메뉴 건너뛰기




Volumn 59, Issue 5, 2013, Pages 421-430

Roles of intracellular cyclic AMP signal transduction in the capacitation and subsequent hyperactivation of mouse and boar spermatozoa

Author keywords

Acrosome reaction; cAMP; Capacitation; Hyperactivation; Protein phosphorylation

Indexed keywords

CYCLIC AMP;

EID: 84886689429     PISSN: 09168818     EISSN: 13484400     Source Type: Journal    
DOI: 10.1262/jrd.2013-056     Document Type: Article
Times cited : (50)

References (148)
  • 1
    • 0000000645 scopus 로고
    • Maturation, transport and fate of spermatozoa in the epididymis
    • Astwood EB, Greep RO (eds.), Washington DC: American Physiological Society
    • Bedford JM. Maturation, transport and fate of spermatozoa in the epididymis. In: Astwood EB, Greep RO (eds.), Handbook of Physiology, Section 7: Washington DC: American Physiological Society; 1975: 303-318.
    • (1975) Handbook of Physiology, Section , vol.7 , pp. 303-318
    • Bedford, J.M.1
  • 2
    • 0001503728 scopus 로고
    • Endocrine control of the development and maintenance of sperm fertilizing ability in the epididymis
    • Astwood EB, Greep RO (eds.), Washington DC: American Physiological Society
    • Orgebin-Crist MC, Danzo BJ, Davies J. Endocrine control of the development and maintenance of sperm fertilizing ability in the epididymis. In: Astwood EB, Greep RO (eds.), Handbook of Physiology, Section 7. Washington DC: American Physiological Society; 1975: 319-338.
    • (1975) Handbook of Physiology, Section , vol.7 , pp. 319-338
    • Orgebin-Crist, M.C.1    Danzo, B.J.2    Davies, J.3
  • 3
    • 0023066385 scopus 로고
    • Changes in sperm surfaces associated with epididymal transit
    • [Medline]
    • Hammerstedt RH, Parks JE. Changes in sperm surfaces associated with epididymal transit. J Reprod Fertil Suppl 1987; 34: 133-149. [Medline]
    • (1987) J Reprod Fertil Suppl , vol.34 , pp. 133-149
    • Hammerstedt, R.H.1    Parks, J.E.2
  • 4
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • Knobil E, Neill JD (eds.), 2nd edition. New York: Raven Press
    • Yanagimachi R. Mammalian fertilization. In: Knobil E, Neill JD (eds.), The Physiology of Reproduction. 2nd edition. New York: Raven Press; 1994: 189-317.
    • (1994) The Physiology of Reproduction , pp. 189-317
    • Yanagimachi, R.1
  • 5
    • 0035027048 scopus 로고    scopus 로고
    • Impact of epididymal maturation on the tyrosine phosphorylation patterns exhibited by rat spermatozoa
    • [Medline]
    • Lewis B, Aitken RJ. Impact of epididymal maturation on the tyrosine phosphorylation patterns exhibited by rat spermatozoa. Biol Reprod 2001; 64: 1545-1556. [Medline]
    • (2001) Biol Reprod , vol.64 , pp. 1545-1556
    • Lewis, B.1    Aitken, R.J.2
  • 6
    • 0017250131 scopus 로고
    • Epididymal function in the boar in relation to the fertilizing ability of spermatozoa
    • [Medline]
    • Hunter RH, Holtz W, Henfrey PJ. Epididymal function in the boar in relation to the fertilizing ability of spermatozoa. J Reprod Fertil 1976; 46: 463-466. [Medline]
    • (1976) J Reprod Fertil , vol.46 , pp. 463-466
    • Hunter, R.H.1    Holtz, W.2    Henfrey, P.J.3
  • 7
    • 0020685108 scopus 로고
    • Head-to-head agglutination of ram and boar epididymal spermatozoa and evidence for an epididymal antagglutinin
    • [Medline]
    • Dacheux JL, Paquignon M, Combarnous Y. Head-to-head agglutination of ram and boar epididymal spermatozoa and evidence for an epididymal antagglutinin. J Reprod Fertil 1983; 67: 181-189. [Medline]
    • (1983) J Reprod Fertil , vol.67 , pp. 181-189
    • Dacheux, J.L.1    Paquignon, M.2    Combarnous, Y.3
  • 8
    • 85011137694 scopus 로고
    • Motility and penetrability into zona-free hamster eggs of boar spermatozoa collected from various regions of the epididymis
    • Harayama H, Kusunoki H, Kato S. Motility and penetrability into zona-free hamster eggs of boar spermatozoa collected from various regions of the epididymis. J Reprod Dev 1993; 39: 41-45.
    • (1993) J Reprod Dev , vol.39 , pp. 41-45
    • Harayama, H.1    Kusunoki, H.2    Kato, S.3
  • 9
    • 0027245392 scopus 로고
    • Capacity of rete testicular and cauda epididymal boar spermatozoa to undergo the acrosome reaction and subsequent fusion with egg plasma membrane
    • [Medline]
    • Harayama H, Kusunoki H, Kato S. Capacity of rete testicular and cauda epididymal boar spermatozoa to undergo the acrosome reaction and subsequent fusion with egg plasma membrane. Mol Reprod Dev 1993; 35: 62-68. [Medline]
    • (1993) Mol Reprod Dev , vol.35 , pp. 62-68
    • Harayama, H.1    Kusunoki, H.2    Kato, S.3
  • 10
    • 0018237365 scopus 로고
    • Stabilizing role of epididymal plasma in relation to the capacitation time of boar spermatozoa
    • Hunter RHF, Holtz W, Herrmann H. Stabilizing role of epididymal plasma in relation to the capacitation time of boar spermatozoa. Anim Reprod Sci 1978; 1: 161-166.
    • (1978) Anim Reprod Sci , vol.1 , pp. 161-166
    • Hunter, R.H.F.1    Holtz, W.2    Herrmann, H.3
  • 11
    • 0000139395 scopus 로고
    • Detection of the 25-kDa antiagglutinin in epididymal plasma and spermatozoa collected from various regions of boar epididymis
    • Harayama H, Miyano T, Masuda H, Miyake M, Kato S. Detection of the 25-kDa antiagglutinin in epididymal plasma and spermatozoa collected from various regions of boar epididymis. J Reprod Dev 1995; 41: 113-121.
