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Volumn 41, Issue 4, 2006, Pages 528-540

Positive role of reactive oxygen species in mammalian sperm capacitation: triggering and modulation of phosphorylation events

Author keywords

Fertilization; Free radicals; Hydrogen peroxide; Nitric oxide; Phosphoproteins; Protein kinases; Signal transduction; Spermatozoa; Superoxide anion

Indexed keywords

CYCLIC AMP DEPENDENT PROTEIN KINASE; FREE RADICAL; GLUTAMINE; HYDROGEN PEROXIDE; MITOGEN ACTIVATED PROTEIN KINASE; NITRIC OXIDE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOPROTEIN; PROLINE; PROTEIN KINASE; PROTEIN KINASE B; REACTIVE OXYGEN METABOLITE; SUPEROXIDE; THREONINE; TYROSINE; XANTHINE; XANTHINE OXIDASE;

EID: 33746077694     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2006.04.027     Document Type: Review
Times cited : (205)

References (134)
  • 1
    • 0032053707 scopus 로고    scopus 로고
    • Oxygen radicals and signaling
    • Finkel T. Oxygen radicals and signaling. Curr. Opin. Cell. Biol. 10 (1998) 248-253
    • (1998) Curr. Opin. Cell. Biol. , vol.10 , pp. 248-253
    • Finkel, T.1
  • 3
    • 0037115158 scopus 로고    scopus 로고
    • Reactive oxygen species and cell signaling: respiratory burst in macrophages signaling
    • Forman J., and Torres M. Reactive oxygen species and cell signaling: respiratory burst in macrophages signaling. Am. J. Respir. Crit. Care Med. 166 (2002) S4-S8
    • (2002) Am. J. Respir. Crit. Care Med. , vol.166
    • Forman, J.1    Torres, M.2
  • 4
    • 0001387519 scopus 로고
    • The role of oxygen in the metabolism and motility of human spermatozoa
    • Macleod J. The role of oxygen in the metabolism and motility of human spermatozoa. Am. J. Physiol. 138 (1943) 512-518
    • (1943) Am. J. Physiol. , vol.138 , pp. 512-518
    • Macleod, J.1
  • 5
    • 0001655470 scopus 로고
    • Formation of hydrogen peroxide by spermatozoa and its inhibitory effect on respiration
    • Tosic J., and Walton A. Formation of hydrogen peroxide by spermatozoa and its inhibitory effect on respiration. Nature 158 (1946) 485
    • (1946) Nature , vol.158 , pp. 485
    • Tosic, J.1    Walton, A.2
  • 6
    • 0000155214 scopus 로고
    • Metabolism of spermatozoa: the formation and elimination of hydrogen peroxide by spermatozoa and effects on motility and survival
    • Tosic J., and Walton A. Metabolism of spermatozoa: the formation and elimination of hydrogen peroxide by spermatozoa and effects on motility and survival. Biochem. J. 47 (1950) 199-212
    • (1950) Biochem. J. , vol.47 , pp. 199-212
    • Tosic, J.1    Walton, A.2
  • 7
    • 0028834966 scopus 로고
    • Impact of reactive oxygen species on spermatozoa: a balancing between beneficial and detrimental effects
    • de Lamirande E., and Gagnon C. Impact of reactive oxygen species on spermatozoa: a balancing between beneficial and detrimental effects. Hum. Reprod. 10 (1995) 15-21
    • (1995) Hum. Reprod. , vol.10 , pp. 15-21
    • de Lamirande, E.1    Gagnon, C.2
  • 8
    • 0028965632 scopus 로고
    • Reactive oxygen species, lipid peroxidation and enzymatic defense systems in human spermatozoa
    • Griveau J.F., Dumont E., Renaud P., Callegari J.P., and Le Lannou D. Reactive oxygen species, lipid peroxidation and enzymatic defense systems in human spermatozoa. J. Reprod. Fertil. 103 (1995) 17-26
    • (1995) J. Reprod. Fertil. , vol.103 , pp. 17-26
    • Griveau, J.F.1    Dumont, E.2    Renaud, P.3    Callegari, J.P.4    Le Lannou, D.5
  • 9
    • 0028918676 scopus 로고
    • Capacitation-associated production of superoxide anion by human spermatozoa
    • de Lamirande E., and Gagnon C. Capacitation-associated production of superoxide anion by human spermatozoa. Free Radic. Biol. Med. 18 (1995) 487-495
    • (1995) Free Radic. Biol. Med. , vol.18 , pp. 487-495
    • de Lamirande, E.1    Gagnon, C.2
  • 10
    • 0031091039 scopus 로고    scopus 로고
    • Capacitation as a regulatory event that primes spermatozoa for the acrosome reaction and fertilization
    • de Lamirande E., Leclerc P., and Gagnon C. Capacitation as a regulatory event that primes spermatozoa for the acrosome reaction and fertilization. Mol. Hum. Reprod. 3 (1997) 175-194
    • (1997) Mol. Hum. Reprod. , vol.3 , pp. 175-194
    • de Lamirande, E.1    Leclerc, P.2    Gagnon, C.3
  • 11
    • 0031890532 scopus 로고    scopus 로고
    • A novel signal transduction cascade in capacitating human spermatozoa characterized by a redox-regulated, cAMP-mediated induction of tyrosine phosphorylation
    • Aitken R.J., Harkiss D., Knox W., Paterson M., and Irvine D.S. A novel signal transduction cascade in capacitating human spermatozoa characterized by a redox-regulated, cAMP-mediated induction of tyrosine phosphorylation. J. Cell Sci. 111 (1998) 645-656
    • (1998) J. Cell Sci. , vol.111 , pp. 645-656
    • Aitken, R.J.1    Harkiss, D.2    Knox, W.3    Paterson, M.4    Irvine, D.S.5
  • 12
    • 0028670194 scopus 로고
    • An in vitro promoting role for hydrogen peroxide in human sperm capacitation
    • Griveau J.F., Renaud P., and Le Lannou D. An in vitro promoting role for hydrogen peroxide in human sperm capacitation. Int. J. Androl. 17 (1994) 300-307
    • (1994) Int. J. Androl. , vol.17 , pp. 300-307
    • Griveau, J.F.1    Renaud, P.2    Le Lannou, D.3
  • 13
    • 0029069155 scopus 로고
    • Superoxide anion production by human spermatozoa as part of the ionophore-induced acrosome reaction process
    • Griveau J.F., Renaud P., and Le Lannou D. Superoxide anion production by human spermatozoa as part of the ionophore-induced acrosome reaction process. Int. J. Androl. 18 (1995) 67-74
    • (1995) Int. J. Androl. , vol.18 , pp. 67-74
    • Griveau, J.F.1    Renaud, P.2    Le Lannou, D.3
  • 14
    • 0033565713 scopus 로고    scopus 로고
    • Reactive oxygen species requirements for bovine sperm capacitation and acrosome reaction
    • O'Flaherty C., Beorelgui B., and Beconi M.T. Reactive oxygen species requirements for bovine sperm capacitation and acrosome reaction. Theriogenology 52 (1999) 289-301
    • (1999) Theriogenology , vol.52 , pp. 289-301
    • O'Flaherty, C.1    Beorelgui, B.2    Beconi, M.T.3
  • 15
    • 0012809557 scopus 로고    scopus 로고
    • Role of superoxide anion and hydrogen peroxide in acrosome reaction of bovine spermatozoa
    • Robaire B., Chemes H., and Morales C. (Eds), Medimond, Milan
    • O'Flaherty C., Beorelgui B., and Beconi M.T. Role of superoxide anion and hydrogen peroxide in acrosome reaction of bovine spermatozoa. In: Robaire B., Chemes H., and Morales C. (Eds). Andrology in the 21st Century (2001), Medimond, Milan 103-108
