메뉴 건너뛰기




Volumn 90, Issue 5, 2014, Pages

Unresolved questions concerning mammalian sperm acrosomal exocytosis

Author keywords

Acrosomal exocytosis; Capacitation; Fertilization; Sperm

Indexed keywords

ACROSOME; EXOCYTOSIS; FEMALE GENITAL SYSTEM; FERTILIZATION; HUMAN; MAMMAL; NONHUMAN; OVIDUCT; PRIORITY JOURNAL; SECRETION (PROCESS); SHORT SURVEY; SPERM; SPERMATOZOON CAPACITATION; TESTIS; ACROSOME REACTION; ANIMAL; FEMALE; FERTILITY; MALE; MOUSE; PHYSIOLOGY; SPERMATOZOON;

EID: 84903766119     PISSN: 00063363     EISSN: 15297268     Source Type: Journal    
DOI: 10.1095/biolreprod.114.117911     Document Type: Short Survey
Times cited : (73)

References (89)
  • 1
    • 84884073858 scopus 로고    scopus 로고
    • The Spermatozoon.
    • In: Knobil E (ed.), Knobil and Neill's Physiology of Reproduction. Boston: Elsevier;
    • Eddy EM. The Spermatozoon. In: Knobil E (ed.), Knobil and Neill's Physiology of Reproduction. Boston: Elsevier; 2006; 3-54.
    • (2006) , pp. 3-54
    • Eddy, E.M.1
  • 2
    • 0001953357 scopus 로고    scopus 로고
    • Function of the sperm acrosome
    • In: Hardy DM (ed.), Fertilization. San Diego: Academic Press;
    • Gerton GL. Function of the sperm acrosome In: Hardy DM (ed.), Fertilization. San Diego: Academic Press; 2002; 265-302.
    • (2002) , pp. 265-302
    • Gerton, G.L.1
  • 3
    • 54249097511 scopus 로고    scopus 로고
    • The role of the acrosomal matrix in fertilization
    • Buffone MG, Foster JA, Gerton GL. The role of the acrosomal matrix in fertilization. Int J Dev Biol 2008; 52(5-6):511-522.
    • (2008) Int J Dev Biol , vol.52 , Issue.5-6 , pp. 511-522
    • Buffone, M.G.1    Foster, J.A.2    Gerton, G.L.3
  • 4
    • 0030974131 scopus 로고    scopus 로고
    • AM67, a secretory component of the guinea pig sperm acrosomal matrix, is related to mouse sperm protein sp56 and the complement component 4-binding proteins
    • Foster JA, Friday BB, Maulit MT, Blobel C, Winfrey VP, Olson GE, Kim KS, Gerton GL. AM67, a secretory component of the guinea pig sperm acrosomal matrix, is related to mouse sperm protein sp56 and the complement component 4-binding proteins. J Biol Chem 1997; 272(19): 12714-12722.
    • (1997) J Biol Chem , vol.272 , Issue.19 , pp. 12714-12722
    • Foster, J.A.1    Friday, B.B.2    Maulit, M.T.3    Blobel, C.4    Winfrey, V.P.5    Olson, G.E.6    Kim, K.S.7    Gerton, G.L.8
  • 5
    • 0035168574 scopus 로고    scopus 로고
    • Mouse sperm protein sp56 is a component of the acrosomal matrix
    • Kim KS, Cha MC, Gerton GL. Mouse sperm protein sp56 is a component of the acrosomal matrix. Biol Reprod 2001; 64(1):36-43.
    • (2001) Biol Reprod , vol.64 , Issue.1 , pp. 36-43
    • Kim, K.S.1    Cha, M.C.2    Gerton, G.L.3
  • 6
    • 0027982658 scopus 로고
    • Structure of acrosomal matrix domains of rabbit sperm
    • Olson GE, Winfrey VP. Structure of acrosomal matrix domains of rabbit sperm. J Struct Biol 1994; 112(1):41-48.
    • (1994) J Struct Biol , vol.112 , Issue.1 , pp. 41-48
    • Olson, G.E.1    Winfrey, V.P.2
  • 7
    • 0028878192 scopus 로고
    • Sorting of the domainspecific acrosomal matrix protein AM50 during spermiogenesis in the guinea pig
    • Westbrook-Case VA, Winfrey VP, Olson GE. Sorting of the domainspecific acrosomal matrix protein AM50 during spermiogenesis in the guinea pig. Dev Biol 1995; 167(1):338-349.
    • (1995) Dev Biol , vol.167 , Issue.1 , pp. 338-349
    • Westbrook-Case, V.A.1    Winfrey, V.P.2    Olson, G.E.3
  • 8
    • 0028343144 scopus 로고
    • A domain-specific 50-kilodalton structural protein of the acrosomal matrix is processed and released during the acrosome reaction in the guinea pig
    • Westbrook-Case VA, Winfrey VP, Olson GE. A domain-specific 50-kilodalton structural protein of the acrosomal matrix is processed and released during the acrosome reaction in the guinea pig. Biol Reprod 1994; 51(1):1-13.
