Hostname: page-component-586b7cd67f-gb8f7 Total loading time: 0 Render date: 2024-11-29T19:12:18.119Z Has data issue: false hasContentIssue false
  • English
  • Français

Capacitation status of activated bovine sperm cultured in media containing methyl-β-cyclodextrin affects the acrosome reaction and fertility

Published online by Cambridge University Press:  23 August 2010

Yoku Kato ,
Sugita Shoei  and
Yoshikazu Nagao
Yoku Kato
Affiliation:
Department of Animal Production Science, United Graduate School of Agricultural Science, Tokyo University of Agriculture and Technology, Fuchu, 183-8509, Japan. University Farm, Faculty of Agriculture, Utsunomiya University, Mohka, Tochigi 321-4415, Japan.
Sugita Shoei
Affiliation:
Department of Animal Production Science, United Graduate School of Agricultural Science, Tokyo University of Agriculture and Technology, Fuchu, 183-8509, Japan. Department of Animal Science, Faculty of Agriculture, Utsunomiya University, Utsunomiya, Tochigi 321-8505, Japan.
Yoshikazu Nagao*
Affiliation:
University Farm, Utsunomiya University Shimokomoriya 443, Mohka, Tochigi 321-4415, Japan. Department of Animal Production Science, United Graduate School of Agricultural Science, Tokyo University of Agriculture and Technology, Fuchu, 183-8509, Japan. University Farm, Faculty of Agriculture, Utsunomiya University, Mohka, Tochigi 321-4415, Japan.
*
All correspondence to: Yoshikazu Nagao. University Farm, Utsunomiya University Shimokomoriya 443, Mohka, Tochigi 321-4415, Japan. Tel: 081-285-84-1321. Fax: 081-285-84-1321. e-mail: [email protected]
Get access Rights & Permissions [Opens in a new window]

Summary

Mammalian sperm undergo a series of biochemical transformations in the female reproductive tract that are collectively known as capacitation. One of the key processes involved in capacitation is the activation of sperm motility. Here, we investigated the capacitation and fertility status of activated sperm which had been cultured in media containing methyl-β-cyclodextrin (MBCD). In order to do this, single activated sperm were caught using a micropipette and stained with chlortetracycline (CTC). Firstly, we investigated the effects of preincubation upon motility, capacitation of activated sperm and fertility. Culture in preincubation media supplemented with MBCD increased the rates of activation and fertilization compared with sperm cultured by control methods (p < 0.05). Following capture, individual activated sperm mostly exhibited a pattern characteristic of capacitation.

Secondly we examined the effects of culturing sperm in media with or without glucose (G) and pyruvate acid (P) upon activated motility, the capacitation of activated sperm and fertility. Supplementation of culture media with G and P resulted in higher proportions of activated sperm and increased fertilization rates compared to culture without G and P (p < 0.05). Most of the sperm activated by culture in G and P exhibited patterns characteristic of capacitation. Without G and P, individual activated sperm mostly exhibited patterns characteristic of the acrosome reaction (p < 0.05). In conclusion, activated sperm exhibited patterns characteristic of capacitation. In addition, sperm activated in media containing an energy source (glucose and pyruvate acid) appeared to exhibit acrosome reactiveness and fertility.

Keywords

Acrosome reactionActivated motilityCapacitationSperm
Type
Research Article
Information
Zygote , Volume 19 , Issue 1 , February 2011 , pp. 21 - 30
Copyright
Copyright © Cambridge University Press 2010

