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Volumn 78, Issue 12, 2011, Pages 930-941

Transitional states of acrosomal exocytosis and proteolytic processing of the acrosomal matrix in guinea pig sperm

Author keywords

Acrosin; Acrosomal exocytosis; Acrosomal matrix; Acrosome

Indexed keywords

ACROSIN; ACROSOMAL MATRIX 50 PROTEIN; ACROSOMAL MATRIX 67 PROTEIN; IONOPHORE; PROTEIN; UNCLASSIFIED DRUG;

EID: 81355127552     PISSN: 1040452X     EISSN: 10982795     Source Type: Journal    
DOI: 10.1002/mrd.21387     Document Type: Article
Times cited : (25)

References (46)
  • 1
    • 0024574187 scopus 로고
    • Guinea pig testicular proacrosin-acrosin system: Further characterization of the active enzyme
    • Adekunle AO, Storey BT, Teuscher C. 1989. Guinea pig testicular proacrosin-acrosin system: Further characterization of the active enzyme. Biol Reprod 40: 127-134.
    • (1989) Biol Reprod , vol.40 , pp. 127-134
    • Adekunle, A.O.1    Storey, B.T.2    Teuscher, C.3
  • 2
    • 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. 1994a. Sperm from mice carrying a targeted mutation of the acrosin gene can penetrate the oocyte zona pellucida and effect fertilization. J Biol Chem 269: 31845-31849.
    • (1994) J Biol Chem , vol.269 , pp. 31845-31849
    • Baba, T.1    Azuma, S.2    Kashiwabara, S.3    Toyoda, Y.4
  • 3
    • 0028229673 scopus 로고
    • An acrosomal protein, sp32, in mammalian sperm is a binding protein specific for two proacrosins and an acrosin intermediate
    • Baba T, Niida Y, Michikawa Y, Kashiwabara S, Kodaira K, Takenaka M, Kohno N, Gerton GL, Arai Y. 1994b. An acrosomal protein, sp32, in mammalian sperm is a binding protein specific for two proacrosins and an acrosin intermediate. J Biol Chem 269: 10133-10140.
    • (1994) J Biol Chem , vol.269 , pp. 10133-10140
    • Baba, T.1    Niida, Y.2    Michikawa, Y.3    Kashiwabara, S.4    Kodaira, K.5    Takenaka, M.6    Kohno, N.7    Gerton, G.L.8    Arai, Y.9
  • 4
    • 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. 2007. Sperm binding to the zona pellucida is not sufficient to induce acrosome exocytosis. Development 134: 933-943.
    • (2007) Development , vol.134 , pp. 933-943
    • Baibakov, B.1    Gauthier, L.2    Talbot, P.3    Rankin, T.L.4    Dean, J.5
  • 5
    • 0016192979 scopus 로고
    • Capacitation of mammalian spermatozoa
    • Coutinho EM, Fuchs F, editors. New York: Plenum Press
    • Barros C. 1974. Capacitation of mammalian spermatozoa. In: Coutinho EM, Fuchs F, editors. Physiology and genetics of reproduction. New York: Plenum Press. p 3-24.
    • (1974) Physiology and genetics of reproduction , pp. 3-24
    • Barros, C.1
  • 6
    • 0142231558 scopus 로고    scopus 로고
    • Processing, localization and binding activity of zonadhesin suggest a function in sperm adhesion to the zona pellucida during exocytosis of the acrosome
    • Bi M, Hickox JR, Winfrey VP, Olson GE, Hardy DM. 2003. Processing, localization and binding activity of zonadhesin suggest a function in sperm adhesion to the zona pellucida during exocytosis of the acrosome. Biochem J 375: 477.
    • (2003) Biochem J , vol.375 , pp. 477
    • Bi, M.1    Hickox, J.R.2    Winfrey, V.P.3    Olson, G.E.4    Hardy, D.M.5
  • 7
    • 54249097511 scopus 로고    scopus 로고
    • The role of the acrosomal matrix in fertilization
    • Buffone MG, Foster JA, Gerton GL. 2008a. The role of the acrosomal matrix in fertilization. Int J Dev Biol 52: 511-522.