    • (1994) Biol Reprod , vol.51 , Issue.1 , pp. 1-13
    • Westbrook-Case, V.A.1    Winfrey, V.P.2    Olson, G.E.3
  • 9
    • 70350351206 scopus 로고    scopus 로고
    • Functional consequences of cleavage, dissociation and exocytotic release of ZP3R, a C4BP-related protein, from the mouse sperm acrosomal matrix
    • Buffone MG, Kim K-S, Doak BJ, Rodriguez-Miranda E, Gerton GL. Functional consequences of cleavage, dissociation and exocytotic release of ZP3R, a C4BP-related protein, from the mouse sperm acrosomal matrix. J Cell Sci 2009; 122(Pt 17):3153-3160.
    • (2009) J Cell Sci , vol.122 , Issue.PART 17 , pp. 3153-3160
    • Buffone, M.G.1    Kim, K.-S.2    Doak, B.J.3    Rodriguez-Miranda, E.4    Gerton, G.L.5
  • 10
    • 0242624744 scopus 로고    scopus 로고
    • Differential release of soluble and matrix components: evidence for intermediate states of secretion during spontaneous acrosomal exocytosis in mouse sperm
    • Kim K-S, Gerton GL. Differential release of soluble and matrix components: evidence for intermediate states of secretion during spontaneous acrosomal exocytosis in mouse sperm. Dev Biol 2003; 264(1):141-152.
    • (2003) Dev Biol , vol.264 , Issue.1 , pp. 141-152
    • Kim, K.-S.1    Gerton, G.L.2
  • 11
    • 81355127552 scopus 로고    scopus 로고
    • Transitional states of acrosomal exocytosis and proteolytic processing of the acrosomal matrix in guinea pig sperm
    • Kim K-S, Foster JA, Kvasnicka KW, Gerton GL. Transitional states of acrosomal exocytosis and proteolytic processing of the acrosomal matrix in guinea pig sperm. Mol Reprod Dev 2011; 78(12):930-941.
    • (2011) Mol Reprod Dev , vol.78 , Issue.12 , pp. 930-941
    • Kim, K.-S.1    Foster, J.A.2    Kvasnicka, K.W.3    Gerton, G.L.4
  • 12
    • 0028569728 scopus 로고
    • The sperm acrosomal matrix contains a novel member of the pentaxin family of calciumdependent binding proteins
    • Noland TD, Friday BB, Maulit MT, Gerton GL. The sperm acrosomal matrix contains a novel member of the pentaxin family of calciumdependent binding proteins. J Biol Chem 1994; 269(51):32607-32614.
    • (1994) J Biol Chem , vol.269 , Issue.51 , pp. 32607-32614
    • Noland, T.D.1    Friday, B.B.2    Maulit, M.T.3    Gerton, G.L.4
  • 13
    • 34248570055 scopus 로고    scopus 로고
    • Acrosomal exocytosis, a special type of regulated secretion
    • Mayorga LS, Tomes CN, Belmonte SA. Acrosomal exocytosis, a special type of regulated secretion. IUBMB Life 2007; 59(4-5):286-292.
    • (2007) IUBMB Life , vol.59 , Issue.4-5 , pp. 286-292
    • Mayorga, L.S.1    Tomes, C.N.2    Belmonte, S.A.3
  • 16
    • 34748822250 scopus 로고    scopus 로고
    • Loss of zona pellucida binding proteins in the acrosomal matrix disrupts acrosome biogenesis and sperm morphogenesis
    • Lin Y-N, Roy A, Yan W, Burns KH, Matzuk MM. Loss of zona pellucida binding proteins in the acrosomal matrix disrupts acrosome biogenesis and sperm morphogenesis. Mol Cell Biol 2007; 27(19):6794-6805.
    • (2007) Mol Cell Biol , vol.27 , Issue.19 , pp. 6794-6805
    • Lin, Y.-N.1    Roy, A.2    Yan, W.3    Burns, K.H.4    Matzuk, M.M.5
  • 17
    • 0022587510 scopus 로고
    • Failure of acrosome assembly in a male sterile mouse mutant
    • Sotomayor RE, Handel MA. Failure of acrosome assembly in a male sterile mouse mutant. Biol Reprod 1986; 34(1):171-182.
    • (1986) Biol Reprod , vol.34 , Issue.1 , pp. 171-182
    • Sotomayor, R.E.1    Handel, M.A.2
  • 19
    • 0018144170 scopus 로고
    • Ultrastructure of the equatorial segment of hamster spermatozoa during penetration of oocytes
    • Moore HDM, Bedford JM. Ultrastructure of the equatorial segment of hamster spermatozoa during penetration of oocytes. J Ultrastruct Res 1978; 62(2):110-117.
    • (1978) J Ultrastruct Res , vol.62 , Issue.2 , pp. 110-117
    • Moore, H.D.M.1    Bedford, J.M.2
  • 20
    • 0025167186 scopus 로고
    • Ultrastructural studies on the fertilization of mammalian gametes
    • Oura C, Toshimori K. Ultrastructural studies on the fertilization of mammalian gametes. Int Rev Cytol 1990; 122:105-151.