    • (2001) Andrology in the 21st Century , pp. 103-108
    • O'Flaherty, C.1    Beorelgui, B.2    Beconi, M.T.3
  • 16
    • 27144544524 scopus 로고    scopus 로고
    • Acrosome reaction in bovine spermatozoa: role of reactive oxygen species and lactate dehydrogenase C4
    • O'Flaherty C., Beorelgui B., and Beconi M.T. Acrosome reaction in bovine spermatozoa: role of reactive oxygen species and lactate dehydrogenase C4. Biochim. Biophys. Acta 1726 (2005) 96-101
    • (2005) Biochim. Biophys. Acta , vol.1726 , pp. 96-101
    • O'Flaherty, C.1    Beorelgui, B.2    Beconi, M.T.3
  • 17
    • 0002494818 scopus 로고
    • The spermatozoon
    • Knobil E., and Neill J.D. (Eds), Raven Press, New York
    • Eddy E.M., and O'Brien A.O. The spermatozoon. In: Knobil E., and Neill J.D. (Eds). The Physiology of Reproduction vol. 2 (1994), Raven Press, New York 29-77
    • (1994) The Physiology of Reproduction , vol.2 , pp. 29-77
    • Eddy, E.M.1    O'Brien, A.O.2
  • 18
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • Knobil E., and Neill J.D. (Eds), Raven Press, New York
    • Yanagimachi R. Mammalian fertilization. In: Knobil E., and Neill J.D. (Eds). The Physiology of Reproduction vol. 2 (1994), Raven Press, New York 189-317
    • (1994) The Physiology of Reproduction , vol.2 , pp. 189-317
    • Yanagimachi, R.1
  • 19
    • 18744368170 scopus 로고    scopus 로고
    • C. Biological basis for human capacitation
    • De Jonge C. C. Biological basis for human capacitation. Hum. Reprod. Update 11 (2005) 205-214
    • (2005) Hum. Reprod. Update , vol.11 , pp. 205-214
    • De Jonge, C.1
  • 20
    • 0025943491 scopus 로고
    • Intracellular calcium accumulation and responsiveness to progesterone in capacitating human spermatozoa
    • Baldi E., Casana R., Falsetti C., Krausz C., Maggi M., and Forti G. Intracellular calcium accumulation and responsiveness to progesterone in capacitating human spermatozoa. J. Androl. 12 (1991) 323-330
    • (1991) J. Androl. , vol.12 , pp. 323-330
    • Baldi, E.1    Casana, R.2    Falsetti, C.3    Krausz, C.4    Maggi, M.5    Forti, G.6
  • 21
    • 0029456702 scopus 로고
    • Ionic control of sperm function
    • Fraser L.R. Ionic control of sperm function. Reprod. Fertil. Dev. 7 (1995) 905-925
    • (1995) Reprod. Fertil. Dev. , vol.7 , pp. 905-925
    • Fraser, L.R.1
  • 22
    • 0028935169 scopus 로고
    • Intracellular pH of bovine sperm increases during capacitation
    • Vredenburgh-Wilberg W.L., and Parrish J.J. Intracellular pH of bovine sperm increases during capacitation. Mol. Reprod. Dev. 40 (1995) 490-502
    • (1995) Mol. Reprod. Dev. , vol.40 , pp. 490-502
    • Vredenburgh-Wilberg, W.L.1    Parrish, J.J.2
  • 23
    • 0029969294 scopus 로고    scopus 로고
    • Progesterone induces Ca-dependent 3′,5′-cyclic adenosine monophosphate increase in human sperm
    • Parinaud J., and Milhet P. Progesterone induces Ca-dependent 3′,5′-cyclic adenosine monophosphate increase in human sperm. J. Clin. Endocrinol. Metab. 81 (1996) 1357-1360
    • (1996) J. Clin. Endocrinol. Metab. , vol.81 , pp. 1357-1360
    • Parinaud, J.1    Milhet, P.2
  • 24
    • 0028061888 scopus 로고
    • Differences in the role of cyclic adenosine 3′,5′-monophosphate during capacitation of bovine sperm by heparin or oviduct fluid
    • Parrish J.J., Susko-Parrish J.L., Uguz C., and First N.L. Differences in the role of cyclic adenosine 3′,5′-monophosphate during capacitation of bovine sperm by heparin or oviduct fluid. Biol. Reprod. 51 (1994) 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
  • 25
    • 0037386320 scopus 로고    scopus 로고
    • Participation of superoxide anion in the capacitation of cryopreserved bovine sperm
    • O'Flaherty C., Beorelgui B., and Beconi M.T. Participation of superoxide anion in the capacitation of cryopreserved bovine sperm. Int. J. Androl. 26 (2003) 109-114
    • (2003) Int. J. Androl. , vol.26 , pp. 109-114
    • O'Flaherty, C.1    Beorelgui, B.2    Beconi, M.T.3
  • 26
    • 0028936801 scopus 로고
    • Capacitation in mouse spermatozoa: II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway
    • Visconti P.E., Moore G.D., Bailey J.L., Leclerc P., Connors S.A., Pan D., Olds-Clarke P., and Kopf G.S. Capacitation in mouse spermatozoa: II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway. Development 121 (1995) 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
  • 27
    • 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., and Gagnon C. Cyclic adenosine 3′,5′ monophosphate-dependent regulation of protein tyrosine phosphorylation in relation to human sperm capacitation and motility. Biol. Reprod. 55 (1996) 684-692
    • (1996) Biol. Reprod. , vol.55 , pp. 684-692
    • Leclerc, P.1    de Lamirande, E.2    Gagnon, C.3
  • 28
    • 0031036435 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphorylation and human sperm capacitation by reactive oxygen derivatives
    • Leclerc P., de Lamirande E., and Gagnon C. Regulation of protein tyrosine phosphorylation and human sperm capacitation by reactive oxygen derivatives. Free Radic. Biol. Med. 22 (1997) 643-656
    • (1997) Free Radic. Biol. Med. , vol.22 , pp. 643-656
    • Leclerc, P.1    de Lamirande, E.2    Gagnon, C.3
  • 30
    • 0027506151 scopus 로고
    • A positive role for the superoxide anion in triggering hyperactivation and capacitation of human spermatozoa
    • de Lamirande E., and Gagnon C. A positive role for the superoxide anion in triggering hyperactivation and capacitation of human spermatozoa. J. Androl. 16 (1993) 21-25
    • (1993) J. Androl. , vol.16 , pp. 21-25
    • de Lamirande, E.1    Gagnon, C.2
  • 31
    • 0030760362 scopus 로고    scopus 로고
    • Effect of natural antioxidants, superoxide dismutase and hydrogen peroxide on capacitation of frozen-thawed bull spermatozoa
    • O'Flaherty C., Beconi M.T., and Beorelgui B. Effect of natural antioxidants, superoxide dismutase and hydrogen peroxide on capacitation of frozen-thawed bull spermatozoa. Andrologia 29 (1997) 269-275
    • (1997) Andrologia , vol.29 , pp. 269-275
    • O'Flaherty, C.1    Beconi, M.T.2    Beorelgui, B.3
  • 32
    • 0019203136 scopus 로고
    • Properties of spermatozoal superoxide dismutase and lack of involvement of superoxides in metal-ion-catalysed lipid peroxidation reaction in semen
    • Menella M.R.F., and Jones R. Properties of spermatozoal superoxide dismutase and lack of involvement of superoxides in metal-ion-catalysed lipid peroxidation reaction in semen. Biochem. J. 1091 (1980) 289-297
