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Volumn 80, Issue 6, 2009, Pages 1239-1252

Identification of protein tyrosine phosphatases and dual-specificity phosphatases in mammalian spermatozoa and their role in sperm motility and protein tyrosine phosphorylation

Author keywords

Dual specificity phosphatases; Gamete biology; Mammalian spermatozoa; Pervanadate; Phosphatases; Signal transduction; Sodium orthovanadate; Sperm capacitation; Sperm motility and transport; Tyrosine phosphatases; Tyrosine phosphorylation

Indexed keywords

CD45 ANTIGEN; DUAL SPECIFICITY PHOSPHATASE; DUAL SPECIFICITY PHOSPHATASE 2; DUAL SPECIFICITY PHOSPHATASE 3; DUAL SPECIFICITY PHOSPHATASE 4; DUAL SPECIFICITY PHOSPHATASE 6; MITOGEN ACTIVATED PROTEIN KINASE PHOSPHATASE 1; NON RECEPTOR PROTEIN TYROSINE PHOSPHATASE 3; PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE SHP 1; PROTEIN TYROSINE PHOSPHATASE SHP 2; UNCLASSIFIED DRUG;

EID: 66149120946     PISSN: 00063363     EISSN: 15297268     Source Type: Journal    
DOI: 10.1095/biolreprod.108.073486     Document Type: Article
Times cited : (59)

References (59)
  • 1
    • 0028149381 scopus 로고
    • The coordinated action of protein tyrosine phosphatases and kinases in cell signaling
    • DOI 10.1016/0968-0004(94)90134-1
    • Sun H, Tonks NK. The coordinated action of protein tyrosine phosphatases and kinases in cell signaling. Trends Biochem Sci 1994; 19:480-485. (Pubitemid 24342761)
    • (1994) Trends in Biochemical Sciences , vol.19 , Issue.11 , pp. 480-485
    • Sun, H.1    Tonks, N.K.2
  • 2
    • 36749010218 scopus 로고    scopus 로고
    • The Age of Crosstalk: Phosphorylation, Ubiquitination, and Beyond
    • DOI 10.1016/j.molcel.2007.11.019, PII S1097276507007988
    • Hunter T. The age of crosstalk: phosphorylation, ubiquitination, and beyond. Mol Cell 2007; 28:730-738. (Pubitemid 350217067)
    • (2007) Molecular Cell , vol.28 , Issue.5 , pp. 730-738
    • Hunter, T.1
  • 4
    • 38149095757 scopus 로고    scopus 로고
    • Sperm activation: Role of reactive oxygen species and kinases
    • de Laminarde E, O'Flaherty C. Sperm activation: role of reactive oxygen species and kinases. Biochim Biophys Acta 2008; 1784:106-115.
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 106-115
    • De Laminarde, E.1    O'Flaherty, C.2
  • 5
    • 34547842771 scopus 로고    scopus 로고
    • Biology of sperm capacitation: Evidence for multiple signalling pathways
    • Tulsiani DR, Zeng HT, bou-Haila A. Biology of sperm capacitation: evidence for multiple signalling pathways. Soc Reprod Fertil Suppl 2007; 63:257-272.
    • (2007) Soc Reprod Fertil Suppl , vol.63 , pp. 257-272
    • Tulsiani, D.R.1    Zeng, H.T.2    Bou-Haila, A.3
  • 6
    • 18144403561 scopus 로고    scopus 로고
    • Role of tyrosine phosphorylation in sperm capacitation/acrosome reaction
    • Naz RK, Rajesh PB. Role of tyrosine phosphorylation in sperm capacitation/acrosome reaction. Reprod Biol Endocrinol 2004; 2:75.
    • (2004) Reprod Biol Endocrinol , vol.2 , pp. 75
    • Naz, R.K.1    Rajesh, P.B.2
  • 8
    • 47749098885 scopus 로고    scopus 로고
    • Changes of PKA and PDK1 in the principal piece of boar spermatozoa treated with a cell-permeable cAMP analog to induce flagellar hyperactivation
    • Harayama H, Nakamura K. Changes of PKA and PDK1 in the principal piece of boar spermatozoa treated with a cell-permeable cAMP analog to induce flagellar hyperactivation. Mol Reprod Dev 2008; 75:1396-1407.
