메뉴 건너뛰기




Volumn 56, Issue 3, 1997, Pages 707-719

Regulation of protein tyrosine phosphorylation during bovine sperm capacitation by a cyclic adenosine 3',5'-monophosphate-dependent pathway

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP; HEPARIN; PROTEIN TYROSINE KINASE;

EID: 0031049037     PISSN: 00063363     EISSN: None     Source Type: Journal    
DOI: 10.1095/biolreprod56.3.707     Document Type: Article
Times cited : (361)

References (65)
  • 1
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • Knobil E, Neill JD (eds.), New York, NY: Raven Press LTD
    • Yanagimachi R. Mammalian fertilization. In: Knobil E, Neill JD (eds.), The Physiology of Reproduction. New York, NY: Raven Press LTD; 1994: 189-317.
    • (1994) The Physiology of Reproduction , pp. 189-317
    • Yanagimachi, R.1
  • 2
    • 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
  • 3
    • 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 B 1951; 4:581-596.
    • (1951) Aust J Sci Res B , vol.4 , pp. 581-596
    • Austin, C.R.1
  • 4
    • 0003178422 scopus 로고
    • The "capacitation" of the mammalian sperm
    • Austin CR. The "capacitation" of the mammalian sperm. Nature 1952; 170:326.
    • (1952) Nature , vol.170 , pp. 326
    • Austin, C.R.1
  • 5
    • 0021160724 scopus 로고
    • Determination of the time course of capacitation in mouse spermatozoa using a chlortetracycline fluorescence assay
    • Ward CR, Storey BT. Determination of the time course of capacitation in mouse spermatozoa using a chlortetracycline fluorescence assay. Dev Biol 1984; 104:287-296.
    • (1984) Dev Biol , vol.104 , pp. 287-296
    • Ward, C.R.1    Storey, B.T.2
  • 6
    • 0001817515 scopus 로고
    • Progress toward understanding the molecular basis of capacitation
    • Wassarman PM (ed.), Boca Ratan, FL: CRC Press
    • Florman HM, Babcock DF. Progress toward understanding the molecular basis of capacitation. In: Wassarman PM (ed.), Elements of Mammalian Fertilization. Boca Ratan, FL: CRC Press; 1991: 105-132.
    • (1991) Elements of Mammalian Fertilization , pp. 105-132
    • Florman, H.M.1    Babcock, D.F.2
  • 7
    • 0001604580 scopus 로고
    • The mammalian sperm acrosome and the acrosome reaction
    • Wassarman PM (ed.), Boca Ratan, FL: CRC Press
    • Kopf GS, Gerton GL. The mammalian sperm acrosome and the acrosome reaction. In: Wassarman PM (ed.), Elements of Mammalian Fertilization. Boca Ratan, FL: CRC Press; 1991: 153-203.
    • (1991) Elements of Mammalian Fertilization , pp. 153-203
    • Kopf, G.S.1    Gerton, G.L.2
  • 8
    • 0028804984 scopus 로고
    • Sperm membrane potential: Hyperpolarization during capacitation regulates zona pellucida-dependent acrosomal secretion
    • Zeng Y, Clark EN, Florman HM. Sperm membrane potential: hyperpolarization during capacitation regulates zona pellucida-dependent acrosomal secretion. Dev Biol 1995; 171:554-563.
    • (1995) Dev Biol , vol.171 , pp. 554-563
    • Zeng, Y.1    Clark, E.N.2    Florman, H.M.3
  • 10
    • 0020363444 scopus 로고
    • Structural comparisons among glycosaminoglycans to promote acrosome reaction in bovine spermatozoa
    • Handrow RR, Lenz RW, Ax RL. Structural comparisons among glycosaminoglycans to promote acrosome reaction in bovine spermatozoa. Biochem Biophys Res Commun 1982; 107:1326-1332.
    • (1982) Biochem Biophys Res Commun , vol.107 , pp. 1326-1332
    • Handrow, R.R.1    Lenz, R.W.2    Ax, R.L.3
  • 11
    • 0022773741 scopus 로고
    • Glycosaminoglycans in ewe reproductive tracts and their influence on acrosome reactions in bovine spermatozoa in vitro
    • Lee CN, Clayton MK, Bushmeyer SM, First NL, Ax RL. Glycosaminoglycans in ewe reproductive tracts and their influence on acrosome reactions in bovine spermatozoa in vitro. J Anim Sci 1986; 63:861-867.