    • (1980) Biochem. J. , vol.1091 , pp. 289-297
    • Menella, M.R.F.1    Jones, R.2
  • 33
    • 0031298159 scopus 로고    scopus 로고
    • Superoxide dismutase isoenzymes in human seminal plasma and spermatozoa
    • Peeker R., Abramsson L., and Marklund S.L. Superoxide dismutase isoenzymes in human seminal plasma and spermatozoa. Mol. Hum. Reprod. 3 (1997) 1061-1066
    • (1997) Mol. Hum. Reprod. , vol.3 , pp. 1061-1066
    • Peeker, R.1    Abramsson, L.2    Marklund, S.L.3
  • 34
    • 13744260785 scopus 로고    scopus 로고
    • Relationship between total superoxide dismutase activity with lipid peroxidation, dynamics and morphological parameters in canine semen
    • Cassani P., Beconi M.T., and O'Flaherty C. Relationship between total superoxide dismutase activity with lipid peroxidation, dynamics and morphological parameters in canine semen. Anim. Reprod. Sci. 86 (2005) 163-173
    • (2005) Anim. Reprod. Sci. , vol.86 , pp. 163-173
    • Cassani, P.1    Beconi, M.T.2    O'Flaherty, C.3
  • 35
    • 0026032205 scopus 로고
    • Hydrogen peroxide is involved in hamster sperm capacitation in vitro
    • Bize I., Santander G., Cabello P., Driscoll D., and Sharpe C. Hydrogen peroxide is involved in hamster sperm capacitation in vitro. Biol. Reprod. 44 (1991) 398-403
    • (1991) Biol. Reprod. , vol.44 , pp. 398-403
    • Bize, I.1    Santander, G.2    Cabello, P.3    Driscoll, D.4    Sharpe, C.5
  • 36
    • 20844462742 scopus 로고    scopus 로고
    • Reactive oxygen species and protein kinases modulate the level of phospho-MEK-like proteins during human sperm capacitation
    • O'Flaherty C., de Lamirande E., and Gagnon C. Reactive oxygen species and protein kinases modulate the level of phospho-MEK-like proteins during human sperm capacitation. Biol. Reprod. 73 (2005) 94-105
    • (2005) Biol. Reprod. , vol.73 , pp. 94-105
    • O'Flaherty, C.1    de Lamirande, E.2    Gagnon, C.3
  • 37
    • 0031090408 scopus 로고    scopus 로고
    • Molecular mechanisms regulating human sperm function
    • Aitken R.J. Molecular mechanisms regulating human sperm function. Mol. Hum. Reprod. 3 (1997) 169-173
    • (1997) Mol. Hum. Reprod. , vol.3 , pp. 169-173
    • Aitken, R.J.1
  • 38
    • 27544443327 scopus 로고    scopus 로고
    • Molecular composition and regulation of the Nox family NAD(P)H oxidases
    • Sumimoto H., Miyano K., and Takeya R. Molecular composition and regulation of the Nox family NAD(P)H oxidases. Biochem. Biophys. Res. Commun. 338 (2005) 677-686
    • (2005) Biochem. Biophys. Res. Commun. , vol.338 , pp. 677-686
    • Sumimoto, H.1    Miyano, K.2    Takeya, R.3
  • 39
    • 4744349398 scopus 로고    scopus 로고
    • Structure and regulation of the neutrophil respiratory burst oxidase: comparison with nonphagocyte oxidases
    • Quinn M.T., and Gauss K.A. Structure and regulation of the neutrophil respiratory burst oxidase: comparison with nonphagocyte oxidases. J. Leukocyte Biol. 76 (2004) 760-781
    • (2004) J. Leukocyte Biol. , vol.76 , pp. 760-781
    • Quinn, M.T.1    Gauss, K.A.2
  • 40
    • 0028142461 scopus 로고
    • phox during neutrophil activation: phosphorylation of sites recognized by protein kinase C and by proline-directed kinases
    • phox during neutrophil activation: phosphorylation of sites recognized by protein kinase C and by proline-directed kinases. J. Biol. Chem. 269 (1994) 23431-23436
    • (1994) J. Biol. Chem. , vol.269 , pp. 23431-23436
    • El Benna, J.1    Faust, L.P.2    Babior, B.M.3
  • 41
    • 0034327804 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase extracellular signal-regulated kinase 1/2 pathway is involved in formyl-methionyl-leucyl-phenylalanine-induced p47phox phosphorylation in human neutrophils
    • Dewas C., Fay M., Gougerot-Pocidalo M.A., and El Benna J., The mitogen-activated protein kinase extracellular signal-regulated kinase 1/2 pathway is involved in formyl-methionyl-leucyl-phenylalanine-induced p47phox phosphorylation in human neutrophils. J. Immunol. 165 (2000) 5238-5244
    • (2000) J. Immunol. , vol.165 , pp. 5238-5244
    • Dewas, C.1    Fay, M.2    Gougerot-Pocidalo, M.A.3    El Benna, J.4
  • 42
    • 0036169665 scopus 로고    scopus 로고
    • The extracellular signal-regulated kinase (ERK) pathway is involved in human sperm function and modulated by superoxide anion
    • de Lamirande E., and Gagnon C. The extracellular signal-regulated kinase (ERK) pathway is involved in human sperm function and modulated by superoxide anion. Mol. Hum. Reprod. 8 (2002) 124-135
    • (2002) Mol. Hum. Reprod. , vol.8 , pp. 124-135
    • de Lamirande, E.1    Gagnon, C.2
  • 43
    • 0027979010 scopus 로고
    • Reactive oxygen species released by activated neutrophils, but not by deficient spermatozoa, are sufficient to affect normal sperm motility
    • Plante M., de Lamirande E., and Gagnon C. Reactive oxygen species released by activated neutrophils, but not by deficient spermatozoa, are sufficient to affect normal sperm motility. Fertil. Steril. 62 (1994) 387-393
    • (1994) Fertil. Steril. , vol.62 , pp. 387-393
    • Plante, M.1    de Lamirande, E.2    Gagnon, C.3
  • 44
    • 0032789427 scopus 로고    scopus 로고
    • Nitric oxide regulates human sperm capacitation and protein tyrosine phosphorylation in vitro
    • Herrero M.B., de Lamirande E., and Gagnon C. Nitric oxide regulates human sperm capacitation and protein tyrosine phosphorylation in vitro. Biol. Reprod. 61 (1999) 575-581
    • (1999) Biol. Reprod. , vol.61 , pp. 575-581
    • Herrero, M.B.1    de Lamirande, E.2    Gagnon, C.3
  • 45
    • 33644863217 scopus 로고    scopus 로고
    • Reactive oxygen species modulate independent protein phosphorylation pathways during human sperm capacitation
    • O'Flaherty C., de Lamirande E., and Gagnon C. Reactive oxygen species modulate independent protein phosphorylation pathways during human sperm capacitation. Free Radic. Biol. Med. 40 (2006) 1045-1055
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 1045-1055
    • O'Flaherty, C.1    de Lamirande, E.2    Gagnon, C.3
  • 46
    • 1542647604 scopus 로고    scopus 로고
    • Inhibition of in vitro capacitation of hamster spermatozoa by nitric oxide synthase inhibitors
    • Kameshwari D.B., Siva A.B., and Shivaji S. Inhibition of in vitro capacitation of hamster spermatozoa by nitric oxide synthase inhibitors. Cell. Mol. Biol. 49 (2003) 421-428
    • (2003) Cell. Mol. Biol. , vol.49 , pp. 421-428
    • Kameshwari, D.B.1    Siva, A.B.2    Shivaji, S.3
  • 48
    • 7044240982 scopus 로고    scopus 로고
