메뉴 건너뛰기




Volumn 83, Issue 6, 2005, Pages 1791-1796

Binding of recombinant human proacrosin/acrosin to zona pellucida glycoproteins. II. Participation of mannose residues in the interaction

Author keywords

Acrosin; Acrosome; Fertilization; Human; Mannose; Sperm egg interaction; Spermatozoa; Zona pellucida

Indexed keywords

ACROSIN; BOVINE SERUM ALBUMIN; GLYCOPROTEIN; MANNOSE; MERCAPTOETHANOL; PROACROSIN; RECOMBINANT PROTEIN; UREA;

EID: 20444443584     PISSN: 00150282     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.fertnstert.2004.12.043     Document Type: Article
Times cited : (8)

References (30)
  • 1
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • E. Knobil J.D. Neill Raven Press Ltd New York
    • R. Yanagimachi Mammalian fertilization E. Knobil J.D. Neill The physiology of reproduction 1994 Raven Press Ltd New York 189 317
    • (1994) The Physiology of Reproduction , pp. 189-317
    • Yanagimachi, R.1
  • 2
    • 0032739851 scopus 로고    scopus 로고
    • Structure of sugar chains included in mammalian zona pellucida glycoproteins and their potential roles in sperm-egg interaction
    • S. Takasaki, E. Mori, T. Mori Structure of sugar chains included in mammalian zona pellucida glycoproteins and their potential roles in sperm-egg interaction Biochim Biophys Acta 1473 1999 206 215
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 206-215
    • Takasaki, S.1    Mori, E.2    Mori, T.3
  • 3
    • 0027756146 scopus 로고
    • Head-specific mannose-ligand receptor expression in human spermatozoa is dependent on capacitation-associated membrane cholesterol loss
    • S. Benoff, I. Hurley, G.W. Cooper, F.S. Mandel, D.L. Rosenfeld, A. Hershlag Head-specific mannose-ligand receptor expression in human spermatozoa is dependent on capacitation-associated membrane cholesterol loss Hum Reprod 8 1993 2141 2154
    • (1993) Hum Reprod , vol.8 , pp. 2141-2154
    • Benoff, S.1    Hurley, I.2    Cooper, G.W.3    Mandel, F.S.4    Rosenfeld, D.L.5    Hershlag, A.6
  • 4
    • 0028932706 scopus 로고
    • Expression of mannose-binding sites on human spermatozoa and their role in sperm-zona pellucida binding
    • J.-S. Chen, G.F. Doncel, C. Alvarez, A.A. Acosta Expression of mannose-binding sites on human spermatozoa and their role in sperm-zona pellucida binding J Androl 16 1995 55 63
    • (1995) J Androl , vol.16 , pp. 55-63
    • Chen, J.-S.1    Doncel, G.F.2    Alvarez, C.3    Acosta, A.A.4
  • 6
    • 79961214892 scopus 로고    scopus 로고
    • Effect of sperm viability, plasmalemma integrity, and capacitation on patterns of expression of mannose-binding sites on human sperm
    • H.M. Youssef, G.F. Doncel, B.A. Bassiouni, A.A. Acosta Effect of sperm viability, plasmalemma integrity, and capacitation on patterns of expression of mannose-binding sites on human sperm Arch Androl 38 1997 67 74
    • (1997) Arch Androl , vol.38 , pp. 67-74
    • Youssef, H.M.1    Doncel, G.F.2    Bassiouni, B.A.3    Acosta, A.A.4
  • 7
    • 0025874204 scopus 로고
    • Expression of D-mannose binding sites on human spermatozoa: Comparison of fertile donors and infertile patients
    • J. Tesarik, C. Mendoza, A. Carreras Expression of D-mannose binding sites on human spermatozoa comparison of fertile donors and infertile patients Fertil Steril 56 1991 113 118