    • (1990) Int Rev Cytol , vol.122 , pp. 105-151
    • Oura, C.1    Toshimori, K.2
  • 21
    • 0023121556 scopus 로고
    • The biology and chemistry of fertilization
    • Wassarman PM. The biology and chemistry of fertilization. Science 1987; 235(4788):553-560.
    • (1987) Science , vol.235 , Issue.4788 , pp. 553-560
    • Wassarman, P.M.1
  • 22
    • 84872226667 scopus 로고    scopus 로고
    • Visualization of the moment of mouse sperm-egg fusion and dynamic localization of IZUMO1
    • Satouh Y, Inoue N, Ikawa M, Okabe M. Visualization of the moment of mouse sperm-egg fusion and dynamic localization of IZUMO1. J Cell Sci 2012; 125(21):4985-4990.
    • (2012) J Cell Sci , vol.125 , Issue.21 , pp. 4985-4990
    • Satouh, Y.1    Inoue, N.2    Ikawa, M.3    Okabe, M.4
  • 24
    • 77954594769 scopus 로고    scopus 로고
    • Analysis of CAPZA3 localization reveals temporally discrete events during the acrosome reaction
    • Sosnik J, Buffone M, Visconti PE. Analysis of CAPZA3 localization reveals temporally discrete events during the acrosome reaction. J Cell Physiol 2010; 224(3):575-580.
    • (2010) J Cell Physiol , vol.224 , Issue.3 , pp. 575-580
    • Sosnik, J.1    Buffone, M.2    Visconti, P.E.3
  • 25
    • 79953232734 scopus 로고    scopus 로고
    • Most fertilizing mouse spermatozoa begin their acrosome reaction before contact with the zona pellucida during in vitro fertilization
    • 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 U S A 2011; 108(12):4892-4896.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , Issue.12 , 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
  • 26
    • 0018502644 scopus 로고
    • An ultrastructural study of epididymal mouse spermatozoa binding to zonae pellucidae in vitro: sequential relationship to the acrosome reaction
    • Saling PM, Sowinski J, Storey BT. An ultrastructural study of epididymal mouse spermatozoa binding to zonae pellucidae in vitro: sequential relationship to the acrosome reaction. J Exp Zool 1979; 209(2):229-238.
    • (1979) J Exp Zool , vol.209 , Issue.2 , pp. 229-238
    • Saling, P.M.1    Sowinski, J.2    Storey, B.T.3
  • 27
    • 34248587212 scopus 로고    scopus 로고
    • Sperm binding to the zona pellucida is not sufficient to induce acrosome exocytosis
    • Baibakov B, Gauthier L, Talbot P, Rankin TL, Dean J. Sperm binding to the zona pellucida is not sufficient to induce acrosome exocytosis. Development 2007; 134(5):933-943.
    • (2007) Development , vol.134 , Issue.5 , pp. 933-943
    • Baibakov, B.1    Gauthier, L.2    Talbot, P.3    Rankin, T.L.4    Dean, J.5
  • 28
    • 54249143638 scopus 로고    scopus 로고
    • Regulation of sperm storage and movement in the mammalian oviduct
    • Suarez SS. Regulation of sperm storage and movement in the mammalian oviduct. Int J Dev Biol 2008; 52(5-6):455-462.
    • (2008) Int J Dev Biol , vol.52 , Issue.5-6 , pp. 455-462
    • Suarez, S.S.1
  • 29
    • 84887168706 scopus 로고    scopus 로고
    • The cell biology of mammalian fertilization
    • Okabe M. The cell biology of mammalian fertilization. Development 2013; 140(22):4471-4479.
    • (2013) Development , vol.140 , Issue.22 , pp. 4471-4479
    • Okabe, M.1
  • 30
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • In: Knobil E, Neill J.D (eds.),. New York: Raven Press;
    • Yanagimachi R. Mammalian fertilization In: Knobil E, Neill JD (eds.), The Physiology of Reproduction. New York: Raven Press; 1994.
    • (1994) The Physiology of Reproduction
    • Yanagimachi, R.1
  • 31
    • 76949114656 scopus 로고
    • Observations on the penetration of the sperm in the mammalian egg
    • Austin CR. Observations on the penetration of the sperm in the mammalian egg. Aust J Sci Res B 1951; 4(4):581-596.
    • (1951) Aust J Sci Res B , vol.4 , Issue.4 , pp. 581-596
    • Austin, C.R.1
  • 32
    • 36949091315 scopus 로고
    • Fertilizing capacity of spermatozoa deposited into the fallopian tubes
    • Chang MC. Fertilizing capacity of spermatozoa deposited into the fallopian tubes. Nature 1951; 168(4277):697-698.
    • (1951) Nature , vol.168 , Issue.4277 , pp. 697-698
    • Chang, M.C.1
  • 33
    • 0033570112 scopus 로고    scopus 로고
    • Cholesterol efflux-mediated signal transduction in mammalian sperm: cholesterol release signals an increase in protein tyrosine phosphorylation during mouse sperm capacitation
    • Visconti PE, Ning X, Fornés MW, Alvarez JG, Stein P, Connors SA, Kopf GS. Cholesterol efflux-mediated signal transduction in mammalian sperm: cholesterol release signals an increase in protein tyrosine phosphorylation during mouse sperm capacitation. Dev Biol 1999; 214(2):429-443.