    • (2008) Mol Reprod Dev , vol.75 , pp. 1396-1407
    • Harayama, H.1    Nakamura, K.2
  • 9
    • 33746659808 scopus 로고    scopus 로고
    • A cyclic adenosine 3′,5′-monophosphate-dependent protein kinase C activation is involved in the hyperactivation of boar spermatozoa
    • DOI 10.1002/mrd.20460
    • Harayama H, Miyake M. A cyclic adenosine 3′,5′-monophosphate- dependent protein kinase C activation is involved in the hyperactivation of boar spermatozoa. Mol Reprod Dev 2006; 73:1169-1178. (Pubitemid 44148375)
    • (2006) Molecular Reproduction and Development , vol.73 , Issue.9 , pp. 1169-1178
    • Harayama, H.1    Miyake, M.2
  • 10
    • 7744238317 scopus 로고    scopus 로고
    • A cyclic adenosine 3′,5′-monophosphate-induced tyrosine phosphorylation of syk protein tyrosine kinase in the flagella of boar spermatozoa
    • DOI 10.1002/mrd.20176
    • Harayama H, Muroga M, Miyake M. A cyclic adenosine 3′,5′- monophosphate-induced tyrosine phosphorylation of Syk protein tyrosine kinase in the flagella of boar spermatozoa. Mol Reprod Dev 2004; 69:436-447. (Pubitemid 39463852)
    • (2004) Molecular Reproduction and Development , vol.69 , Issue.4 , pp. 436-447
    • Harayama, H.1    Muroga, M.2    Miyake, M.3
  • 11
    • 4444280587 scopus 로고    scopus 로고
    • A unique mechanism for cyclic adenosine 3′,5′-monophosphate- Induced increase of 32-kDa tyrosine-phosphorylated protein in boar spermatozoa
    • DOI 10.1002/mrd.20099
    • Harayama H, Sasaki K, Miyake M. A unique mechanism for cyclic adenosine 3′,5′-monophosphate-induced increase of 32-kDa tyrosine- phosphorylated protein in boar spermatozoa. Mol Reprod Dev 2004; 69:194-204. (Pubitemid 39195610)
    • (2004) Molecular Reproduction and Development , vol.69 , Issue.2 , pp. 194-204
    • Harayama, H.1    Sasaki, K.2    Miyake, M.3
  • 12
    • 10944221735 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the a Kinase Anchoring Protein 3 (AKAP3) and soluble adenylate cyclase are involved in the increase of human sperm motility by bicarbonate
    • DOI 10.1095/biolreprod.104.032490
    • Luconi M, Porazzi I, Ferruzzi P, Marchiani S, Forti G, Baldi E. Tyrosine phosphorylation of the A kinase anchoring protein 3 (AKAP3) and soluble adenylate cyclase are involved in the increase of human sperm motility by bicarbonate. Biol Reprod 2005; 72:22-32. (Pubitemid 40013750)
    • (2005) Biology of Reproduction , vol.72 , Issue.1 , pp. 22-32
    • Luconi, M.1    Porazzi, I.2    Ferruzzi, P.3    Marchiani, S.4    Forti, G.5    Baldi, E.6
  • 13
    • 0031687185 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphorylation in boar sperm through a cAMP-dependent pathway
    • DOI 10.1002/(SICI)1098-2795(199811)51:3<304::AID-MRD10>3.0.CO;2-2
    • 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. (Pubitemid 28445411)
    • (1998) Molecular Reproduction and Development , vol.51 , Issue.3 , pp. 304-314
    • Kalab, P.1    Peknicova, J.2    Geussova, G.3    Moos, J.4
  • 14
    • 7744234998 scopus 로고    scopus 로고
    • Implication of cAMP during porcine sperm capacitation and protein tyrosine phosphorylation
    • DOI 10.1002/mrd.20178
    • Tardif S, Lefievre L, Gagnon C, Bailey JL. Implication of cAMP during porcine sperm capacitation and protein tyrosine phosphorylation. Mol Reprod Dev 2004; 69:428-435. (Pubitemid 39463851)
    • (2004) Molecular Reproduction and Development , vol.69 , Issue.4 , pp. 428-435
    • Tardif, S.1    Lefievre, L.2    Gagnon, C.3    Bailey, J.L.4
  • 16
    • 3042818148 scopus 로고    scopus 로고
    • Inhibitors of phosphoinositide 3-kinase, LY294002 and wortmannin, affect sperm capacitation and associated phosphorylation of proteins differently: Ca2+-dependent divergences
    • Nauc V, de Laminarde E, Leclerc P, Gagnon C. Inhibitors of phosphoinositide 3-kinase, LY294002 and wortmannin, affect sperm capacitation and associated phosphorylation of proteins differently: Ca2+-dependent divergences. J Androl 2004; 25:573-585.