    • (1991) Fertil Steril , vol.56 , pp. 113-118
    • Tesarik, J.1    Mendoza, C.2    Carreras, A.3
  • 8
    • 0027498916 scopus 로고
    • Human sperm fertilizing potential in vitro is correlated with differential expression of a head-specific mannose-ligand receptor
    • S. Benoff, G.W. Cooper, I. Hurley, B. Napolitano, D.L. Rosenfeld, G.M. Scholl Human sperm fertilizing potential in vitro is correlated with differential expression of a head-specific mannose-ligand receptor Fertil Steril 59 1993 854 862
    • (1993) Fertil Steril , vol.59 , pp. 854-862
    • Benoff, S.1    Cooper, G.W.2    Hurley, I.3    Napolitano, B.4    Rosenfeld, D.L.5    Scholl, G.M.6
  • 9
    • 0024381288 scopus 로고
    • Significance of D-mannose as a sperm receptor site on the zona pellucida in human fertilization
    • K. Mori, T. Daitoh, M. Irahara, M. Kamada, T. Aono Significance of D-mannose as a sperm receptor site on the zona pellucida in human fertilization Am J Obstet Gynecol 161 1989 207 211
    • (1989) Am J Obstet Gynecol , vol.161 , pp. 207-211
    • Mori, K.1    Daitoh, T.2    Irahara, M.3    Kamada, M.4    Aono, T.5
  • 12
    • 0031241776 scopus 로고    scopus 로고
    • Induction of the human sperm acrosome reaction with mannose containing neoglycoprotein ligands
    • S. Benoff, I.R. Hurley, F.S. Mandel, G.W. Cooper, A. Hershlag Induction of the human sperm acrosome reaction with mannose containing neoglycoprotein ligands Mol Hum Reprod 3 1997 827 837
    • (1997) Mol Hum Reprod , vol.3 , pp. 827-837
    • Benoff, S.1    Hurley, I.R.2    Mandel, F.S.3    Cooper, G.W.4    Hershlag, A.5
  • 13
    • 0029155587 scopus 로고
    • Co-expression of mannose-ligand and non-nuclear progesterone receptors on motile human sperm identifies an acrosome-reaction inducible subpopulation
    • S. Benoff, J.I. Rushbrook, I.R. Hurley, F.S. Mandel, M. Barcia, G.W. Cooper Co-expression of mannose-ligand and non-nuclear progesterone receptors on motile human sperm identifies an acrosome-reaction inducible subpopulation Am J Reprod Immunol 34 1995 100 115
    • (1995) Am J Reprod Immunol , vol.34 , pp. 100-115
    • Benoff, S.1    Rushbrook, J.I.2    Hurley, I.R.3    Mandel, F.S.4    Barcia, M.5    Cooper, G.W.6
  • 14
    • 0031241721 scopus 로고    scopus 로고
    • Use of mannose ligands in IVF screens to mimic zona pellucida-induced acrosome reactions and predict fertilization success
    • S. Benoff, I.R. Hurley, F.S. Mandel, T. Paine, A. Jacob, G.W. Cooper Use of mannose ligands in IVF screens to mimic zona pellucida-induced acrosome reactions and predict fertilization success Mol Hum Reprod 3 1997 839 846
    • (1997) Mol Hum Reprod , vol.3 , pp. 839-846
    • Benoff, S.1    Hurley, I.R.2    Mandel, F.S.3    Paine, T.4    Jacob, A.5    Cooper, G.W.6
  • 15
    • 0033049429 scopus 로고    scopus 로고
    • The neoglycoprotein mannose-bovine serum albumin, but not progesterone, activated T-type calcium channels in human spermatozoa
    • P.F. Blackmore, S. Eisoldt The neoglycoprotein mannose-bovine serum albumin, but not progesterone, activated T-type calcium channels in human spermatozoa Mol Hum Reprod 5 1999 498 506
    • (1999) Mol Hum Reprod , vol.5 , pp. 498-506
