes: inhibitors of capacitation and modulators of cellular signalling in human sperm
    • Pons-Rejraji H., Artonne C., Sion B., Brugnon F., Canis M., Janny L., et al. Prostasomes: inhibitors of capacitation and modulators of cellular signalling in human sperm. Int J Androl 2011, 34:568-580.
    • (2011) Int J Androl , vol.34 , pp. 568-580
    • Pons-Rejraji, H.1    Artonne, C.2    Sion, B.3    Brugnon, F.4    Canis, M.5    Janny, L.6
  • 30
    • 40749112313 scopus 로고    scopus 로고
    • Prostasome-like vesicles stimulate acrosome reaction of pig spermatozoa
    • Siciliano L., Marciano V., Carpino A. Prostasome-like vesicles stimulate acrosome reaction of pig spermatozoa. Reprod Biol Endocrinol 2008, 6:5.
    • (2008) Reprod Biol Endocrinol , vol.6 , pp. 5
    • Siciliano, L.1    Marciano, V.2    Carpino, A.3
  • 31
    • 79956148593 scopus 로고    scopus 로고
    • Prostasomes as potential modulators of tyrosine phosphorylation in human spermatozoa
    • Bechoua S., Rieu I., Sion B., Grizard G. Prostasomes as potential modulators of tyrosine phosphorylation in human spermatozoa. Syst Biol Reprod Med 2011, 57:139-148.
    • (2011) Syst Biol Reprod Med , vol.57 , pp. 139-148
    • Bechoua, S.1    Rieu, I.2    Sion, B.3    Grizard, G.4
  • 32
    • 0024391478 scopus 로고
    • Capacitation of bovine spermatozoa by lysophospholipids and trypsin
    • Wheeler M.B., Seidel G.E. Capacitation of bovine spermatozoa by lysophospholipids and trypsin. Gamete Res 1989, 22:193-204.
    • (1989) Gamete Res , vol.22 , pp. 193-204
    • Wheeler, M.B.1    Seidel, G.E.2
  • 33
    • 0033061672 scopus 로고    scopus 로고
    • Simple histochemical stain for acrosomes on sperm from several species
    • Larson J.L., Miller D.J. Simple histochemical stain for acrosomes on sperm from several species. Mol Reprod Dev 1999, 52:445-449.
    • (1999) Mol Reprod Dev , vol.52 , pp. 445-449
    • Larson, J.L.1    Miller, D.J.2
  • 34
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 36
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko A., Wilm M., Vorm O., Mann M. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal Chem 1996, 68:850-858.
    • (1996) Anal Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 37
    • 0019216903 scopus 로고
    • Evaluation of the purity of boar sperm plasma membranes prepared by nitrogen cavitation
    • Peterson R., Russell L., Bundman D., Freund M. Evaluation of the purity of boar sperm plasma membranes prepared by nitrogen cavitation. Biol Reprod 1980, 23:637-645.
    • (1980) Biol Reprod , vol.23 , pp. 637-645
    • Peterson, R.1    Russell, L.2    Bundman, D.3    Freund, M.4
  • 38
    • 0001061501 scopus 로고
    • Lipid spin labels in biological membranes
    • Academic Press, New York, L.J. Berliner (Ed.)
    • Griffith O.H., Jost P.J. Lipid spin labels in biological membranes. Spin labeling, theory and applications 1976, 453-523. Academic Press, New York. L.J. Berliner (Ed.).
    • (1976) Spin labeling, theory and applications , pp. 453-523
    • Griffith, O.H.1    Jost, P.J.2
  • 39
    • 0018871935 scopus 로고
    • Isolation, physicochemical properties, and macromolecular composition of zona pellucida from porcine oocytes
    • Dunbar B.S., Wardrip N.J., Hedrick J.L. Isolation, physicochemical properties, and macromolecular composition of zona pellucida from porcine oocytes. Biochemistry 1980, 19:356-365.
