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Volumn 2, Issue 8, 1996, Pages 597-605

Inhibition of sperm-zona binding by suramin, a potential 'lead' compound for design of new anti-fertility agents

Author keywords

Fertilization; Proacrosin; Suramin; Zona pellucida

Indexed keywords

ACROSIN; CELL SURFACE RECEPTOR; DRUG DERIVATIVE; EGG PROTEIN; ENZYME PRECURSOR; MALE CONTRACEPTIVE AGENT; MEMBRANE PROTEIN; PROACROSIN; SURAMIN; ZONA PELLUCIDA GLYCOPROTEINS;

EID: 0030202144     PISSN: 13609947     EISSN: None     Source Type: Journal    
DOI: 10.1093/molehr/2.8.597     Document Type: Article
Times cited : (27)

References (42)
  • 2
    • 0024371030 scopus 로고
    • Activation and maturation mechanisms of boar acrosin zymogen based on the deduced primary structure
    • Baba, T., Kashiwabora, S., Watanbe, M. et al. (1989) Activation and maturation mechanisms of boar acrosin zymogen based on the deduced primary structure. J. Biol. Chem., 264, 11920-11927.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11920-11927
    • Baba, T.1    Kashiwabora, S.2    Watanbe, M.3
  • 3
    • 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. et al. (1994) 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
  • 4
    • 0023731968 scopus 로고
    • Identification of a secondary sperm receptor in the mouse egg zona pellucida: Role in maintenance of binding of acrosome-reacted sperm to eggs
    • Bleil, J.D., Greve, J.M. and Wassarman, P.M. (1988) Identification of a secondary sperm receptor in the mouse egg zona pellucida: role in maintenance of binding of acrosome-reacted sperm to eggs. Dev. Biol., 128, 376-385.
    • (1988) Dev. Biol. , vol.128 , pp. 376-385
    • Bleil, J.D.1    Greve, J.M.2    Wassarman, P.M.3
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem., 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0029163860 scopus 로고
    • Targeting the mouse genome: A compendium of knock-outs (part 1)
    • Brandon, E.P., Idzerda, R.L. and McKnight, G.S. (1995) Targeting the mouse genome: a compendium of knock-outs (part 1). Current Biol., 5, 625-634.
    • (1995) Current Biol. , vol.5 , pp. 625-634
    • Brandon, E.P.1    Idzerda, R.L.2    McKnight, G.S.3
  • 7
    • 0022619367 scopus 로고
    • Clinical pharmacokinetics of suramin in patients with HTLV-III/LAV infection
    • Collins, J.M., Klecker, R.J., Yarchoan, R. et al. (1986) Clinical pharmacokinetics of suramin in patients with HTLV-III/LAV infection. J. Clin. Pharmacol., 26, 22-26.
    • (1986) J. Clin. Pharmacol. , vol.26 , pp. 22-26
    • Collins, J.M.1    Klecker, R.J.2    Yarchoan, R.3
  • 8
    • 0025013025 scopus 로고
    • Specific recognition of sulphate esters by bindin, a sperm adhesion protein from sea urchins
    • De Angelis, P.L. and Glabe, C.G. (1990) Specific recognition of sulphate esters by bindin, a sperm adhesion protein from sea urchins. Biochim. Biophys. Acta, 1037, 100-105.
    • (1990) Biochim. Biophys. Acta , vol.1037 , pp. 100-105
    • De Angelis, P.L.1    Glabe, C.G.2
  • 9
    • 0018704110 scopus 로고
    • Suramin: A potent inhibitor of the reverse transcriptase of RNA tumor viruses
    • De Clercq, E. (1979) Suramin: a potent inhibitor of the reverse transcriptase of RNA tumor viruses. Cancer Lett., 8, 9-22.
    • (1979) Cancer Lett. , vol.8 , pp. 9-22
    • De Clercq, E.1
  • 10
    • 0023261299 scopus 로고
    • Suramin in the treatment of AIDS: Mechanism of action
    • De Clercq, E. (1987) Suramin in the treatment of AIDS: mechanism of action. Antiviral Res., 7, 1-10.