    • (2004) J Androl , vol.25 , pp. 573-585
    • Nauc, V.1    De Laminarde, E.2    Leclerc, P.3    Gagnon, C.4
  • 17
    • 33745223069 scopus 로고    scopus 로고
    • Regulation of acrosome reaction of fowl spermatozoa: Evidence for the involvement of protein kinase C and protein phosphatase-type 1 and/or -type 2A
    • DOI 10.1530/rep.1.01069
    • Ashizawa K, Wishart GJ, Katayama S, Takano D, Ranasinghe AR, Narumi K, Tsuzuki Y. Regulation of acrosome reaction of fowl spermatozoa: evidence for the involvement of protein kinase C and protein phosphatase-type 1 and/or -type 2A. Reproduction 2006; 131:1017-1024. (Pubitemid 43904975)
    • (2006) Reproduction , vol.131 , Issue.6 , pp. 1017-1024
    • Ashizawa, K.1    Wishart, G.J.2    Katayama, S.3    Takano, D.4    Ranasinghe, A.R.A.H.5    Narumi, K.6    Tsuzuki, Y.7
  • 18
    • 66149130780 scopus 로고    scopus 로고
    • Isoform identification and subcellular distribution of protein kinase D (PKD) in boar sperm
    • Gonzalez-Fernandez L, Tapia JA. Isoform identification and subcellular distribution of protein kinase D (PKD) in boar sperm. Reprod Domest Anim 2007; 42:94-99.
    • (2007) Reprod Domest Anim , vol.42 , pp. 94-99
    • Gonzalez-Fernandez, L.1    Tapia, J.A.2
  • 20
    • 47249158958 scopus 로고    scopus 로고
    • Identification of extracellular signal-regulated kinase 1/2 and p38 MAPK as regulators of human sperm motility and acrosome reaction and as predictors of poor spermatozoan quality
    • Almog T, Lazar S, Reiss N, Etkovitz N, Milch E, Rahamim N, Dobkin- Bekman M, Rotem R, Kalina M, Ramon J, Raziel A, Brietbart H, et al. Identification of extracellular signal-regulated kinase 1/2 and p38 MAPK as regulators of human sperm motility and acrosome reaction and as predictors of poor spermatozoan quality. J Biol Chem 2008; 283:14479-14489.