    • l-Arginine promotes capacitation and acrosome reaction in cryopreserved bovine spermatozoa
    • O'Flaherty C., Rodriguez P., and Srivastava S. l-Arginine promotes capacitation and acrosome reaction in cryopreserved bovine spermatozoa. Biochim. Biophys. Acta 1674 (2004) 215-221
    • (2004) Biochim. Biophys. Acta , vol.1674 , pp. 215-221
    • O'Flaherty, C.1    Rodriguez, P.2    Srivastava, S.3
  • 49
    • 33644778746 scopus 로고    scopus 로고
    • Heparin- and superoxide anion-dependent capacitation of cryopreserved bovine spermatozoa: requirement of dehydrogenases and protein kinases
    • O'Flaherty C., Beorelgui B., and Beconi M.T. Heparin- and superoxide anion-dependent capacitation of cryopreserved bovine spermatozoa: requirement of dehydrogenases and protein kinases. Free Radic. Res. 40 (2006) 427-432
    • (2006) Free Radic. Res. , vol.40 , pp. 427-432
    • O'Flaherty, C.1    Beorelgui, B.2    Beconi, M.T.3
  • 50
    • 0031893173 scopus 로고    scopus 로고
    • Effects of low concentrations of nitric oxide on the zona pellucida binding ability of human spermatozoa
    • Sengoku K., Tamate K., Yoshida T., Takaoka Y., Miyamoto T., and Ishikawa M. Effects of low concentrations of nitric oxide on the zona pellucida binding ability of human spermatozoa. Fertil. Steril. 69 (1998) 522-527
    • (1998) Fertil. Steril. , vol.69 , pp. 522-527
    • Sengoku, K.1    Tamate, K.2    Yoshida, T.3    Takaoka, Y.4    Miyamoto, T.5    Ishikawa, M.6
  • 51
    • 9644289356 scopus 로고    scopus 로고
    • Nitric oxide-induced capacitation of cryopreserved bull spermatozoa and assessment of participating regulatory pathways
    • Rodriguez P.C., O'Flaherty C.M., Beconi M.T., and Beorlegui N.B. Nitric oxide-induced capacitation of cryopreserved bull spermatozoa and assessment of participating regulatory pathways. Anim. Reprod. 85 (2005) 231-242
    • (2005) Anim. Reprod. , vol.85 , pp. 231-242
    • Rodriguez, P.C.1    O'Flaherty, C.M.2    Beconi, M.T.3    Beorlegui, N.B.4
  • 52
    • 0030275612 scopus 로고    scopus 로고
    • Nitric oxide synthase and nitrite production in human spermatozoa: evidence that endogenous nitric oxide is beneficial to sperm motility
    • Lewis S.E., Donnelly E.T., Sterling E.S., Kennedy M.S., Thompson W., and Chakravarthy U. Nitric oxide synthase and nitrite production in human spermatozoa: evidence that endogenous nitric oxide is beneficial to sperm motility. Mol. Hum. Reprod. 2 (1996) 873-878
    • (1996) Mol. Hum. Reprod. , vol.2 , pp. 873-878
    • Lewis, S.E.1    Donnelly, E.T.2    Sterling, E.S.3    Kennedy, M.S.4    Thompson, W.5    Chakravarthy, U.6
  • 53
    • 0032403539 scopus 로고    scopus 로고
    • Human sperm endothelial nitric oxide synthase expression: correlation with sperm motility
    • O'Bryan M.K., Zini A., Cheng C.Y., and Schlegel P.N. Human sperm endothelial nitric oxide synthase expression: correlation with sperm motility. Fertil. Steril. 70 (1998) 1143-1147
    • (1998) Fertil. Steril. , vol.70 , pp. 1143-1147
    • O'Bryan, M.K.1    Zini, A.2    Cheng, C.Y.3    Schlegel, P.N.4
  • 54
    • 2142702798 scopus 로고    scopus 로고
    • Detection and localization of two constitutive NOS isoforms in bull spermatozoa
    • Meiser H., and Schulz R. Detection and localization of two constitutive NOS isoforms in bull spermatozoa. Anat. Histol. Embryol. 32 (2003) 321-325
    • (2003) Anat. Histol. Embryol. , vol.32 , pp. 321-325
    • Meiser, H.1    Schulz, R.2
  • 55
    • 0029095967 scopus 로고
    • Oxidant stress enhances adenylyl cyclase activation
    • Tan C.M., Xenoyannis S., and Feldman R.D. Oxidant stress enhances adenylyl cyclase activation. Circ. Res. 77 (1995) 710-717
    • (1995) Circ. Res. , vol.77 , pp. 710-717
    • Tan, C.M.1    Xenoyannis, S.2    Feldman, R.D.3
  • 56
    • 0031080272 scopus 로고    scopus 로고
    • Beta-adrenoceptor-linked signal transduction in ischemic-reperfused heart and scavenging of oxyradicals
    • Persad S., Takeda S., Panagia V., and Dhalla N.S. Beta-adrenoceptor-linked signal transduction in ischemic-reperfused heart and scavenging of oxyradicals. J. Mol. Cell. Cardiol. 29 (1997) 545-558
    • (1997) J. Mol. Cell. Cardiol. , vol.29 , pp. 545-558
    • Persad, S.1    Takeda, S.2    Panagia, V.3    Dhalla, N.S.4
  • 57
    • 0042856454 scopus 로고    scopus 로고
    • Evidence for multiple distinctly localized adenylyl cyclase isoforms in mammalian spermatozoa
    • Baxendale R.W., and Fraser L.R. Evidence for multiple distinctly localized adenylyl cyclase isoforms in mammalian spermatozoa. Mol. Reprod. Dev. 66 (2003) 181-189
    • (2003) Mol. Reprod. Dev. , vol.66 , pp. 181-189
    • Baxendale, R.W.1    Fraser, L.R.2
  • 58
    • 0037386903 scopus 로고    scopus 로고
    • Cyclic AMP signaling during mammalian sperm capacitation-Still largely terra incognita
    • Harrison R.A.P. Cyclic AMP signaling during mammalian sperm capacitation-Still largely terra incognita. Reprod. Dom. Anim. 38 (2003) 102-110
    • (2003) Reprod. Dom. Anim. , vol.38 , pp. 102-110
    • Harrison, R.A.P.1
  • 59
    • 11144282376 scopus 로고    scopus 로고
    • Bicarbonate-induced membrane processing in sperm capacitation
    • Harrison R.A.P., and Gadella B.M. Bicarbonate-induced membrane processing in sperm capacitation. Theriogenology 63 (2005) 342-351
    • (2005) Theriogenology , vol.63 , pp. 342-351
    • Harrison, R.A.P.1    Gadella, B.M.2
  • 60
    • 0022257352 scopus 로고
    • Sodium bicarbonate in seminal plasma stimulates the motility of mammalian spermatozoa through direct activation of adenylate cyclase
    • Okamura N., Tajima Y., Soejima A., Masuda H., and Sugita Y. Sodium bicarbonate in seminal plasma stimulates the motility of mammalian spermatozoa through direct activation of adenylate cyclase. J. Biol. Chem. 260 (1985) 9699-9705
    • (1985) J. Biol. Chem. , vol.260 , pp. 9699-9705
    • Okamura, N.1    Tajima, Y.2    Soejima, A.3    Masuda, H.4    Sugita, Y.5
  • 61
    • 0037844844 scopus 로고    scopus 로고
    • Kinetic properties of "soluble" adenylyl cyclase: synergism between calcium and bicarbonate
    • Litvin T.N., Kamenetsky M., Zarifyan A., Buck J., and Levin L.R. Kinetic properties of "soluble" adenylyl cyclase: synergism between calcium and bicarbonate. J. Biol. Chem. 278 (2003) 15922-15926
    • (2003) J. Biol. Chem. , vol.278 , pp. 15922-15926
    • Litvin, T.N.1    Kamenetsky, M.2    Zarifyan, A.3    Buck, J.4    Levin, L.R.5
  • 62
    • 0020568086 scopus 로고
    • Forskolin does not activate sperm adenylate cyclase
    • Forte L.R., Bylund D.B., and Zahler W.L. Forskolin does not activate sperm adenylate cyclase. Mol. Pharmacol. 24 (1983) 42-47