    • (1986) J Anim Sci , vol.63 , pp. 861-867
    • Lee, C.N.1    Clayton, M.K.2    Bushmeyer, S.M.3    First, N.L.4    Ax, R.L.5
  • 12
    • 0024843557 scopus 로고
    • Effect of sulfated glycoconjugates on capacitation and the acrosome reaction of bovine and hamster spermatozoa
    • Parrish JJ, Susko-Parrish JL, Handrow RR, Ax RL, First NL. Effect of sulfated glycoconjugates on capacitation and the acrosome reaction of bovine and hamster spermatozoa Gamete Res 1989; 24:403-413.
    • (1989) Gamete Res , vol.24 , pp. 403-413
    • Parrish, J.J.1    Susko-Parrish, J.L.2    Handrow, R.R.3    Ax, R.L.4    First, N.L.5
  • 14
    • 0025284297 scopus 로고
    • Heparin-binding proteins from seminal plasma bind to bovine spermatozoa and modulate capacitation by heparin
    • Miller DJ, Winer MA, Ax RL. Heparin-binding proteins from seminal plasma bind to bovine spermatozoa and modulate capacitation by heparin. Biol Reprod 1990; 42:899-915.
    • (1990) Biol Reprod , vol.42 , pp. 899-915
    • Miller, D.J.1    Winer, M.A.2    Ax, R.L.3
  • 15
    • 0029008083 scopus 로고
    • Phosphatidylcholine-binding proteins of bovine seminal plasma modulate capacitation of spermatozoa by heparin
    • Therien I, Bleau G, Manjunath P. Phosphatidylcholine-binding proteins of bovine seminal plasma modulate capacitation of spermatozoa by heparin. Biol Reprod 1995; 52:1372-1379.
    • (1995) Biol Reprod , vol.52 , pp. 1372-1379
    • Therien, I.1    Bleau, G.2    Manjunath, P.3
  • 16
    • 0023522461 scopus 로고
    • 2+ uptake by guinea pig epididymal spermatozoa
    • 2+ uptake by guinea pig epididymal spermatozoa. Biol Reprod 1987; 37:1097-1107.
    • (1987) Biol Reprod , vol.37 , pp. 1097-1107
    • Coronel, C.E.1    Lardy, H.A.2
  • 17
    • 0024845616 scopus 로고
    • Calcium requirement and increased association with bovine sperm during capacitation by heparin
    • Handrow RR, First NL, Parrish JJ. Calcium requirement and increased association with bovine sperm during capacitation by heparin. J Exp Zool 1989; 252:174-182.
    • (1989) J Exp Zool , vol.252 , pp. 174-182
    • Handrow, R.R.1    First, N.L.2    Parrish, J.J.3
  • 18
    • 0024828501 scopus 로고
    • Capacitation of bovine sperm by heparin: Inhibitory effect of glucose and role of intracellular pH
    • Parrish JJ, Susko-Parrish JL, First NL. Capacitation of bovine sperm by heparin: inhibitory effect of glucose and role of intracellular pH. Biol Reprod 1989; 41:683-699.
    • (1989) Biol Reprod , vol.41 , pp. 683-699
    • Parrish, J.J.1    Susko-Parrish, J.L.2    First, N.L.3
  • 19
    • 0018894016 scopus 로고
    • The regulation of spermatozoa by calcium and cyclic nucleotides
    • Garbers DL, Kopf GS. The regulation of spermatozoa by calcium and cyclic nucleotides. Adv Cyclic Nucleotide Res 1980; 13:251-306.
    • (1980) Adv Cyclic Nucleotide Res , vol.13 , pp. 251-306
    • Garbers, D.L.1    Kopf, G.S.2
  • 20
    • 0020623097 scopus 로고
    • Cyclic adenosine 3′,5′ monophosphate, calcium and protein phosphorylation in flagellar motility
    • Tash JS, Means AR. Cyclic adenosine 3′,5′ monophosphate, calcium and protein phosphorylation in flagellar motility. Biol Reprod 1983; 28: 75-104.