    • (1999) Dev Biol , vol.214 , Issue.2 , pp. 429-443
    • Visconti, P.E.1    Ning, X.2    Fornés, M.W.3    Alvarez, J.G.4    Stein, P.5    Connors, S.A.6    Kopf, G.S.7
  • 34
    • 84884737607 scopus 로고    scopus 로고
    • Phospholipase B is activated in response to sterol removal and stimulates acrosome exocytosis in murine sperm
    • Asano A, Nelson-Harrington JL, Travis AJ. Phospholipase B is activated in response to sterol removal and stimulates acrosome exocytosis in murine sperm. J Biol Chem 2013; 288(39):28104-28115.
    • (2013) J Biol Chem , vol.288 , Issue.39 , pp. 28104-28115
    • Asano, A.1    Nelson-Harrington, J.L.2    Travis, A.J.3
  • 35
    • 84895063008 scopus 로고    scopus 로고
    • Removal of GPI-anchored membrane proteins causes clustering of lipid microdomains in the apical head area of porcine sperm
    • Boerke A, van der Lit J, Lolicato F, Stout TAE, Helms JB, Gadella BM. Removal of GPI-anchored membrane proteins causes clustering of lipid microdomains in the apical head area of porcine sperm. Theriogenology 2014; 81(4):613-624.
    • (2014) Theriogenology , vol.81 , Issue.4 , pp. 613-624
    • Boerke, A.1    Van der Lit, J.2    Lolicato, F.3    Stout, T.A.E.4    Helms, J.B.5    Gadella, B.M.6
  • 36
    • 84858141674 scopus 로고    scopus 로고
    • Flow cytometry analysis reveals a decrease in intracellular sodium during sperm capacitation
    • Escoffier J, Krapf D, Navarrete F, Darszon A, Visconti PE. Flow cytometry analysis reveals a decrease in intracellular sodium during sperm capacitation. J Cell Sci 2012; 125(Pt 2):473-485.
    • (2012) J Cell Sci , vol.125 , Issue.PART 2 , pp. 473-485
    • Escoffier, J.1    Krapf, D.2    Navarrete, F.3    Darszon, A.4    Visconti, P.E.5
  • 38
    • 0028804984 scopus 로고
    • Sperm membrane potential: hyperpolarization during capacitation regulates zona pellucida-dependent acrosomal secretion
    • Zeng Y, Clark EN, Florman HM. Sperm membrane potential: hyperpolarization during capacitation regulates zona pellucida-dependent acrosomal secretion. Dev Biol 1995; 171(2):554-563.
    • (1995) Dev Biol , vol.171 , Issue.2 , pp. 554-563
    • Zeng, Y.1    Clark, E.N.2    Florman, H.M.3
  • 39
    • 0033535956 scopus 로고    scopus 로고
    • Control of the low voltage-activated calcium channel of mouse sperm by egg ZP3 and by membrane hyperpolarization during capacitation
    • Arnoult C, Kazam IG, Visconti PE, Kopf GS, Villaz M, Florman HM. Control of the low voltage-activated calcium channel of mouse sperm by egg ZP3 and by membrane hyperpolarization during capacitation. Proc Natl Acad Sci U S A 1999; 96(12):6757-6762.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , Issue.12 , pp. 6757-6762
    • Arnoult, C.1    Kazam, I.G.2    Visconti, P.E.3    Kopf, G.S.4    Villaz, M.5    Florman, H.M.6
  • 41
    • 68049126532 scopus 로고    scopus 로고
    • Acrosomal swelling and membrane docking are required for hybrid vesicle formation during the human sperm acrosome reaction
    • Zanetti N, Mayorga LS. Acrosomal swelling and membrane docking are required for hybrid vesicle formation during the human sperm acrosome reaction. Biol Reprod 2009; 81(2):396-405.
    • (2009) Biol Reprod , vol.81 , Issue.2 , pp. 396-405
    • Zanetti, N.1    Mayorga, L.S.2
  • 43
    • 77956401827 scopus 로고    scopus 로고
    • Identification and disruption of sperm-specific angiotensin converting enzyme-3 (ACE3) in mouse
    • Inoue N, Kasahara T, Ikawa M, Okabe M. Identification and disruption of sperm-specific angiotensin converting enzyme-3 (ACE3) in mouse. Plos One 2010; 5(4):e10301.
    • (2010) Plos One , vol.5 , Issue.4
    • Inoue, N.1    Kasahara, T.2    Ikawa, M.3    Okabe, M.4
  • 44
    • 4544250782 scopus 로고    scopus 로고
    • Possible function of the ADAM1a/ADAM2 fertilin complex in the appearance of ADAM3 on the sperm surface
    • Nishimura H, Kim E, Nakanishi T, Baba T. Possible function of the ADAM1a/ADAM2 fertilin complex in the appearance of ADAM3 on the sperm surface. J Biol Chem 2004; 279(33):34957-34962.
