Hostname: page-component-76fb5796d-5g6vh Total loading time: 0 Render date: 2024-04-28T20:23:50.170Z Has data issue: false hasContentIssue false
  • English
  • Français

Identification of porcine sperm plasma membrane proteins that may play a role in sperm–egg fusion

Published online by Cambridge University Press:  26 September 2008

Kendall Ash ,
Trish Berger ,
Catherine M. Horner  and
C. Chris Calvert
Kendall Ash
Affiliation:
Department of Animal Science, University of California, Davis, California, USA.
Trish Berger*
Affiliation:
Department of Animal Science, University of California, Davis, California, USA.
Catherine M. Horner
Affiliation:
Department of Animal Science, University of California, Davis, California, USA.
C. Chris Calvert
Affiliation:
Department of Animal Science, University of California, Davis, California, USA.
*
Trish Berger, Department of Animal Science, University of California, Davis, CA 95616-8521, USA. Telephone: 916-752-1267. Fax: 916-752-0175.
Get access Rights & Permissions [Opens in a new window]

Summary

Sperm plasma membrane (PM) proteins that demonstrate affinity for egg PM preparations have the potential to be biologically important during sperm-egg binding and/or fusion. In this study four such proteins have been identified. To provide quantitative evidence for possible biological function, the large natural variation among different porcine sperm populations with regard to their ability to interact with the egg was compared with the relative binding of egg PM material to individual proteins. An aliquot from each of 24 porcine ejaculates was evaluated by the zona-free hamster ova bioassay and the remainder processed to yield sperm PM vesicles. Aliquots of sperm PM were solubilised, separated by SDS-PAGE, western blotted and probed with partially purified, biotinylated egg PM protein. Bound egg PM proteins were visualised on western blots by an avidin/biotin/horseradish peroxidase system and analysed by scanning laser densitometry. Four sperm PM proteins (62, 39, 27 and 7 kDa estimated molecular mass) were the predominant binders of egg PM. The amount of egg PM bound to the 62 kDa protein was significantly correlated with the ability of sperm from the 24 ejaculates to penetrate zona-free hamster ova (percentage of ova penetrated, p = 0.01, R = 0.65; number of penetrated sperm per ovum, p = 0.02, R = 0.63)

Keywords

Male fertilityOocytePigsperm-egg interaction
Type
Article
Information
Zygote , Volume 3 , Issue 2 , May 1995 , pp. 163 - 170
Copyright
Copyright © Cambridge University Press 1995