    • (1983) Biol Reprod , vol.28 , pp. 75-104
    • Tash, J.S.1    Means, A.R.2
  • 21
    • 84907123783 scopus 로고
    • Regulation of mammalian sperm motility
    • Lindemann CB, Kanous KS. Regulation of mammalian sperm motility. Arch Androl 1989; 23:1-22.
    • (1989) Arch Androl , vol.23 , pp. 1-22
    • Lindemann, C.B.1    Kanous, K.S.2
  • 22
    • 0020574820 scopus 로고
    • Adenylate cyclase activity in porcine sperm in response to female reproductive tract secretions
    • Berger T, Clegg ED. Adenylate cyclase activity in porcine sperm in response to female reproductive tract secretions. Gamete Res 1983; 7: 169-177.
    • (1983) Gamete Res , vol.7 , pp. 169-177
    • Berger, T.1    Clegg, E.D.2
  • 23
    • 0021707391 scopus 로고
    • Cyclic nucleotide metabolism in mouse epididymal spermatozoa during capacitation in vitro
    • Stein DM, Fraser LR. Cyclic nucleotide metabolism in mouse epididymal spermatozoa during capacitation in vitro. Gamete Res 1984; 10: 283-299.
    • (1984) Gamete Res , vol.10 , pp. 283-299
    • Stein, D.M.1    Fraser, L.R.2
  • 24
    • 0022490254 scopus 로고
    • Adenylate cyclase activity of mouse sperm during capacitation in vitro: Effect of calcium and a GTP analogue
    • Monks NJ, Stein DM, Fraser LR. Adenylate cyclase activity of mouse sperm during capacitation in vitro: effect of calcium and a GTP analogue. Int J Androl 1986; 9:67-76.
    • (1986) Int J Androl , vol.9 , pp. 67-76
    • Monks, N.J.1    Stein, D.M.2    Fraser, L.R.3
  • 25
    • 0028936801 scopus 로고
    • Capacitation of mouse spermatozoa: II. Protein tyrosinephosphorylation and capacitation are regulated by a cAMP-dependent pathway
    • Visconti PE, Moore GD, Bailey JL, Leclerc P, Connors SA, Pan D, Olds-Clarke P, Kopf GS. Capacitation of mouse spermatozoa: II. Protein tyrosinephosphorylation and capacitation are regulated by a cAMP-dependent pathway. Development 1995; 121:1139-1150.
    • (1995) Development , vol.121 , pp. 1139-1150
    • Visconti, P.E.1    Moore, G.D.2    Bailey, J.L.3    Leclerc, P.4    Connors, S.A.5    Pan, D.6    Olds-Clarke, P.7    Kopf, G.S.8
  • 26
    • 0028061888 scopus 로고
    • Differences in the role of cyclic adenosine 3′,5′-monophosphate during capacitation of bovine sperm by heparin or oviduct fluid
    • Parrish JJ, Susko-Parrish JL, Uguz C, First NL. Differences in the role of cyclic adenosine 3′,5′-monophosphate during capacitation of bovine sperm by heparin or oviduct fluid. Biol Reprod 1994; 51:1099-1108.
    • (1994) Biol Reprod , vol.51 , pp. 1099-1108
    • Parrish, J.J.1    Susko-Parrish, J.L.2    Uguz, C.3    First, N.L.4
  • 27
    • 0028072139 scopus 로고
    • Heparin-induced capacitation but not intracellular alkalinization of bovine sperm is inhibited by Rp-adenosine-3′,5′-cyclic monophosphorothioate
    • Uguz C, Vredenburgh WL, Parrish JJ. Heparin-induced capacitation but not intracellular alkalinization of bovine sperm is inhibited by Rp-adenosine-3′,5′-cyclic monophosphorothioate. Biol Reprod 1994; 51:1031-1039.
    • (1994) Biol Reprod , vol.51 , pp. 1031-1039
    • Uguz, C.1    Vredenburgh, W.L.2    Parrish, J.J.3
  • 28
    • 0025653672 scopus 로고
    • Cyclic nucleotides and mammalian sperm capacitation
    • Fraser LR, Monks NJ. Cyclic nucleotides and mammalian sperm capacitation. J Reprod Fertil Suppl 1990; 42:9-21.