    • (2004) J Biol Chem , vol.279 , Issue.33 , pp. 34957-34962
    • Nishimura, H.1    Kim, E.2    Nakanishi, T.3    Baba, T.4
  • 46
    • 33750845874 scopus 로고    scopus 로고
    • Aberrant distribution of ADAM3 in sperm from both angiotensin-converting enzyme (Ace)- and calmegin (Clgn)-deficient mice
    • Yamaguchi R, Yamagata K, Ikawa M, Moss SB, Okabe M. Aberrant distribution of ADAM3 in sperm from both angiotensin-converting enzyme (Ace)- and calmegin (Clgn)-deficient mice. Biol Reprod 2006; 75(5):760-766.
    • (2006) Biol Reprod , vol.75 , Issue.5 , pp. 760-766
    • Yamaguchi, R.1    Yamagata, K.2    Ikawa, M.3    Moss, S.B.4    Okabe, M.5
  • 47
    • 0014944131 scopus 로고
    • Proteolytic reaction of mammalian spermatozoa on gelatin membranes
    • Gaddum P, Blandau RJ. Proteolytic reaction of mammalian spermatozoa on gelatin membranes. Science 1970; 170(3959):749-751.
    • (1970) Science , vol.170 , Issue.3959 , pp. 749-751
    • Gaddum, P.1    Blandau, R.J.2
  • 48
    • 0032906356 scopus 로고    scopus 로고
    • Real-time observation of acrosomal dispersal from mouse sperm using GFP as a marker protein
    • Nakanishi T, Ikawa M, Yamada S, Parvinen M, Baba T, Nishimune Y, Okabe M. Real-time observation of acrosomal dispersal from mouse sperm using GFP as a marker protein. FEBS Lett 1999; 449(2-3): 277-283.
    • (1999) FEBS Lett , vol.449 , Issue.2-3 , pp. 277-283
    • Nakanishi, T.1    Ikawa, M.2    Yamada, S.3    Parvinen, M.4    Baba, T.5    Nishimune, Y.6    Okabe, M.7
  • 49
    • 33646173507 scopus 로고    scopus 로고
    • Identification of novel gamete receptors that mediate sperm adhesion to the egg coat
    • Shur BD, Rodeheffer C, Ensslin MA, Lyng R, Raymond A. Identification of novel gamete receptors that mediate sperm adhesion to the egg coat. Mol Cell Endocrinol 2006; 250(1-2):137-148.
    • (2006) Mol Cell Endocrinol , vol.250 , Issue.1-2 , pp. 137-148
    • Shur, B.D.1    Rodeheffer, C.2    Ensslin, M.A.3    Lyng, R.4    Raymond, A.5
  • 50
    • 21644466386 scopus 로고    scopus 로고
    • Contribution of mouse egg zona pellucida glycoproteins to gamete recognition during fertilization
    • Wassarman PM. Contribution of mouse egg zona pellucida glycoproteins to gamete recognition during fertilization. J Cell Physiol 2005; 204(2): 388-391.
    • (2005) J Cell Physiol , vol.204 , Issue.2 , pp. 388-391
    • Wassarman, P.M.1
  • 51
    • 0021281679 scopus 로고
    • Successful fertilization in vitro of fresh intact oocytes by perivitelline (acrosome-reacted) spermatozoa of the rabbit
    • Kuzan FB, Fleming AD, Seidel JRGE. Successful fertilization in vitro of fresh intact oocytes by perivitelline (acrosome-reacted) spermatozoa of the rabbit. Fertil Steril 1984; 41(5):766-770.
    • (1984) Fertil Steril , vol.41 , Issue.5 , pp. 766-770
    • Kuzan, F.B.1    Fleming, A.D.2    Seidel, J.R.G.E.3
  • 52
    • 84894371193 scopus 로고    scopus 로고
    • Regulation of acrosome reaction by Liprin α3, LAR and its ligands in mouse spermatozoa
    • Joshi CS, Khan SA, Khole VV. Regulation of acrosome reaction by Liprin α3, LAR and its ligands in mouse spermatozoa. Andrology 2014; 2(2): 165-174.
    • (2014) Andrology , vol.2 , Issue.2 , pp. 165-174
    • Joshi, C.S.1    Khan, S.A.2    Khole, V.V.3
  • 53
    • 84055200837 scopus 로고    scopus 로고
    • Acrosomereacted mouse spermatozoa recovered from the perivitelline space can fertilize other eggs
    • Inoue N, Satouh Y, Ikawa M, Okabe M, Yanagimachi R. Acrosomereacted mouse spermatozoa recovered from the perivitelline space can fertilize other eggs. Proc Natl Acad Sci U S A 2011; 108(50): 20008-20011.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , Issue.50 , pp. 20008-20011
    • Inoue, N.1    Satouh, Y.2    Ikawa, M.3    Okabe, M.4    Yanagimachi, R.5
  • 54
    • 15044362481 scopus 로고    scopus 로고
    • The immunoglobulin superfamily protein Izumo is required for sperm to fuse with eggs
    • Inoue N, Ikawa M, Isotani A, Okabe M. The immunoglobulin superfamily protein Izumo is required for sperm to fuse with eggs. Nature 2005; 434(7030):234-238.