    • (2008) Int J Dev Biol , vol.52 , pp. 511-522
    • Buffone, M.G.1    Foster, J.A.2    Gerton, G.L.3
  • 8
    • 45549097542 scopus 로고    scopus 로고
    • Recombinant mouse sperm ZP3-binding protein (ZP3R/sp56) forms a high order oligomer that binds eggs and inhibits mouse fertilization in vitro
    • Buffone MG, Zhuang T, Ord TS, Hui L, Moss SB, Gerton GL. 2008b. Recombinant mouse sperm ZP3-binding protein (ZP3R/sp56) forms a high order oligomer that binds eggs and inhibits mouse fertilization in vitro. J Biol Chem 283: 12438-12445.
    • (2008) J Biol Chem , vol.283 , pp. 12438-12445
    • Buffone, M.G.1    Zhuang, T.2    Ord, T.S.3    Hui, L.4    Moss, S.B.5    Gerton, G.L.6
  • 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. 2009. Functional consequences of cleavage, dissociation and exocytotic release of ZP3R, a C4BP-related protein, from the mouse sperm acrosomal matrix. J Cell Sci 122: 3153-3160.
    • (2009) J Cell Sci , vol.122 , pp. 3153-3160
    • Buffone, M.G.1    Kim, K.-S.2    Doak, B.J.3    Rodriguez-Miranda, E.4    Gerton, G.L.5
  • 10
    • 0028227343 scopus 로고
    • Sperm-egg recognition in the mouse: Characterization of sp56, a sperm protein having specific affinity for ZP3
    • Cheng A, Le T, Palacios M, Bookbinder LH, Wassarman PM, Suzuki F, Bleil JD. 1994. Sperm-egg recognition in the mouse: Characterization of sp56, a sperm protein having specific affinity for ZP3. J Cell Biol 125: 867-878.
    • (1994) J Cell Biol , vol.125 , pp. 867-878
    • Cheng, A.1    Le, T.2    Palacios, M.3    Bookbinder, L.H.4    Wassarman, P.M.5    Suzuki, F.6    Bleil, J.D.7
  • 11
    • 39049187602 scopus 로고    scopus 로고
    • Dense-core granules in neuroendocrine cells and neurons release their secretory constituents by piecemeal degranulation (review)
    • Crivellato E, Nico B, Bertelli E, Nussdorfer GG, Ribatti D. 2006. Dense-core granules in neuroendocrine cells and neurons release their secretory constituents by piecemeal degranulation (review). Int J Mol Med 18: 1037-1046.
    • (2006) Int J Mol Med , vol.18 , pp. 1037-1046
    • Crivellato, E.1    Nico, B.2    Bertelli, E.3    Nussdorfer, G.G.4    Ribatti, D.5
  • 12
    • 0023908166 scopus 로고
    • Membrane domains in guinea pig sperm and their role in the membrane fusion events of the acrosome reaction
    • Flaherty SP, Olson GE. 1988. Membrane domains in guinea pig sperm and their role in the membrane fusion events of the acrosome reaction. Anat Rec 220: 267-280.
    • (1988) Anat Rec , vol.220 , pp. 267-280
    • Flaherty, S.P.1    Olson, G.E.2
  • 13
    • 0026090087 scopus 로고
    • Ultrastructural analysis of the acrosome reaction in a population of single guinea pig sperm
    • Flaherty SP, Olson GE. 1991. Ultrastructural analysis of the acrosome reaction in a population of single guinea pig sperm. Anat Rec 229: 186-194.
    • (1991) Anat Rec , vol.229 , pp. 186-194
    • Flaherty, S.P.1    Olson, G.E.2
  • 14
    • 0027415872 scopus 로고
    • Proteases are not involved in the membrane fusion events of the lysolecithin-mediated guinea pig sperm acrosome reaction
    • Flaherty SP, Swann NJ. 1993. Proteases are not involved in the membrane fusion events of the lysolecithin-mediated guinea pig sperm acrosome reaction. J Cell Sci 104: 163-172.
    • (1993) J Cell Sci , vol.104 , pp. 163-172
    • Flaherty, S.P.1    Swann, N.J.2
  • 15
    • 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. 1997. 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 272: 12714-12722.