    • (1990) J Reprod Fertil Suppl , vol.42 , pp. 9-21
    • Fraser, L.R.1    Monks, N.J.2
  • 29
    • 0024614764 scopus 로고
    • Phorbol esters stimulate cyclic adenosine 3′,5′ monophosphate accumulation in hamster spermatozoa during in vitro capacitation
    • Visconti P, Tezon JG. Phorbol esters stimulate cyclic adenosine 3′,5′ 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.1    Tezon, J.G.2
  • 30
    • 0021238674 scopus 로고
    • Stimulation of rhesus monkey sperm capacitation by cyclic nucleotide mediators
    • Boatman DE, Bavister BD. Stimulation of rhesus monkey sperm capacitation by cyclic nucleotide mediators. J Reprod Fertil 1984; 71:357-366.
    • (1984) J Reprod Fertil , vol.71 , pp. 357-366
    • Boatman, D.E.1    Bavister, B.D.2
  • 31
    • 0028316159 scopus 로고
    • Separate effects of caffeine and dbcAMP on macaque sperm motility and interaction with the zona pellucida
    • Vandevoort CA, Tollner TL, Overstreet JW. Separate effects of caffeine and dbcAMP on macaque sperm motility and interaction with the zona pellucida. Mol Reprod Dev 1994; 37:299-304.
    • (1994) Mol Reprod Dev , vol.37 , pp. 299-304
    • Vandevoort, C.A.1    Tollner, T.L.2    Overstreet, J.W.3
  • 32
    • 0024356430 scopus 로고
    • 95 kd sperm proteins bind ZP3 and serve as tyrosine kinase substrates in response to zona binding
    • Leyton L, Saling P. 95 kd sperm proteins bind ZP3 and serve as tyrosine kinase substrates in response to zona binding. Cell 1989; 57:1123-1130.
    • (1989) Cell , vol.57 , pp. 1123-1130
    • Leyton, L.1    Saling, P.2
  • 33
    • 0027510718 scopus 로고
    • r 95 000 phosphotyrosine-containing protein
    • r 95 000 phosphotyrosine-containing protein. J Reprod Fertil 1993; 97:287-299.
    • (1993) J Reprod Fertil , vol.97 , pp. 287-299
    • Duncan, A.E.1    Fraser, L.R.2
  • 34
    • 0028957362 scopus 로고
    • Capacitation of mouse spermatozoa: I. 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: 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
  • 35
    • 0029792629 scopus 로고    scopus 로고
    • Cyclic 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. Cyclic adenosine 3′,5′-monophosphate-dependent regulation of protein tyrosine phosphorylation in relation to human sperm capacitation and motility. Biol Reprod 1996; 55:684-692.
    • (1996) Biol Reprod , vol.55 , pp. 684-692
    • Leclerc, P.1    De Lamirande, E.2    Gagnon, C.3
  • 36
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 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
  • 37
    • 0028934067 scopus 로고
    • Capacitation in vitro of stallion spermatozoa: Comparison of progesterone-induced acrosome reactions in fertile and subfertile males
    • Meyers SA, Overstreet JW, Liu IKM, Drobnis EZ. Capacitation in vitro of stallion spermatozoa: comparison of progesterone-induced acrosome reactions in fertile and subfertile males. J Androl 1995; 16:47-54.
    • (1995) J Androl , vol.16 , pp. 47-54
    • Meyers, S.A.1    Overstreet, J.W.2    Liu, I.K.M.3    Drobnis, E.Z.4
  • 38
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin TH, Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 1979; 76:4358-4364.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4358-4364
    • Towbin, H.1    Staehelin, T.H.2    Gordon, J.3
  • 39
    • 0028111490 scopus 로고
    • p95, the major phosphotyrosine containing protein in mouse spermatozoa, is a hexokinase with unique properties
    • Kalab P, Visconti P, Leclerc P, Kopf GS. p95, the major phosphotyrosine containing protein in mouse spermatozoa, is a hexokinase with unique properties. J Biol Chem 1994; 269:3810-3817.