    • (2005) Nature , vol.434 , Issue.7030 , pp. 234-238
    • Inoue, N.1    Ikawa, M.2    Isotani, A.3    Okabe, M.4
  • 56
    • 0031080921 scopus 로고    scopus 로고
    • Progesterone triggers a wave of increased free calcium during the human sperm acrosome reaction
    • Meizel S, Turner KO, Nuccitelli R. Progesterone triggers a wave of increased free calcium during the human sperm acrosome reaction. Dev Biol 1997; 182(1):67-75.
    • (1997) Dev Biol , vol.182 , Issue.1 , pp. 67-75
    • Meizel, S.1    Turner, K.O.2    Nuccitelli, R.3
  • 57
    • 79952800026 scopus 로고    scopus 로고
    • Progesterone activates the principal Ca2+ channel of human sperm
    • Lishko PV, Botchkina IL, Kirichok Y. Progesterone activates the principal Ca2+ channel of human sperm. Nature 2011; 471(7338):387-391.
    • (2011) Nature , vol.471 , Issue.7338 , pp. 387-391
    • Lishko, P.V.1    Botchkina, I.L.2    Kirichok, Y.3
  • 59
    • 77955538603 scopus 로고    scopus 로고
    • Calcium signaling through CatSper channels in mammalian fertilization
    • Ren D, Xia J. Calcium signaling through CatSper channels in mammalian fertilization. Physiol (Bethesda) 2010; 25(3):165-175.
    • (2010) Physiol (Bethesda) , vol.25 , Issue.3 , pp. 165-175
    • Ren, D.1    Xia, J.2
  • 60
    • 67650364012 scopus 로고    scopus 로고
    • Acrosomal exocytosis of mouse sperm progresses in a consistent direction in response to zona pellucida
    • Buffone MG, Rodriguez-Miranda E, Storey BT, Gerton GL. Acrosomal exocytosis of mouse sperm progresses in a consistent direction in response to zona pellucida. J Cell Physiol 2009; 220(3):611-620.
    • (2009) J Cell Physiol , vol.220 , Issue.3 , pp. 611-620
    • Buffone, M.G.1    Rodriguez-Miranda, E.2    Storey, B.T.3    Gerton, G.L.4
  • 61
    • 63649156363 scopus 로고    scopus 로고
    • Progestin functions in vertebrate gametes mediated by membrane progestin receptors (mPRs): identification of mPR[alpha] on human sperm and its association with sperm motility
    • Thomas P, Tubbs C, Garry VF. Progestin functions in vertebrate gametes mediated by membrane progestin receptors (mPRs): identification of mPR[alpha] on human sperm and its association with sperm motility. Steroids 2009; 74(7):614-621.
    • (2009) Steroids , vol.74 , Issue.7 , pp. 614-621
    • Thomas, P.1    Tubbs, C.2    Garry, V.F.3
  • 62
    • 36849058592 scopus 로고    scopus 로고
    • Membrane-permeant Rab3A triggers acrosomal exocytosis in living human sperm
    • Lopez CI, Belmonte SA, De Blas GA, Mayorga LS. Membrane-permeant Rab3A triggers acrosomal exocytosis in living human sperm. FASEB J 2007; 21(14):4121-4130.
    • (2007) FASEB J , vol.21 , Issue.14 , pp. 4121-4130
    • Lopez, C.I.1    Belmonte, S.A.2    De Blas, G.A.3    Mayorga, L.S.4
  • 63
    • 26444433186 scopus 로고    scopus 로고
    • Dynamics of SNARE assembly and disassembly during sperm acrosomal exocytosis
    • De Blas GA, Roggero CM, Tomes CN, Mayorga LS. Dynamics of SNARE assembly and disassembly during sperm acrosomal exocytosis. PLoS Biol 2005; 3(10):e323.
    • (2005) PLoS Biol , vol.3 , Issue.10
    • De Blas, G.A.1    Roggero, C.M.2    Tomes, C.N.3    Mayorga, L.S.4
  • 64
    • 79960572472 scopus 로고    scopus 로고
    • a-SNAP prevents docking of the acrosome during sperm exocytosis because it sequesters monomeric syntaxin
    • Rodríguez F, Bustos MA, Zanetti MN, Ruete MC, Mayorga LS, Tomes CN. a-SNAP prevents docking of the acrosome during sperm exocytosis because it sequesters monomeric syntaxin. Plos One 2011; 6(7):e21925.
    • (2011) Plos One , vol.6 , Issue.7
    • Rodríguez, F.1    Bustos, M.A.2    Zanetti, M.N.3    Ruete, M.C.4    Mayorga, L.S.5    Tomes, C.N.6
  • 67
    • 34548391033 scopus 로고    scopus 로고
    • Complexin I is required for mammalian sperm acrosomal exocytosis
    • Zhao L, Burkin HR, Shi X, Li L, Reim K, Miller DJ. Complexin I is required for mammalian sperm acrosomal exocytosis. Dev Biol 2007; 309(2):236-244.
