메뉴 건너뛰기




Volumn 81, Issue 2, 2009, Pages 396-405

Acrosomal swelling and membrane docking are required for hybrid vesicle formation during the human sperm acrosome reaction

Author keywords

Acrosome reaction; Gamete biology; Membrane docking; Membrane fusion; Regulated exocytosis; Secretory granules; SNARE; Sperm

Indexed keywords

BOTULINUM TOXIN; SNARE PROTEIN; STREPTOLYSIN O; TETANUS TOXIN;

EID: 68049126532     PISSN: 00063363     EISSN: 15297268     Source Type: Journal    
DOI: 10.1095/biolreprod.109.076166     Document Type: Article
Times cited : (81)

References (54)
  • 1
    • 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; 20:11-24.
    • (1988) Gamete Res , vol.20 , pp. 11-24
    • Yudin, A.I.1    Gottlieb, W.2    Meizel, S.3
  • 3
    • 0018198579 scopus 로고
    • The induction of the acrosome reaction in guinea-pig sperm by the divalent metal cation ionophore A23187
    • Green DP. The induction of the acrosome reaction in guinea-pig sperm by the divalent metal cation ionophore A23187. J Cell Sci 1978; 32:137-151.
    • (1978) J Cell Sci , vol.32 , pp. 137-151
    • Green, D.P.1
  • 4
    • 0014857747 scopus 로고
    • The acrosomal region and the acrosome reaction in sperm of the golden hamster
    • Franklin LE, Barros C, Fussell EN. The acrosomal region and the acrosome reaction in sperm of the golden hamster. Biol Reprod 1970; 3: 180-200.
    • (1970) Biol Reprod , vol.3 , pp. 180-200
    • Franklin, L.E.1    Barros, C.2    Fussell, E.N.3
  • 5
    • 0014123988 scopus 로고
    • Membrane vesiculation as a feature of the mammalian acrosome reaction
    • Barros C, Bedford JM, Franklin LE, Austin CR. Membrane vesiculation as a feature of the mammalian acrosome reaction. J Cell Biol 1967; 34:C1-C5.
    • (1967) J Cell Biol , vol.34
    • Barros, C.1    Bedford, J.M.2    Franklin, L.E.3    Austin, C.R.4
  • 6
    • 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; 59:286-292.
    • (2007) IUBMB Life , vol.59 , pp. 286-292
    • Mayorga, L.S.1    Tomes, C.N.2    Belmonte, S.A.3
  • 7
    • 34248558655 scopus 로고    scopus 로고
    • Acrosomal exocytosis
    • Regazzi R ed, Georgetown, TX: Landes Bioscience;
    • Tomes C. Acrosomal exocytosis. In: Regazzi R (ed.), Molecular Mechanisms of Exocytosis. Georgetown, TX: Landes Bioscience; 2006: 117-147.
    • (2006) Molecular Mechanisms of Exocytosis , pp. 117-147
    • Tomes, C.1
  • 9
    • 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; 21:4121-4130.
    • (2007) FASEB J , vol.21 , pp. 4121-4130
    • Lopez, C.I.1    Belmonte, S.A.2    De Blas, G.A.3    Mayorga, L.S.4
  • 10
    • 0034730154 scopus 로고    scopus 로고
    • Calciumtriggered acrosomal exocytosis in human spermatozoa requires the coordinated activation of Rab3A and N-ethylmaleimide-sensitive factor
    • Michaut M, Tomes CN, De Blas G, Yunes R, Mayorga LS. Calciumtriggered acrosomal exocytosis in human spermatozoa requires the coordinated activation of Rab3A and N-ethylmaleimide-sensitive factor. Proc Natl Acad Sci U S A 2000; 97:9996-10001.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 9996-10001
    • Michaut, M.1    Tomes, C.N.2    De Blas, G.3    Yunes, R.4    Mayorga, L.S.5
  • 11
    • 0033168842 scopus 로고    scopus 로고
    • Identification of Rab3A GTPase as an acrosome-associated small GTP-binding protein in rat sperm
