메뉴 건너뛰기




Volumn 81, Issue 5, 2009, Pages 889-897

Equatorin: Identification and characterization of the epitope of the MN9 antibody in the mouse

Author keywords

Fertilization; Gamete biology; Gamete interaction; MN9 equatorin; Sperm

Indexed keywords

ACROSIN; EPITOPE; GLYCOPROTEIN; MEMBRANE PROTEIN; N,O SIALOGLYCOPROTEIN; PROTEIN EQUATORIN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; ANTIGEN; MESSENGER RNA;

EID: 73349142368     PISSN: 00063363     EISSN: 15297268     Source Type: Journal    
DOI: 10.1095/biolreprod.109.077438     Document Type: Article
Times cited : (30)

References (46)
  • 1
    • 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: 234-238.
    • (2005) Nature , vol.434 , pp. 234-238
    • Inoue, N.1    Ikawa, M.2    Isotani, A.3    Okabe, M.4
  • 5
    • 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; 279:34957-34962.
    • (2004) J Biol Chem , vol.279 , pp. 34957-34962
    • Nishimura, H.1    Kim, E.2    Nakanishi, T.3    Baba, T.4
  • 7
    • 0035337709 scopus 로고    scopus 로고
    • Analysis of loss of adhesive function in sperm lacking cyritestin or fertilin beta
    • Nishimura H, Cho C, Branciforte DR, Myles DG, Primakoff P. Analysis of loss of adhesive function in sperm lacking cyritestin or fertilin beta. Dev Biol 2001; 233:204-213.
    • (2001) Dev Biol , vol.233 , pp. 204-213
    • Nishimura, H.1    Cho, C.2    Branciforte, D.R.3    Myles, D.G.4    Primakoff, P.5
  • 11
    • 0031777110 scopus 로고    scopus 로고
    • An MN9 antigenic molecule, equatorin, is required for successful sperm-oocyte fusion in mice
    • Toshimori K, Saxena DK, Tanii I, Yoshinaga K. An MN9 antigenic molecule, equatorin, is required for successful sperm-oocyte fusion in mice. Biol Reprod 1998; 59:22-29.
    • (1998) Biol Reprod , vol.59 , pp. 22-29
    • Toshimori, K.1    Saxena, D.K.2    Tanii, I.3    Yoshinaga, K.4
  • 12
    • 0034769291 scopus 로고    scopus 로고
    • Inhibition of mouse fertilization in vivo by intra-oviductal injection of an anti-equatorin monoclonal antibody
    • Yoshinaga K, Saxena DK, Oh-oka T, Tanü I, Toshimori K. Inhibition of mouse fertilization in vivo by intra-oviductal injection of an anti-equatorin monoclonal antibody. Reproduction 2001; 122:649-655.
    • (2001) Reproduction , vol.122 , pp. 649-655
    • Yoshinaga, K.1    Saxena, D.K.2    Oh-oka, T.3    Tanü, I.4    Toshimori, K.5
  • 14
    • 43449097896 scopus 로고    scopus 로고
    • Equatorial segment protein (ESP) is a human alloantigen involved in sperm-egg binding and fusion
    • Wolkowicz MJ, Digilio L, Klotz K, Shetty J, Flickinger CJ, Herr JC. Equatorial segment protein (ESP) is a human alloantigen involved in sperm-egg binding and fusion. J Androl 2008; 29:272-282.
    • (2008) J Androl , vol.29 , pp. 272-282
    • Wolkowicz, M.J.1    Digilio, L.2    Klotz, K.3    Shetty, J.4    Flickinger, C.J.5    Herr, J.C.6
  • 17
    • 23244434065 scopus 로고    scopus 로고
    • Mouse SLLP1, a sperm lysozyme-like protein involved in sperm-egg binding and fertilization
    • Herrero MB, Mandal A, Digilio LC, Coonrod SA, Maier B, Herr JC. Mouse SLLP1, a sperm lysozyme-like protein involved in sperm-egg binding and fertilization. Dev Biol 2005; 284:126-142.
    • (2005) Dev Biol , vol.284 , pp. 126-142
    • Herrero, M.B.1    Mandal, A.2    Digilio, L.C.3    Coonrod, S.A.4    Maier, B.5    Herr, J.C.6