    • (2007) Dev Biol , vol.309 , Issue.2 , pp. 236-244
    • Zhao, L.1    Burkin, H.R.2    Shi, X.3    Li, L.4    Reim, K.5    Miller, D.J.6
  • 68
    • 20144379204 scopus 로고    scopus 로고
    • Synaptotagmin VI and VIII and syntaxin 2 are essential for the mouse sperm acrosome reaction
    • Hutt DM, Baltz JM, Ngsee JK, Synaptotagmin VI. and VIII and syntaxin 2 are essential for the mouse sperm acrosome reaction. J Biol Chem 2005; 280(21):20197-20203.
    • (2005) J Biol Chem , vol.280 , Issue.21 , pp. 20197-20203
    • Hutt, D.M.1    Baltz, J.M.2    Ngsee, J.K.3
  • 69
    • 0035879141 scopus 로고    scopus 로고
    • Synaptotagmin VI participates in the acrosome reaction of human spermatozoa
    • Michaut M, De Blas G, Tomes CN, Yunes R, Fukuda M, Mayorga LS. Synaptotagmin VI participates in the acrosome reaction of human spermatozoa. Dev Biol 2001; 235(2):521-529.
    • (2001) Dev Biol , vol.235 , Issue.2 , pp. 521-529
    • Michaut, M.1    De Blas, G.2    Tomes, C.N.3    Yunes, R.4    Fukuda, M.5    Mayorga, L.S.6
  • 70
    • 0037077705 scopus 로고    scopus 로고
    • Rab3A and calmodulin regulate acrosomal exocytosis by mechanisms that do not require a direct interaction
    • Yunes R, Tomes C, Michaut M, De Blas G, Rodriguez F, Regazzi R, Mayorga LS. Rab3A and calmodulin regulate acrosomal exocytosis by mechanisms that do not require a direct interaction. FEBS Lett 2002; 525(1-3):126-130.
    • (2002) FEBS Lett , vol.525 , Issue.1-3 , pp. 126-130
    • Yunes, R.1    Tomes, C.2    Michaut, M.3    De Blas, G.4    Rodriguez, F.5    Regazzi, R.6    Mayorga, L.S.7
  • 71
    • 84868326542 scopus 로고    scopus 로고
    • Dynamin regulates specific membrane fusion events necessary for acrosomal exocytosis in mouse spermatozoa
    • Reid AT, Lord T, Stanger SJ, Roman SD, McCluskey A, Robinson PJ, Aitken RJ, Nixon B. Dynamin regulates specific membrane fusion events necessary for acrosomal exocytosis in mouse spermatozoa. J Biol Chem 2012; 287(45):37659-37672.
    • (2012) J Biol Chem , vol.287 , Issue.45 , pp. 37659-37672
    • Reid, A.T.1    Lord, T.2    Stanger, S.J.3    Roman, S.D.4    McCluskey, A.5    Robinson, P.J.6    Aitken, R.J.7    Nixon, B.8
  • 72
    • 71449086186 scopus 로고    scopus 로고
    • CaMKIIα interacts with multi-PDZ domain protein MUPP1 in spermatozoa and prevents spontaneous acrosomal exocytosis
    • Ackermann F, Zitranski N, Borth H, Buech T, Gudermann T, BoekhoffI. CaMKIIα interacts with multi-PDZ domain protein MUPP1 in spermatozoa and prevents spontaneous acrosomal exocytosis. J Cell Sci 2009; 122(24):4547-4557.
    • (2009) J Cell Sci , vol.122 , Issue.24 , pp. 4547-4557
    • Ackermann, F.1    Zitranski, N.2    Borth, H.3    Buech, T.4    Gudermann, T.5    Boekhoff, I.6
  • 74
  • 75
    • 55649088022 scopus 로고    scopus 로고
    • Capacitationdependent reorganization of microdomains in the apical sperm head plasma membrane: Functional relationship with zona binding and the zona-induced acrosome reaction
    • Boerke A, Tsai PS, Garcia-Gil N, Brewis IA, Gadella BM. Capacitationdependent reorganization of microdomains in the apical sperm head plasma membrane: Functional relationship with zona binding and the zona-induced acrosome reaction. Theriogenology 2008; 70(8):1188-1196.
    • (2008) Theriogenology , vol.70 , Issue.8 , pp. 1188-1196
    • Boerke, A.1    Tsai, P.S.2    Garcia-Gil, N.3    Brewis, I.A.4    Gadella, B.M.5
  • 76
    • 0037119363 scopus 로고    scopus 로고
    • Mouse sperm lacking cell surface hyaluronidase PH-20 can pass through the layer of cumulus cells and fertilize the egg
    • Baba D, Kashiwabara S, Honda A, Yamagata K, Wu Q, Ikawa M, Okabe M, Baba T. Mouse sperm lacking cell surface hyaluronidase PH-20 can pass through the layer of cumulus cells and fertilize the egg. J Biol Chem 2002; 277(33):30310-30314.
    • (2002) J Biol Chem , vol.277 , Issue.33 , pp. 30310-30314
    • Baba, D.1    Kashiwabara, S.2    Honda, A.3    Yamagata, K.4    Wu, Q.5    Ikawa, M.6    Okabe, M.7    Baba, T.8
  • 77
    • 0027948083 scopus 로고
    • Sperm from mice carrying a targeted mutation of the acrosin gene can penetrate the oocyte zona pellucida and effect fertilization
    • Baba T, Azuma S, Kashiwabara S, Toyoda Y. Sperm from mice carrying a targeted mutation of the acrosin gene can penetrate the oocyte zona pellucida and effect fertilization. J Biol Chem 1994; 269(50): 31845-31849.