    • (2008) J Biol Chem , vol.283 , pp. 14479-14489
    • Almog, T.1    Lazar, S.2    Reiss, N.3    Etkovitz, N.4    Milch, E.5    Rahamim, N.6    Dobkin- Bekman, M.7    Rotem, R.8    Kalina, M.9    Ramon, J.10    Raziel, A.11    Brietbart, H.12
  • 21
    • 0032779471 scopus 로고    scopus 로고
    • Expression and phosphorylation of mitogen-activated protein kinases during spermatogenesis and epididymal sperm maturation in mice
    • DOI 10.1080/014850199262733
    • Lu Q, Sun QY, Breitbart H, Chen DY. Expression and phosphorylation of mitogen-activated protein kinases during spermatogenesis and epididymal sperm maturation in mice. Arch Androl 1999; 43:55-66. (Pubitemid 29331083)
    • (1999) Archives of Andrology , vol.43 , Issue.1 , pp. 55-66
    • Lu, Q.1    Sun, Q.Y.2    Breitbart, H.3    Chen, D.-Y.4
  • 22
    • 40949143524 scopus 로고    scopus 로고
    • Cytochrome C upregulation during capacitation and spontaneous acrosome reaction determines the fate of pig sperm cells: Linking proteome analysis
    • Choi YJ, Uhm SJ, Song SJ, Song H, Park JK, Kim T, Park C, Kim JH. Cytochrome C upregulation during capacitation and spontaneous acrosome reaction determines the fate of pig sperm cells: linking proteome analysis. J Reprod Dev 2008; 54:68-83.
    • (2008) J Reprod Dev , vol.54 , pp. 68-83
    • Choi, Y.J.1    Uhm, S.J.2    Song, S.J.3    Song, H.4    Park, J.K.5    Kim, T.6    Park, C.7    Kim, J.H.8
  • 23
    • 33748374699 scopus 로고    scopus 로고
    • Identification of the proteins present in the bull sperm cytosolic fraction enriched in tyrosine kinase activity: A proteomic approach
    • DOI 10.1002/pmic.200500578
    • Lalancette C, Faure RL, Leclerc P. Identification of the proteins present in the bull sperm cytosolic fraction enriched in tyrosine kinase activity: a proteomic approach. Proteomics 2006; 6:4523-4540. (Pubitemid 44336969)
    • (2006) Proteomics , vol.6 , Issue.16 , pp. 4523-4540
    • Lalancette, C.1    Faure, R.L.2    Leclerc, P.3
  • 24
    • 46049094886 scopus 로고    scopus 로고
    • The mouse sperm proteome characterized via IPG strip prefractionation and LC-MS/MS identification
    • Baker MA, Hetherington L, Reeves GM, Aitken RJ. The mouse sperm proteome characterized via IPG strip prefractionation and LC-MS/MS identification. Proteomics 2008; 8:1720-1730.
    • (2008) Proteomics , vol.8 , pp. 1720-1730
    • Baker, M.A.1    Hetherington, L.2    Reeves, G.M.3    Aitken, R.J.4
  • 25
    • 42049123062 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of bovine spermatozoa of varying fertility rates and identification of biomarkers associated with fertility
    • Peddinti D, Nanduri B, Kaya A, Feugang JM, Burgess SC, Memili E. Comprehensive proteomic analysis of bovine spermatozoa of varying fertility rates and identification of biomarkers associated with fertility. BMC Syst Biol 2008; 2:e19.
    • (2008) BMC Syst Biol , vol.2
    • Peddinti, D.1    Nanduri, B.2    Kaya, A.3    Feugang, J.M.4    Burgess, S.C.5    Memili, E.6
  • 27
    • 33747783640 scopus 로고    scopus 로고
    • Proteomic identification of human sperm proteins
    • DOI 10.1002/pmic.200600094
    • Martinez-Heredia J, Estanyol JM, Ballesca JL, Oliva R. Proteomic identification of human sperm proteins. Proteomics 2006; 6:4356-4369. (Pubitemid 44277037)
    • (2006) Proteomics , vol.6 , Issue.15 , pp. 4356-4369
    • Martinez-Heredia, J.1    Estanyol, J.M.2    Ballesca, J.L.3    Oliva, R.4
  • 28
    • 33646949472 scopus 로고    scopus 로고
    • Proteomic profiling of accessory structures from the mouse sperm flagellum
    • DOI 10.1074/mcp.M500322-MCP200
    • Cao W, Gerton GL, Moss SB. Proteomic profiling of accessory structures from the mouse sperm flagellum. Mol Cell Proteomics 2006; 5:801-810. (Pubitemid 43792790)
    • (2006) Molecular and Cellular Proteomics , vol.5 , Issue.5 , pp. 801-810