    • (1987) Antiviral Res. , vol.7 , pp. 1-10
    • De Clercq, E.1
  • 11
    • 0000198066 scopus 로고
    • The discovery of germanin
    • Dressel, J. and Oesper, R.E. (1961) The discovery of germanin. J. Chem. Ed., 38, 620-621.
    • (1961) J. Chem. Ed. , vol.38 , pp. 620-621
    • Dressel, J.1    Oesper, R.E.2
  • 12
    • 0030175750 scopus 로고    scopus 로고
    • Boar sperm proacrosin infrared investigation: Secondary structure analysis after antoactivation and suramin binding
    • in press
    • Fini, C., Tanfani, F., Bertoli, E. et al. (1996) Boar sperm proacrosin infrared investigation: secondary structure analysis after antoactivation and suramin binding. Biochem. Mol. Med., (in press).
    • (1996) Biochem. Mol. Med.
    • Fini, C.1    Tanfani, F.2    Bertoli, E.3
  • 13
    • 0020401889 scopus 로고
    • The localisation of acrosin and proacrosin in ram spermatozoa
    • Harrison, R.A.P., Fléchon, J.-E. and Brown, C.R. (1982) The localisation of acrosin and proacrosin in ram spermatozoa. J. Reprod. Fertil., 66, 349-358.
    • (1982) J. Reprod. Fertil. , vol.66 , pp. 349-358
    • Harrison, R.A.P.1    Fléchon, J.-E.2    Brown, C.R.3
  • 14
    • 0019598514 scopus 로고
    • Only acrosome-reacted spermatozoa can bind to and penetrate the zona pellucida: A study using the guinea-pig
    • Huang, T.T.F. Jr., Fleming, A.D. and Yanagimachi, T. (1981) Only acrosome-reacted spermatozoa can bind to and penetrate the zona pellucida: a study using the guinea-pig. J. Exp. Zool., 217, 287-290.
    • (1981) J. Exp. Zool. , vol.217 , pp. 287-290
    • Huang Jr., T.T.F.1    Fleming, A.D.2    Yanagimachi, T.3
  • 15
    • 0029096663 scopus 로고
    • Analysis of polysulfate-binding domains in porcine proacrosin, a putative zona adhesion protein from mammalian spermatozoa
    • Jansen, S., Quigley, M., Reik, W. et al. (1995) Analysis of polysulfate-binding domains in porcine proacrosin, a putative zona adhesion protein from mammalian spermatozoa. Int. J. Dev. Biol., 39, 501-510.
    • (1995) Int. J. Dev. Biol. , vol.39 , pp. 501-510
    • Jansen, S.1    Quigley, M.2    Reik, W.3
  • 16
    • 0023392434 scopus 로고
    • Inhibition of human immune-deficiency virus type I reverse transcriptase by suramin-related compounds
    • Jentsch, K.D., Hunsman, G., Hartmann, H. et al. (1987) Inhibition of human immune-deficiency virus type I reverse transcriptase by suramin-related compounds. J. Gen. Virol., 68, 2183-2192.
    • (1987) J. Gen. Virol. , vol.68 , pp. 2183-2192
    • Jentsch, K.D.1    Hunsman, G.2    Hartmann, H.3
  • 17
    • 0025619642 scopus 로고
    • Identification and functions of mammalian sperm-egg recognition molecules during fertilization
    • Jones, R. (1990) Identification and functions of mammalian sperm-egg recognition molecules during fertilization. J. Reprod. Fertil. 42, Suppl., 89-105.
    • (1990) J. Reprod. Fertil. , vol.42 , Issue.SUPPL. , pp. 89-105
    • Jones, R.1
  • 18
    • 0025801953 scopus 로고
    • Interaction of zona pellucida glycoproteins, sulphated carbohydrates and synthetic polymers, the putative egg-binding protein from mammalian spermatozoa
    • Jones, R. (1991) Interaction of zona pellucida glycoproteins, sulphated carbohydrates and synthetic polymers, the putative egg-binding protein from mammalian spermatozoa. Development, 111, 1155-1163.
    • (1991) Development , vol.111 , pp. 1155-1163
    • Jones, R.1
  • 19
    • 0023483241 scopus 로고