    • (1980) Biochemistry , vol.19 , pp. 356-365
    • Dunbar, B.S.1    Wardrip, N.J.2    Hedrick, J.L.3
  • 40
    • 0023868452 scopus 로고
    • A quantitative assay for capacitation: evaluation of multiple sperm penetration through the zona pellucida of salt-stored hamster eggs
    • Boatman D.E., Andrews J.C., Bavister B.D. A quantitative assay for capacitation: evaluation of multiple sperm penetration through the zona pellucida of salt-stored hamster eggs. Gamete Res 1988, 19:19-29.
    • (1988) Gamete Res , vol.19 , pp. 19-29
    • Boatman, D.E.1    Andrews, J.C.2    Bavister, B.D.3
  • 41
    • 0023942614 scopus 로고
    • The hemizona assay (HZA): development of a diagnostic test for the binding of human spermatozoa to the human hemizona pellucida to predict fertilization potential
    • Burkman L.J., Coddington C.C., Franken D.R., Krugen T.F., Rosenwaks Z., Hogen G.D. The hemizona assay (HZA): development of a diagnostic test for the binding of human spermatozoa to the human hemizona pellucida to predict fertilization potential. Fertil Steril 1988, 49:688-697.
    • (1988) Fertil Steril , vol.49 , pp. 688-697
    • Burkman, L.J.1    Coddington, C.C.2    Franken, D.R.3    Krugen, T.F.4    Rosenwaks, Z.5    Hogen, G.D.6
  • 42
    • 0020467462 scopus 로고
    • A zinc-dependent peptidase in prostatic organelles present in seminal plasma
    • Laurell C.B., Weiber H., Ohlsson K., Rannevik G. A zinc-dependent peptidase in prostatic organelles present in seminal plasma. Clin Chim Acta 1982, 126:161-170.
    • (1982) Clin Chim Acta , vol.126 , pp. 161-170
    • Laurell, C.B.1    Weiber, H.2    Ohlsson, K.3    Rannevik, G.4
  • 44
    • 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., Ning X., Fornes M.W., Alvarez J.G., Stein P., Connors S.A., 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 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
  • 46
    • 80053384968 scopus 로고    scopus 로고
    • Comparative proteome and lipid profiles of bovine epididymosomes collected in the intraluminal compartment of the caput and cauda epididymidis
    • Girouard J., Frenette G., Sullivan R. Comparative proteome and lipid profiles of bovine epididymosomes collected in the intraluminal compartment of the caput and cauda epididymidis. Int J Androl 2011, 34:e475-e486.
    • (2011) Int J Androl , vol.34
    • Girouard, J.1    Frenette, G.2    Sullivan, R.3
  • 48
    • 18844430042 scopus 로고    scopus 로고
    • Identification, proteomic profiling, and origin of ram epididymal fluid exosome-like vesicles
    • Gatti J.L., Metayer S., Belghazi M., Dacheux F., Dacheux J.L. Identification, proteomic profiling, and origin of ram epididymal fluid exosome-like vesicles. Biol Reprod 2005, 72:1452-1465.
    • (2005) Biol Reprod , vol.72 , pp. 1452-1465
    • Gatti, J.L.1    Metayer, S.2    Belghazi, M.3    Dacheux, F.4    Dacheux, J.L.5
  • 49
    • 16344366170 scopus 로고    scopus 로고
    • Changes in tyrosine phosphorylation associated with true capacitation and capacitation-like state in boar spermatozoa
    • Bravo M.M., Aparicio I.M., Garcia-Herreros M., Gil M.C., Pena F.J., Garcia-Marin L.J. Changes in tyrosine phosphorylation associated with true capacitation and capacitation-like state in boar spermatozoa. Mol Reprod Dev 2005, 71:88-96.
    • (2005) Mol Reprod Dev , vol.71 , pp. 88-96
    • Bravo, M.M.1    Aparicio, I.M.2    Garcia-Herreros, M.3    Gil, M.C.4    Pena, F.J.5    Garcia-Marin, L.J.6
  • 50
    • 0642343056 scopus 로고    scopus 로고
    • The importance of calcium in the appearance of p32, a boar sperm tyrosine phosphoprotein, during in vitro capacitation
    • Dube C., Tardif S., Leclerc P., Bailey J.L. The importance of calcium in the appearance of p32, a boar sperm tyrosine phosphoprotein, during in vitro capacitation. J Androl 2003, 24:727-733.