    • (1997) J Biol Chem , vol.272 , 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
  • 16
    • 0019983914 scopus 로고
    • p-Aminobenzamidine, an acrosin inhibitor, inhibits mouse sperm penetration of the zona pellucida but not the acrosome reaction
    • Fraser LR. 1982. p-Aminobenzamidine, an acrosin inhibitor, inhibits mouse sperm penetration of the zona pellucida but not the acrosome reaction. J Reprod Fertil 65: 185-194.
    • (1982) J Reprod Fertil , vol.65 , pp. 185-194
    • Fraser, L.R.1
  • 17
    • 77954600245 scopus 로고    scopus 로고
    • Gamete recognition in mice depends on the cleavage status of an egg's zona pellucida protein
    • Gahlay G, Gauthier L, Baibakov B, Epifano O, Dean J. 2010. Gamete recognition in mice depends on the cleavage status of an egg's zona pellucida protein. Science 329: 216-219.
    • (2010) Science , vol.329 , pp. 216-219
    • Gahlay, G.1    Gauthier, L.2    Baibakov, B.3    Epifano, O.4    Dean, J.5
  • 18
    • 0001953357 scopus 로고    scopus 로고
    • Function of the sperm acrosome
    • Hardy DM, editor. San Diego, CA: Academic Press
    • Gerton GL. 2002. Function of the sperm acrosome. In: Hardy DM, editor. Fertilization. San Diego, CA: Academic Press. p 265-302.
    • (2002) Fertilization , pp. 265-302
    • Gerton, G.L.1
  • 20
    • 0018198580 scopus 로고
    • The activation of proteolysis in the acrosome reaction of guinea-pig sperm
    • Green DP. 1978. The activation of proteolysis in the acrosome reaction of guinea-pig sperm. J Cell Sci 32: 153-164.
    • (1978) J Cell Sci , vol.32 , pp. 153-164
    • Green, D.P.1
  • 21
    • 0020004950 scopus 로고
    • The course of the acrosome reaction in guinea-pig sperm
    • Green DP. 1982. The course of the acrosome reaction in guinea-pig sperm. J Cell Sci 54: 161-171.
    • (1982) J Cell Sci , vol.54 , pp. 161-171
    • Green, D.P.1
  • 22
    • 0021235172 scopus 로고
    • Mechanical hypothesis of sperm penetration
    • Green DP, Purves RD. 1984. Mechanical hypothesis of sperm penetration. Biophys J 45: 659-662.
    • (1984) Biophys J , vol.45 , pp. 659-662
    • Green, D.P.1    Purves, R.D.2
  • 23
    • 0025791006 scopus 로고
    • A mechanism for differential release of acrosomal enzymes during the acrosome reaction
    • Hardy DM, Oda MN, Friend DS, Huang TT. 1991. A mechanism for differential release of acrosomal enzymes during the acrosome reaction. Biochem J 275: 759-766.
    • (1991) Biochem J , vol.275 , pp. 759-766
    • Hardy, D.M.1    Oda, M.N.2    Friend, D.S.3    Huang, T.T.4
  • 24
    • 81355165389 scopus 로고    scopus 로고
    • Video imaging of the sperm acrosome reaction during in vitro fertilization
    • Hirohashi N, Gerton GL, Buffone MG. 2011. Video imaging of the sperm acrosome reaction during in vitro fertilization. Comm Integr Biol 4: 471-476.
    • (2011) Comm Integr Biol , vol.4 , pp. 471-476
    • Hirohashi, N.1    Gerton, G.L.2    Buffone, M.G.3
  • 25
    • 0021918912 scopus 로고
    • pH and protease control of acrosomal content stasis and release during the guinea pig sperm acrosome reaction
    • Huang TTF, Hardy D, Yanagimachi H, Teuscher C, Tung K, Wild G, Yanagimachi R. 1985. pH and protease control of acrosomal content stasis and release during the guinea pig sperm acrosome reaction. Biol Reprod 32: 451-462.