    • Cao, W.1    Gerton, G.L.2    Moss, S.B.3
  • 29
    • 11144326201 scopus 로고    scopus 로고
    • Use of phosphoproteomics to study tyrosine kinase activity in capacitating boar sperm: Kinase activity and capacitation
    • DOI 10.1016/j.theriogenology.2004.09.034, PII S0093691X04003255
    • Bailey JL, Tardif S, Dube C, Beaulieu M, Reyes-Moreno C, Lefievre L, Leclerc P. Use of phosphoproteomics to study tyrosine kinase activity in capacitating boar sperm: kinase activity and capacitation. Theriogenology 2005; 63:599-614. (Pubitemid 40033976)
    • (2005) Theriogenology , vol.63 , Issue.2 , pp. 599-614
    • Bailey, J.L.1    Tardif, S.2    Dube, C.3    Beaulieu, M.4    Reyes-Moreno, C.5    Lefievre, L.6    Leclerc, P.7
  • 30
    • 46349088983 scopus 로고    scopus 로고
    • Effects of protein phosphatase inhibitor calyculin a on the postacrosomal protein serine/threonine phosphorylation state and acrosome reaction in boar spermatozoa incubated with a cAMP analog
    • Adachi J, Tate S, Miyake M, Harayama H. Effects of protein phosphatase inhibitor calyculin A on the postacrosomal protein serine/threonine phosphorylation state and acrosome reaction in boar spermatozoa incubated with a cAMP analog. J Reprod Dev 2008; 54:171-176.
    • (2008) J Reprod Dev , vol.54 , pp. 171-176
    • Adachi, J.1    Tate, S.2    Miyake, M.3    Harayama, H.4
  • 31
    • 79961205333 scopus 로고    scopus 로고
    • Role(s) of the serine/threonine protein phosphatase 1 on mammalian sperm motility
    • DOI 10.1080/01485010701314032, PII 781952892
    • Han Y, Haines CJ, Feng HL. Role(s) of the serine/threonine protein phosphatase 1 on mammalian sperm motility. Arch Androl 2007; 53:169-177. (Pubitemid 47402848)
    • (2007) Archives of Andrology , vol.53 , Issue.4 , pp. 169-177
    • Han, Y.1    Haines, C.J.2    Feng, H.L.3
  • 32
    • 0027437525 scopus 로고
    • Effect of epidermal growth factor on human sperm capacitation
    • Furuya S, Endo Y, Oba M, Suzuki S, Nozawa S. Effect of epidermal growth factor on human sperm capacitation. Fertil Steril 1993; 60:905-910. (Pubitemid 23324783)
    • (1993) Fertility and Sterility , vol.60 , Issue.5 , pp. 905-910
    • Furuya, S.1    Endo, Y.2    Oba, M.3    Suzuki, S.4    Nozawa, S.5
  • 34
    • 33748316506 scopus 로고    scopus 로고
    • Identification of SRC as a key PKA-stimulated tyrosine kinase involved in the capacitation-associated hyperactivation of murine spermatozoa
    • DOI 10.1242/jcs.03055
    • Baker MA, Hetherington L, Aitken RJ. Identification of SRC as a key PKA-stimulated tyrosine kinase involved in the capacitation-associated hyperactivation of murine spermatozoa. J Cell Sci 2006; 119:3182-3192. (Pubitemid 44322132)
    • (2006) Journal of Cell Science , vol.119 , Issue.15 , pp. 3182-3192
    • Baker, M.A.1    Hetherington, L.2    Aitken, R.J.3
  • 35
    • 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, 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 2002; 67:301-307.
    • (2002) Biol Reprod , vol.67 , pp. 301-307
    • Leclerc, P.1    Goupil, S.2
  • 37
    • 4243193738 scopus 로고    scopus 로고
    • Tyrosine phosphorylation, thiol status, and protein tyrosine phosphatase in rat epididymal spermatozoa
    • DOI 10.1095/biolreprod.104.028035
    • Seligman J, Zipser Y, Kosower NS. Tyrosine phosphorylation, thiol status, and protein tyrosine phosphatase in rat epididymal spermatozoa. Biol Reprod 2004; 71:1009-1015. (Pubitemid 39108665)
    • (2004) Biology of Reproduction , vol.71 , Issue.3 , pp. 1009-1015
    • Seligman, J.1    Zipser, Y.2    Kosower, N.S.3
  • 38
    • 38949123682 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: Dual-specificity phosphatases in health and disease
    • Pulido R, Hooft van HR. Protein tyrosine phosphatases: dual-specificity phosphatases in health and disease. FEBS J 2008; 275:848-866.