    • Iida H, Yoshinaga Y, Tanaka S, Toshimori K, Mori T. Identification of Rab3A GTPase as an acrosome-associated small GTP-binding protein in rat sperm. Dev Biol 1999; 211:144-155.
    • (1999) Dev Biol , vol.211 , pp. 144-155
    • Iida, H.1    Yoshinaga, Y.2    Tanaka, S.3    Toshimori, K.4    Mori, T.5
  • 12
    • 0032990170 scopus 로고    scopus 로고
    • The monomeric GTP binding protein, Rab3A, is associated with the acrosome in mouse sperm
    • Ward CR, Faundes D, Foster JA. The monomeric GTP binding protein, Rab3A, is associated with the acrosome in mouse sperm. Mol Reprod Dev 1999; 53:413-421.
    • (1999) Mol Reprod Dev , vol.53 , pp. 413-421
    • Ward, C.R.1    Faundes, D.2    Foster, J.A.3
  • 13
    • 53749103998 scopus 로고    scopus 로고
    • Complexin-I-deficient sperm are subfertile due to a defect in zona pellucida penetration
    • Zhao L, Reim K, Miller DJ. Complexin-I-deficient sperm are subfertile due to a defect in zona pellucida penetration. Reproduction 2008; 136: 323-334.
    • (2008) Reproduction , vol.136 , pp. 323-334
    • Zhao, L.1    Reim, K.2    Miller, D.J.3
  • 15
    • 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; 280:20197-20203.
    • (2005) J Biol Chem , vol.280 , pp. 20197-20203
    • Hutt, D.M.1    Baltz, J.M.2    Ngsee, J.K.3
  • 16
    • 0036136446 scopus 로고    scopus 로고
    • Synaptotagmin VIII is localized to the mouse sperm head and may function in acrosomal exocytosis
    • Hutt DM, Cardullo RA, Baltz JM, Ngsee JK. Synaptotagmin VIII is localized to the mouse sperm head and may function in acrosomal exocytosis. Biol Reprod 2002; 66:50-56.
    • (2002) Biol Reprod , vol.66 , pp. 50-56
    • Hutt, D.M.1    Cardullo, R.A.2    Baltz, J.M.3    Ngsee, J.K.4
  • 17
  • 18
    • 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; 3:1801-1812.
    • (2005) PLoS Biol , vol.3 , pp. 1801-1812
    • De Blas, G.A.1    Roggero, C.M.2    Tomes, C.N.3    Mayorga, L.S.4
  • 21
    • 49749084725 scopus 로고    scopus 로고
    • Vesicle docking in regulated exocytosis
    • Verhage M, Sorensen JB. Vesicle docking in regulated exocytosis. Traffic 2008; 9:1414-1424.
    • (2008) Traffic , vol.9 , pp. 1414-1424
    • Verhage, M.1    Sorensen, J.B.2
  • 22
    • 0034106739 scopus 로고    scopus 로고
    • Rab3A triggers the acrosome reaction in permeabilized human spermatozoa
    • Yunes R, Michaut M, Tomes C, Mayorga LS. Rab3A triggers the acrosome reaction in permeabilized human spermatozoa. Biol Reprod 2000; 62:1084-1089.
    • (2000) Biol Reprod , vol.62 , pp. 1084-1089
    • Yunes, R.1    Michaut, M.2    Tomes, C.3    Mayorga, L.S.4
  • 23
    • 0015620349 scopus 로고
    • A technique for ultracryotomy of cell suspensions and tissues
    • Tokuyasu KT. A technique for ultracryotomy of cell suspensions and tissues. J Cell Biol 1973; 57:551-565.
    • (1973) J Cell Biol , vol.57 , pp. 551-565
    • Tokuyasu, K.T.1
  • 24
    • 0035281595 scopus 로고    scopus 로고
    • 2+ channels in liver cells, and acts through a mechanism which does not involve inositol trisphosphate receptors
    • 2+ channels in liver cells, and acts through a mechanism which does not involve inositol trisphosphate receptors. Biochem J 2001; 354:285-290.
    • (2001) Biochem J , vol.354 , pp. 285-290
    • Gregory, R.B.1    Rychkov, G.2    Barritt, G.J.3
  • 25
    • 0024359965 scopus 로고
    • Activation of phospholipase D by the fucose-sulfate glycoconjugate that induces an acrosome reaction in spermatozoa