    • (1995) J Reprod Dev , vol.41 , pp. 113-121
    • Harayama, H.1    Miyano, T.2    Masuda, H.3    Miyake, M.4    Kato, S.5
  • 12
    • 0029783090 scopus 로고    scopus 로고
    • Electrophoretic characterization of boar epididymal antiagglutinin
    • [Medline]
    • Harayama H, Kato S, Hammerstedt RH. Electrophoretic characterization of boar epididymal antiagglutinin. Biol Reprod 1996; 55: 325-332. [Medline]
    • (1996) Biol Reprod , vol.55 , pp. 325-332
    • Harayama, H.1    Kato, S.2    Hammerstedt, R.H.3
  • 13
    • 0033992268 scopus 로고    scopus 로고
    • Biochemical characterization of sialoprotein "anti-agglutinin" purified from boar epididymal and seminal plasma
    • [Medline]
    • Harayama H, Liao PC, Gage DA, Miyake M, Kato S, Hammerstedt RH. Biochemical characterization of sialoprotein "anti-agglutinin" purified from boar epididymal and seminal plasma. Mol Reprod Dev 2000; 55: 96-103. [Medline]
    • (2000) Mol Reprod Dev , vol.55 , pp. 96-103
    • Harayama, H.1    Liao, P.C.2    Gage, D.A.3    Miyake, M.4    Kato, S.5    Hammerstedt, R.H.6
  • 14
    • 0022257352 scopus 로고
    • Sodium bicarbonate in seminal plasma stimulates the motility of mammalian spermatozoa through direct activation of adenylate cyclase
    • [Medline]
    • Okamura N, Tajima Y, Soejima A, Masuda H, Sugita Y. Sodium bicarbonate in seminal plasma stimulates the motility of mammalian spermatozoa through direct activation of adenylate cyclase. J Biol Chem 1985; 260: 9699-9705. [Medline]
    • (1985) J Biol Chem , vol.260 , pp. 9699-9705
    • Okamura, N.1    Tajima, Y.2    Soejima, A.3    Masuda, H.4    Sugita, Y.5
  • 15
    • 0026264261 scopus 로고
    • Histochemical localization of carbonic anhydrase in the testis and epididymis of the boar
    • [Medline]
    • Ekstedt E, Ridderstråle Y, Plöen L, Rodriguez-Martinez H. Histochemical localization of carbonic anhydrase in the testis and epididymis of the boar. Acta Anat (Basel) 1991; 141: 257-261. [Medline]
    • (1991) Acta Anat (Basel) , vol.141 , pp. 257-261
    • Ekstedt, E.1    Ridderstråle, Y.2    Plöen, L.3    Rodriguez-Martinez, H.4
  • 16
    • 0025973451 scopus 로고
    • A high activity carbonic anhydrase isoenzyme (CA II) is present in mammalian spermatozoa
    • [Medline]
    • Parkkila S, Kaunisto K, Kellokumpu S, Rajaniemi H. A high activity carbonic anhydrase isoenzyme (CA II) is present in mammalian spermatozoa. Histochemistry 1991; 95: 477-482. [Medline]
    • (1991) Histochemistry , vol.95 , pp. 477-482
    • Parkkila, S.1    Kaunisto, K.2    Kellokumpu, S.3    Rajaniemi, H.4
  • 18
    • 0027198165 scopus 로고
    • Polarized expression of a band 3-related protein in mammalian sperm cells
    • [Medline]
    • Parkkila S, Rajaniemi H, Kellokumpu S. Polarized expression of a band 3-related protein in mammalian sperm cells. Biol Reprod 1993; 49: 326-331. [Medline]
    • (1993) Biol Reprod , vol.49 , pp. 326-331
    • Parkkila, S.1    Rajaniemi, H.2    Kellokumpu, S.3
  • 20
  • 22
    • 77952643989 scopus 로고    scopus 로고
    • Evidence of the existence of adenylyl cyclase 10 (ADCY10) ortholog proteins in the heads and connecting pieces of boar spermatozoa
    • [Medline]
    • Tate S, Nakamura K, Suzuki C, Noda T, Lee J, Harayama H. Evidence of the existence of adenylyl cyclase 10 (ADCY10) ortholog proteins in the heads and connecting pieces of boar spermatozoa. J Reprod Dev 2010; 56: 271-278. [Medline]
    • (2010) J Reprod Dev , vol.56 , pp. 271-278
    • Tate, S.1    Nakamura, K.2    Suzuki, C.3    Noda, T.4    Lee, J.5    Harayama, H.6
  • 23
    • 84874484295 scopus 로고    scopus 로고
    • Novel approach for the detection of the vestiges of testicular mRNA splicing errors in mature spermatozoa of Japanese Black bulls
    • [Medline]
    • Noda T, Sakase M, Fukushima M, Harayama H. Novel approach for the detection of the vestiges of testicular mRNA splicing errors in mature spermatozoa of Japanese Black bulls. PLoS One 2013; 8: e57296. [Medline]
    • (2013) PLoS One , vol.e57296 , pp. 8
    • Noda, T.1    Sakase, M.2    Fukushima, M.3    Harayama, H.4
  • 24
    • 0019992417 scopus 로고
    • Regulation of protein phosphorylation and motility of sperm by cyclic adenosine monophosphate and calcium
    • [Medline]
    • Tash JS, Means AR. Regulation of protein phosphorylation and motility of sperm by cyclic adenosine monophosphate and calcium. Biol Reprod 1982; 26: 745-763. [Medline]
    • (1982) Biol Reprod , vol.26 , pp. 745-763
    • Tash, J.S.1    Means, A.R.2
  • 25
    • 0020623097 scopus 로고
    • Cyclic adenosine 3́,5́ monophosphate, calcium and protein phosphorylation in flagellar motility
    • [Medline]
    • Tash JS, Means AR. Cyclic adenosine 3́,5́ monophosphate, calcium and protein phosphorylation in flagellar motility. Biol Reprod 1983; 28: 75-104. [Medline]
    • (1983) Biol Reprod , vol.28 , pp. 75-104
    • Tash, J.S.1    Means, A.R.2
  • 26
    • 0028605927 scopus 로고
    • Regulation of sperm motility: Emerging evidence for a major role for protein phosphatases
    • [Medline]
    • Tash JS, Bracho GE. Regulation of sperm motility: emerging evidence for a major role for protein phosphatases. J Androl 1994; 15: 505-509. [Medline]
    • (1994) J Androl , vol.15 , pp. 505-509
    • Tash, J.S.1    Bracho, G.E.2
  • 27
    • 0021184785 scopus 로고
    • Flagellar motility requires the cAMP-dependent phosphorylation of a heat-stable NP-40-soluble 56 kd protein, axokinin
    • [Medline]
    • Tash JS, Kakar SS, Means AR. Flagellar motility requires the cAMP-dependent phosphorylation of a heat-stable NP-40-soluble 56 kd protein, axokinin. Cell 1984; 38: 551-559. [Medline]
    • (1984) Cell , vol.38 , pp. 551-559
    • Tash, J.S.1    Kakar, S.S.2    Means, A.R.3
  • 28
    • 84884102082 scopus 로고    scopus 로고
    • Fertilization in Mammals
    • Neill JD, Plant TM, Pfaff DW, Challis JRG, de Kretser DM, Richards JS, Wassarman PM (eds.), 3rd edition. Waltham: Academic Press
    • Florman HM, Ducibella T. Fertilization in Mammals. In: Neill JD, Plant TM, Pfaff DW, Challis JRG, de Kretser DM, Richards JS, Wassarman PM (eds.), Knobil and Neill's Physiology of Reproduction. 3rd edition. Waltham: Academic Press; 2006: 55-112.
    • (2006) Knobil and Neill's Physiology of Reproduction , pp. 55-112
    • Florman, H.M.1    Ducibella, T.2
  • 30
    • 0034759226 scopus 로고    scopus 로고
    • Bicarbonate stimulated phospholipid scrambling induces cholesterol redistribution and enables cholesterol depletion in the sperm plasma membrane
    • [Medline]
    • Flesch FM, Brouwers JF, Nievelstein PF, Verkleij AJ, van Golde LM, Colenbrander B, Gadella BM. Bicarbonate stimulated phospholipid scrambling induces cholesterol redistribution and enables cholesterol depletion in the sperm plasma membrane. J Cell Sci 2001; 114: 3543-3555. [Medline]
    • (2001) J Cell Sci , vol.114 , pp. 3543-3555
    • Flesch, F.M.1    Brouwers, J.F.2    Nievelstein, P.F.3    Verkleij, A.J.4    van Golde, L.M.5    Colenbrander, B.6    Gadella, B.M.7
  • 31
    • 0036082781 scopus 로고    scopus 로고
    • Capacitation induces cyclic adenosine 3́,5́-monophosphatedependent, but apoptosis-unrelated, exposure of aminophospholipids at the apical head plasma membrane of boar sperm cells
    • [Medline]
    • Gadella BM, Harrison RA. Capacitation induces cyclic adenosine 3́,5́-monophosphatedependent, but apoptosis-unrelated, exposure of aminophospholipids at the apical head plasma membrane of boar sperm cells. Biol Reprod 2002; 67: 340-350. [Medline]
    • (2002) Biol Reprod , vol.67 , pp. 340-350
    • Gadella, B.M.1    Harrison, R.A.2
  • 32
    • 25444440315 scopus 로고    scopus 로고
    • Effects of methyl-β-cyclodextrinmediated cholesterol depletion in porcine sperm compared to somatic cells
    • [Medline]
    • van Gestel RA, Helms JB, Brouwers JF, Gadella BM. Effects of methyl-β-cyclodextrinmediated cholesterol depletion in porcine sperm compared to somatic cells. Mol Reprod Dev 2005; 72: 386-395. [Medline]
    • (2005) Mol Reprod Dev , vol.72 , pp. 386-395
    • van Gestel, R.A.1    Helms, J.B.2    Brouwers, J.F.3    Gadella, B.M.4