    • (1994) J Biol Chem , vol.269 , pp. 3810-3817
    • Kalab, P.1    Visconti, P.2    Leclerc, P.3    Kopf, G.S.4
  • 40
    • 0023715942 scopus 로고
    • The regulation of acrosomal exocytosis: I. Sperm capacitation is required for the induction of acrosome reactions by the bovine zona pellucida in vitro
    • Florman HM, First NL. The regulation of acrosomal exocytosis: I. Sperm capacitation is required for the induction of acrosome reactions by the bovine zona pellucida in vitro. Dev Biol 1988; 128:453-463.
    • (1988) Dev Biol , vol.128 , pp. 453-463
    • Florman, H.M.1    First, N.L.2
  • 41
    • 0025248571 scopus 로고
    • Inhibition of forskolin-induced neurite outgrowth and protein phosphorylation by a newly synthesized selective inhibitor of cyclic AMP-dependent protein kinase. N-[2-(p-bromocinnamylamino) ethyl]-5-isoquinolinesulfonamide (H-89), of PC12D pheochromocytoma cells
    • Chijiwa T, Mishima A, Hagiwara M, Sano M, Hayashi K, Inoue T, Naito K, Toshioko T, Hidaka H. Inhibition of forskolin-induced neurite outgrowth and protein phosphorylation by a newly synthesized selective inhibitor of cyclic AMP-dependent protein kinase. N-[2-(p-bromocinnamylamino) ethyl]-5-isoquinolinesulfonamide (H-89), of PC12D pheochromocytoma cells. J Biol Chem 1990; 265:5267-5272.
    • (1990) J Biol Chem , vol.265 , pp. 5267-5272
    • Chijiwa, T.1    Mishima, A.2    Hagiwara, M.3    Sano, M.4    Hayashi, K.5    Inoue, T.6    Naito, K.7    Toshioko, T.8    Hidaka, H.9
  • 42
    • 0027297159 scopus 로고
    • Molecular events mediating sperm activation
    • Ward CR, Kopf GS. Molecular events mediating sperm activation. Dev Biol 1993; 158:9-34.
    • (1993) Dev Biol , vol.158 , pp. 9-34
    • Ward, C.R.1    Kopf, G.S.2
  • 43
    • 0019028155 scopus 로고
    • Calcium and a fucose-sulfate-rich polymer regulate sperm cyclic nucleotide metabolism and the acrosome reaction
    • Kopf GS, Garbers DL. Calcium and a fucose-sulfate-rich polymer regulate sperm cyclic nucleotide metabolism and the acrosome reaction. Biol Reprod 1980; 22:1118-1126.
    • (1980) Biol Reprod , vol.22 , pp. 1118-1126
    • Kopf, G.S.1    Garbers, D.L.2
  • 44
    • 0029030462 scopus 로고
    • Mouse sperm adenylyl cyclase: General properties and regulation by the zona pellucida
    • Leclerc P, Kopf GS. Mouse sperm adenylyl cyclase: general properties and regulation by the zona pellucida. Biol Reprod 1995; 52:1227-1233.
    • (1995) Biol Reprod , vol.52 , pp. 1227-1233
    • Leclerc, P.1    Kopf, G.S.2
  • 45
    • 0016775686 scopus 로고
    • The effect of divalent cations on bovine spermatozoal adenylate cyclase activity
    • Braun T. The effect of divalent cations on bovine spermatozoal adenylate cyclase activity. J Cyclic Nucleotide Res 1975; 1:227-281.
    • (1975) J Cyclic Nucleotide Res , vol.1 , pp. 227-281
    • Braun, T.1
  • 46
    • 0020000349 scopus 로고
    • ++-induced elevations of cyclic AMP in guinea pig spermatozoa
    • ++-induced elevations of cyclic AMP in guinea pig spermatozoa. J Biol Chem 1982; 257:8980-8984.
    • (1982) J Biol Chem , vol.257 , pp. 8980-8984
    • Garbers, D.L.1    Tubb, D.J.2    Hyne, R.V.3
  • 47
    • 0018604999 scopus 로고
    • Regulation of guinea pig sperm adenylate cyclase by calcium
    • Hyne RV, Garbers DL. Regulation of guinea pig sperm adenylate cyclase by calcium. Biol Reprod 1979; 21:1135-1142.