    • Domino SE, Bocckino SB, Garbers DL. Activation of phospholipase D by the fucose-sulfate glycoconjugate that induces an acrosome reaction in spermatozoa. J Biol Chem 1989; 264:9412-9419.
    • (1989) J Biol Chem , vol.264 , pp. 9412-9419
    • Domino, S.E.1    Bocckino, S.B.2    Garbers, D.L.3
  • 26
    • 0024605263 scopus 로고
    • 2+/ionophore-induced acrosome reaction of mammalian spermatozoa
    • 2+/ionophore-induced acrosome reaction of mammalian spermatozoa. Biochem J 1989; 259:397-406.
    • (1989) Biochem J , vol.259 , pp. 397-406
    • Roldan, E.R.1    Harrison, R.A.2
  • 28
    • 3042546955 scopus 로고    scopus 로고
    • Phospholipase D1 regulates secretagogue-stimulated insulin release in pancreatic betacells
    • Hughes WE, Elgundi Z, Huang P, Frohman MA, Biden TJ. Phospholipase D1 regulates secretagogue-stimulated insulin release in pancreatic betacells. J Biol Chem 2004; 279:27534-27541.
    • (2004) J Biol Chem , vol.279 , pp. 27534-27541
    • Hughes, W.E.1    Elgundi, Z.2    Huang, P.3    Frohman, M.A.4    Biden, T.J.5
  • 30
    • 25844453368 scopus 로고    scopus 로고
    • Protein kinase C-mediated phosphorylation of the two polybasic regions of synaptotagmin VI regulates their function in acrosomal exocytosis
    • Roggero CM, Tomes CN, De Blas GA, Castillo J, Michaut MA, Fukuda M, Mayorga LS. Protein kinase C-mediated phosphorylation of the two polybasic regions of synaptotagmin VI regulates their function in acrosomal exocytosis. Dev Biol 2005; 285:422-435.
    • (2005) Dev Biol , vol.285 , pp. 422-435
    • Roggero, C.M.1    Tomes, C.N.2    De Blas, G.A.3    Castillo, J.4    Michaut, M.A.5    Fukuda, M.6    Mayorga, L.S.7
  • 31
    • 0018399384 scopus 로고
    • Morphologic characteristics of the chemically induced acrosome reaction in human spermatozoa
    • Russell L, Peterson RN, Freund M. Morphologic characteristics of the chemically induced acrosome reaction in human spermatozoa. Fertil Steril 1979; 32:87-92.
    • (1979) Fertil Steril , vol.32 , pp. 87-92
    • Russell, L.1    Peterson, R.N.2    Freund, M.3
  • 35
    • 0028800686 scopus 로고
    • Granule swelling in stimulated bovine adrenal chromaffin cells: Regulation by internal granule pH
    • Ornberg RL, Furuya S, Goping G, Kuijpers GA. Granule swelling in stimulated bovine adrenal chromaffin cells: regulation by internal granule pH. Cell Tissue Res 1995; 279:85-92.
    • (1995) Cell Tissue Res , vol.279 , pp. 85-92
    • Ornberg, R.L.1    Furuya, S.2    Goping, G.3    Kuijpers, G.A.4
  • 36
    • 0005521375 scopus 로고
    • Simultaneous electrical and optical measurements show that membrane fusion precedes secretory granule swelling during exocytosis of beige mouse mast cells
    • Zimmerberg J, Curran M, Cohen FS, Brodwick M. Simultaneous electrical and optical measurements show that membrane fusion precedes secretory granule swelling during exocytosis of beige mouse mast cells. Proc Natl Acad Sci U S A 1987; 84:1585-1589.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 1585-1589
    • Zimmerberg, J.1    Curran, M.2    Cohen, F.S.3    Brodwick, M.4
  • 37
    • 18344403104 scopus 로고
    • Granule swelling and membrane fusion in exocytosis
    • Green DP. Granule swelling and membrane fusion in exocytosis. J Cell Sci 1987; 88:547-549.
    • (1987) J Cell Sci , vol.88 , pp. 547-549
    • Green, D.P.1
  • 38