    • Blackmore, P.F.1    Eisoldt, S.2
  • 16
    • 0034772360 scopus 로고    scopus 로고
    • Effect of freezing-thawing on the expression of mannose-ligand receptors on human spermatozoa: The impact on sperm capacitation and acrosome reaction
    • H. Yavetz, Y. Rosenblat, L. Yogev, A. Botchan, J.B. Lessing, G. Paz Effect of freezing-thawing on the expression of mannose-ligand receptors on human spermatozoa the impact on sperm capacitation and acrosome reaction Andrologia 33 2001 272 276
    • (2001) Andrologia , vol.33 , pp. 272-276
    • Yavetz, H.1    Rosenblat, Y.2    Yogev, L.3    Botchan, A.4    Lessing, J.B.5    Paz, G.6
  • 17
    • 0001667679 scopus 로고
    • Biochemistry and function of acrosin
    • P. Wassarman CRC Press Boca Raton
    • U.A. Urch Biochemistry and function of acrosin P. Wassarman Elements of mammalian fertilization 1991 CRC Press Boca Raton 233 248
    • (1991) Elements of Mammalian Fertilization , pp. 233-248
    • Urch, U.A.1
  • 19
    • 20444459926 scopus 로고    scopus 로고
    • Binding of recombinant human proacrosin/acrosin to ZP glycoproteins. I. studies with recombinant human ZPA, ZPB, and ZPC
    • L.I. Furlong, J. Harris, M.H. Vazquez-Levin Binding of recombinant human proacrosin/acrosin to ZP glycoproteins. I. studies with recombinant human ZPA, ZPB, and ZPC Fertil Steril 83 2005 xxxx-xx.
    • (2005) Fertil Steril , vol.83
    • Furlong, L.I.1    Harris, J.2    Vazquez-Levin, M.H.3
  • 20
    • 0025805799 scopus 로고
    • The interaction of boar sperm proacrosin with its natural substrate, the zona pellucida, and with polysulfated polysaccharides
    • U.A. Urch, H. Patel The interaction of boar sperm proacrosin with its natural substrate, the zona pellucida, and with polysulfated polysaccharides Development 111 1991 1165 1172
    • (1991) Development , vol.111 , pp. 1165-1172
    • Urch, U.A.1    Patel, H.2
  • 21
    • 0028913751 scopus 로고
    • Amino acid sequences of porcine Sp38 and proacrosin required for binding to the zona pellucida
    • E. Mori, S. Kashiwabara, T. Baba, Y. Inagaki, T. Mori Amino acid sequences of porcine Sp38 and proacrosin required for binding to the zona pellucida Dev Biol 168 1995 575 583
    • (1995) Dev Biol , vol.168 , pp. 575-583
    • Mori, E.1    Kashiwabara, S.2    Baba, T.3    Inagaki, Y.4    Mori, T.5
  • 22
    • 0023873193 scopus 로고
    • Zona pellucida-binding and frucose-binding of boar sperm acrosin is not correlated with proteolytic activity
    • E. Töpfer-Petersen, A. Henschen Zona pellucida-binding and frucose-binding of boar sperm acrosin is not correlated with proteolytic activity Biol Chem Hoppe Seyler 369 1988 69 76
    • (1988) Biol Chem Hoppe Seyler , vol.369 , pp. 69-76
    • Töpfer-Petersen, E.1    Henschen, A.2
  • 23
    • 0035202973 scopus 로고    scopus 로고
    • Interactions between mouse ZP2 glycoprotein and proacrosin; A mechanism for secondary binding of sperm to the zona pellucida during fertilization
    • E. Howes, J.C. Pascall, W. Engel, R. Jones Interactions between mouse ZP2 glycoprotein and proacrosin; a mechanism for secondary binding of sperm to the zona pellucida during fertilization J Cell Sci 114 2001 4127 4136
    • (2001) J Cell Sci , vol.114 , pp. 4127-4136