    • (1985) Biol Reprod , vol.32 , pp. 451-462
    • Huang, T.T.F.1    Hardy, D.2    Yanagimachi, H.3    Teuscher, C.4    Tung, K.5    Wild, G.6    Yanagimachi, R.7
  • 26
    • 0023819893 scopus 로고
    • Characterization of isolated acrosomal matrices from hamster spermatozoa
    • Hyatt H, Gwatkin RB. 1988. Characterization of isolated acrosomal matrices from hamster spermatozoa. J Reprod Fertil 83: 419-429.
    • (1988) J Reprod Fertil , vol.83 , pp. 419-429
    • Hyatt, H.1    Gwatkin, R.B.2
  • 27
    • 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. 2011. Most fertilizing mouse spermatozoa begin their acrosome reaction before contact with the zona pellucida during in vitro fertilization. Proc Natl Acad Sci 108: 4892-4896.
    • (2011) Proc Natl Acad Sci , 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
  • 28
    • 0023483241 scopus 로고
    • Identification of a zona-binding protein from boar spermatozoa as proacrosin
    • Jones R, Brown CR. 1987. Identification of a zona-binding protein from boar spermatozoa as proacrosin. Exp Cell Res 171: 503-508.
    • (1987) Exp Cell Res , vol.171 , pp. 503-508
    • Jones, R.1    Brown, C.R.2
  • 29
    • 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. 2003. Differential release of soluble and matrix components: Evidence for intermediate states of secretion during spontaneous acrosomal exocytosis in mouse sperm. Dev Biol 264: 141-152.
    • (2003) Dev Biol , vol.264 , pp. 141-152
    • Kim, K.-S.1    Gerton, G.L.2
  • 30
    • 0035168574 scopus 로고    scopus 로고
    • Mouse sperm protein sp56 is a component of the acrosomal matrix
    • Kim KS, Cha MC, Gerton GL. 2001a. Mouse sperm protein sp56 is a component of the acrosomal matrix. Biol Reprod 64: 36-43.
    • (2001) Biol Reprod , vol.64 , pp. 36-43
    • Kim, K.S.1    Cha, M.C.2    Gerton, G.L.3
  • 31
    • 0035159305 scopus 로고    scopus 로고
    • Differential release of guinea pig sperm acrosomal components during exocytosis
    • Kim K-S, Foster JA, Gerton GL. 2001b. Differential release of guinea pig sperm acrosomal components during exocytosis. Biol Reprod 64: 148-156.
    • (2001) Biol Reprod , vol.64 , pp. 148-156
    • Kim, K.-S.1    Foster, J.A.2    Gerton, G.L.3
  • 32
    • 0030728461 scopus 로고    scopus 로고
    • Sperm from beta 1,4-galactosyltransferase-null mice are refractory to ZP3-induced acrosome reactions and penetrate the zona pellucida poorly
    • Lu Q, Shur BD. 1997. Sperm from beta 1, 4-galactosyltransferase-null mice are refractory to ZP3-induced acrosome reactions and penetrate the zona pellucida poorly. Development 124: 4121-4131.
    • (1997) Development , vol.124 , pp. 4121-4131
    • Lu, Q.1    Shur, B.D.2
  • 33
    • 0027427324 scopus 로고
    • Purification and characterization of a 38-kDa protein, sp38, with zona pellucida-binding property from porcine epididymal sperm
    • Mori E, Baba T, Iwamatsu A, Mori T. 1993. Purification and characterization of a 38-kDa protein, sp38, with zona pellucida-binding property from porcine epididymal sperm. Biochem Biophys Res Commun 196: 196-202.
    • (1993) Biochem Biophys Res Commun , vol.196 , pp. 196-202
    • Mori, E.1    Baba, T.2    Iwamatsu, A.3    Mori, T.4
  • 35
    • 0023176969 scopus 로고
    • Binding of both acrosome-intact and acrosome-reacted guinea pig sperm to the zona pellucida during in vitro fertilization
    • Myles DG, Hyatt H, Primakoff P. 1987. Binding of both acrosome-intact and acrosome-reacted guinea pig sperm to the zona pellucida during in vitro fertilization. Dev Biol 121: 559-567.