    • (1994) J Biol Chem , vol.269 , Issue.50 , pp. 31845-31849
    • Baba, T.1    Azuma, S.2    Kashiwabara, S.3    Toyoda, Y.4
  • 78
    • 84856907447 scopus 로고    scopus 로고
    • Function of the acrosomal matrix: zona pellucida 3 receptor (ZP3R/sp56) is not essential for mouse fertilization
    • Muro Y, Buffone MG, Okabe M, Gerton GL. Function of the acrosomal matrix: zona pellucida 3 receptor (ZP3R/sp56) is not essential for mouse fertilization. Biol Reprod 2012; 86(1):1-6.
    • (2012) Biol Reprod , vol.86 , Issue.1 , pp. 1-6
    • Muro, Y.1    Buffone, M.G.2    Okabe, M.3    Gerton, G.L.4
  • 80
    • 0021815276 scopus 로고
    • Evidence for plasma membrane impermeability to small ions in acrosome-intact mouse spermatozoa bound to mouse zonae pellucidae, using an aminoacridine fluorescent pH probe: time course of the zona-induced acrosome reaction monitored by both chlortetracycline and pH probe fluorescence
    • Lee MA, Storey BT. Evidence for plasma membrane impermeability to small ions in acrosome-intact mouse spermatozoa bound to mouse zonae pellucidae, using an aminoacridine fluorescent pH probe: time course of the zona-induced acrosome reaction monitored by both chlortetracycline and pH probe fluorescence. Biol Reprod 1985; 33(1):235-246.
    • (1985) Biol Reprod , vol.33 , Issue.1 , pp. 235-246
    • Lee, M.A.1    Storey, B.T.2
  • 81
    • 0023177789 scopus 로고
    • The acrosome reaction in human sperm from men of proven fertility
    • Stock CE, Fraser LR. The acrosome reaction in human sperm from men of proven fertility. Hum Reprod 1987; 2(2):109-119.
    • (1987) Hum Reprod , vol.2 , Issue.2 , pp. 109-119
    • Stock, C.E.1    Fraser, L.R.2
  • 82
    • 0023922798 scopus 로고
    • Ultrastructural studies of the early events of the human sperm acrosome reaction as initiated by human follicular fluid
    • Yudin AI, Gottlieb W, Meizel S. Ultrastructural studies of the early events of the human sperm acrosome reaction as initiated by human follicular fluid. Gamete Res 1988; 20(1):11-24.
    • (1988) Gamete Res , vol.20 , Issue.1 , pp. 11-24
    • Yudin, A.I.1    Gottlieb, W.2    Meizel, S.3
  • 83
    • 77955288978 scopus 로고    scopus 로고
    • How pig sperm prepares to fertilize: stable acrosome docking to the plasma membrane
    • Tsai P-S, 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(6):e11204.
    • (2010) PLoS ONE , vol.5 , Issue.6
    • Tsai, P.-S.1    Garcia-Gil, N.2    van Haeften, T.3    Gadella, B.M.4
  • 84
    • 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
    • Tsai P-SJ, 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(3):e32603.
    • (2012) PLoS ONE , vol.7 , Issue.3
    • Tsai, P.-S.J.1    Brewis, I.A.2    van Maaren, J.3    Gadella, B.M.4
  • 85
    • 0035159305 scopus 로고    scopus 로고
    • Differential release of guinea pig sperm acrosomal components during exocytosis
    • Kim K-S, Foster JA, Gerton GL. Differential release of guinea pig sperm acrosomal components during exocytosis. Biol Reprod 2001; 64(1): 148-156.
    • (2001) Biol Reprod , vol.64 , Issue.1 , pp. 148-156
    • Kim, K.-S.1    Foster, J.A.2    Gerton, G.L.3
  • 86
    • 0031035977 scopus 로고    scopus 로고
    • Spermatozoa lacking acrosin protein show delayed fertilization
    • Adham IM, Nayernia K, Engel W. Spermatozoa lacking acrosin protein show delayed fertilization. Mol Reprod Dev 1997; 46(3):370-376.
    • (1997) Mol Reprod Dev , vol.46 , Issue.3 , pp. 370-376
    • Adham, I.M.1    Nayernia, K.2    Engel, W.3
  • 88
    • 0016965631 scopus 로고
    • Ionophore A23187 induces acrosome reactions in sea urchin and guinea pig spermatozoa
    • Summers RG, Talbot P, Keough EM, Hylander BL, Franklin LE. Ionophore A23187 induces acrosome reactions in sea urchin and guinea pig spermatozoa. J Exp Zool 1976; 196(3):381-385.
    • (1976) J Exp Zool , vol.196 , Issue.3 , pp. 381-385
    • Summers, R.G.1    Talbot, P.2    Keough, E.M.3    Hylander, B.L.4    Franklin, L.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.