    • Identification of a zona-binding protein from boar spermatozoa as proacrosin
    • Jones, R. and Brown, C.R. (1987) Identification of a zona-binding protein from boar spermatozoa as proacrosin. Exp. Cell Res., 171, 505-508.
    • (1987) Exp. Cell Res. , vol.171 , pp. 505-508
    • Jones, R.1    Brown, C.R.2
  • 20
    • 0025281770 scopus 로고
    • Identification of zona- and fucoidan-binding proteins in guinea-pig spermatozoa and mechanism of recognition
    • Jones, R. and Williams, R.M. (1990) Identification of zona- and fucoidan-binding proteins in guinea-pig spermatozoa and mechanism of recognition. Development, 109, 41-50.
    • (1990) Development , vol.109 , pp. 41-50
    • Jones, R.1    Williams, R.M.2
  • 21
    • 0023885039 scopus 로고
    • Carbohydrate-binding properties of boar sperm proacrosin and assessment of its role in sperm-egg recognition and adhesion during fertilization
    • Jones, R., Brown, C.R. and Lancaster, R.T. (1988) Carbohydrate-binding properties of boar sperm proacrosin and assessment of its role in sperm-egg recognition and adhesion during fertilization. Development, 102, 781-792.
    • (1988) Development , vol.102 , pp. 781-792
    • Jones, R.1    Brown, C.R.2    Lancaster, R.T.3
  • 22
    • 0025324503 scopus 로고
    • Mouse preproacrosin: CDNA sequence, primary structure and postmeiotic expression in spermatogenesis
    • Klemm, U., Maier, W.-M., Tsousidou, S. et al. (1990) Mouse preproacrosin: cDNA sequence, primary structure and postmeiotic expression in spermatogenesis. Differentiation, 42, 160-166.
    • (1990) Differentiation , vol.42 , pp. 160-166
    • Klemm, U.1    Maier, W.-M.2    Tsousidou, S.3
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0023026214 scopus 로고
    • Biosynthesis of heparin
    • Lindahl, U., Feingold, D.S. and Rodén, L. (1986) Biosynthesis of heparin. TIBS, 11, 221-225.
    • (1986) TIBS , vol.11 , pp. 221-225
    • Lindahl, U.1    Feingold, D.S.2    Rodén, L.3
  • 26
    • 0028264864 scopus 로고
    • Some effects of zona pellucida glycoproteins and sulphated polymers on the autoactivation of boar sperm proacrosin and activity of β-acrosin
    • Lo Leggio, L., Williams, R.M. and Jones, R. (1994) Some effects of zona pellucida glycoproteins and sulphated polymers on the autoactivation of boar sperm proacrosin and activity of β-acrosin. J. Reprod. Fertil., 100, 177-185.
    • (1994) J. Reprod. Fertil. , vol.100 , pp. 177-185
    • Lo Leggio, L.1    Williams, R.M.2    Jones, R.3
  • 27
    • 0026640068 scopus 로고
    • Nature of the interaction of growth factors with suramin
    • Middaugh, C.R., Mach, H., Burke, C.J. et al. (1992) Nature of the interaction of growth factors with suramin. Biochem., 31, 9016-9024.
    • (1992) Biochem. , vol.31 , pp. 9016-9024
    • Middaugh, C.R.1    Mach, H.2    Burke, C.J.3
  • 28
  • 29
    • 26944438255 scopus 로고
    • Suramin
    • Corcoram, J.W. and Hahn, F.E. (eds)
    • Olenick, J.G. (1975) Suramin. In Corcoram, J.W. and Hahn, F.E. (eds), Antibiotics. Vol. 3, pp. 699-703.
    • (1975) Antibiotics , vol.3 , pp. 699-703
    • Olenick, J.G.1
  • 30
    • 0017365296 scopus 로고
    • Boar proacrosin. Purification and preliminary activation studies of proacrosin isolated from ejaculated boar sperm
    • Polakoski, K.L. and Parrish, R.F. (1977) Boar proacrosin. Purification and preliminary activation studies of proacrosin isolated from ejaculated boar sperm. J. Biol. Chem., 252, 1888-1894.
    • (1977) J. Biol. Chem. , vol.252 , pp. 1888-1894