  • 33
    • 54249144760 scopus 로고    scopus 로고
    • Sperm head membrane reorganisation during capacitation
    • [Medline]
    • Gadella BM, Tsai PS, Boerke A, Brewis IA. Sperm head membrane reorganisation during capacitation. Int J Dev Biol 2008; 52: 473-480. [Medline]
    • (2008) Int J Dev Biol , vol.52 , pp. 473-480
    • Gadella, B.M.1    Tsai, P.S.2    Boerke, A.3    Brewis, I.A.4
  • 34
    • 77955288978 scopus 로고    scopus 로고
    • How pig sperm prepares to fertilize: Stable acrosome docking to the plasma membrane
    • [Medline]
    • Tsai PS, Garcia-Gil N, van Haeften T, Gadella BM. How pig sperm prepares to fertilize: stable acrosome docking to the plasma membrane. PLoS One 2010; 5: e11204. [Medline]
    • (2010) PLoS One , vol.5
    • Tsai, P.S.1    Garcia-Gil, N.2    van Haeften, T.3    Gadella, B.M.4
  • 35
    • 84857871578 scopus 로고    scopus 로고
    • Involvement of complexin 2 in docking, locking and unlocking of different SNARE complexes during sperm capacitation and induced acrosomal exocytosis
    • [Medline]
    • Tsai PS, Brewis IA, van Maaren J, Gadella BM. Involvement of complexin 2 in docking, locking and unlocking of different SNARE complexes during sperm capacitation and induced acrosomal exocytosis. PLoS One 2012; 7: e32603. [Medline]
    • (2012) PLoS One , vol.7
    • Tsai, P.S.1    Brewis, I.A.2    van Maaren, J.3    Gadella, B.M.4
  • 36
    • 0028911816 scopus 로고
    • Flow cytometric detection of bicarbonate-induced changes in lectin binding in boar and ram sperm populations
    • [Medline]
    • Ashworth PJ, Harrison RA, Miller NG, Plummer JM, Watson PF. Flow cytometric detection of bicarbonate-induced changes in lectin binding in boar and ram sperm populations. Mol Reprod Dev 1995; 40: 164-176. [Medline]
    • (1995) Mol Reprod Dev , vol.40 , pp. 164-176
    • Ashworth, P.J.1    Harrison, R.A.2    Miller, N.G.3    Plummer, J.M.4    Watson, P.F.5
  • 37
    • 0942297993 scopus 로고    scopus 로고
    • Rapid PKA-catalysed phosphorylation of boar sperm proteins induced by the capacitating agent bicarbonate
    • [Medline]
    • Harrison RA. Rapid PKA-catalysed phosphorylation of boar sperm proteins induced by the capacitating agent bicarbonate. Mol Reprod Dev 2004; 67: 337-352. [Medline]
    • (2004) Mol Reprod Dev , vol.67 , pp. 337-352
    • Harrison, R.A.1
  • 38
    • 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
    • [Medline]
    • 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. [Medline]
    • (2008) J Reprod Dev , vol.54 , pp. 171-176
    • Adachi, J.1    Tate, S.2    Miyake, M.3    Harayama, H.4
  • 39
    • 0027339443 scopus 로고
    • Forskolin stimulates porcine sperm capacitation by increasing calcium uptake
    • [Medline]
    • Okamura N, Tanba M, Fukuda A, Sugita Y, Nagai T. Forskolin stimulates porcine sperm capacitation by increasing calcium uptake. FEBS Lett 1993; 316: 283-286. [Medline]
    • (1993) FEBS Lett , vol.316 , pp. 283-286
    • Okamura, N.1    Tanba, M.2    Fukuda, A.3    Sugita, Y.4    Nagai, T.5
  • 40
    • 0242657079 scopus 로고    scopus 로고
    • Involvement of cytoplasmic free calcium in boar sperm: Head-to-head agglutination induced by a cell-permeable cyclic adenosine monophosphate analog
    • [Medline]
    • Harayama H, Okada K, Miyake M. Involvement of cytoplasmic free calcium in boar sperm: head-to-head agglutination induced by a cell-permeable cyclic adenosine monophosphate analog. J Androl 2003; 24: 91-99. [Medline]
    • (2003) J Androl , vol.24 , pp. 91-99
    • Harayama, H.1    Okada, K.2    Miyake, M.3
  • 41
    • 4444280587 scopus 로고    scopus 로고
    • A unique mechanism for cyclic adenosine 3́,5́-monophosphate-induced increase of 32-kDa tyrosine-phosphorylated protein in boar spermatozoa
    • [Medline]
    • Harayama H, Sasaki K, Miyake M. A unique mechanism for cyclic adenosine 3́,5́-monophosphate-induced increase of 32-kDa tyrosine-phosphorylated protein in boar spermatozoa. Mol Reprod Dev 2004; 69: 194-204. [Medline]
    • (2004) Mol Reprod Dev , vol.69 , pp. 194-204
    • Harayama, H.1    Sasaki, K.2    Miyake, M.3
  • 42
    • 0030569051 scopus 로고    scopus 로고
    • Bicarbonate/CO2 induces rapid activation of phospholipase A2 and renders boar spermatozoa capable of undergoing acrosomal exocytosis in response to progesterone
    • [Medline]
    • Roldan ER, Vazquez JM. Bicarbonate/CO2 induces rapid activation of phospholipase A2 and renders boar spermatozoa capable of undergoing acrosomal exocytosis in response to progesterone. FEBS Lett 1996; 396: 227-232. [Medline]
    • (1996) FEBS Lett , vol.396 , pp. 227-232
    • Roldan, E.R.1    Vazquez, J.M.2
  • 45
    • 0032469166 scopus 로고    scopus 로고
    • Effects of calcium and bicarbonate on head-to-head agglutination in ejaculated boar spermatozoa
    • [Medline]
    • Harayama H, Miyake M, Shidara O, Iwamoto E, Kato S. Effects of calcium and bicarbonate on head-to-head agglutination in ejaculated boar spermatozoa. Reprod Fertil Dev 1998; 10: 445-450. [Medline]
    • (1998) Reprod Fertil Dev , vol.10 , pp. 445-450
    • Harayama, H.1    Miyake, M.2    Shidara, O.3    Iwamoto, E.4    Kato, S.5
  • 47
    • 0034438444 scopus 로고    scopus 로고
    • Role of cyclic adenosine 3́,5́-monophosphate and serum albumin in head-to-head agglutination of boar spermatozoa
    • [Medline]
    • Harayama H, Miyake M, Kato S. Role of cyclic adenosine 3́,5́-monophosphate and serum albumin in head-to-head agglutination of boar spermatozoa. Reprod Fertil Dev 2000; 12: 307-318. [Medline]
    • (2000) Reprod Fertil Dev , vol.12 , pp. 307-318
    • Harayama, H.1    Miyake, M.2    Kato, S.3
  • 48
    • 0035987217 scopus 로고    scopus 로고
    • Relationship between bicarbonate and cyclic nucleotide in the promoting effects on head-to-head agglutination in boar spermatozoa
    • [Medline]
    • Harayama H, Kato S. Relationship between bicarbonate and cyclic nucleotide in the promoting effects on head-to-head agglutination in boar spermatozoa. Asian J Androl 2002; 4: 87-96. [Medline]
    • (2002) Asian J Androl , vol.4 , pp. 87-96
    • Harayama, H.1    Kato, S.2
  • 49
    • 0242625885 scopus 로고    scopus 로고
    • Viability and protein phosphorylation patterns of boar spermatozoa agglutinated by treatment with a cell-permeable cyclic adenosine 3́,5́-monophosphate analog
    • [Medline]
    • Harayama H. Viability and protein phosphorylation patterns of boar spermatozoa agglutinated by treatment with a cell-permeable cyclic adenosine 3́,5́-monophosphate analog. J Androl 2003; 24: 831-842. [Medline]
    • (2003) J Androl , vol.24 , pp. 831-842
    • Harayama, H.1
  • 50
    • 0031328329 scopus 로고    scopus 로고
    • Sperm plasma membrane characteristics and boar semen fertility
    • [Medline]
    • Harrison RA. Sperm plasma membrane characteristics and boar semen fertility. J Reprod Fertil (Suppl) 1997; 52: 195-211. [Medline]
    • (1997) J Reprod Fertil (Suppl) , vol.52 , pp. 195-211
    • Harrison, R.A.1
  • 51
    • 0000413412 scopus 로고
    • Formation of a cyclic adenine ribonucleotide by tissue particles
    • [Medline]
    • Rall TW, Sutherland EW. Formation of a cyclic adenine ribonucleotide by tissue particles. J Biol Chem 1958; 232: 1065-1076. [Medline]
    • (1958) J Biol Chem , vol.232 , pp. 1065-1076
    • Rall, T.W.1    Sutherland, E.W.2
  • 52
    • 0001559662 scopus 로고
    • Fractionation and characterization of a cyclic adenine ribonucleotide formed by tissue particles
    • Medline
    • Sutherland EW, Rall TW. Fractionation and characterization of a cyclic adenine ribonucleotide formed by tissue particles. J Biol Chem 1958; 232: 1077-1091. [Medline]
    • (1958) J Biol Chem , vol.232 , pp. 1077-1091
    • Sutherland, E.W.1    Rall, T.W.2
  • 53
    • 33645889302 scopus 로고    scopus 로고
    • Sutherland's discovery of cyclic adenine monophosphate and the second messenger system
    • Kresge N, Simoni RD, Hill RL, Earl W. Sutherland's discovery of cyclic adenine monophosphate and the second messenger system. J Biol Chem 2005; 280: e39.