  • 18
    • 43249115593 scopus 로고    scopus 로고
    • The role of proteomics in understanding sperm cell biology
    • Aitken RJ, Baker MA. The role of proteomics in understanding sperm cell biology. Int J Androl 2008; 31:295-302.
    • (2008) Int J Androl , vol.31 , pp. 295-302
    • Aitken, R.J.1    Baker, M.A.2
  • 20
    • 0031829606 scopus 로고    scopus 로고
    • Maturation of mammalian spermatozoa: Modifications of the acrosome and plasma membrane leading to fertilization
    • Toshimori K. Maturation of mammalian spermatozoa: modifications of the acrosome and plasma membrane leading to fertilization. Cell Tissue Res 1998; 293:177-187.
    • (1998) Cell Tissue Res , vol.293 , pp. 177-187
    • Toshimori, K.1
  • 23
    • 0034761261 scopus 로고    scopus 로고
    • Exposure of sperm head equatorin after acrosome reaction and its fate after fertilization in mice
    • Manandhar G, Toshimori K. Exposure of sperm head equatorin after acrosome reaction and its fate after fertilization in mice. Biol Reprod 2001; 65:1425-1436.
    • (2001) Biol Reprod , vol.65 , pp. 1425-1436
    • Manandhar, G.1    Toshimori, K.2
  • 24
    • 0026458684 scopus 로고
    • Characterization of the antigen recognized by a monoclonal antibody MN9: Unique transport pathway to the equatorial segment of sperm head during spermiogenesis
    • Toshimori K, Tanii I, Araki S, Oura C. Characterization of the antigen recognized by a monoclonal antibody MN9: unique transport pathway to the equatorial segment of sperm head during spermiogenesis. Cell Tissue Res 1992; 270:459-468.
    • (1992) Cell Tissue Res , vol.270 , pp. 459-468
    • Toshimori, K.1    Tanii, I.2    Araki, S.3    Oura, C.4
  • 25
    • 0018396021 scopus 로고
    • Significance of the equatorial segment of the acrosome of the spermatozoon in eutherian mammals
    • Bedford JM, Moore HD, Franklin LE. Significance of the equatorial segment of the acrosome of the spermatozoon in eutherian mammals. Exp Cell Res 1979; 119:119-126.
    • (1979) Exp Cell Res , vol.119 , pp. 119-126
    • Bedford, J.M.1    Moore, H.D.2    Franklin, L.E.3
  • 26
    • 0025167186 scopus 로고
    • Ultrastructural studies on the fertilization of mammahan gametes
    • Oura C, Toshimori K. Ultrastructural studies on the fertilization of mammahan gametes. Int Rev Cytol 1990; 122:105-151.
    • (1990) Int Rev Cytol , vol.122 , pp. 105-151
    • Oura, C.1    Toshimori, K.2
  • 27
    • 0019951830 scopus 로고
    • Penetration of the mouse sperm head through the zona pellucida in vivo: An electron-microscope study at 200 KV
    • Toshimori K. Penetration of the mouse sperm head through the zona pellucida in vivo: an electron-microscope study at 200 KV. Biol Reprod 1982; 26:475-481.
    • (1982) Biol Reprod , vol.26 , pp. 475-481
    • Toshimori, K.1
  • 28
    • 0014804212 scopus 로고
    • Physiological changes in the postnuclear cap region of mammahan spermatozoa: A necessary preliminary to the membrane fusion between sperm and egg cells
    • Yanagimachi R, Noda YD. Physiological changes in the postnuclear cap region of mammahan spermatozoa: a necessary preliminary to the membrane fusion between sperm and egg cells. J Ultrastruct Res 1970; 31:486-493.
    • (1970) J Ultrastruct Res , vol.31 , pp. 486-493
