Hostname: page-component-77c89778f8-fv566 Total loading time: 0 Render date: 2024-07-18T07:57:23.141Z Has data issue: false hasContentIssue false
  • English
  • Français

Localization of the Rho GTPases and some Rho effector proteins in the sperm of several mammalian species

Published online by Cambridge University Press:  01 August 2006

Carl C. Ducummon  and
Trish Berger
Carl C. Ducummon*
Affiliation:
Department of Animal Science, One Shields Avenue, University of California, Davis, Davis, CA 95616, USA.
Trish Berger
Affiliation:
Department of Animal Science, One Shields Avenue, University of California, Davis, Davis, CA 95616, USA.
*
All correspondence to: Carl C. Ducummon, Pacific Reproductive Services, 444 De Haro Street, Suite #222, San Francisco, CA 94107, USA. Tel: +1 (415) 4872288, ext 231. Fax: +1 (415) 8634358. e-mail: carld@pacrepro.com
Get access Rights & Permissions [Opens in a new window]

Summary

The acrosome reaction is a fundamental event in the biology of the sperm and is a prerequisite to fertilization of the egg. Members of the Rho family of GTPases and their effectors are present in the cytoplasm and/or plasma membrane overlying the acrosome of porcine sperm. We have implicated the Rho family of GTPases and the Rho-activated kinase, ROCK-1, in mediating the zona-pellucida-induced acrosome reaction. Others have implicated the Rho GTPase in regulating the ionophore-induced acrosome reaction in the sperm of several mammalian species as well as in motility of bovine sperm. In this study, the localization of the Rho GTPases (RhoA, RhoB, Rac1 and Cdc42) as well as the effectors RhoGDI, PI(4)P5K and ROCK-1, was determined in boar, human, rat, ram, bull and elephant sperm. The four GTPases were each present in the sperm head of all species examined. RhoGDI was expressed in the head and tail of sperm from all species except pig, where it was present only in the head. PI(4)P5K was expressed in both head and tail of sperm from all species, but expression was typically weaker in the tail. Finally, ROCK-1 was expressed in the heads and tails of all sperm except that of the boar, where it was present only in the acrosomal region. These observations taken together suggest that the expression of Rho GTPases in sperm has been conserved throughout mammalian evolution, most likely due to the role of these GTPases in regulating acrosomal exocytosis.

Keywords

Effector proteinsEutherian mammalsImmunolocalizationRho family GTPasesSperm
Type
Research Article
Information
Zygote , Volume 14 , Issue 3 , August 2006 , pp. 249 - 257
Copyright
Copyright © Cambridge University Press 2006

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

Berger, T. & Horton, M. (1988). Evaluation of assay conditions for the zona-free hamster ova bioassay of boar sperm fertility. Gamete Res. 19, 101–11.CrossRefGoogle ScholarPubMed
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
Castellano, L.E., Martínez-Cadena, G., López-Godínez, J., Obregón, A. & García-Soto, J. (1997). Subcellular localization of the GTP-binding protein Rho in the sea urchin sperm. Eur. J. Cell Biol. 74, 329–35.Google ScholarPubMed
Cuéllar-Mata, P., Martínez-Cadena, G., López-Godínez, J., Obregón, A. & García-Soto, J. (2000). The GTP-binding protein RhoA localizes to the cortical granules of Strongylocentrotus purpuratus sea urchin egg and is secreted during fertilization. Eur. J. Cell Biol. 79, 81–91.CrossRefGoogle Scholar
Foltz, K.R. & Lennarz, W.J. (1993). The molecular basis of sea urchin gamete interactions at the egg plasma membrane. Dev. Biol. 158, 46–61.CrossRefGoogle ScholarPubMed
Fujita, A., Nakamura, K.-I., Kato, T., Watanabe, N., Ishizaki, T., Kimura, K., Mizoguchi, A. & Narumiya, S. (2000). Ropporin, a sperm-specific binding protein of rhophilin, that is localized in the fibrous sheath of sperm flagella. J. Cell Sci. 113, 103–12.CrossRefGoogle ScholarPubMed
Holloway, A.J., Moore, H.D.M. & Foster, P.M.D. (1990). The use of rat in vitro fertilization to detect reductions in the fertility of spermatozoa from males exposed to ethylene glycol monomethyl ether. Reprod. Toxicol. 4, 21–7.CrossRefGoogle ScholarPubMed
Murphy, W.J., Eizirik, E., Johnson, W.E., Zhang, Y.P., Ryder, O.A. & O'Brien, S.J. (2001). Molecular phylogenetics and the origin of placental mammals. Nature 409, 614–18.CrossRefGoogle Scholar
Nakamura, K.-I., Fujita, A., Murata, T., Watanabe, G., Mori, C., Fujita, J., Watanabe, N., Ishizaki, T., Yoshida, O. & Narumiya, S. (1999). Rhophilin, a small GTPase Rho-binding protein, is abundantly expressed in the mouse testis and localized in the principal piece of the sperm tail. FEBS Lett. 445, 9–13.CrossRefGoogle ScholarPubMed
Peterson, K.J. (2004). Isolation of Hox and Parahox genes in the hemichordate Ptychodera flava and the evolution of deuterostome Hox genes. Mol. Phylogenet. Evol. 31, 1208–15.CrossRefGoogle ScholarPubMed
Primakoff, P. & Myles, D.G. (2002). Penetration, adhesion, and fusion in mammalian sperm–egg interaction. Science 296, 2183–5.CrossRefGoogle ScholarPubMed
Van Aelst, L. & D'Souza-Schorey, C. (1997). Rho GTPases and signalling networks. Genes Dev. 11, 2295–322.CrossRefGoogle Scholar
Wilde, C., Genth, H., Aktories, K. & Just, I. (2000). Recognition of RhoA by Clostridium botulinum C3 exoenzyme. J. Biol. Chem. 275, 16478–83.CrossRefGoogle ScholarPubMed
Winchell, C.J., Sullivan, J., Cameron, C.B., Swalla, B.J. & Mallatt, J. (2002). Evaluating hypotheses of deuterostome phylogeny and chordate evolution with new LSU and SSU ribosomal DNA data. Mol. Biol. Evol. 19, 762–76.CrossRefGoogle ScholarPubMed
Yanagimachi, R. (1994). Mammalian fertilization. In The Physiology of Reproduction (ed. Knobil, E. & Neil, J.D.), pp. 189–317. New York: Raven Press.Google Scholar
Yudin, A.I., Gottlieb, W. & Meizel, S. (1988). Ultrastructural studies of the early events of the human sperm acrosome reaction as initiated by human follicular fluid. Gamete Res. 20, 11–24.CrossRefGoogle ScholarPubMed