    • (2005) J Biol Chem , vol.e39 , pp. 280
    • Kresge, N.1    Simoni, R.D.2    Hill, R.L.3    Earl, W.4
  • 54
    • 0141703301 scopus 로고    scopus 로고
    • Calcium regulation of the soluble adenylyl cyclase expressed in mammalian spermatozoa
    • Medline
    • Jaiswal BS, Conti M. Calcium regulation of the soluble adenylyl cyclase expressed in mammalian spermatozoa. Proc Natl Acad Sci USA 2003; 100: 10676-10681. [Medline]
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 10676-10681
    • Jaiswal, B.S.1    Conti, M.2
  • 59
    • 36549022192 scopus 로고    scopus 로고
    • External Ca2+ acts upstream of adenylyl cyclase SACY in the bicarbonate signaled activation of sperm motility
    • Medline
    • Carlson AE, Hille B, Babcock DF. External Ca2+ acts upstream of adenylyl cyclase SACY in the bicarbonate signaled activation of sperm motility. Dev Biol 2007; 312: 183-192. [Medline]
    • (2007) Dev Biol , vol.312 , pp. 183-192
    • Carlson, A.E.1    Hille, B.2    Babcock, D.F.3
  • 60
    • 38549116059 scopus 로고    scopus 로고
    • Soluble adenylyl cyclase is required for activation of sperm but does not have a direct effect on hyperactivation
    • Medline
    • Marquez B, Suarez SS. Soluble adenylyl cyclase is required for activation of sperm but does not have a direct effect on hyperactivation. Reprod Fertil Dev 2008; 20: 247-252. [Medline]
    • (2008) Reprod Fertil Dev , vol.20 , pp. 247-252
    • Marquez, B.1    Suarez, S.S.2
  • 61
    • 0042856454 scopus 로고    scopus 로고
    • Evidence for multiple distinctly localized adenylyl cyclase isoforms in mammalian spermatozoa
    • Medline
    • Baxendale RW, Fraser LR. Evidence for multiple distinctly localized adenylyl cyclase isoforms in mammalian spermatozoa. Mol Reprod Dev 2003; 66: 181-189. [Medline]
    • (2003) Mol Reprod Dev , vol.66 , pp. 181-189
    • Baxendale, R.W.1    Fraser, L.R.2
  • 62
    • 17644378592 scopus 로고    scopus 로고
    • Inactivation of the mouse adenylyl cyclase 3 gene disrupts male fertility and spermatozoon function
    • Medline
    • Livera G, Xie F, Garcia MA, Jaiswal B, Chen J, Law E, Storm DR, Conti M. Inactivation of the mouse adenylyl cyclase 3 gene disrupts male fertility and spermatozoon function. Mol Endocrinol 2005; 19: 1277-1290. [Medline]
    • (2005) Mol Endocrinol , vol.19 , pp. 1277-1290
    • Livera, G.1    Xie, F.2    Garcia, M.A.3    Jaiswal, B.4    Chen, J.5    Law, E.6    Storm, D.R.7    Conti, M.8
  • 64
    • 7744238317 scopus 로고    scopus 로고
    • A cyclic adenosine 3́,5́-monophosphate-induced tyrosine phosphorylation of Syk protein tyrosine kinase in the flagella of boar spermatozoa
    • Medline
    • Harayama H, Muroga M, Miyake M. A cyclic adenosine 3́,5́-monophosphate-induced tyrosine phosphorylation of Syk protein tyrosine kinase in the flagella of boar spermatozoa. Mol Reprod Dev 2004; 69: 436-447. [Medline]
    • (2004) Mol Reprod Dev , vol.69 , pp. 436-447
    • Harayama, H.1    Muroga, M.2    Miyake, M.3
  • 65
    • 26944494894 scopus 로고    scopus 로고
    • A cyclic adenosine 3́,5́-monophosphate stimulates phospholipase Cγ1-calcium signaling via the activation of tyrosine kinase in boar spermatozoa
    • Medline
    • Harayama H, Murase T, Miyake M. A cyclic adenosine 3́,5́-monophosphate stimulates phospholipase Cγ1-calcium signaling via the activation of tyrosine kinase in boar spermatozoa. J Androl 2005; 26: 732-740. [Medline]
    • (2005) J Androl , vol.26 , pp. 732-740
    • Harayama, H.1    Murase, T.2    Miyake, M.3
  • 66
    • 33746659808 scopus 로고    scopus 로고
    • A cyclic adenosine 3́,5́-monophosphate-dependent protein kinase C activation is involved in the hyperactivation of boar spermatozoa
    • Medline
    • Harayama H, Miyake M. A cyclic adenosine 3́,5́-monophosphate-dependent protein kinase C activation is involved in the hyperactivation of boar spermatozoa. Mol Reprod Dev 2006; 73: 1169-1178. [Medline]
    • (2006) Mol Reprod Dev , vol.73 , pp. 1169-1178
    • Harayama, H.1    Miyake, M.2
  • 67
    • 78649618272 scopus 로고    scopus 로고
    • Relationship of protein tyrosine phosphorylation state with tolerance to frozen storage and the potential to undergo cyclic AMP-dependent hyperactivation in the spermatozoa of Japanese Black bulls
    • Medline
    • Harayama H, Nishijima K, Murase T, Sakase M, Fukushima M. Relationship of protein tyrosine phosphorylation state with tolerance to frozen storage and the potential to undergo cyclic AMP-dependent hyperactivation in the spermatozoa of Japanese Black bulls. Mol Reprod Dev 2010; 77: 910-921. [Medline]
    • (2010) Mol Reprod Dev , vol.77 , pp. 910-921
    • Harayama, H.1    Nishijima, K.2    Murase, T.3    Sakase, M.4    Fukushima, M.5
  • 68
    • 0041836339 scopus 로고    scopus 로고
    • Epac: A new cAMP target and new avenues in cAMP research
    • Medline
    • Bos JL. Epac: a new cAMP target and new avenues in cAMP research. Nat Rev Mol Cell Biol 2003; 4: 733-738. [Medline]
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 733-738
    • Bos, J.L.1
  • 69
    • 47749143964 scopus 로고    scopus 로고
    • Epac mediates cyclic AMP-dependent axon growth, guidance and regeneration
    • Medline
    • Murray AJ, Shewan DA. Epac mediates cyclic AMP-dependent axon growth, guidance and regeneration. Mol Cell Neurosci 2008; 38: 578-588. [Medline]
    • (2008) Mol Cell Neurosci , vol.38 , pp. 578-588
    • Murray, A.J.1    Shewan, D.A.2
  • 70
    • 0016182875 scopus 로고
    • Criteria for the classification of protein kinases
    • Medline
    • Traugh JA, Ashby CD, Walsh DA. Criteria for the classification of protein kinases. Methods Enzymol 1974; 38: 290-299. [Medline]
    • (1974) Methods Enzymol , vol.38 , pp. 290-299
    • Traugh, J.A.1    Ashby, C.D.2    Walsh, D.A.3
  • 71
    • 0028898390 scopus 로고
    • Phosphorylation modulates catalytic function and regulation in the cAMP-dependent protein kinase
    • Medline
    • Adams JA, McGlone ML, Gibson R, Taylor SS. Phosphorylation modulates catalytic function and regulation in the cAMP-dependent protein kinase. Biochemistry 1995; 34: 2447-2454. [Medline]
    • (1995) Biochemistry , vol.34 , pp. 2447-2454
    • Adams, J.A.1    McGlone, M.L.2    Gibson, R.3    Taylor, S.S.4
  • 72
    • 0037033032 scopus 로고    scopus 로고
    • Phosphorylation of the catalytic subunit of protein kinase A. Autophosphorylation versus phosphorylation by phosphoinositidedependent kinase-1
    • Medline
    • Moore MJ, Kanter JR, Jones KC, Taylor SS. Phosphorylation of the catalytic subunit of protein kinase A. Autophosphorylation versus phosphorylation by phosphoinositidedependent kinase-1. J Biol Chem 2002; 277: 47878-47884. [Medline]
    • (2002) J Biol Chem , vol.277 , pp. 47878-47884
    • Moore, M.J.1    Kanter, J.R.2    Jones, K.C.3    Taylor, S.S.4
  • 77
    • 24144444059 scopus 로고    scopus 로고
    • Epac1 regulates integrity of endothelial cell junctions through VE-cadherin
    • Medline
    • Kooistra MR, Corada M, Dejana E, Bos JL. Epac1 regulates integrity of endothelial cell junctions through VE-cadherin. FEBS Lett 2005; 579: 4966-4972. [Medline]