    • (2008) FEBS J , vol.275 , pp. 848-866
    • Pulido, R.1    Hooft Van, H.R.2
  • 39
    • 11444267367 scopus 로고    scopus 로고
    • Boar sperm velocity and motility patterns under capacitating and non-capacitating incubation conditions
    • DOI 10.1016/j.theriogenology.2004.05.003, PII S0093691X04001566
    • Garcia HM, Aparicio IM, Nunez I, Garcia-Marin LJ, Gil MC, Pena Vega FJ. Boar sperm velocity and motility patterns under capacitating and noncapacitating incubation conditions. Theriogenology 2005; 63:795-805. (Pubitemid 40078152)
    • (2005) Theriogenology , vol.63 , Issue.3 , pp. 795-805
    • Garcia Herreros, M.1    Aparicio, I.M.2    Nunez, I.3    Garcia-Marin, L.J.4    Gil, M.C.5    Pena Vega, F.J.6
  • 40
    • 34547195786 scopus 로고    scopus 로고
    • Identification of sperm morphometric subpopulations in the canine ejaculate: Do they reflect different subpopulations in sperm chromatin integrity?
    • Nunez-Martinez I, Moran JM, Pena FJ. Identification of sperm morphometric subpopulations in the canine ejaculate: do they reflect different subpopulations in sperm chromatin integrity? Zygote 2007; 15:257-266.
    • (2007) Zygote , vol.15 , pp. 257-266
    • Nunez-Martinez, I.1    Moran, J.M.2    Pena, F.J.3
  • 42
    • 32144454027 scopus 로고    scopus 로고
    • Rottlerin inhibits stimulated enzymatic secretion and several intracellular signaling transduction pathways in pancreatic acinar cells by a non-PKC-δ;-dependent mechanism
    • DOI 10.1016/j.bbamcr.2005.10.007, PII S0167488905002211
    • Tapia JA, Jensen RT, Garcia-Marin LJ. Rottlerin inhibits stimulated enzymatic secretion and several intracellular signaling transduction pathways in pancreatic acinar cells by a non-PKC-delta-dependent mechanism. Biochim Biophys Acta 2006; 1763:25-38. (Pubitemid 43208729)
    • (2006) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1763 , Issue.1 , pp. 25-38
    • Tapia, J.A.1    Jensen, R.T.2    Garcia-Marin, L.J.3
  • 43
    • 0025953405 scopus 로고
    • Use of vanadate as protein-phosphotyrosine phosphatase inhibitor
    • Gordon JA. Use of vanadate as protein-phosphotyrosine phosphatase inhibitor. Methods Enzymol 1991; 201:477-482.
    • (1991) Methods Enzymol , vol.201 , pp. 477-482
    • Gordon, J.A.1
  • 44
    • 0032540221 scopus 로고    scopus 로고
    • Properties of pervanadate and permolybdate
    • Mikalsen SO, Kaalhus O. Properties of pervanadate and permolybdate. J Biol Chem 1998; 273:10036-10045.