    • (1983) Mol. Pharmacol. , vol.24 , pp. 42-47
    • Forte, L.R.1    Bylund, D.B.2    Zahler, W.L.3
  • 63
    • 0029456702 scopus 로고
    • Ionic control of sperm function
    • Fraser L.R. Ionic control of sperm function. Reprod. Fertil. Dev. 7 (1995) 905-925
    • (1995) Reprod. Fertil. Dev. , vol.7 , pp. 905-925
    • Fraser, L.R.1
  • 65
    • 0029961745 scopus 로고    scopus 로고
    • Promotion of human sperm capacitation by superoxide anion
    • Zhang H., and Zheng R. Promotion of human sperm capacitation by superoxide anion. Free Radic. Res. 24 (1996) 261-268
    • (1996) Free Radic. Res. , vol.24 , pp. 261-268
    • Zhang, H.1    Zheng, R.2
  • 66
    • 4544223127 scopus 로고    scopus 로고
    • Regulation of sperm function by reactive oxygen species
    • Ford C. Regulation of sperm function by reactive oxygen species. Hum. Reprod. Update 10 (2004) 387-399
    • (2004) Hum. Reprod. Update , vol.10 , pp. 387-399
    • Ford, C.1
  • 67
    • 0033230607 scopus 로고    scopus 로고
    • Role of redox potential and reactive oxygen species in stress signaling
    • Adler V., Yin Z., Tew K.D., and Ronai Z. Role of redox potential and reactive oxygen species in stress signaling. Oncogene 18 (1999) 6104-6111
    • (1999) Oncogene , vol.18 , pp. 6104-6111
    • Adler, V.1    Yin, Z.2    Tew, K.D.3    Ronai, Z.4
  • 70
    • 0015919035 scopus 로고
    • Properties of adenosine 3′,5′-monophosphate-dependent protein kinases isolated from bovine epididymal spermatozoa
    • Garbes D.L., First N.L., and Lardy H.A. Properties of adenosine 3′,5′-monophosphate-dependent protein kinases isolated from bovine epididymal spermatozoa. J. Biol. Chem. 248 (1973) 875-879
    • (1973) J. Biol. Chem. , vol.248 , pp. 875-879
    • Garbes, D.L.1    First, N.L.2    Lardy, H.A.3
  • 71
    • 0036708433 scopus 로고    scopus 로고
    • Activation of protein kinase A during human sperm capacitation and acrosome reaction
    • Lefièvre L., Jha K.N., de Lamirande E., Visconti P.E., and Gagnon C. Activation of protein kinase A during human sperm capacitation and acrosome reaction. J. Androl. 23 (2002) 709-716
    • (2002) J. Androl. , vol.23 , pp. 709-716
    • Lefièvre, L.1    Jha, K.N.2    de Lamirande, E.3    Visconti, P.E.4    Gagnon, C.5
  • 72
    • 2642516261 scopus 로고    scopus 로고
    • Phosphorylation of the arginine-X-X-(serine/threonine) motif in human sperm proteins during capacitation: modulation and protein kinase A dependency
    • O'Flaherty C., de Lamirande E., and Gagnon C. Phosphorylation of the arginine-X-X-(serine/threonine) motif in human sperm proteins during capacitation: modulation and protein kinase A dependency. Mol. Hum. Reprod. 10 (2004) 355-363
    • (2004) Mol. Hum. Reprod. , vol.10 , pp. 355-363
    • O'Flaherty, C.1    de Lamirande, E.2    Gagnon, C.3
  • 73
    • 0942297993 scopus 로고    scopus 로고
    • Rapid PKA-catalyzed phosphorylation of boar proteins induced by the capacitating agent bicarbonate
    • Harrison R.A.P. Rapid PKA-catalyzed phosphorylation of boar proteins induced by the capacitating agent bicarbonate. Mol. Reprod. Dev. 76 (2004) 337-352
    • (2004) Mol. Reprod. Dev. , vol.76 , pp. 337-352
    • Harrison, R.A.P.1
  • 74
    • 0031049037 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphorylation during bovine sperm capacitation by a cyclic adenosine 3′, 5′-monophosphate-dependent pathway
    • Galantino-Homer H.L., Visconti P.E., and Kopf G.S. Regulation of protein tyrosine phosphorylation during bovine sperm capacitation by a cyclic adenosine 3′, 5′-monophosphate-dependent pathway. Biol. Reprod. 56 (1997) 707-719
    • (1997) Biol. Reprod. , vol.56 , pp. 707-719
    • Galantino-Homer, H.L.1    Visconti, P.E.2    Kopf, G.S.3
  • 75
    • 0034887719 scopus 로고    scopus 로고
    • Capacitation is associated with tyrosine phosphorylation and tyrosine-like activity of pig sperm proteins
    • Tardif S., Dubé C., Chevalier S., and Bailey J.L. Capacitation is associated with tyrosine phosphorylation and tyrosine-like activity of pig sperm proteins. Biol. Reprod. 65 (2001) 784-792
    • (2001) Biol. Reprod. , vol.65 , pp. 784-792
    • Tardif, S.1    Dubé, C.2    Chevalier, S.3    Bailey, J.L.4
  • 76
    • 0032985619 scopus 로고    scopus 로고
    • Roles of bicarbonate, cAMP, and protein tyrosine phosphorylation on capacitation and the spontaneous acrosome reaction of hamster sperm
    • Visconti P.E., Stewart-Savage J., Blasco A., Battaglia L., Miranda P., Kopf G.S., and Tezon J.G. Roles of bicarbonate, cAMP, and protein tyrosine phosphorylation on capacitation and the spontaneous acrosome reaction of hamster sperm. Biol. Reprod. 61 (1999) 76-84
    • (1999) Biol. Reprod. , vol.61 , pp. 76-84
    • Visconti, P.E.1    Stewart-Savage, J.2    Blasco, A.3    Battaglia, L.4    Miranda, P.5    Kopf, G.S.6    Tezon, J.G.7
  • 77
    • 0034947017 scopus 로고    scopus 로고
    • A redox-regulated tyrosine phosphorylation cascade in rat spermatozoa
    • Lewis B., and Aitken R.J. A redox-regulated tyrosine phosphorylation cascade in rat spermatozoa. J. Androl. 22 (2001) 611-622
    • (2001) J. Androl. , vol.22 , pp. 611-622
    • Lewis, B.1    Aitken, R.J.2
  • 78
    • 0037379268 scopus 로고    scopus 로고
    • Phosphorylation of protein tyrosine residues in fresh and cryopreserved stallion spermatozoa under capacitating conditions
    • Pommer A., Rutllant J., and Meyers S.A. Phosphorylation of protein tyrosine residues in fresh and cryopreserved stallion spermatozoa under capacitating conditions. Biol. Reprod. 68 (2003) 1208-1214
    • (2003) Biol. Reprod. , vol.68 , pp. 1208-1214
    • Pommer, A.1    Rutllant, J.2    Meyers, S.A.3
  • 79
    • 0141695189 scopus 로고    scopus 로고
    • Specific order in the appearance of protein tyrosine phosphorylation patterns is functionally coordinated with dog sperm hyperactivation and capacitation
    • Petrunkina A.M., Simon K., Guzel-Apel A., and Topfer-Petersen E. Specific order in the appearance of protein tyrosine phosphorylation patterns is functionally coordinated with dog sperm hyperactivation and capacitation. J. Androl. 24 (2003) 423-437
    • (2003) J. Androl. , vol.24 , pp. 423-437
    • Petrunkina, A.M.1    Simon, K.2    Guzel-Apel, A.3    Topfer-Petersen, E.4
  • 80
    • 0030602027 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphorylation in human sperm by a calcium/calmodulin-dependent mechanism: identification of A kinase anchor proteins as major substrates for tyrosine phosphorylation