    • (1987) Dev Biol , vol.121 , pp. 559-567
    • Myles, D.G.1    Hyatt, H.2    Primakoff, P.3
  • 36
    • 0024659879 scopus 로고
    • Calcium-induced modification of the acrosomal matrix in digitonin-permeabilized guinea pig spermatozoa
    • Noland TD, Olson GE. 1989. Calcium-induced modification of the acrosomal matrix in digitonin-permeabilized guinea pig spermatozoa. Biol Reprod 40: 1057-1066.
    • (1989) Biol Reprod , vol.40 , pp. 1057-1066
    • Noland, T.D.1    Olson, G.E.2
  • 37
    • 0028569728 scopus 로고
    • The sperm acrosomal matrix contains a novel member of the pentaxin family of calcium-dependent binding proteins
    • Noland TD, Friday BB, Maulit MT, Gerton GL. 1994. The sperm acrosomal matrix contains a novel member of the pentaxin family of calcium-dependent binding proteins. J Biol Chem 269: 32607-32614.
    • (1994) J Biol Chem , vol.269 , pp. 32607-32614
    • Noland, T.D.1    Friday, B.B.2    Maulit, M.T.3    Gerton, G.L.4
  • 39
    • 4544371385 scopus 로고    scopus 로고
    • Zonadhesin assembly into the hamster sperm acrosomal matrix occurs by distinct targeting strategies during spermiogenesis and maturation in the epididymis
    • Olson GE, Winfrey VP, Bi M, Hardy DM, NagDas SK. 2004. Zonadhesin assembly into the hamster sperm acrosomal matrix occurs by distinct targeting strategies during spermiogenesis and maturation in the epididymis. Biol Reprod 71: 1128-1134.
    • (2004) Biol Reprod , vol.71 , pp. 1128-1134
    • Olson, G.E.1    Winfrey, V.P.2    Bi, M.3    Hardy, D.M.4    NagDas, S.K.5
  • 40
    • 0020336509 scopus 로고
    • Effect of trypsin inhibitors on acrosome reaction of guinea pig spermatozoa
    • Perreault SD, Zirkin BR, Rogers BJ. 1982. Effect of trypsin inhibitors on acrosome reaction of guinea pig spermatozoa. Biol Reprod 26: 343-351.
    • (1982) Biol Reprod , vol.26 , pp. 343-351
    • Perreault, S.D.1    Zirkin, B.R.2    Rogers, B.J.3
  • 41
    • 0028569729 scopus 로고
    • Apexin, an acrosomal pentaxin
    • Reid MS, Blobel CP. 1994. Apexin, an acrosomal pentaxin. J Biol Chem 269: 32615-32620.
    • (1994) J Biol Chem , vol.269 , pp. 32615-32620
    • Reid, M.S.1    Blobel, C.P.2
  • 42
    • 0016796862 scopus 로고
    • Cleavage specificity of boar acrosin on polypeptide substrates, ribonuclease and insulin B-chain
    • Schiessler H, Schleuning WD, Fritz H. 1975. Cleavage specificity of boar acrosin on polypeptide substrates, ribonuclease and insulin B-chain. Hoppe Seyler's Z Physiol Chem 356: 1931-1936.
    • (1975) Hoppe Seyler's Z Physiol Chem , vol.356 , pp. 1931-1936
    • Schiessler, H.1    Schleuning, W.D.2    Fritz, H.3
  • 43
    • 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. 1994. 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 51: 1-13.
    • (1994) Biol Reprod , vol.51 , pp. 1-13
    • Westbrook-Case, V.A.1    Winfrey, V.P.2    Olson, G.E.3
  • 44
    • 0020791670 scopus 로고
    • Correlation of increased intraacrosomal pH with the hamster sperm acrosome reaction
    • Working PK, Meizel S. 1983. Correlation of increased intraacrosomal pH with the hamster sperm acrosome reaction. J Exp Zool 227: 97-107.
    • (1983) J Exp Zool , vol.227 , pp. 97-107
    • Working, P.K.1    Meizel, S.2
  • 46
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • Knobil E, Neill JD, editors. New York: Raven Press.
    • Yanagimachi R. 1994. Mammalian fertilization. In: Knobil E, Neill JD, editors. The physiology of reproduction, 3e. New York: Raven Press.
    • (1994) The physiology of reproduction, 3e
    • Yanagimachi, R.1


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