    • (1998) J Biol Chem , vol.273 , pp. 10036-10045
    • Mikalsen, S.O.1    Kaalhus, O.2
  • 45
    • 0024416087 scopus 로고
    • Pervanadate [peroxide(s) of vanadate] mimics insulin action in rat adipocytes via activation of the insulin receptor tyrosine kinase
    • Fantus IG, Kadota S, Deragon G, Foster B, Posner BI. Pervanadate [peroxide(s) of vanadate] mimics insulin action in rat adipocytes via activation of the insulin receptor tyrosine kinase. Biochemistry 1989; 28:8864-8871. (Pubitemid 19278548)
    • (1989) Biochemistry , vol.28 , Issue.22 , pp. 8864-8871
    • Fantus, I.G.1    Kadota, S.2    Deragon, G.3    Foster, B.4    Posner, B.I.5
  • 46
    • 20544432079 scopus 로고    scopus 로고
    • The proacrosin binding protein, sp32, is tyrosine phosphorylated during capacitation of pig sperm
    • DOI 10.2164/jandrol.04163
    • Dube C, Leclerc P, Baba T, Reyes-Moreno C, Bailey JL. The proacrosin binding protein, sp32, is tyrosine phosphorylated during capacitation of pig sperm. J Androl 2005; 26:519-528. (Pubitemid 40847865)
    • (2005) Journal of Andrology , vol.26 , Issue.4 , pp. 519-528
    • Dube, C.1    Leclerc, P.2    Baba, T.3    Reyes-Moreno, C.4    Bailey, J.L.5
  • 47
    • 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 JL. Capacitation is associated with tyrosine phosphorylation and tyrosine kinase-like activity of pig sperm proteins. Biol Reprod 2001; 65:784-792. (Pubitemid 32777364)
    • (2001) Biology of Reproduction , vol.65 , Issue.3 , pp. 784-792
    • Tardif, S.1    Dube, C.2    Chevalier, S.3    Bailey, J.L.4
  • 48
    • 0345643446 scopus 로고    scopus 로고
    • Plasma membrane-associated protein tyrosine phosphatase activity in hamster spermatozoa
    • DOI 10.1002/(SICI)1098-2795(199905)53:1<42::AID-MRD5>3.0.CO;2-5
    • Devi KU, Jha K, Shivaji S. Plasma membrane-associated protein tyrosine phosphatase activity in hamster spermatozoa. Mol Reprod Dev 1999; 53:42-50. (Pubitemid 29222101)
    • (1999) Molecular Reproduction and Development , vol.53 , Issue.1 , pp. 42-50
    • Uma Devi, K.1    Jha, K.2    Shivaji, S.3
  • 49
    • 0347284250 scopus 로고    scopus 로고
    • Requirement of protein tyrosine kinase and phosphatase activities for human sperm exocytosis
    • DOI 10.1016/j.ydbio.2003.09.032
    • Tomes CN, Roggero CM, de Blas G, Saling PM, Mayorga LS. Requirement of protein tyrosine kinase and phosphatase activities for human sperm exocytosis. Dev Biol 2004; 265:399-415. (Pubitemid 38077266)
    • (2004) Developmental Biology , vol.265 , Issue.2 , pp. 399-415
    • Tomes, C.N.1    Roggero, C.M.2    De Blas, G.3    Saling, P.M.4    Mayorga, L.S.5
  • 50
    • 0032817012 scopus 로고    scopus 로고
    • Relationship between sperm motility and the processing and tyrosine phosphorylation of two human sperm fibrous sheath proteins, pro-hAKAP82 and hAKAP82
    • DOI 10.1093/molehr/5.9.816
    • Turner RM, Eriksson RL, Gerton GL, Moss SB. Relationship between sperm motility and the processing and tyrosine phosphorylation of two human sperm fibrous sheath proteins, pro-hAKAP82 and hAKAP82. Mol Hum Reprod 1999; 5:816-824. (Pubitemid 29406744)
    • (1999) Molecular Human Reproduction , vol.5 , Issue.9 , pp. 816-824
    • Turner, R.M.O.1    Eriksson, R.L.M.2    Gerton, G.L.3    Moss, S.B.4
  • 53
    • 3142769033 scopus 로고    scopus 로고
    • The murine testicular transcriptome: Characterizing gene expression in the testis during the progression of spermatogenesis
    • DOI 10.1095/biolreprod.103.026880