    • 0018074153 scopus 로고
    • The nature and occurrence of the acrosome reaction in spermatozoa of the domestic pig, Sus scrofa
    • Szollosi D, Hunter RH. The nature and occurrence of the acrosome reaction in spermatozoa of the domestic pig, Sus scrofa. J Anat 1978; 127: 33-41.
    • (1978) J Anat , vol.127 , pp. 33-41
    • Szollosi, D.1    Hunter, R.H.2
  • 40
    • 0024085388 scopus 로고
    • The acrosome reaction in spermatozoa of the grey-headed flying fox (Pteropus poliocephalus: Chiroptera) exposes barbed subacrosomal material
    • Cummins JM, Robson SK, Rouse GW. The acrosome reaction in spermatozoa of the grey-headed flying fox (Pteropus poliocephalus: Chiroptera) exposes barbed subacrosomal material. Gamete Res 1988; 21: 11-22.
    • (1988) Gamete Res , vol.21 , pp. 11-22
    • Cummins, J.M.1    Robson, S.K.2    Rouse, G.W.3
  • 41
    • 0026027313 scopus 로고
    • Stability of the acrosome of the brush-tailed possum (Trichosurus vulpecula) and tammar wallaby (Macropus eugenii) in vitro and after exposure to conditions and agents known to cause capacitation or acrosome reaction of eutherian spermatozoa
    • Mate KE, Rodger JC. Stability of the acrosome of the brush-tailed possum (Trichosurus vulpecula) and tammar wallaby (Macropus eugenii) in vitro and after exposure to conditions and agents known to cause capacitation or acrosome reaction of eutherian spermatozoa. J Reprod Fertil 1991; 91:41-48.
    • (1991) J Reprod Fertil , vol.91 , pp. 41-48
    • Mate, K.E.1    Rodger, J.C.2
  • 42
    • 84907037229 scopus 로고
    • Induction of acrosomal reaction in sperm with ionophore A23187 and calcium
    • Jamil K, White IG. Induction of acrosomal reaction in sperm with ionophore A23187 and calcium. Arch Androl 1981; 7:283-292.
    • (1981) Arch Androl , vol.7 , pp. 283-292
    • Jamil, K.1    White, I.G.2
  • 43
    • 0015608175 scopus 로고
    • Changes occurring in the head of boar spermatozoa: Vesiculation or vacuolation of the acrosome?
    • Jones RC. Changes occurring in the head of boar spermatozoa: vesiculation or vacuolation of the acrosome? J Reprod Fertil 1973; 33: 113-118.
    • (1973) J Reprod Fertil , vol.33 , pp. 113-118
    • Jones, R.C.1
  • 46
    • 0032506543 scopus 로고    scopus 로고
    • Defining the functions of trans-SNARE pairs
    • Ungermann C, Sato K, Wickner W. Defining the functions of trans-SNARE pairs. Nature 1998; 396:543-548.
    • (1998) Nature , vol.396 , pp. 543-548
    • Ungermann, C.1    Sato, K.2    Wickner, W.3
  • 53
    • 34547652970 scopus 로고    scopus 로고
    • Rab3a deletion reduces vesicle docking and transmitter release at the mouse diaphragm synapse
    • Coleman WL, Bill CA, Bykhovskaia M. Rab3a deletion reduces vesicle docking and transmitter release at the mouse diaphragm synapse. Neuroscience 2007; 148:1-6.
    • (2007) Neuroscience , vol.148 , pp. 1-6
    • Coleman, W.L.1    Bill, C.A.2    Bykhovskaia, M.3
  • 54
    • 0036180245 scopus 로고    scopus 로고
    • Vacuole fusion at a ring of vertex docking sites leaves membrane fragments within the organelle
    • Wang L, Seeley ES, Wickner W, Merz AJ. Vacuole fusion at a ring of vertex docking sites leaves membrane fragments within the organelle. Cell 2002; 108:357-369.
    • (2002) Cell , vol.108 , pp. 357-369
    • Wang, L.1    Seeley, E.S.2    Wickner, W.3    Merz, A.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.