    • Carrera A., Moos J., Nig X.P., Gerton G.L., Kopf G.S., and Moss S.B. Regulation of protein tyrosine phosphorylation in human sperm by a calcium/calmodulin-dependent mechanism: identification of A kinase anchor proteins as major substrates for tyrosine phosphorylation. Dev. Biol. 180 (1996) 284-296
    • (1996) Dev. Biol. , vol.180 , pp. 284-296
    • Carrera, A.1    Moos, J.2    Nig, X.P.3    Gerton, G.L.4    Kopf, G.S.5    Moss, S.B.6
  • 82
    • 0032211431 scopus 로고    scopus 로고
    • Paradoxical effect of reagents for sulfhydryl and disulfide groups on human sperm capacitation and superoxide production
    • de Lamirande E., and Gagnon C. Paradoxical effect of reagents for sulfhydryl and disulfide groups on human sperm capacitation and superoxide production. Free Radic. Biol. Med. 25 (1998) 803-817
    • (1998) Free Radic. Biol. Med. , vol.25 , pp. 803-817
    • de Lamirande, E.1    Gagnon, C.2
  • 84
    • 1642397122 scopus 로고    scopus 로고
    • Novel tyrosine-phosphorylated post-pyruvate metabolic enzyme, dihydrolipoamide dehydrogenase, involved in capacitation of hamster spermatozoa
    • Mitra K., and Shivaji S. Novel tyrosine-phosphorylated post-pyruvate metabolic enzyme, dihydrolipoamide dehydrogenase, involved in capacitation of hamster spermatozoa. Biol. Reprod. 70 (2004) 887-899
    • (2004) Biol. Reprod. , vol.70 , pp. 887-899
    • Mitra, K.1    Shivaji, S.2
  • 85
    • 21844463288 scopus 로고    scopus 로고
    • Novelty of the pyruvate metabolic enzyme dihydrolipoamide dehydrogenase in spermatozoa
    • Mitra K., Rangaraj N., and Shivaji S. Novelty of the pyruvate metabolic enzyme dihydrolipoamide dehydrogenase in spermatozoa. J. Biol. Chem. 280 (2005) 25743-25753
    • (2005) J. Biol. Chem. , vol.280 , pp. 25743-25753
    • Mitra, K.1    Rangaraj, N.2    Shivaji, S.3
  • 87
    • 0029789196 scopus 로고    scopus 로고
    • Extracellular calcium negatively modulates tyrosine phosphorylation and tyrosine kinase activity during capacitation of human spermatozoa
    • Luconi M., Krausz C., Forti G., and Baldi E. Extracellular calcium negatively modulates tyrosine phosphorylation and tyrosine kinase activity during capacitation of human spermatozoa. Biol. Reprod. 55 (1996) 207-216
    • (1996) Biol. Reprod. , vol.55 , pp. 207-216
    • Luconi, M.1    Krausz, C.2    Forti, G.3    Baldi, E.4
  • 88
    • 0036085646 scopus 로고    scopus 로고
    • Regulation of the human sperm tyrosine kinase c-yes: activation by cyclic adenosine 3′,5′-monophosphate and inhibition by Ca(2+)
    • Leclerc P., and Goupil S. Regulation of the human sperm tyrosine kinase c-yes: activation by cyclic adenosine 3′,5′-monophosphate and inhibition by Ca(2+). Biol. Reprod. 67 (2002) 301-307
    • (2002) Biol. Reprod. , vol.67 , pp. 301-307
    • Leclerc, P.1    Goupil, S.2
  • 89
    • 0026446999 scopus 로고
    • Effects of modulators of protein kinases and phosphatases on mouse sperm capacitation
    • Furuya S., Endo Y., Oba M., Nozawa S., and Suzuki S. Effects of modulators of protein kinases and phosphatases on mouse sperm capacitation. J. Assist. Reprod. Genet. 9 (1992) 391-399
    • (1992) J. Assist. Reprod. Genet. , vol.9 , pp. 391-399
    • Furuya, S.1    Endo, Y.2    Oba, M.3    Nozawa, S.4    Suzuki, S.5
  • 90
    • 0027510718 scopus 로고
    • Cyclic AMP-dependent phosphorylation of epididymal mouse sperm proteins during capacitation in vitro: identification of a M(r) 95,000 phosphotyrosine-containing protein
    • Duncan A.E., and Fraser L.R. Cyclic AMP-dependent phosphorylation of epididymal mouse sperm proteins during capacitation in vitro: identification of a M(r) 95,000 phosphotyrosine-containing protein. J. Reprod. Fertil. 97 (1993) 287-299
    • (1993) J. Reprod. Fertil. , vol.97 , pp. 287-299
    • Duncan, A.E.1    Fraser, L.R.2
  • 91
    • 0031573950 scopus 로고    scopus 로고
    • Regulation, localization, and anchoring of protein kinase A subunits during mouse sperm capacitation
    • Visconti P.E., Johnson L.R., Oyaski M., Fornes M., Moss S.B., Gerton G.L., and Kopf G.S. Regulation, localization, and anchoring of protein kinase A subunits during mouse sperm capacitation. Dev. Biol. 192 (1997) 351-363
    • (1997) Dev. Biol. , vol.192 , pp. 351-363
    • Visconti, P.E.1    Johnson, L.R.2    Oyaski, M.3    Fornes, M.4    Moss, S.B.5    Gerton, G.L.6    Kopf, G.S.7
  • 92
    • 0031595786 scopus 로고    scopus 로고
    • 2+, cyclic 3′,5′adenosine monophosphate, the superoxide anion, and tyrosine phosphorylation in relation to human sperm capacitation and motility
    • 2+, cyclic 3′,5′adenosine monophosphate, the superoxide anion, and tyrosine phosphorylation in relation to human sperm capacitation and motility. J. Androl. 19 (1998) 434-443
    • (1998) J. Androl. , vol.19 , pp. 434-443
    • Leclerc, P.1    de Lamirande, E.2    Gagnon, C.3
  • 93
    • 0035653735 scopus 로고    scopus 로고
    • A-kinase anchor proteins in endocrine systems and reproduction
    • Moss S.B., and Gerton G.L. A-kinase anchor proteins in endocrine systems and reproduction. Trends Endocrinol. Metab. 12 (2001) 434-440
    • (2001) Trends Endocrinol. Metab. , vol.12 , pp. 434-440
    • Moss, S.B.1    Gerton, G.L.2
  • 95
    • 0032878514 scopus 로고    scopus 로고
    • Single amino acid determines specificity of binding of protein kinase A regulatory subunits by protein kinase A anchoring proteins
    • Mikki K., and Eddy E.M. Single amino acid determines specificity of binding of protein kinase A regulatory subunits by protein kinase A anchoring proteins. J. Biol. Chem. 274 (1999) 34384-34390
    • (1999) J. Biol. Chem. , vol.274 , pp. 34384-34390
    • Mikki, K.1    Eddy, E.M.2
  • 96
    • 0036712098 scopus 로고    scopus 로고
    • Different signal transduction pathways are involved during human sperm capacitation induced by biological and pharmacological agents
    • Thundathil J., De Lamirande E., and Gagnon C. Different signal transduction pathways are involved during human sperm capacitation induced by biological and pharmacological agents. Mol. Hum. Reprod. 8 (2002) 811-816
    • (2002) Mol. Hum. Reprod. , vol.8 , pp. 811-816
    • Thundathil, J.1    De Lamirande, E.2    Gagnon, C.3
  • 97
    • 0037377892 scopus 로고    scopus 로고
    • Nitric oxide regulates the phosphorylation of the threonine(glutamine(tyrosine motif in proteins of human spermatozoa during capacitation
    • Thundathil J., De Lamirande E., and Gagnon C. Nitric oxide regulates the phosphorylation of the threonine(glutamine(tyrosine motif in proteins of human spermatozoa during capacitation. Biol. Reprod. 68 (2003) 1291-1298
    • (2003) Biol. Reprod. , vol.68 , pp. 1291-1298