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Alberts, B. & Miake-Lye, R. (1992). Unscrambling the puzzle of biological membranes: the importance of the details. Cell 68, 415–20.CrossRefGoogle Scholar
Almeida, E.A.C., Calarco, P.G., sutherlands, A.E., Myles, D.G., Primakoff, P. & White, J.M.(1993). Role of integrins in sperm–egg binding and fusion. Mol.Biol.Cell 4 (suppl), 103a.Google Scholar
Anderson, D.J., Abbott, A.F. & Jack, R.M. (1993).The role of complement component C3b and its receptors in spermoocyte interaction. Proc.Natl. Acad Sci USA. 90, 10051–5.CrossRefGoogle ScholarPubMed
Ash, K., Berger, T., Munn, R.J. & Horner, C.M. (1994).Isolation and partial Purification of plasma membrane from porcine oocytes. Mol.Reprod.Dev. 38, 334–7.CrossRefGoogle ScholarPubMed
Bedford, J.M. & Cooper, G.W. (1987). Membrane fusion events in the fertilization of vertebrate eggs. Cell Surface Rev. 5, 65–125.Google Scholar
Bedford, J.M.Moore, H.D.M. & Franklin, L.E. (1979). Significance of the equatorial segment of the acrosome of the spermatozoon in eutherian mammals. Exp.Cell Res. 119, 119–26.CrossRefGoogle Scholar
Berger, T. & Parker, K. (1989). Modification of the zona-free hamster ova bioassay of boar sperm fertility and correlation with in vivo fertility. Gamete Res. 22, 385–97.CrossRefGoogle ScholarPubMed
Blobel, C.P., Myles, D.G., Primakoff, P. & White, J.M. (1990). Proteolytic processing of protein involved in sperm–egg fusion correlates with acquisition of fertilization competence. J. Cell Biol. 111, 68–78.CrossRefGoogle ScholarPubMed
Blobel, C.P.Wolfsberg, T.G., Turck, C.W., Myles, D.G., Primakoff, P. & White, J.M. (1992). A potential fusion peptide and an integrin ligand domain in a protein active in sperm–egg fusion. Nature, 356, 248–52.CrossRefGoogle Scholar
Boldt, J.Howe, A.M. & Preble, J. (1988). Enzymatic alteration of the ability of mouse egg plasma membrane to interact with sperm. Biol.Reprod. 39. 19–27.CrossRefGoogle ScholarPubMed
Boldt, J., Gunter, L.E. & Howe, A.M. (1989). Charaterization of cell surface polypeptides of unfertilized, fertilized, and protease-treated zona-free mouse eggs. Gamete Res. 23, 91–101.CrossRefGoogle Scholar
Bronson, R.A. & Fusi, F. (1990a). Sperm–oolemmal interaction: role of the Arg-Gly-Asp(RGD) adhesion peptide. Fertil.Steril. 54, 527–9.CrossRefGoogle ScholarPubMed
Bronson, R.A. & Fusi, F. (1990b).Evidence that an Arg-Gly-Asp adhesion sequence plays a role in mammalian fertilization. Biol.Reprod. 43, 1019–25.CrossRefGoogle Scholar
Draper, N.R. & Smith, H. (1981). More complicated models: the correlation matrix. In Applied Regression Analysis,2nd edn, pp. 262–5.New York:Wiley.Google Scholar
Eddy, E.M., Vernon, R.B., Muller, C.H.Hahnel, A.C. & Fenderson, B.A. (1985). Immunodissection of sperm surface modifications during epedidymal maturation. Am. J. Anat. 174, 225–37.CrossRefGoogle Scholar
Fusi, F., Bronson, R.A., Hong, Y. & Ghebrehiwet, B. (1991). Complement component C1q and its receptor are involved in the interaction of human sperm with zonafree hamster eggs. Mol.Reprod.Dev. 29, 180–8.CrossRefGoogle ScholarPubMed
Fusi, F., Vignali, M.,Busacca, M. & Bronson, R.A. (1992). Evidence for the presence of an integrin cell adhesion receptor on the oolemma of unfertilzed cell adhesion receptor on the oolemma of unfertilized human oocytes. Mol.Reprod.Dev. 31, 215–22.CrossRefGoogle Scholar
Gillis, G., Peterson, R., Russell, L., Hook, L. & Freund, M. (1978). Isolation and characterization of membrane vesicles from human and boar spermatozoa: methods using nitrogen cavitation and ionophore induced vesiculation. Prep.Biochem. 8, 363–78.Google ScholarPubMed
Green, D.P.L. (1993). Mammalian fertilization as a biological machine: a model for adhesion and fusion of sperm and oocyte. Hum.Reprod. 8, 91–6.CrossRefGoogle Scholar
Hanahan, D.J. & Ekholm, J.E. (1974). The preparation of red blood cell ghosts (membranes). Methods Enzymol. 31, 168–72.CrossRefGoogle ScholarPubMed
Keenan, T.W., Valivullah, H.M. & Dunlevy, J.T. (1989). Isolation of plasma membranes from mammary gland by two-phase polymer partitioning. Anal.Biochem. 177, 194–8.CrossRefGoogle ScholarPubMed
Klint, M., Sege, K.Curman, B.Ploen, L. & Peterson, P.A. (1985). Solubilization and enrichment of boar sperm membrane proteins. Gamete Res. 11, 335–48.CrossRefGoogle Scholar
Klint, M., Fridberger, A., Menge, A., Sallstrom, J. & Ploen, L. (1987). Boar sperm surface glycoproteins: isolation, localization, and temporal expression during spermatogenesis. Gamete Res. 17, 173–90.CrossRefGoogle ScholarPubMed