    • Yanagimachi, R.1    Noda, Y.D.2
  • 29
    • 0024795060 scopus 로고
    • Inhibition of mucin glycosylation by aryl-N-acetyl-alpha-galactosaminides in human colon cancer cells
    • Kuan SF, Byrd JC, Basbaum C, Kim YS. Inhibition of mucin glycosylation by aryl-N-acetyl-alpha-galactosaminides in human colon cancer cells. J Biol Chem 1989; 264:19271-19277.
    • (1989) J Biol Chem , vol.264 , pp. 19271-19277
    • Kuan, S.F.1    Byrd, J.C.2    Basbaum, C.3    Kim, Y.S.4
  • 30
    • 33646428686 scopus 로고    scopus 로고
    • Testicular proteins associated with the germ cemarker, TEX101: Involvement of cellubrevin in TEX101-trafficking to the cell surface during spermatogenesis
    • Tsukamoto H, Yoshitake H, Mori M, Yanagida M, Takamori K, Ogawa H, Takizawa T, Araki Y. Testicular proteins associated with the germ cemarker, TEX101: involvement of cellubrevin in TEX101-trafficking to the cell surface during spermatogenesis. Biochem Biophys Res Commun 2006; 345:229-238.
    • (2006) Biochem Biophys Res Commun , vol.345 , pp. 229-238
    • Tsukamoto, H.1    Yoshitake, H.2    Mori, M.3    Yanagida, M.4    Takamori, K.5    Ogawa, H.6    Takizawa, T.7    Araki, Y.8
  • 32
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame C, Higgins DG, Heringa J. T-Coffee: a novel method for fast and accurate multiple sequence alignment. J Mol Biol 2000; 302:205-217.
    • (2000) J Mol Biol , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 33
    • 0043123123 scopus 로고    scopus 로고
    • Tcoffee@igs: A web server for computing, evaluating and combining multiple sequence alignments
    • Poirot O, O'Toole E, Notredame C. Tcoffee@igs: a web server for computing, evaluating and combining multiple sequence alignments. Nucleic Acids Res 2003; 31:3503-3506.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3503-3506
    • Poirot, O.1    O'Toole, E.2    Notredame, C.3
  • 35
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H, Engelbrecht J, Brunak S, von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng 1997; 10:1-6.
    • (1997) Protein Eng , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    von Heijne, G.4
  • 36
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh A, Larsson B, von Heijne G, Sonnhammer EL. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J Mol Biol 2001; 305:567-580.
    • (2001) J Mol Biol , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.4
  • 37
  • 38
    • 0000617199 scopus 로고
    • Studies on the fertilization of mouse eggs in vitro. I. In vitro fertilization of eggs by fresh epididymal sperm
    • Toyoda Y, Yokoyama M, Hoshi T. Studies on the fertilization of mouse eggs in vitro. I. In vitro fertilization of eggs by fresh epididymal sperm. Jpn J Anim Reprod 1971; 16:147-151.
    • (1971) Jpn J Anim Reprod , vol.16 , pp. 147-151
    • Toyoda, Y.1    Yokoyama, M.2    Hoshi, T.3
  • 39
    • 0034672519 scopus 로고    scopus 로고
    • Isolation and characterization of a novel human gene (C9orf11) on chromosome 9p21, a region frequently deleted in human cancer
    • Ruiz A, Pujana MA, Estivill X. Isolation and characterization of a novel human gene (C9orf11) on chromosome 9p21, a region frequently deleted in human cancer. Biochim Biophys Acta 2000; 1517:128-134.
    • (2000) Biochim Biophys Acta , vol.1517 , pp. 128-134