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

Austin, C.R. (1951). Observations on the penetration of the sperm into the mammalian egg. Aust. J. Sci. Res. B. 4, 581–96.Google Scholar
Ambhaikar, M. & Puri, C. (1998). Cell surface binding sites for progesterone on human spermatozoa. Mol. Hum. Reprod. 4, 413–21.Google Scholar
Brackett, B.G. & Oliphant, G. (1975). Capacitation of rabbit spermatozoa in vitro. Biol. Reprod. 12, 260–74.Google Scholar
Breitbart, H. (2002). Role and regulation of intracellular calcium in acrosomal exocytosis. J. Reprod. Immun. 53, 151–9.Google Scholar
Brener, E., Rubinstein, S., Cohen, G., Shternall, K., Rivlin, J. & Breitbart, H. (2003). Remodeling of the actin cytoskeleton during mammalian sperm capacitation and acrosome reaction. Biol. Reprod. 68, 837–45.CrossRefGoogle ScholarPubMed
Chang, M.C. (1951). Fertilizing capacity of spermatozoa deposited into fallopian tubes. Nature 168, 697–8.Google Scholar
Choi, Y.H. & Toyoda, Y. (1998). Cyclodextrin removes cholesterol from mouse b sperm and induces capacitation in a protein-free medium. Biol. Reprod. 59, 1328–33.Google Scholar
Davis, B.K. (1981). Timing of fertilization in mammals: sperm cholesterol/phospholipid ratio as a determinant of the capacitation interval. Proc. Natl. Acad. Sci. USA 78, 7560–4.Google Scholar
Dinkins, M.B. & Brackett, B.G. (2000). Chlortetracycline staining patterns of frozen–thawed bull spermatozoa treated with beta-cyclodextrins, dibutyryl cAMP and progesterone. Zygote 8, 245–56.CrossRefGoogle Scholar
Etkovitz, N., Rubinstein, S., Daniel, L. & Breitbart, H. (2008). Role of PI3-Kinase and PI4-kinase in actin polymerization during bovine sperm capacitation. Biol. Reprod. 77, 263–73.Google Scholar
Fraser, L.R., Abeydeera, L.R. & Niwa, K. (1995). Ca2+-regulating mechanisms that modulate bull sperm capacitation and acrosomal exocytosis as determined by chlortetracycline analysis. Mol. Reprod. Dev. 40, 233–41.Google Scholar
Gadkar, S., Shah, C.A., Sachdeva, G., Samant, U. & Puri, C.P. (2002). Progesterone receptor as an indicator of sperm function. Biol. Reprod. 67, 1327–36.CrossRefGoogle ScholarPubMed
Grasa, P., Cebrián-Pérez, J.A. & Muiño-Blanco, T. (2006). Signal transduction mechanisms involved in in vitro ram sperm capacitation. Reproduction 132, 721–32.CrossRefGoogle ScholarPubMed
Gur, Y. & Breitbart, H. (2006). Mammalian sperm translate nuclear-encoded proteins by mitochondrial-type ribosomes. Genes Dev. 20, 411–6.Google Scholar
Gur, Y. & Breitbart, H. (2007). Protein translation in mammalian sperm. Soc. Reprod. Fertil. Suppl. 65, 391–7.Google Scholar
Ho, H.C. & Suarez, S.S., (2001). Hyperactivation of mammalian spermatozoa: function and regulation. Reproduction. 122, 519–26.Google Scholar
Ho, H.C., Granish, K.A. & Suarez, S.S. (2002). Hyperactivated motility of bull sperm is triggered at the axoneme by Ca2+ and not cAMP. Dev. Biol. 250, 208–17.CrossRefGoogle Scholar
Hung, P.H., Miller, M.G., Meyers, S.A. & VandeVoort, C.A. (2008). Sperm mitochondrial integrity is not required for hyperactivated motility, zona binding, or acrosome reaction in rhesus macaque. Biol. Reprod. 79, 367–75.Google Scholar
Kumar, V., Rangaraj, N. & Shivaji, S. (2006). Activity of pyruvate dehydrogenase A (PDHA) in hamster spermatozoa correlates positively with hyperactivation and is associated with sperm capacitation. Biol. Reprod. 75, 767–77.Google Scholar
Lamirande, E. & O'Flaherty, C. (2008). Sperm activation: role of reactive oxygen species and kinases. Biochim. Biophys. Acta 1784, 106–15.CrossRefGoogle ScholarPubMed
Moseley, C.L.F., Jha, N.K., Björndahl, L., Brewis, A.I., Publicover, S.J., Barratt, R. L.C. & Lefièvre, L. (2005). Protein tyrosine phosphorylation, hyperactivation and progesterone-induced acrosome reaction are enhanced in IVF media: an effect that is not associated with an increase in protein kinase A activation. Mol. Hum. Reprod. 11, 523–9.CrossRefGoogle Scholar
Marquez, B. & Suarez, S.S. (2004). Different signalling pathways in bovine sperm regulate capacitation and hyperactivation. Biol. Reprod. 70, 1626–33.Google Scholar
Marquez, B & Suarez, S.S. (2008). Soluble adenylyl cyclase is required for activation of sperm but does not have a direct effect on hyperactivation. Reprod. Fertil. Dev. 20, 247–52.CrossRefGoogle Scholar
Naz, R.K & Rajesh, P.B. (2004). Role of tyrosine phosphorylation in sperm capacitation/acrosome reaction. Reprod. Biol. Endocrinol. 2, 75–86.CrossRefGoogle ScholarPubMed
Osman, R.A., Andria, M.L., Jones, A.D., Meizel, S. (1989). Steroid induced exocytosis: the human sperm acrosome reaction. Biochem. Biophys. Res. Commun. 160, 828–33.Google Scholar
Parrish, J.J., Susko-Parrish, J.L. & Graham, J.K. (1999). In vitro capacitation of bovine spermatozoa: role of intracellular calcium. Theriogenology 51, 461–72.Google Scholar
Perl, A., Qian, Y., Chohan, K.R., Shirley, C.R., Amidon, W., Banerjee, S., Middleton, F.A., Conkrite, K.L., Barcza, M., Gonchoroff, N., Suarez, S.S. & Banki, K. (2006) Transaldolase is essential for maintenance of the mitochondrial transmembrane potential and fertility of spermatozoa. Proc. Natl. Acad. Sci. USA 103, 14813–8.CrossRefGoogle ScholarPubMed
Saeki, K., Hoshi, M., Leibfried-Rutledge, ML & First, N.L. (1990). In vitro fertilization and development of bovine oocytes matured with commercially available follicle stimulating hormone. Theriogenology 34, 1035–9.CrossRefGoogle Scholar
Suarez, S.S. (2007). Interactions of spermatozoa with the female reproductive tract: inspiration for assisted reproduction. Reprod. Fertil. Dev. 19, 103–10.CrossRefGoogle ScholarPubMed
Suarez, S.S. (2008). Control of hyperactivation in sperm. Hum. Reprod. Update 14, 647–57.CrossRefGoogle ScholarPubMed
Tesarik, J., Mendoza, C., Moos, J., Fenichel, P. & Fehlmann, M. (1992). Progesterone action through aggregation of a receptor on the sperm plasma membrane. FEBS Letts. 306, 116–20.Google Scholar
Witte, T.S. & Schäfer-Somi, S. (2007). Involvement of cholesterol, calcium and progesterone in the induction of capacitation and acrosome reaction of mammalian spermatozoa. Anim. Reprod. Sci. 102, 181–93.Google Scholar
WHO Health Organization. (1999). Organization laboratory manual for the examination of human semen and sperm-cervical mucus interaction, vol. 4. Cambridge University Press.Google Scholar
Yanagimachi, R. (1994). Mammalian fertilization. In The Physiology of Reproduction (eds. Knobil, E. & Neill, J.D.), pp. 189–317. New York, USA: Raven Press Ltd.Google Scholar