    • (2003) J Androl , vol.24 , pp. 727-733
    • Dube, C.1    Tardif, S.2    Leclerc, P.3    Bailey, J.L.4
  • 51
    • 0031687185 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphorylation in boar sperm through a cAMP-dependent pathway
    • Kalab P., Peknicova J., Geussova G., Moos J. Regulation of protein tyrosine phosphorylation in boar sperm through a cAMP-dependent pathway. Mol Reprod Dev 1998, 51:304-314.
    • (1998) Mol Reprod Dev , vol.51 , pp. 304-314
    • Kalab, P.1    Peknicova, J.2    Geussova, G.3    Moos, J.4
  • 52
    • 0034887719 scopus 로고    scopus 로고
    • Capacitation is associated with tyrosine phosphorylation and tyrosine kinase-like activity of pig sperm proteins
    • Tardif S., Dube C., Chevalier S., Bailey J.L. Capacitation is associated with tyrosine phosphorylation and tyrosine kinase-like activity of pig sperm proteins. Biol Reprod 2001, 65:784-792.
    • (2001) Biol Reprod , vol.65 , pp. 784-792
    • Tardif, S.1    Dube, C.2    Chevalier, S.3    Bailey, J.L.4
  • 53
    • 0037230256 scopus 로고    scopus 로고
    • Porcine sperm capacitation and tyrosine kinase activity are dependent on bicarbonate and calcium but protein tyrosine phosphorylation is only associated with calcium
    • Tardif S., Dube C., Bailey J.L. Porcine sperm capacitation and tyrosine kinase activity are dependent on bicarbonate and calcium but protein tyrosine phosphorylation is only associated with calcium. Biol Reprod 2003, 68:207-213.
    • (2003) Biol Reprod , vol.68 , pp. 207-213
    • Tardif, S.1    Dube, C.2    Bailey, J.L.3
  • 54
    • 80052947283 scopus 로고    scopus 로고
    • Impact of epididymal maturation, ejaculation and in vitro capacitation on tyrosine phosphorylation patterns exhibited of boar (Sus domesticus) spermatozoa
    • Fabrega A., Puigmule M., Yeste M., Casas I., Bonet S., Pinart E. Impact of epididymal maturation, ejaculation and in vitro capacitation on tyrosine phosphorylation patterns exhibited of boar (Sus domesticus) spermatozoa. Theriogenology 2011, 76:1356-1366.
    • (2011) Theriogenology , vol.76 , pp. 1356-1366
    • Fabrega, A.1    Puigmule, M.2    Yeste, M.3    Casas, I.4    Bonet, S.5    Pinart, E.6
  • 55
    • 0033533489 scopus 로고    scopus 로고
    • Capacitation induces tyrosine phosphorylation of proteins in the boar sperm plasma membrane
    • Flesch F.M., Colenbrander B., van Golde L.M., Gadella B.M. Capacitation induces tyrosine phosphorylation of proteins in the boar sperm plasma membrane. Biochem Biophys Res Commun 1999, 262:787-792.
    • (1999) Biochem Biophys Res Commun , vol.262 , pp. 787-792
    • Flesch, F.M.1    Colenbrander, B.2    van Golde, L.M.3    Gadella, B.M.4
  • 56
    • 20544432079 scopus 로고    scopus 로고
    • The proacrosin binding protein, sp32, is tyrosine phosphorylated during capacitation of pig sperm
    • Dube C., Leclerc P., Baba T., Reyes-Moreno C., Bailey J.L. The proacrosin binding protein, sp32, is tyrosine phosphorylated during capacitation of pig sperm. J Androl 2005, 26:519-528.