    • Howes, E.1    Pascall, J.C.2    Engel, W.3    Jones, R.4
  • 24
    • 0034435876 scopus 로고    scopus 로고
    • Effector sites in the three-dimensional structure of mammalian sperm beta-acrosin
    • R. Tranter, J.A. Read, R. Jones, R.L. Brady Effector sites in the three-dimensional structure of mammalian sperm beta-acrosin Structure Fold Des 8 2000 1179 1188
    • (2000) Structure Fold des , vol.8 , pp. 1179-1188
    • Tranter, R.1    Read, J.A.2    Jones, R.3    Brady, R.L.4
  • 25
    • 0025353025 scopus 로고
    • Zona pellucida-binding of boar sperm acrosin is associated with the N-terminal peptide of the acrosin B-chain (heavy chain)
    • E. Töpfer-Petersen, M. Steinberger, C.E. von Eschenbach, A. Zucker Zona pellucida-binding of boar sperm acrosin is associated with the N-terminal peptide of the acrosin B-chain (heavy chain) FEBS Lett 265 1990 51 54
    • (1990) FEBS Lett , vol.265 , pp. 51-54
    • Töpfer-Petersen, E.1    Steinberger, M.2    Von Eschenbach, C.E.3    Zucker, A.4
  • 26
    • 0035816624 scopus 로고    scopus 로고
    • CDNA cloning and functional analysis of ascidian sperm proacrosin
    • E. Kodama, T. Baba, H. Yokosawa, H. Sawada cDNA cloning and functional analysis of ascidian sperm proacrosin J Biol Chem 276 2001 24594 24600
    • (2001) J Biol Chem , vol.276 , pp. 24594-24600
    • Kodama, E.1    Baba, T.2    Yokosawa, H.3    Sawada, H.4
  • 27
    • 0026058935 scopus 로고
    • Acrosin, the peculiar sperm-specific serine protease
    • U. Klemm, W. Muller-Esterl, W. Engel Acrosin, the peculiar sperm-specific serine protease Hum Genet 87 1991 635 641
    • (1991) Hum Genet , vol.87 , pp. 635-641
    • Klemm, U.1    Muller-Esterl, W.2    Engel, W.3
  • 28
    • 0031657480 scopus 로고    scopus 로고
    • Site-directed mutagenesis of boar proacrosin reveals residues involved in binding of zona pellucida glycoproteins
    • S. Jansen, R. Jones, I. Jenneckens, B. Marschall, B. Kriegesmann, J. Coadwell Site-directed mutagenesis of boar proacrosin reveals residues involved in binding of zona pellucida glycoproteins Mol Reprod Dev 51 1998 184 192
    • (1998) Mol Reprod Dev , vol.51 , pp. 184-192
    • Jansen, S.1    Jones, R.2    Jenneckens, I.3    Marschall, B.4    Kriegesmann, B.5    Coadwell, J.6
  • 29
    • 0031942285 scopus 로고    scopus 로고
    • Characterization of the functional domains of boar acrosin involved in nonenzymatic binding to homologous zona pellucida glycoproteins
    • J.A. Crosby, R. Jones, C. Barros, P. Carvallo Characterization of the functional domains of boar acrosin involved in nonenzymatic binding to homologous zona pellucida glycoproteins Mol Reprod Dev 49 1998 426 434
    • (1998) Mol Reprod Dev , vol.49 , pp. 426-434
    • Crosby, J.A.1    Jones, R.2    Barros, C.3    Carvallo, P.4
  • 30
    • 0029848427 scopus 로고    scopus 로고
    • Site-directed mutagenesis of rabbit proacrosin-identification of residues involved in zona pellucida binding
    • R.T. Richardson, M.G. O'Rand Site-directed mutagenesis of rabbit proacrosin-identification of residues involved in zona pellucida binding J Biol Chem 271 1996 24069 24074
    • (1996) J Biol Chem , vol.271 , pp. 24069-24074
    • Richardson, R.T.1    O'Rand, M.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.