Laemmli, U.K. (1970). Cleavage of structure proteins during the assembly of the head of bacteriophage T4. Nature. 227. 680–5.CrossRefGoogle ScholarPubMed
Myles, D.G., Kimmel, L.H., Blobel, C., Hunnicutt, G.R.Cho, C., White, J. & Primakoff, P. (1993). Molecular mechanism of mammalian sperm–egg fusion: the role of fertilin. Mol.Biol.Cell 4,(suppl), 231a.Google Scholar
North, P. & Fleischer, S. (1983). Use of nonspecific lipid transfer protein to modify the cholesterol content of synaptic membranes. Methods Enzymol. 98, 599–613.CrossRefGoogle ScholarPubMed
Okabe, M., Yagasaki, M., Oda, H., Matzno, S.Kohama, Y. & Mimura, T. (1988). Effect on a monoclonal anti-mouse sperm antibody (OBF13) on the interaction of mouse sperm with zona-free mouse and hamster eggs. J Reprod.Immunol. 13, 211–19.CrossRefGoogle ScholarPubMed
Okabe, M., Matzno, S., Nagira, M., Mimura, T., Kawai, Y. & Mayumi, T. (1990).A human sperm antigen possibly involved in binding and/or fusion with zona-free hamster eggs. Fertil.Steril. 54 1121–6.CrossRefGoogle ScholarPubMed
O'rand, M.G. & Irons, G. (1984). Monoclonal antibodies to rabbit sperm autoantigens. II. Inhibition of human sperm penetration of zona-free hamster eggs. Biol.Reprod. 30, 731–6.CrossRefGoogle ScholarPubMed
Peterson, R., Russell, L., Bundman, D. & Freund, M. (1980). Evaluation of the purity of boar sperm plasma membranes prepared by nitrogen cavitation. Biol.Reprod 23, 637–45.CrossRefGoogle ScholarPubMed
Pheps, B.M.Koppel, D.E.Primakoff, P. & Myles, D.G. (1990). Evidence that proteolysis of the surface is an initial step in the mechanism of formation of sperm cell surface domains. J Cell Biol. 111, 1839–47.CrossRefGoogle Scholar
Primakoff, P. & Myles, D.G. (1983). A map of the guinea pig sperm surface constructed with monoclonal antibodies. Dev.Biol. 98, 417–28.CrossRefGoogle ScholarPubMed
primakoff, P., Hyatt, H. & Tredick-Kline, J. (1987) Identification and purification of a sperm surface protein with a potential role in sperm–egg membrane fusion. J Cell Biol. 104, 141–9.CrossRefGoogle ScholarPubMed
Rochwerger, L. & Cuasnicu, P.S. (1992). Redistribution of a rat sperm epididymal glycoprotein after in vivo and in vitro capacitation. Mol.Reprod.Dev. 31, 34–41.CrossRefGoogle Scholar
Rochwerger, L., Cohen, D.J. & Cuasnicu, P.S. (1992). Mammalian sperm–egg fusion: the rat egg has complementary sites for a sperm protein that mediates gamete fusion. Dev.Biol. 153, 83–90.CrossRefGoogle ScholarPubMed
Russell, L.D., Peterson, R.N.Rusell, T.A. & Hunt, W. (1983). Electrophoretic map of boar sperm plasma membrane polypeptides and localization and fractionation of specific polypeptide subclasses. Biol.Reprod. 28, 393–413.CrossRefGoogle ScholarPubMed
Saling, P.M.lrons, G. & Waibel, R. (1985). Mouse sperm antigens that participate in fertilization.I.Inhibition of sperm fusion with the egg plasma membrane using monoclonal antibodies. Biol.Reprod. 33, 515–26.CrossRefGoogle ScholarPubMed
Saxena, N.K., Russell, L.D., Saxena, N.Peterson, R.N. (1986). Immunofluorescence antigen localization on boar sperm plasma membranes: monoclonal antibodies reveal apparent new domains and apparent redistribution of surface antigens during sperm maturation and ejaculation. Anat.Rec. 214, 238–52.CrossRefGoogle ScholarPubMed
Towbin, H., Staehelin, T. & Gordon, J. (1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc.Natl.Acad.Sci.USA. 76, 4850–4.CrossRefGoogle ScholarPubMed
Wassarman, P.M. (1994). Gamete interactions during mammalian fertilization. Theriogenology 41, 31–44.CrossRefGoogle Scholar
Wolfsberg, T.G.Bazan, J.F., Blobel, C.P., Myles, D.G.Primakoff, P. & White, J.M. (1993). The precursor region of a protein active in sperm–egg fusion contains a metalloprotease and a disintegrin domain: structural, functional, and evolutionary implications Proc.Natl.Acad.Sci.USA 90, 10783–7.CrossRefGoogle Scholar
Yanagimachi, R. (1994). Mammalian fertilization. In The physiology of Reproduction, ed. Knobil, E. & Neill, J.D., 2nd edn, pp. 189–317. New York: Raven Press.Google Scholar
Yanagimachi, R. & Noda, Y.D.(1970a). Electron microscopic studies of sperm incorporation into the hamster egg. AM.J.Anat. 128, 429–62.CrossRefGoogle Scholar
Yanagimachi, R. & Noda, Y.D. (1970b).Physiological changes in the the post-nuclear cap region of mammalian spermatozoa: a necessary preliminary to the memabrane fusion between sperm and egg cells. J. Ultrastruct.Res. 31, 486–93.CrossRefGoogle Scholar