    • (1979) Biol Reprod , vol.21 , pp. 1135-1142
    • Hyne, R.V.1    Garbers, D.L.2
  • 48
    • 0022354346 scopus 로고
    • Characterization of a calcium-modulated adenylate cyclase from abalone sperm
    • Kopf GS, Vacquier VD. Characterization of a calcium-modulated adenylate cyclase from abalone sperm. Biol Reprod 1985; 33:1094-1104.
    • (1985) Biol Reprod , vol.33 , pp. 1094-1104
    • Kopf, G.S.1    Vacquier, V.D.2
  • 49
    • 0021251345 scopus 로고
    • Characterization of a calmodulin-stimulated adenylate cyclase from abalone spermatozoa
    • Kopf GS, Vacquier VD. Characterization of a calmodulin-stimulated adenylate cyclase from abalone spermatozoa. J Biol Chem 1984; 259: 7590-7596.
    • (1984) J Biol Chem , vol.259 , pp. 7590-7596
    • Kopf, G.S.1    Vacquier, V.D.2
  • 50
    • 0024147411 scopus 로고
    • Control of ram sperm adenylate cyclase by divalent cations
    • Goh PP, White IG. Control of ram sperm adenylate cyclase by divalent cations. Aust J Biol Sci 1988; 41:377-385.
    • (1988) Aust J Biol Sci , vol.41 , pp. 377-385
    • Goh, P.P.1    White, I.G.2
  • 51
    • 0023258569 scopus 로고
    • Calmodulin-mediated adenylate cyclase from mammalian sperm
    • Gross MK, Toscano DG, Toscano WA Jr. Calmodulin-mediated adenylate cyclase from mammalian sperm. J Biol Chem 1987; 262:8672-8676.
    • (1987) J Biol Chem , vol.262 , pp. 8672-8676
    • Gross, M.K.1    Toscano, D.G.2    Toscano W.A., Jr.3
  • 52
    • 0023662356 scopus 로고
    • Stimulation of partially purified adenylate cyclase from bull sperm by bicarbonate
    • Garty NB, Salomon Y. Stimulation of partially purified adenylate cyclase from bull sperm by bicarbonate. FEBS Lett 1987; 218:148-152.
    • (1987) FEBS Lett , vol.218 , pp. 148-152
    • Garty, N.B.1    Salomon, Y.2
  • 53
    • 0022257352 scopus 로고
    • Sodium bicarbonate in seminal plasma stimulates the motility of mammalian sperm through the direct activation of adenylate cyclase
    • Okamura N, Tajima Y, Soejimas A, Masuda H, Sugita Y. Sodium bicarbonate in seminal plasma stimulates the motility of mammalian sperm through the direct activation of adenylate cyclase. J Biol Chem 1986; 260:9699-9705.
    • (1986) J Biol Chem , vol.260 , pp. 9699-9705
    • Okamura, N.1    Tajima, Y.2    Soejimas, A.3    Masuda, H.4    Sugita, Y.5
  • 54
    • 0025046490 scopus 로고
    • Bicarbonate dependence of cAMP accumulation induced by phorbol esters in hamster spermatozoa
    • Visconti PE, Muschietti JP, Flawia MM, Tezon JG. Bicarbonate dependence of cAMP accumulation induced by phorbol esters in hamster spermatozoa. Biochim Biophys Acta 1990; 1054:231-236.
    • (1990) Biochim Biophys Acta , vol.1054 , pp. 231-236
    • Visconti, P.E.1    Muschietti, J.P.2    Flawia, M.M.3    Tezon, J.G.4
  • 55
    • 0024788833 scopus 로고
    • Intracellular pH regulates bovine sperm motility and protein phosphorylation
    • Carr DW, Acott TS. Intracellular pH regulates bovine sperm motility and protein phosphorylation. Biol Reprod 1989; 41:907-920.
    • (1989) Biol Reprod , vol.41 , pp. 907-920
    • Carr, D.W.1    Acott, T.S.2
  • 56
    • 0018763770 scopus 로고
    • The cAMP phosphodiesterase of bovine sperm: Multiple forms, kinetic properties and changes during development
    • Stephens DT, Wang JL, Hoskins DD. The cAMP phosphodiesterase of bovine sperm: multiple forms, kinetic properties and changes during development. Biol Reprod 1979; 20:483-491.