    • Ruiz, A.1    Pujana, M.A.2    Estivill, X.3
  • 40
    • 33745852175 scopus 로고    scopus 로고
    • Li YC, Hu XQ, Zhang KY, Guo J, Hu ZY, Tao SX, Xiao LJ, Wang QZ, Han CS, Liu YX. Afaf, a novel vesicle membrane protein, is related to acrosome formation in murine testis. FEBS Lett 2006; 580:4266-4273.
    • Li YC, Hu XQ, Zhang KY, Guo J, Hu ZY, Tao SX, Xiao LJ, Wang QZ, Han CS, Liu YX. Afaf, a novel vesicle membrane protein, is related to acrosome formation in murine testis. FEBS Lett 2006; 580:4266-4273.
  • 41
    • 0035886760 scopus 로고    scopus 로고
    • Green fluorescent protein rendered susceptible to proteolysis: Positions for protease-sensitive insertions
    • Chiang CF, Okou DT, Griffin TB, Verret CR, Williams MN. Green fluorescent protein rendered susceptible to proteolysis: positions for protease-sensitive insertions. Arch Biochem Biophys 2001; 394:229-235.
    • (2001) Arch Biochem Biophys , vol.394 , pp. 229-235
    • Chiang, C.F.1    Okou, D.T.2    Griffin, T.B.3    Verret, C.R.4    Williams, M.N.5
  • 42
    • 33751373089 scopus 로고    scopus 로고
    • Flagellasialin: A novel sulfated alpha2,9-linked polysialic acid glycoprotein of sea urchin sperm flagella
    • Miyata S, Sato C, Kumita H, Toriyama M, Vacquier VD, Kitajima K. Flagellasialin: a novel sulfated alpha2,9-linked polysialic acid glycoprotein of sea urchin sperm flagella. Glycobiology 2006; 16:1229-1241.
    • (2006) Glycobiology , vol.16 , pp. 1229-1241
    • Miyata, S.1    Sato, C.2    Kumita, H.3    Toriyama, M.4    Vacquier, V.D.5    Kitajima, K.6
  • 43
    • 0022527678 scopus 로고
    • Reversible defects in O-linked glycosylation and LDL receptor expression in a UDP-Gal/UDP-GalNAc 4-epimerase deficient mutant
    • Kingsley DM, Kozarsky KF, Hobbie L, Krieger M. Reversible defects in O-linked glycosylation and LDL receptor expression in a UDP-Gal/UDP-GalNAc 4-epimerase deficient mutant. Cell 1986; 44:749-759.
    • (1986) Cell , vol.44 , pp. 749-759
    • Kingsley, D.M.1    Kozarsky, K.F.2    Hobbie, L.3    Krieger, M.4
  • 44
    • 0024347197 scopus 로고
    • Effects of O-linked glycosylation on the cell surface expression and stability of decay-accelerating factor, a glycophospholipid-anchored membrane protein
    • Reddy P, Caras I, Krieger M. Effects of O-linked glycosylation on the cell surface expression and stability of decay-accelerating factor, a glycophospholipid-anchored membrane protein. J Biol Chem 1989; 264:17329-17336.
    • (1989) J Biol Chem , vol.264 , pp. 17329-17336
    • Reddy, P.1    Caras, I.2    Krieger, M.3
  • 45
    • 0022003140 scopus 로고
    • Deglycosylation of asparagine-linked glycans by peptide:N-glycosidase F
    • Tarentino AL, Gomez CM, Plummer TH Jr. Deglycosylation of asparagine-linked glycans by peptide:N-glycosidase F. Biochemistry 1985; 24:4665-4671.
    • (1985) Biochemistry , vol.24 , pp. 4665-4671
    • Tarentino, A.L.1    Gomez, C.M.2    Plummer Jr., T.H.3
  • 46
    • 0018706876 scopus 로고
    • Enzymatic properties of neuraminidases from Arthrobacter ureafaciens
    • Uchida Y, Tsukada Y, Sugimori T. Enzymatic properties of neuraminidases from Arthrobacter ureafaciens. J Biochem 1979; 86:1573-1585.
    • (1979) J Biochem , vol.86 , pp. 1573-1585
    • Uchida, Y.1    Tsukada, Y.2    Sugimori, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.