    • Thundathil, J.1    De Lamirande, E.2    Gagnon, C.3
  • 98
    • 1242272860 scopus 로고    scopus 로고
    • Crosstalk between protein kinase A and C regulates phospholipase D and F-actin formation during sperm capacitation
    • Cohen G., Rubinstein S., Gur Y., and Breitbart H. Crosstalk between protein kinase A and C regulates phospholipase D and F-actin formation during sperm capacitation. Dev. Biol. 267 (2004) 230-241
    • (2004) Dev. Biol. , vol.267 , pp. 230-241
    • Cohen, G.1    Rubinstein, S.2    Gur, Y.3    Breitbart, H.4
  • 99
    • 0037059766 scopus 로고    scopus 로고
    • Phosphorylation of inositol 1,4,5-triphosphate receptors in parotid acinar cells
    • Bruce J.I.E., Shuttleworth T.J., Giovannucci D.R., and Yule D.I. Phosphorylation of inositol 1,4,5-triphosphate receptors in parotid acinar cells. J. Biol. Chem. 277 (2002) 1340-1348
    • (2002) J. Biol. Chem. , vol.277 , pp. 1340-1348
    • Bruce, J.I.E.1    Shuttleworth, T.J.2    Giovannucci, D.R.3    Yule, D.I.4
  • 100
    • 0036652968 scopus 로고    scopus 로고
    • A mass spectrometry-based proteomic approach for identification of serine/threonine-phosphorylated proteins by enrichment with phospho-specific antibodies
    • Grøndborg M., Kristiansen T.Z., Stensballe A., Andersen J.S., Ohara O., Mann M., Jensen O.N., and Pandey A. A mass spectrometry-based proteomic approach for identification of serine/threonine-phosphorylated proteins by enrichment with phospho-specific antibodies. Mol. Cell. Proteom. 1 (2002) 517-527
    • (2002) Mol. Cell. Proteom. , vol.1 , pp. 517-527
    • Grøndborg, M.1    Kristiansen, T.Z.2    Stensballe, A.3    Andersen, J.S.4    Ohara, O.5    Mann, M.6    Jensen, O.N.7    Pandey, A.8
  • 101
    • 0032552855 scopus 로고    scopus 로고
    • Evidence for a tyrosine kinase-dependent activation of the adenylyl cyclase/PKA cascade downstream from the G-protein-linked endothelin ETA receptor in vascular smooth muscle
    • El-Mowafy A.M., and White R.E. Evidence for a tyrosine kinase-dependent activation of the adenylyl cyclase/PKA cascade downstream from the G-protein-linked endothelin ETA receptor in vascular smooth muscle. Biochem. Biophys. Res. Commun. 251 (1998) 494-500
    • (1998) Biochem. Biophys. Res. Commun. , vol.251 , pp. 494-500
    • El-Mowafy, A.M.1    White, R.E.2
  • 102
    • 0030747751 scopus 로고    scopus 로고
    • Modulation of cyclic AMP levels in a clonal neural cell line by inhibitors of tyrosine phosphorylation
    • Stringfield T.M., and Morimoto B.H. Modulation of cyclic AMP levels in a clonal neural cell line by inhibitors of tyrosine phosphorylation. Biochem. Pharmacol. 53 (1997) 1271-1278
    • (1997) Biochem. Pharmacol. , vol.53 , pp. 1271-1278
    • Stringfield, T.M.1    Morimoto, B.H.2
  • 103
    • 0031978060 scopus 로고    scopus 로고
    • Phosphorylation of Shc proteins in human sperm in response to capacitation and progesterone treatment
    • Morte C., Iborra A., and Martinez P. Phosphorylation of Shc proteins in human sperm in response to capacitation and progesterone treatment. Mol. Reprod. Dev. 50 (1998) 113-120
    • (1998) Mol. Reprod. Dev. , vol.50 , pp. 113-120
    • Morte, C.1    Iborra, A.2    Martinez, P.3
  • 104
    • 18644383152 scopus 로고    scopus 로고
    • Various protein kinases regulate human sperm acrosome reaction and the associated phosphorylation of Tyr residues and of the Thr-Glu-Thr motif
    • Liguori L., de Lamirande E., Minelli A., and Gagnon C. Various protein kinases regulate human sperm acrosome reaction and the associated phosphorylation of Tyr residues and of the Thr-Glu-Thr motif. Mol. Hum. Reprod. 3 (2005) 211-221
    • (2005) Mol. Hum. Reprod. , vol.3 , pp. 211-221
    • Liguori, L.1    de Lamirande, E.2    Minelli, A.3    Gagnon, C.4
  • 105
    • 0034667593 scopus 로고    scopus 로고
    • Meaningful relationships: the regulation of the Ras/Raf/MEK/ERK pathway by protein interactions
    • Kolch W. Meaningful relationships: the regulation of the Ras/Raf/MEK/ERK pathway by protein interactions. Biochem. J. 351 (2000) 289-306
    • (2000) Biochem. J. , vol.351 , pp. 289-306
    • Kolch, W.1
  • 106
    • 0032928614 scopus 로고    scopus 로고
    • Mitogen activated protein kinase: conservation of a three-kinase module from yeast to human
    • Windmann C., Gibson S., Jarpe M.B., and Johnson G.L. Mitogen activated protein kinase: conservation of a three-kinase module from yeast to human. Physiol. Rev. 79 (1999) 143-180
    • (1999) Physiol. Rev. , vol.79 , pp. 143-180
    • Windmann, C.1    Gibson, S.2    Jarpe, M.B.3    Johnson, G.L.4
  • 107
    • 0029055761 scopus 로고
    • Components of a new human protein kinase signal transduction pathway
    • Zhou G., Bao Z.Q., and Dixon J.E. Components of a new human protein kinase signal transduction pathway. J. Biol. Chem. 270 (1995) 12665-12669
    • (1995) J. Biol. Chem. , vol.270 , pp. 12665-12669
    • Zhou, G.1    Bao, Z.Q.2    Dixon, J.E.3
  • 108
    • 0033590164 scopus 로고    scopus 로고
    • Distantly related cousins of MAP kinase: biochemical properties and possible physiological functions
    • Miyata Y., and Nishida E. Distantly related cousins of MAP kinase: biochemical properties and possible physiological functions. Biochem. Biophys. Res. Commun. 266 (1999) 291-295
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 291-295
    • Miyata, Y.1    Nishida, E.2
  • 109
    • 0035815665 scopus 로고    scopus 로고
    • Molecular cloning of mouse ERK5/BMK1 splice variants and characterization of ERK5 functional domains
    • Yan C., Lui H., Lee J.D., Abe J., and Berk B.C. Molecular cloning of mouse ERK5/BMK1 splice variants and characterization of ERK5 functional domains. J. Biol. Chem. 276 (2001) 10870-10878
    • (2001) J. Biol. Chem. , vol.276 , pp. 10870-10878
    • Yan, C.1    Lui, H.2    Lee, J.D.3    Abe, J.4    Berk, B.C.5
  • 112
    • 0029807306 scopus 로고    scopus 로고
    • Differential activation of mitogen-activated protein kinases by nitric oxide-related species
    • Lander H.M., Jacovina A.T., Davis R.J., and Tauras J.M. Differential activation of mitogen-activated protein kinases by nitric oxide-related species. J. Biol. Chem. 271 (1996) 19705-19709
    • (1996) J. Biol. Chem. , vol.271 , pp. 19705-19709
    • Lander, H.M.1    Jacovina, A.T.2    Davis, R.J.3    Tauras, J.M.4
  • 113
    • 0028047288 scopus 로고    scopus 로고
    • Westendorf, J.M.; Rao, P.N.; Gerace, L. Cloning of cDNA for M-phase phosphoproteins recognized by the MPM2 monoclonal antibody and determination of the phosphorylated state. Proc. Natl. Acad. Sci. USA 91:714-718; 1004.