    • (1979) Biol Reprod , vol.20 , pp. 483-491
    • Stephens, D.T.1    Wang, J.L.2    Hoskins, D.D.3
  • 57
    • 0027772672 scopus 로고
    • Inhibition of the EGF-activated MAP kinase signaling pathway by adenosine 3′,5′-monophosphate
    • Wu J, Dent P, Jelinek T, Wolfman A, Weber MJ, Sturgill TW. Inhibition of the EGF-activated MAP kinase signaling pathway by adenosine 3′,5′-monophosphate. Science 1993; 262:1065-1069.
    • (1993) Science , vol.262 , pp. 1065-1069
    • Wu, J.1    Dent, P.2    Jelinek, T.3    Wolfman, A.4    Weber, M.J.5    Sturgill, T.W.6
  • 58
    • 0027716596 scopus 로고
    • Inhibition by cAMP of ras-dependent activation of raf
    • Cook SJ, McCormick F. Inhibition by cAMP of ras-dependent activation of raf. Science 1993; 262:1069-1073.
    • (1993) Science , vol.262 , pp. 1069-1073
    • Cook, S.J.1    McCormick, F.2
  • 59
    • 0026606813 scopus 로고
    • Role of cAMP in mediating effects of fasting on dephosphorylation of the insulin receptor
    • Begum N, Graham AL, Sussman KE, Draznin B. Role of cAMP in mediating effects of fasting on dephosphorylation of the insulin receptor. Am J Physiol 1992; 262:E142-E149.
    • (1992) Am J Physiol , vol.262
    • Begum, N.1    Graham, A.L.2    Sussman, K.E.3    Draznin, B.4
  • 60
    • 0028129146 scopus 로고
    • PTP-PEST: A protein tyrosine phosphatase regulated by serine phosphorylation
    • Garton AJ, Tonks NK. PTP-PEST: a protein tyrosine phosphatase regulated by serine phosphorylation. EMBO J 1994; 13:3763-3771.
    • (1994) EMBO J , vol.13 , pp. 3763-3771
    • Garton, A.J.1    Tonks, N.K.2
  • 63
    • 0023646056 scopus 로고
    • Involvement of tyrosine protein kinase in the initiation of flagellar movement in rainbow trout spermatozoa
    • Hayashi H, Yamamoto K, Yonekawa H, Morisawa M. Involvement of tyrosine protein kinase in the initiation of flagellar movement in rainbow trout spermatozoa. J Biol Chem 1987; 262:16692-16698.
    • (1987) J Biol Chem , vol.262 , pp. 16692-16698
    • Hayashi, H.1    Yamamoto, K.2    Yonekawa, H.3    Morisawa, M.4
  • 64
    • 0026355272 scopus 로고
    • Activation of Ciona sperm motility: Phosphorylation of dynein polypeptides and effects of a tyrosine kinase inhibitor
    • Dey CS, Brokaw CJ. Activation of Ciona sperm motility: phosphorylation of dynein polypeptides and effects of a tyrosine kinase inhibitor. J Cell Sci 1991; 100:815-824.
    • (1991) J Cell Sci , vol.100 , pp. 815-824
    • Dey, C.S.1    Brokaw, C.J.2
  • 65
    • 0028065529 scopus 로고
    • Calcium influx into mouse spermatozoa activated by solubilized mouse zona pellucida, monitored with the calcium fluorescent indicator, fluo-3. Inhibition of the influx by three inhibitors of the zona pellucida induced acrosome reaction: Tyrphostin A48, pertussis toxin, and 3-quinuclidinyl benzilate
    • Bailey JL, Storey BT. Calcium influx into mouse spermatozoa activated by solubilized mouse zona pellucida, monitored with the calcium fluorescent indicator, fluo-3. Inhibition of the influx by three inhibitors of the zona pellucida induced acrosome reaction: tyrphostin A48, pertussis toxin, and 3-quinuclidinyl benzilate. Mol Reprod Dev 1994; 39:297-308.
    • (1994) Mol Reprod Dev , vol.39 , pp. 297-308
    • Bailey, J.L.1    Storey, B.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.