    • (2005) J Androl , vol.26 , pp. 519-528
    • Dube, C.1    Leclerc, P.2    Baba, T.3    Reyes-Moreno, C.4    Bailey, J.L.5
  • 57
    • 0020666396 scopus 로고
    • Binding by glycoproteins of seminal plasma membrane vesicles accelerates decapacitation in rabbit spermatozoa
    • Davis B.K., Davis N.V. Binding by glycoproteins of seminal plasma membrane vesicles accelerates decapacitation in rabbit spermatozoa. Biochim Biophys Acta 1983, 727:70-76.
    • (1983) Biochim Biophys Acta , vol.727 , pp. 70-76
    • Davis, B.K.1    Davis, N.V.2
  • 58
    • 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 D.A., Mitchell L.A., Gibbs G.M., O'Bryan M., Aitken R.J. 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
  • 59
    • 0032732658 scopus 로고    scopus 로고
    • Regulation of human sperm capacitation by a cholesterol efflux-stimulated signal transduction pathway leading to protein kinase A-mediated up-regulation of protein tyrosine phosphorylation
    • Osheroff J.E., Visconti P.E., Valenzuela J.P., Travis A.J., Alvarez J., Kopf G.S. Regulation of human sperm capacitation by a cholesterol efflux-stimulated signal transduction pathway leading to protein kinase A-mediated up-regulation of protein tyrosine phosphorylation. Mol Hum Reprod 1999, 5:1017-1026.
    • (1999) Mol Hum Reprod , vol.5 , pp. 1017-1026
    • Osheroff, J.E.1    Visconti, P.E.2    Valenzuela, J.P.3    Travis, A.J.4    Alvarez, J.5    Kopf, G.S.6
  • 60
    • 0029813137 scopus 로고    scopus 로고
    • Unesterified cholesterol content of human sperm regulates the response of the acrosome to the agonist, progesterone
    • Zarintash R.J., Cross N.L. Unesterified cholesterol content of human sperm regulates the response of the acrosome to the agonist, progesterone. Biol Reprod 1996, 55:19-24.
    • (1996) Biol Reprod , vol.55 , pp. 19-24
    • Zarintash, R.J.1    Cross, N.L.2
  • 61
    • 0024031405 scopus 로고
    • Cholesterol efflux from bovine sperm. I. Induction of the acrosome reaction with lysophosphatidylcholine after reducing sperm cholesterol
    • Ehrenwald E., Parks J.E., Foote R.H. Cholesterol efflux from bovine sperm. I. Induction of the acrosome reaction with lysophosphatidylcholine after reducing sperm cholesterol. Gamete Res 1988, 20:145-157.
    • (1988) Gamete Res , vol.20 , pp. 145-157
    • Ehrenwald, E.1    Parks, J.E.2    Foote, R.H.3
  • 62
    • 0031770661 scopus 로고    scopus 로고
    • Cyclodextrin removes cholesterol from mouse sperm and induces capacitation in a protein-free medium
    • Choi Y.H., Toyoda Y. Cyclodextrin removes cholesterol from mouse sperm and induces capacitation in a protein-free medium. Biol Reprod 1998, 59:1328-1333.
    • (1998) Biol Reprod , vol.59 , pp. 1328-1333
    • Choi, Y.H.1    Toyoda, Y.2
  • 63
    • 0028725566 scopus 로고
    • Functional and biochemical characteristics of human prostasomes. Minireview based on a doctoral thesis
    • Fabiani R. Functional and biochemical characteristics of human prostasomes. Minireview based on a doctoral thesis. Ups J Med Sci 1994, 99:73-111.
    • (1994) Ups J Med Sci , vol.99 , pp. 73-111
    • Fabiani, R.1
  • 64
    • 0035173281 scopus 로고    scopus 로고
    • Incorporating lipids into boar sperm decreases chilling sensitivity but not capacitation potential
    • He L., Bailey J.L., Buhr M.M. Incorporating lipids into boar sperm decreases chilling sensitivity but not capacitation potential. Biol Reprod 2001, 64:69-79.