  • 114
    • 15044338824 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase in disease: timing, location, and scaffolding
    • Wymann M.P., and Marone R. Phosphoinositide 3-kinase in disease: timing, location, and scaffolding. Curr. Opin. Cell. Biol. 17 (2005) 141-149
    • (2005) Curr. Opin. Cell. Biol. , vol.17 , pp. 141-149
    • Wymann, M.P.1    Marone, R.2
  • 115
    • 2442483229 scopus 로고
    • Role of protein kinase C in human sperm acrosome reaction
    • Human Sperm Acrosome Reaction. Fenichel P., and Parinaud J. (Eds), John Libbey Eurotext, Montrouge
    • Naor Z., Rotem R., and Kalina M. Role of protein kinase C in human sperm acrosome reaction. In: Fenichel P., and Parinaud J. (Eds). Human Sperm Acrosome Reaction. Colloque INSERM No. 236 (1995), John Libbey Eurotext, Montrouge 217-223
    • (1995) Colloque INSERM No. 236 , pp. 217-223
    • Naor, Z.1    Rotem, R.2    Kalina, M.3
  • 116
    • 0024724936 scopus 로고
    • 2+- and phospholipid-independent activation of protein kinase C by selective oxidation of the regulatory domain
    • 2+- and phospholipid-independent activation of protein kinase C by selective oxidation of the regulatory domain. Proc. Natl. Acad. Sci. USA 86 (1989) 6758-6762
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6758-6762
    • Gopalakrishna, R.1    Anderson, W.2
  • 118
    • 0029068249 scopus 로고
    • Activation of the lck tyrosine protein kinase by hydrogen peroxide requires the phosphorylation of Tyr-394
    • Hardwick J.S., and Sefton B.M. Activation of the lck tyrosine protein kinase by hydrogen peroxide requires the phosphorylation of Tyr-394. Proc. Natl. Acad. Sci. USA 92 (1995) 4527-4531
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4527-4531
    • Hardwick, J.S.1    Sefton, B.M.2
  • 120
    • 0028872649 scopus 로고
    • Specificity of receptor tyrosine kinase signaling-Transient versus sustained extracellular signal-regulated kinase activation
    • Marshall C.J. Specificity of receptor tyrosine kinase signaling-Transient versus sustained extracellular signal-regulated kinase activation. Cell 80 (1995) 179-185
    • (1995) Cell , vol.80 , pp. 179-185
    • Marshall, C.J.1
  • 121
  • 122
    • 0642276003 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatases during receptor tyrosine kinase signal transduction
    • Chiarugi P., and Cirr P. Redox regulation of protein tyrosine phosphatases during receptor tyrosine kinase signal transduction. Trends Biochem. Sci. 28 (2003) 509-514
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 509-514
    • Chiarugi, P.1    Cirr, P.2
  • 123
    • 0033650023 scopus 로고    scopus 로고
    • Cellular thiols and redox-regulated signal transduction
    • Sen C.K. Cellular thiols and redox-regulated signal transduction. Curr. Top. Cell. Regul. 36 (2000) 1-30
    • (2000) Curr. Top. Cell. Regul. , vol.36 , pp. 1-30
    • Sen, C.K.1
  • 124
    • 0242321027 scopus 로고    scopus 로고
    • Redox control of changes in protein sulfhydryl levels during human sperm capacitation
    • de Lamirande E., and Gagnon C. Redox control of changes in protein sulfhydryl levels during human sperm capacitation. Free Radic. Biol. Med. 35 (2003) 1271-1285
    • (2003) Free Radic. Biol. Med. , vol.35 , pp. 1271-1285
    • de Lamirande, E.1    Gagnon, C.2
  • 125
    • 9944235916 scopus 로고    scopus 로고
    • The role of cysteine residues as redox-sensitive regulatory switches
    • Barford D. The role of cysteine residues as redox-sensitive regulatory switches. Curr. Opin. Struct. Biol. 14 (2004) 679-686
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 679-686
    • Barford, D.1
  • 126
    • 17644371347 scopus 로고    scopus 로고
    • Functions and mechanisms of redox regulation of cysteine-based phosphatases
    • Salmen A., and Barford D. Functions and mechanisms of redox regulation of cysteine-based phosphatases. Antioxid. Redox Signaling 7 (2005) 560-577
    • (2005) Antioxid. Redox Signaling , vol.7 , pp. 560-577
    • Salmen, A.1    Barford, D.2
  • 127
    • 0037102481 scopus 로고    scopus 로고
    • Differential susceptibilities of serine/threonine phosphatases to oxidative and nitrosative stress
    • Sommer D., Coleman S., Swanson S.A., and Stemmer P.M. Differential susceptibilities of serine/threonine phosphatases to oxidative and nitrosative stress. Arch. Biochem. Biophys. 404 (2002) 271-278
    • (2002) Arch. Biochem. Biophys. , vol.404 , pp. 271-278
    • Sommer, D.1    Coleman, S.2    Swanson, S.A.3    Stemmer, P.M.4
  • 128
    • 0026452478 scopus 로고
    • Selective inhibition of protein tyrosine phosphatase activities by H2O2 and vanadate in vitro
    • Hecht D., and Zick Y. Selective inhibition of protein tyrosine phosphatase activities by H2O2 and vanadate in vitro. Biochem. Biophys. Res. Commun. 188 (1992) 773-779
    • (1992) Biochem. Biophys. Res. Commun. , vol.188 , pp. 773-779
    • Hecht, D.1    Zick, Y.2
  • 129
    • 0037108204 scopus 로고    scopus 로고
    • 2 regulates the activation of distinct MAPK pathways
    • 2 regulates the activation of distinct MAPK pathways. Free Radic. Biol. Med. 33 (2002) 1121-1132
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 1121-1132
    • Lee, K.1    Esselman, W.J.2
  • 130
    • 0030028222 scopus 로고    scopus 로고
    • MKP-3, a novel cytosolic protein-tyrosine phosphatase that exemplifies a new class of mitogen-activated protein kinase phosphatase
    • Muda M., Boschert U., Dickinson R., Martinou J.C., Martinou I., Camps M., Schlegel W., and Arkinstall S. MKP-3, a novel cytosolic protein-tyrosine phosphatase that exemplifies a new class of mitogen-activated protein kinase phosphatase. J. Biol. Chem. 271 (1996) 4319-4326
    • (1996) J. Biol. Chem. , vol.271 , pp. 4319-4326
    • Muda, M.1    Boschert, U.2    Dickinson, R.3    Martinou, J.C.4    Martinou, I.5    Camps, M.6    Schlegel, W.7    Arkinstall, S.8
  • 132
    • 0033970533 scopus 로고    scopus 로고
    • Dual specificity phosphatases: a gene family for control of MAP kinase function
    • Camps M., Nichols A., and Arkinstall S. Dual specificity phosphatases: a gene family for control of MAP kinase function. FASEB J. 14 (1999) 6-16
    • (1999) FASEB J. , vol.14 , pp. 6-16
    • Camps, M.1    Nichols, A.2    Arkinstall, S.3
  • 133
    • 14044277677 scopus 로고    scopus 로고
    • Reversible oxidation of ERK-directed protein phosphatases drives oxidative toxicity in neurons
    • Levinthal D.J., and DeFranco D.B. Reversible oxidation of ERK-directed protein phosphatases drives oxidative toxicity in neurons. J. Biol. Chem. 280 (2005) 5875-5883
    • (2005) J. Biol. Chem. , vol.280 , pp. 5875-5883
    • Levinthal, D.J.1    DeFranco, D.B.2


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