    • (2005) FEBS Lett , vol.579 , pp. 4966-4972
    • Kooistra, M.R.1    Corada, M.2    Dejana, E.3    Bos, J.L.4
  • 78
    • 0037424363 scopus 로고    scopus 로고
    • Epac-selective cAMP analog 8-pCPT-2́-O-Me-cAMP as a stimulus for Ca2+-induced Ca2+ release and exocytosis in pancreatic β-cells
    • Medline
    • Kang G, Joseph JW, Chepurny OG, Monaco M, Wheeler MB, Bos JL, Schwede F, Genieser HG, Holz GG. Epac-selective cAMP analog 8-pCPT-2́-O-Me-cAMP as a stimulus for Ca2+-induced Ca2+ release and exocytosis in pancreatic β-cells. J Biol Chem 2003; 278: 8279-8285. [Medline]
    • (2003) J Biol Chem , vol.278 , pp. 8279-8285
    • Kang, G.1    Joseph, J.W.2    Chepurny, O.G.3    Monaco, M.4    Wheeler, M.B.5    Bos, J.L.6    Schwede, F.7    Genieser, H.G.8    Holz, G.G.9
  • 79
    • 33748316506 scopus 로고    scopus 로고
    • Identification of SRC as a key PKA-stimulated tyrosine kinase involved in the capacitation-associated hyperactivation of murine spermatozoa
    • Medline
    • 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. [Medline]
    • (2006) J Cell Sci , vol.119 , pp. 3182-3192
    • Baker, M.A.1    Hetherington, L.2    Aitken, R.J.3
  • 80
    • 0031573950 scopus 로고    scopus 로고
    • Regulation, localization, and anchoring of protein kinase A subunits during mouse sperm capacitation
    • Medline
    • Visconti PE, Johnson LR, Oyaski M, Fornés M, Moss SB, Gerton GL, Kopf GS. Regulation, localization, and anchoring of protein kinase A subunits during mouse sperm capacitation. Dev Biol 1997; 192: 351-363. [Medline]
    • (1997) Dev Biol , vol.192 , pp. 351-363
    • Visconti, P.E.1    Johnson, L.R.2    Oyaski, M.3    Fornés, M.4    Moss, S.B.5    Gerton, G.L.6    Kopf, G.S.7
  • 81
    • 4544242678 scopus 로고    scopus 로고
    • Sperm-specific protein kinase A catalytic subunit Cα2 orchestrates cAMP signaling for male fertility
    • Medline
    • Nolan MA, Babcock DF, Wennemuth G, Brown W, Burton KA, McKnight GS. Sperm-specific protein kinase A catalytic subunit Cα2 orchestrates cAMP signaling for male fertility. Proc Natl Acad Sci USA 2004; 101: 13483-13488. [Medline]
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 13483-13488
    • Nolan, M.A.1    Babcock, D.F.2    Wennemuth, G.3    Brown, W.4    Burton, K.A.5    McKnight, G.S.6
  • 82
    • 0030716780 scopus 로고    scopus 로고
    • Subcellular localization of the regulatory subunits of cyclic adenosine 3́,5́-monophosphate-dependent protein kinase in bovine spermatozoa
    • Medline
    • Vijayaraghavan S, Olson GE, NagDas S, Winfrey VP, Carr DW. Subcellular localization of the regulatory subunits of cyclic adenosine 3́,5́-monophosphate-dependent protein kinase in bovine spermatozoa. Biol Reprod 1997; 57: 1517-1523. [Medline]
    • (1997) Biol Reprod , vol.57 , pp. 1517-1523
    • Vijayaraghavan, S.1    Olson, G.E.2    Nagdas, S.3    Winfrey, V.P.4    Carr, D.W.5
  • 83
    • 0028138371 scopus 로고
    • Differential localization of two isoforms of the regulatory subunit RIIα of cAMP-dependent protein kinase in human sperm: Biochemical and cytochemical study
    • Medline
    • Pariset C, Weinman S. Differential localization of two isoforms of the regulatory subunit RIIα of cAMP-dependent protein kinase in human sperm: biochemical and cytochemical study. Mol Reprod Dev 1994; 39: 415-422. [Medline]
    • (1994) Mol Reprod Dev , vol.39 , pp. 415-422
    • Pariset, C.1    Weinman, S.2
  • 84
    • 0033873638 scopus 로고    scopus 로고
    • A novel isoform of human cyclic 3́,5́-adenosine monophosphate-dependent protein kinase, c α-s, localizes to sperm midpiece
    • Medline
    • Reinton N, Orstavik S, Haugen TB, Jahnsen T, Taskén K, Skålhegg BS. A novel isoform of human cyclic 3́,5́-adenosine monophosphate-dependent protein kinase, c α-s, localizes to sperm midpiece. Biol Reprod 2000; 63: 607-611. [Medline]
    • (2000) Biol Reprod , vol.63 , pp. 607-611
    • Reinton, N.1    Orstavik, S.2    Haugen, T.B.3    Jahnsen, T.4    Taskén, K.5    Skålhegg, B.S.6
  • 85
    • 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
    • Medline
    • 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. [Medline]
    • (2008) Mol Reprod Dev , vol.75 , pp. 1396-1407
    • Harayama, H.1    Nakamura, K.2
  • 86
    • 33947143017 scopus 로고    scopus 로고
    • Evidence for existence of cAMP-Epac signaling in the heads of mouse epididymal spermatozoa
    • Medline
    • Amano R, Lee J, Goto N, Harayama H. Evidence for existence of cAMP-Epac signaling in the heads of mouse epididymal spermatozoa. J Reprod Dev 2007; 53: 127-133. [Medline]
    • (2007) J Reprod Dev , vol.53 , pp. 127-133
    • Amano, R.1    Lee, J.2    Goto, N.3    Harayama, H.4
  • 87
    • 65449172899 scopus 로고    scopus 로고
    • cAMP-Epac2-mediated activation of Rap1 in developing male germ cells: RA-RhoGAP as a possible direct down-stream effector
    • Medline
    • Aivatiadou E, Ripolone M, Brunetti F, Berruti G. cAMP-Epac2-mediated activation of Rap1 in developing male germ cells: RA-RhoGAP as a possible direct down-stream effector. Mol Reprod Dev 2009; 76: 407-416. [Medline]
    • (2009) Mol Reprod Dev , vol.76 , pp. 407-416
    • Aivatiadou, E.1    Ripolone, M.2    Brunetti, F.3    Berruti, G.4
  • 88
    • 33646837333 scopus 로고    scopus 로고
    • Calcium-induced acrosomal exocytosis requires cAMP acting through a protein kinase A-independent, Epac-mediated pathway
    • Medline
    • Branham MT, Mayorga LS, Tomes CN. Calcium-induced acrosomal exocytosis requires cAMP acting through a protein kinase A-independent, Epac-mediated pathway. J Biol Chem 2006; 281: 8656-8666. [Medline]
    • (2006) J Biol Chem , vol.281 , pp. 8656-8666
    • Branham, M.T.1    Mayorga, L.S.2    Tomes, C.N.3
  • 90
    • 32344439330 scopus 로고    scopus 로고
    • Roles of cAMP in regulating microtubule sliding and flagellar bending in demembranated hamster spermatozoa
    • Medline
    • Kinukawa M, Oda S, Shirakura Y, Okabe M, Ohmuro J, Baba SA, Nagata M, Aoki F. Roles of cAMP in regulating microtubule sliding and flagellar bending in demembranated hamster spermatozoa. FEBS Lett 2006; 580: 1515-1520. [Medline]
    • (2006) FEBS Lett , vol.580 , pp. 1515-1520
    • Kinukawa, M.1    Oda, S.2    Shirakura, Y.3    Okabe, M.4    Ohmuro, J.5    Baba, S.A.6    Nagata, M.7    Aoki, F.8
  • 92
    • 84863838423 scopus 로고    scopus 로고
    • Kinases, phosphatases and proteases during sperm capacitation
    • Medline
    • Signorelli J, Diaz ES, Morales P. Kinases, phosphatases and proteases during sperm capacitation. Cell Tissue Res 2012; 349: 765-782. [Medline]
    • (2012) Cell Tissue Res , vol.349 , pp. 765-782
    • Signorelli, J.1    Diaz, E.S.2    Morales, P.3
  • 93
    • 84884073858 scopus 로고    scopus 로고
    • The Spermatozoon
    • Neill JD, Plant TM, Pfaff DW, Challis JRG, de Kretser DM, Richards JS, Wassarman PM (eds.), 3rd edition. Waltham: Academic Press
    • Eddy EM. The Spermatozoon. In: Neill JD, Plant TM, Pfaff DW, Challis JRG, de Kretser DM, Richards JS, Wassarman PM (eds.), Knobil and Neill's Physiology of Reproduction. 3rd edition. Waltham: Academic Press; 2006: 3-54.