    • Polakoski, K.L.1    Parrish, R.F.2
  • 31
    • 0026444071 scopus 로고
    • 2+ signalling and cell growth by polysulphonated azo dyes related to the anti-tumor asent suramin
    • 2+ signalling and cell growth by polysulphonated azo dyes related to the anti-tumor asent suramin. Cancer Chemother. Pharmacol., 31, 223-228.
    • (1992) Cancer Chemother. Pharmacol. , vol.31 , pp. 223-228
    • Powis, G.1    Sewald, M.J.2    Melder, D.3
  • 34
    • 0028367551 scopus 로고
    • The intact and cleaved human antithrombin III complex as a model for serpin-proteinase interactions
    • Schreuder, H.A., de Boer, B., Dijkema, R. et al. (1994) The intact and cleaved human antithrombin III complex as a model for serpin-proteinase interactions. Struct. Biol., 1, 48-54.
    • (1994) Struct. Biol. , vol.1 , pp. 48-54
    • Schreuder, H.A.1    De Boer, B.2    Dijkema, R.3
  • 35
    • 0022618897 scopus 로고
    • The role of carbohydrates in sperm-egg interaction in rats
    • Shalgi, R., Matityahu, A. and Nebel, L. (1986) The role of carbohydrates in sperm-egg interaction in rats. Biol. Reprod., 34, 446-452.
    • (1986) Biol. Reprod. , vol.34 , pp. 446-452
    • Shalgi, R.1    Matityahu, A.2    Nebel, L.3
  • 36
    • 0020641707 scopus 로고
    • In vitro biosynthesis of three sulphated glycoproteins of mutine zona pellucidae by oocytes grown in culture
    • Shimizu, S., Tsuji, M. and Dean, J. (1983) In vitro biosynthesis of three sulphated glycoproteins of mutine zona pellucidae by oocytes grown in culture. J. Biol. Chem., 258, 5858-5863.
    • (1983) J. Biol. Chem. , vol.258 , pp. 5858-5863
    • Shimizu, S.1    Tsuji, M.2    Dean, J.3
  • 37
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T.T. and Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA., 76, 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.T.2    Gordon, J.3
  • 38
    • 0025805799 scopus 로고
    • The interaction of boar sperm proacrosin with its natural substrate, the zona pellucida, and with polysulphated polysaccharides
    • Urch, U.A. and Patel, H. (1991) The interaction of boar sperm proacrosin with its natural substrate, the zona pellucida, and with polysulphated polysaccharides. Development 111, 1165-1172.
    • (1991) Development , vol.111 , pp. 1165-1172
    • Urch, U.A.1    Patel, H.2
  • 39
    • 0025044472 scopus 로고
    • Profile of a mammalian sperm receptor
    • Wassarman, P.M. (1990) Profile of a mammalian sperm receptor. Development, 108, 1-17.
    • (1990) Development , vol.108 , pp. 1-17
    • Wassarman, P.M.1
  • 40
    • 26944491383 scopus 로고
    • Physiological control of population growth
    • Whitten, W.K. (1956) Physiological control of population growth. Nature, 178, 992.
    • (1956) Nature , vol.178 , pp. 992
    • Whitten, W.K.1
  • 41
    • 0015077885 scopus 로고
    • Culture of mouse ova
    • Whittingham, D.G. (1971) Culture of mouse ova. J. Reprod. Fertil. 14, Suppl., 7-21.
    • (1971) J. Reprod. Fertil. , vol.14 , Issue.SUPPL. , pp. 7-21
    • Whittingham, D.G.1
  • 42
    • 0027917459 scopus 로고
    • Specificity of binding of zona pellucida glycoproteins to sperm proacrosin and related proteins
    • Williams, R.M. and Jones, R. (1993) Specificity of binding of zona pellucida glycoproteins to sperm proacrosin and related proteins. J. Erp. Zool., 266, 65-73.
    • (1993) J. Erp. Zool. , vol.266 , pp. 65-73
    • Williams, R.M.1    Jones, R.2


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