    • Shima JE, McLean DJ, McCarrey JR, Griswold MD. The murine testicular transcriptome: characterizing gene expression in the testis during the progression of spermatogenesis. Biol Reprod 2004; 71:319-330. (Pubitemid 38915339)
    • (2004) Biology of Reproduction , vol.71 , Issue.1 , pp. 319-330
    • Shima, J.E.1    McLean, D.J.2    McCarrey, J.R.3    Griswold, M.D.4
  • 54
    • 0033572856 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel deal-specificity protein phosphatase possibly involved in spermatogenesis
    • DOI 10.1042/0264-6021:3440819
    • Nakamura K, Shima H, Watanabe M, Haneji T, Kikuchi K. Molecular cloning and characterization of a novel dual-specificity protein phosphatase possibly involved in spermatogenesis. Biochem J 1999; 344(pt 3):819-825. (Pubitemid 30032530)
    • (1999) Biochemical Journal , vol.344 , Issue.3 , pp. 819-825
    • Nakamura, K.1    Shima, H.2    Watanabe, M.3    Haneji, T.4    Kikuchi, K.5
  • 56
    • 13844270779 scopus 로고    scopus 로고
    • Disruption of two putative nuclear localization sequences is required for cytosolic localization of mitogen-activated protein kinase phosphatase-2
    • DOI 10.1016/j.cellsig.2004.10.010
    • Sloss CM, Cadalbert L, Finn SG, Fuller SJ, Plevin R. Disruption of two putative nuclear localization sequences is required for cytosolic localization of mitogen-activated protein kinase phosphatase-2. Cell Signal 2005; 17:709-716. (Pubitemid 40250171)
    • (2005) Cellular Signalling , vol.17 , Issue.6 , pp. 709-716
    • Sloss, C.M.1    Cadalbert, L.2    Finn, S.G.3    Fuller, S.J.4    Plevin, R.5
  • 57
    • 0028966773 scopus 로고
    • Stimulation of protein tyrosine phosphorylation by platelet-activating factor and progesterone in human spermatozoa
    • Luconi M, Bonaccorsi L, Krausz C, Gervasi G, Forti G, Baldi E. Stimulation of protein tyrosine phosphorylation by platelet-activating factor and progesterone in human spermatozoa. Mol Cell Endocrinol 1995; 108:35-42.
    • (1995) Mol Cell Endocrinol , vol.108 , pp. 35-42
    • Luconi, M.1    Bonaccorsi, L.2    Krausz, C.3    Gervasi, G.4    Forti, G.5    Baldi, E.6
  • 58
    • 0031558794 scopus 로고    scopus 로고
    • The addition of mitogen-activated protein kinase and p34(cdc2) kinase substrate peptides inhibits the flagellar motility of demembranated fowl spermatozoa
    • DOI 10.1006/bbrc.1997.7626
    • Ashizawa K, Hashimoto K, Higashio M, Tsuzuki Y. The addition of mitogen-activated protein kinase and p34cdc2 kinase substrate peptides inhibits the flagellar motility of demembranated fowl spermatozoa. Biochem Biophys Res Commun 1997; 240:116-121. (Pubitemid 27503759)
    • (1997) Biochemical and Biophysical Research Communications , vol.240 , Issue.1 , pp. 116-121
    • Ashizawa, K.1    Hashimoto, K.2    Higashio, M.3    Tsuzuki, Y.4
  • 59
    • 14044250914 scopus 로고    scopus 로고
    • Tryptase inhibits motility of human spermatozoa mainly by activation of the mitogen-activated protein kinase pathway
    • DOI 10.1093/humrep/deh618
    • Weidinger S, Mayerhofer A, Kunz L, Albrecht M, Sbornik M, Wunn E, Hollweck R, Ring J, Kohn FM. Tryptase inhibits motility of human spermatozoa mainly by activation of the mitogen-activated protein kinase pathway. Hum Reprod 2005; 20:456-461. (Pubitemid 40277617)
    • (2005) Human Reproduction , vol.20 , Issue.2 , pp. 456-461
    • Weidinger, S.1    Mayerhofer, A.2    Kunz, L.3    Albrecht, M.4    Sbornik, M.5    Wunn, E.6    Hollweck, R.7    Ring, J.8    Kohn, F.M.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.