    • (2006) Knobil and Neill's Physiology of Reproduction , pp. 3-54
    • Eddy, E.M.1
  • 94
    • 84871793424 scopus 로고    scopus 로고
    • Mouse sperm membrane potential hyperpolarization is necessary and sufficient to prepare sperm for the acrosome reaction
    • , Medline
    • De La Vega-Beltran JL, Sánchez-Cárdenas C, Krapf D, Hernandez-González EO, Wertheimer E, Treviño CL, Visconti PE, Darszon A. Mouse sperm membrane potential hyperpolarization is necessary and sufficient to prepare sperm for the acrosome reaction. J Biol Chem 2012; 287: 44384-44393. [Medline]
    • (2012) J Biol Chem , vol.287 , pp. 44384-44393
    • De La Vega-Beltran, J.L.1
  • 95
    • 69749113641 scopus 로고    scopus 로고
    • Zona pellucida glycoprotein ZP3 and fertilization in mammals
    • Medline
    • Litscher ES, Williams Z, Wassarman PM. Zona pellucida glycoprotein ZP3 and fertilization in mammals. Mol Reprod Dev 2009; 76: 933-941. [Medline]
    • (2009) Mol Reprod Dev , vol.76 , pp. 933-941
    • Litscher, E.S.1    Williams, Z.2    Wassarman, P.M.3
  • 96
    • 77954600245 scopus 로고    scopus 로고
    • Gamete recognition in mice depends on the cleavage status of an egg's zona pellucida protein
    • Medline
    • Gahlay G, Gauthier L, Baibakov B, Epifano O, Dean J. Gamete recognition in mice depends on the cleavage status of an egg's zona pellucida protein. Science 2010; 329: 216-219. [Medline]
    • (2010) Science , vol.329 , pp. 216-219
    • Gahlay, G.1    Gauthier, L.2    Baibakov, B.3    Epifano, O.4    Dean, J.5
  • 97
    • 79953232734 scopus 로고    scopus 로고
    • Most fertilizing mouse spermatozoa begin their acrosome reaction before contact with the zona pellucida during in vitro fertilization
    • Medline
    • Jin M, Fujiwara E, Kakiuchi Y, Okabe M, Satouh Y, Baba SA, Chiba K, Hirohashi N. Most fertilizing mouse spermatozoa begin their acrosome reaction before contact with the zona pellucida during in vitro fertilization. Proc Natl Acad Sci USA 2011; 108: 4892-4896. [Medline]
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 4892-4896
    • Jin, M.1    Fujiwara, E.2    Kakiuchi, Y.3    Okabe, M.4    Satouh, Y.5    Baba, S.A.6    Chiba, K.7    Hirohashi, N.8
  • 98
    • 79952800026 scopus 로고    scopus 로고
    • Progesterone activates the principal Ca2+ channel of human sperm
    • Medline
    • Lishko PV, Botchkina IL, Kirichok Y. Progesterone activates the principal Ca2+ channel of human sperm. Nature 2011; 471: 387-391. [Medline]
    • (2011) Nature , vol.471 , pp. 387-391
    • Lishko, P.V.1    Botchkina, I.L.2    Kirichok, Y.3
  • 99
    • 0024825076 scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate hydrolysis in human sperm stimulated with follicular fluid or progesterone is dependent upon Ca2+ influx
    • Medline
    • Thomas P, Meizel S. Phosphatidylinositol 4,5-bisphosphate hydrolysis in human sperm stimulated with follicular fluid or progesterone is dependent upon Ca2+ influx. Biochem J 1989; 264: 539-546. [Medline]
    • (1989) Biochem J , vol.264 , pp. 539-546
    • Thomas, P.1    Meizel, S.2
  • 100
    • 0026318851 scopus 로고
    • Cell surface localization of a novel non-genomic progesterone receptor on the head of human sperm
    • Medline
    • Blackmore PF, Lattanzio FA. Cell surface localization of a novel non-genomic progesterone receptor on the head of human sperm. Biochem Biophys Res Commun 1991; 181: 331-336. [Medline]
    • (1991) Biochem Biophys Res Commun , vol.181 , pp. 331-336
    • Blackmore, P.F.1    Lattanzio, F.A.2
  • 101
    • 0028650360 scopus 로고
    • Exocytosis in spermatozoa in response to progesterone and zona pellucida
    • Medline
    • Roldan ER, Murase T, Shi QX. Exocytosis in spermatozoa in response to progesterone and zona pellucida. Science 1994; 266: 1578-1581. [Medline]
    • (1994) Science , vol.266 , pp. 1578-1581
    • Roldan, E.R.1    Murase, T.2    Shi, Q.X.3
  • 102
    • 0028033799 scopus 로고
    • Comparison of the ability of progesterone and heat solubilized porcine zona pellucida to initiate the porcine sperm acrosome reaction in vitro
    • Medline
    • Melendrez CS, Meizel S, Berger T. Comparison of the ability of progesterone and heat solubilized porcine zona pellucida to initiate the porcine sperm acrosome reaction in vitro. Mol Reprod Dev 1994; 39: 433-438. [Medline]
    • (1994) Mol Reprod Dev , vol.39 , pp. 433-438
    • Melendrez, C.S.1    Meizel, S.2    Berger, T.3
  • 103
    • 77956096971 scopus 로고    scopus 로고
    • Mice lacking two sperm serine proteases, ACR and PRSS21, are subfertile, but the mutant sperm are infertile in vitro
    • Medline
    • Kawano N, Kang W, Yamashita M, Koga Y, Yamazaki T, Hata T, Miyado K, Baba T. Mice lacking two sperm serine proteases, ACR and PRSS21, are subfertile, but the mutant sperm are infertile in vitro. Biol Reprod 2010; 83: 359-369. [Medline]
    • (2010) Biol Reprod , vol.83 , pp. 359-369
    • Kawano, N.1    Kang, W.2    Yamashita, M.3    Koga, Y.4    Yamazaki, T.5    Hata, T.6    Miyado, K.7    Baba, T.8
  • 104
    • 15044362481 scopus 로고    scopus 로고
    • The immunoglobulin superfamily protein Izumo is required for sperm to fuse with eggs
    • Medline
    • Inoue N, Ikawa M, Isotani A, Okabe M. The immunoglobulin superfamily protein Izumo is required for sperm to fuse with eggs. Nature 2005; 434: 234-238. [Medline]
    • (2005) Nature , vol.434 , pp. 234-238
    • Inoue, N.1    Ikawa, M.2    Isotani, A.3    Okabe, M.4
  • 105
    • 77951751489 scopus 로고    scopus 로고
    • Sperm equatorial segment protein 1, SPESP1, is required for fully fertile sperm in mouse
    • Medline
    • Fujihara Y, Murakami M, Inoue N, Satouh Y, Kaseda K, Ikawa M, Okabe M. Sperm equatorial segment protein 1, SPESP1, is required for fully fertile sperm in mouse. J Cell Sci 2010; 123: 1531-1536. [Medline]
    • (2010) J Cell Sci , vol.123 , pp. 1531-1536
    • Fujihara, Y.1    Murakami, M.2    Inoue, N.3    Satouh, Y.4    Kaseda, K.5    Ikawa, M.6    Okabe, M.7
  • 106
    • 84872226667 scopus 로고    scopus 로고
    • Visualization of the moment of mouse spermegg fusion and dynamic localization of IZUMO1
    • Medline
    • Satouh Y, Inoue N, Ikawa M, Okabe M. Visualization of the moment of mouse spermegg fusion and dynamic localization of IZUMO1. J Cell Sci 2012; 125: 4985-4990. [Medline]
    • (2012) J Cell Sci , vol.125 , pp. 4985-4990
    • Satouh, Y.1    Inoue, N.2    Ikawa, M.3    Okabe, M.4
  • 107
    • 84055200837 scopus 로고    scopus 로고
    • Acrosome-reacted mouse spermatozoa recovered from the perivitelline space can fertilize other eggs
    • Medline
    • Inoue N, Satouh Y, Ikawa M, Okabe M, Yanagimachi R. Acrosome-reacted mouse spermatozoa recovered from the perivitelline space can fertilize other eggs. Proc Natl Acad Sci USA 2011; 108: 20008-20011. [Medline]
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 20008-20011
    • Inoue, N.1    Satouh, Y.2    Ikawa, M.3    Okabe, M.4    Yanagimachi, R.5
  • 108
    • 0242541073 scopus 로고    scopus 로고
    • Tales from the tail: What do we really know about sperm motility?