    • (2001) Biol Reprod , vol.64 , pp. 69-79
    • He, L.1    Bailey, J.L.2    Buhr, M.M.3
  • 65
    • 27744516733 scopus 로고    scopus 로고
    • Lysophosphatidylcholine, a component of atherogenic lipoproteins, induces the change of calcium mobilization via TRPC ion channels in cultured human corporal smooth muscle cells
    • So I., Chae M.R., Kim S.J., Lee S.W. Lysophosphatidylcholine, a component of atherogenic lipoproteins, induces the change of calcium mobilization via TRPC ion channels in cultured human corporal smooth muscle cells. Int J Impot Res 2005, 17:475-483.
    • (2005) Int J Impot Res , vol.17 , pp. 475-483
    • So, I.1    Chae, M.R.2    Kim, S.J.3    Lee, S.W.4
  • 66
    • 0342800102 scopus 로고
    • Timing of fertilization in mammals: sperm cholesterol/phospholipid ratio as a determinant of the capacitation interval
    • Davis B.K. Timing of fertilization in mammals: sperm cholesterol/phospholipid ratio as a determinant of the capacitation interval. Proc Natl Acad Sci U S A 1981, 78:7560-7564.
    • (1981) Proc Natl Acad Sci U S A , vol.78 , pp. 7560-7564
    • Davis, B.K.1
  • 67
    • 0001002614 scopus 로고
    • Cholesterol efflux from mammalian sperm and its potential role in capacitation
    • Serono Symposia, Norwell, MA, B.D. Bavister, J. Cummins, E.R.S. Roldan (Eds.)
    • Parks JE., Ehrenwald E. Cholesterol efflux from mammalian sperm and its potential role in capacitation. Fertilization in Mammals 1990, 155-167. Serono Symposia, Norwell, MA. B.D. Bavister, J. Cummins, E.R.S. Roldan (Eds.).
    • (1990) Fertilization in Mammals , pp. 155-167
    • Parks, J.E.1    Ehrenwald, E.2
  • 68
    • 0030831291 scopus 로고    scopus 로고
    • Transfer of CD26/dipeptidyl peptidase IV (E.C. 3.5.4.4) from prostasomes to sperm
    • Arienti G., Polci A., Carlini E., Palmerini C.A. Transfer of CD26/dipeptidyl peptidase IV (E.C. 3.5.4.4) from prostasomes to sperm. FEBS Lett 1997, 410:343-346.
    • (1997) FEBS Lett , vol.410 , pp. 343-346
    • Arienti, G.1    Polci, A.2    Carlini, E.3    Palmerini, C.A.4
  • 70
    • 34447254517 scopus 로고    scopus 로고
    • Epididymosomes are involved in the acquisition of new sperm proteins during epididymal transit
    • Sullivan R., Frenette G., Girouard J. Epididymosomes are involved in the acquisition of new sperm proteins during epididymal transit. Asian J Androl 2007, 9:483-491.
    • (2007) Asian J Androl , vol.9 , pp. 483-491
    • Sullivan, R.1    Frenette, G.2    Girouard, J.3
  • 71
    • 77956124980 scopus 로고    scopus 로고
    • Characterization of two distinct populations of epididymosomes collected in the intraluminal compartment of the bovine cauda epididymis
    • Frenette G., Girouard J., D'amours O., Allard N., Tessier L., Sullivan R. Characterization of two distinct populations of epididymosomes collected in the intraluminal compartment of the bovine cauda epididymis. Biol Reprod 2010, 83:473-480.
    • (2010) Biol Reprod , vol.83 , pp. 473-480
    • Frenette, G.1    Girouard, J.2    D'amours, O.3    Allard, N.4    Tessier, L.5    Sullivan, R.6
  • 72
    • 0031034693 scopus 로고    scopus 로고
    • Fusion of human sperm to prostasomes at acidic pH
    • Arienti G., Carlini E., Palmerini C.A. Fusion of human sperm to prostasomes at acidic pH. J Membr Biol 1997, 155:89-94.
    • (1997) J Membr Biol , vol.155 , pp. 89-94
    • Arienti, G.1    Carlini, E.2    Palmerini, C.A.3
  • 73


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.