    • Medline
    • Turner RM. Tales from the tail: what do we really know about sperm motility? J Androl 2003; 24: 790-803. [Medline]
    • (2003) J Androl , vol.24 , pp. 790-803
    • Turner, R.M.1
  • 110
    • 33645812936 scopus 로고    scopus 로고
    • Glycolysis and sperm motility: Does a spoonful of sugar help the flagellum go round?
    • Medline
    • Ford WC. Glycolysis and sperm motility: does a spoonful of sugar help the flagellum go round? Hum Reprod Update 2006; 12: 269-274. [Medline]
    • (2006) Hum Reprod Update , vol.12 , pp. 269-274
    • Ford, W.C.1
  • 111
    • 0032545434 scopus 로고    scopus 로고
    • Identification of tethering domains for protein kinase A type Iα regulatory subunits on sperm fibrous sheath protein FSC1
    • Medline
    • Miki K, Eddy EM. Identification of tethering domains for protein kinase A type Iα regulatory subunits on sperm fibrous sheath protein FSC1. J Biol Chem 1998; 273: 34384-34390. [Medline]
    • (1998) J Biol Chem , vol.273 , pp. 34384-34390
    • Miki, K.1    Eddy, E.M.2
  • 112
    • 0037405197 scopus 로고    scopus 로고
    • Fibrous sheath of mammalian spermatozoa
    • Medline
    • Eddy EM, Toshimori K, O'Brien DA. Fibrous sheath of mammalian spermatozoa. Microsc Res Tech 2003; 61: 103-115. [Medline]
    • (2003) Microsc Res Tech , vol.61 , pp. 103-115
    • Eddy, E.M.1    Toshimori, K.2    O'Brien, D.A.3
  • 113
    • 0017817925 scopus 로고
    • Movement characteristics and power output of guinea-pig and hamster spermatozoa in relation to activation
    • Medline
    • Katz DF, Yanagimachi R, Dresdner RD. Movement characteristics and power output of guinea-pig and hamster spermatozoa in relation to activation. J Reprod Fertil 1978; 52: 167-172. [Medline]
    • (1978) J Reprod Fertil , vol.52 , pp. 167-172
    • Katz, D.F.1    Yanagimachi, R.2    Dresdner, R.D.3
  • 114
  • 115
    • 54249143638 scopus 로고    scopus 로고
    • Regulation of sperm storage and movement in the mammalian oviduct
    • Medline
    • Suarez SS. Regulation of sperm storage and movement in the mammalian oviduct. Int J Dev Biol 2008; 52: 455-462. [Medline]
    • (2008) Int J Dev Biol , vol.52 , pp. 455-462
    • Suarez, S.S.1
  • 116
    • 0036389888 scopus 로고    scopus 로고
    • Hyperactivated motility of bull sperm is triggered at the axoneme by Ca2+ and not cAMP
    • Medline
    • Ho HC, Granish KA, Suarez SS. Hyperactivated motility of bull sperm is triggered at the axoneme by Ca2+ and not cAMP. Dev Biol 2002; 250: 208-217. [Medline]
    • (2002) Dev Biol , vol.250 , pp. 208-217
    • Ho, H.C.1    Granish, K.A.2    Suarez, S.S.3
  • 117
    • 0034766933 scopus 로고    scopus 로고
    • An inositol 1,4,5-trisphosphate receptor-gated intracellular Ca2+ store is involved in regulating sperm hyperactivated motility
    • Medline
    • Ho HC, Suarez SS. An inositol 1,4,5-trisphosphate receptor-gated intracellular Ca2+ store is involved in regulating sperm hyperactivated motility. Biol Reprod 2001; 65: 1606-1615. [Medline]
    • (2001) Biol Reprod , vol.65 , pp. 1606-1615
    • Ho, H.C.1    Suarez, S.S.2
  • 118
    • 0037406578 scopus 로고    scopus 로고
    • Characterization of the intracellular calcium store at the base of the sperm flagellum that regulates hyperactivated motility
    • Medline
    • Ho HC, Suarez SS. Characterization of the intracellular calcium store at the base of the sperm flagellum that regulates hyperactivated motility. Biol Reprod 2003; 68: 1590-1596. [Medline]
    • (2003) Biol Reprod , vol.68 , pp. 1590-1596
    • Ho, H.C.1    Suarez, S.S.2
  • 119
    • 79955675153 scopus 로고    scopus 로고
    • Calcium channels in the development, maturation, and function of spermatozoa
    • Medline
    • Darszon A, Nishigaki T, Beltran C, Treviño CL. Calcium channels in the development, maturation, and function of spermatozoa. Physiol Rev 2011; 91: 1305-1355. [Medline]
    • (2011) Physiol Rev , vol.91 , pp. 1305-1355
    • Darszon, A.1    Nishigaki, T.2    Beltran, C.3    Treviño, C.L.4
  • 123
    • 0035940492 scopus 로고    scopus 로고
    • A voltage-gated ion channel expressed specifically in spermatozoa
    • Medline
    • Quill TA, Ren D, Clapham DE, Garbers DL. A voltage-gated ion channel expressed specifically in spermatozoa. Proc Natl Acad Sci USA 2001; 98: 12527-12531. [Medline]
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 12527-12531
    • Quill, T.A.1    Ren, D.2    Clapham, D.E.3    Garbers, D.L.4
  • 126
    • 80052554188 scopus 로고    scopus 로고
    • Two distinct Ca2+ signaling pathways modulate sperm flagellar beating patterns in mice
    • Medline
    • Chang H, Suarez SS. Two distinct Ca2+ signaling pathways modulate sperm flagellar beating patterns in mice. Biol Reprod 2011; 85: 296-305. [Medline]
    • (2011) Biol Reprod , vol.85 , pp. 296-305
    • Chang, H.1    Suarez, S.S.2
  • 127
    • 2642534406 scopus 로고    scopus 로고
    • Different signaling pathways in bovine sperm regulate capacitation and hyperactivation
    • Medline
    • Marquez B, Suarez SS. Different signaling pathways in bovine sperm regulate capacitation and hyperactivation. Biol Reprod 2004; 70: 1626-1633. [Medline]
    • (2004) Biol Reprod , vol.70 , pp. 1626-1633
    • Marquez, B.1    Suarez, S.S.2
  • 128
    • 67649642113 scopus 로고    scopus 로고
    • Hyperactivation of stallion sperm is required for successful in vitro fertilization of equine oocytes
    • Medline
    • McPartlin LA, Suarez SS, Czaya CA, Hinrichs K, Bedford-Guaus SJ. Hyperactivation of stallion sperm is required for successful in vitro fertilization of equine oocytes. Biol Reprod 2009; 81: 199-206. [Medline]
    • (2009) Biol Reprod , vol.81 , pp. 199-206
    • McPartlin, L.A.1    Suarez, S.S.2    Czaya, C.A.3    Hinrichs, K.4    Bedford-Guaus, S.J.5
  • 129
    • 84864022588 scopus 로고    scopus 로고
    • Unexpected flagellar movement patterns and epithelial binding behavior of mouse sperm in the oviduct
    • Medline
    • Chang H, Suarez SS. Unexpected flagellar movement patterns and epithelial binding behavior of mouse sperm in the oviduct. Biol Reprod 2012; 86: 140,1-8. [Medline]
    • (2012) Biol Reprod , vol.86 , Issue.140 , pp. 1-8
    • Chang, H.1    Suarez, S.S.2
  • 130
    • 54149100366 scopus 로고    scopus 로고
    • Physiology of the male accessory sex structures: The prostate gland, seminal vesicles, and bulbourethral glands
    • Neill JD, Plant TM, Pfaff DW, Challis JRG, de Kretser DM, Richards JS, Wassarman PM (eds.), 3rd ed. Waltham: Academic Press
    • Risbridger GP, Taylor RA. Physiology of the male accessory sex structures: the prostate gland, seminal vesicles, and bulbourethral glands. In: Neill JD, Plant TM, Pfaff DW, Challis JRG, de Kretser DM, Richards JS, Wassarman PM (eds.), Knobil and Neill's Physiology of Reproduction. 3rd ed. Waltham: Academic Press; 2006: 1149-1172.
    • (2006) Knobil and Neill's Physiology of Reproduction , pp. 1149-1172
    • Risbridger, G.P.1    Taylor, R.A.2
  • 131
    • 68149098845 scopus 로고    scopus 로고
    • Calyculin A-sensitive protein phosphatases are involved in maintenance of progressive movement in mouse spermatozoa in vitro by suppression of autophosphorylation of protein kinase A
    • Medline
    • Goto N, Harayama H. Calyculin A-sensitive protein phosphatases are involved in maintenance of progressive movement in mouse spermatozoa in vitro by suppression of autophosphorylation of protein kinase A. J Reprod Dev 2009; 55: 327-334. [Medline]
    • (2009) J Reprod Dev , vol.55 , pp. 327-334
    • Goto, N.1    Harayama, H.2
  • 132
    • 58849163274 scopus 로고    scopus 로고
    • Understanding the molecular basis of sperm capacitation through kinase design
    • Medline
    • Visconti PE. Understanding the molecular basis of sperm capacitation through kinase design. Proc Natl Acad Sci USA 2009; 106: 667-668. [Medline]
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 667-668
    • Visconti, P.E.1
  • 134
    • 0031778295 scopus 로고    scopus 로고
    • Regulation of protein phosphorylation during sperm capacitation
    • Medline
    • Visconti PE, Kopf GS. Regulation of protein phosphorylation during sperm capacitation. Biol Reprod 1998; 59: 1-6. [Medline]
    • (1998) Biol Reprod , vol.59 , pp. 1-6
    • Visconti, P.E.1    Kopf, G.S.2
  • 135
    • 84867650900 scopus 로고    scopus 로고
    • Relationship between cyclic AMP-dependent protein tyrosine phosphorylation and extracellular calcium during hyperactivation of boar spermatozoa
    • Medline
    • Harayama H, Noda T, Ishikawa S, Shidara O. Relationship between cyclic AMP-dependent protein tyrosine phosphorylation and extracellular calcium during hyperactivation of boar spermatozoa. Mol Reprod Dev 2012; 79: 727-739. [Medline]
    • (2012) Mol Reprod Dev , vol.79 , pp. 727-739
    • Harayama, H.1    Noda, T.2    Ishikawa, S.3    Shidara, O.4
  • 136
    • 0344668550 scopus 로고    scopus 로고
    • A new sperm-specific Na+/ H+ exchanger required for sperm motility and fertility
    • Medline
    • Wang D, King SM, Quill TA, Doolittle LK, Garbers DL. A new sperm-specific Na+/ H+ exchanger required for sperm motility and fertility. Nat Cell Biol 2003; 5: 1117-1122. [Medline]
    • (2003) Nat Cell Biol , vol.5 , pp. 1117-1122
    • Wang, D.1    King, S.M.2    Quill, T.A.3    Doolittle, L.K.4    Garbers, D.L.5
  • 138
    • 79955032438 scopus 로고    scopus 로고
    • Deletion of the Slo3 gene abolishes alkalization-activated K+ current in mouse spermatozoa
    • Medline
    • Zeng XH, Yang C, Kim ST, Lingle CJ, Xia XM. Deletion of the Slo3 gene abolishes alkalization-activated K+ current in mouse spermatozoa. Proc Natl Acad Sci USA 2011; 108: 5879-5884. [Medline]
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 5879-5884
    • Zeng, X.H.1    Yang, C.2    Kim, S.T.3    Lingle, C.J.4    Xia, X.M.5
  • 142
    • 83455199148 scopus 로고    scopus 로고
    • Heads or tails? Structural events and molecular mechanisms that promote mammalian sperm acrosomal exocytosis and motility
    • Medline
    • Buffone MG, Ijiri TW, Cao W, Merdiushev T, Aghajanian HK, Gerton GL. Heads or tails? Structural events and molecular mechanisms that promote mammalian sperm acrosomal exocytosis and motility. Mol Reprod Dev 2012; 79: 4-18. [Medline]
    • (2012) Mol Reprod Dev , vol.79 , pp. 4-18
    • Buffone, M.G.1    Ijiri, T.W.2    Cao, W.3    Merdiushev, T.4    Aghajanian, H.K.5    Gerton, G.L.6
  • 143
    • 0034887719 scopus 로고    scopus 로고
    • Capacitation is associated with tyrosine phosphorylation and tyrosine kinase-like activity of pig sperm proteins
    • Medline
    • Tardif S, Dubé 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. [Medline]
    • (2001) Biol Reprod , vol.65 , pp. 784-792
    • Tardif, S.1    Dubé, C.2    Chevalier, S.3    Bailey, J.L.4
  • 144
    • 0037120980 scopus 로고    scopus 로고
    • Capacitation-like alterations in cooled boar spermatozoa: Assessment by the chlortetracycline staining assay and immunodetection of tyrosine-phosphorylated sperm proteins
    • Medline
    • Kaneto M, Harayama H, Miyake M, Kato S. Capacitation-like alterations in cooled boar spermatozoa: assessment by the chlortetracycline staining assay and immunodetection of tyrosine-phosphorylated sperm proteins. Anim Reprod Sci 2002; 73: 197-209. [Medline]
    • (2002) Anim Reprod Sci , vol.73 , pp. 197-209
    • Kaneto, M.1    Harayama, H.2    Miyake, M.3    Kato, S.4
  • 145
    • 16344366170 scopus 로고    scopus 로고
    • Changes in tyrosine phosphorylation associated with true capacitation and capacitationlike state in boar spermatozoa
    • Medline
    • Bravo MM, Aparicio IM, Garcia-Herreros M, Gil MC, Peña FJ, Garcia-Marin LJ. Changes in tyrosine phosphorylation associated with true capacitation and capacitationlike state in boar spermatozoa. Mol Reprod Dev 2005; 71: 88-96. [Medline]
    • (2005) Mol Reprod Dev , vol.71 , pp. 88-96
    • Bravo, M.M.1    Aparicio, I.M.2    Garcia-Herreros, M.3    Gil, M.C.4    Peña, F.J.5    Garcia-Marin, L.J.6
  • 146
    • 3543140227 scopus 로고    scopus 로고
    • AMP-activated protein kinase: A master switch in glucose and lipid metabolism
    • Medline
    • Hardie DG. AMP-activated protein kinase: a master switch in glucose and lipid metabolism. Rev Endocr Metab Disord 2004; 5: 119-125. [Medline]
    • (2004) Rev Endocr Metab Disord , vol.5 , pp. 119-125
    • Hardie, D.G.1
  • 147
    • 20844451123 scopus 로고    scopus 로고
    • AMP-activated protein kinase: Ancient energy gauge provides clues to modern understanding of metabolism
    • Medline
    • Kahn BB, Alquier T, Carling D, Hardie DG. AMP-activated protein kinase: ancient energy gauge provides clues to modern understanding of metabolism. Cell Metab 2005; 1: 15-25. [Medline]
    • (2005) Cell Metab , vol.1 , pp. 15-25
    • Kahn, B.B.1    Alquier, T.2    Carling, D.3    Hardie, D.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.