Abstract
Prior to fertilization, spermatozoa of many animals and plants show chemotactic behavior toward eggs. Chemotactic behavior was first described in ferns (1), and their attractant was identified as the bimalate ion (2). In animals, sperm chemotaxis to the egg was first observed in the hydrozoan Spirocodon saltatrix (3) and is now widely recognized in all species from cnidarians to human (for reviews, see refs. 4–6).
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Pfeffer, W. (1884) Locomotorische Richtungsbewegungen durch chemische Reize. Unters. Bot. Inst. Tübingen 1, 363–482.
Brokaw, C. J. (1958) Chemotaxis of bracken spermatozoids. The role of bimalate ions. J. Exp. Biol. 35, 192–196.
Dan, J. C. (1950) Fertilization in the medusan, Spirocodon saltatrix. Biol. Bull. Mar. Biol. Lab. Woods Hole 99, 412–415.
Miller, R. L. (1985) Sperm chemo-orientation in metazoa, in Biology of Fertilization (Metz, C. B. and Monroy, A., eds.), Academic, New York, Vol. 2, pp. 275–337.
Cosson, M. P. (1990) Sperm chemotaxis, in Controls of Sperm Motility: Biological and Clinical Aspects (Gagnon, C., ed.), CRC, Boca Raton, FL, pp. 104–135.
Eisenbach, M. (1999) Sperm chemotaxis. Rev. Reprod. 4, 56–66.
Miller, R. L. (1975) Chemotaxis of the spermatozoa of Ciona intestinalis. Nature 254, 244–245.
Miller, R. L. (1982) Sperm chemotaxis in ascidians. Am. Zool. 22, 827–840.
Yoshida, M., Inaba, K., and Morisawa, M. (1993) Sperm chemotaxis during the process of fertilization in the ascidians Ciona savignyi and Ciona intestinalis. Dev. Biol. 157, 497–506.
Yoshida, M., Inaba, K., Ishida, K., et al. (1994) Calcium and cyclic AMP mediate sperm activation, but Ca2+ alone contributes sperm chemotaxis in the ascidian, Ciona savignyi. Dev. Growth Differ. 36, 589–595.
Ward, G. E., Brokaw, C. J., Garbers, D. L., et al. (1985) Chemotaxis of Arbacia punctulata spermatozoa to resact, a peptide from the egg jelly layer. J. Cell Biol. 101, 2324–2329.
Carré, D. and Sardet, C. (1981) Sperm chemotaxis in siphonophores. Biol. Cell 40, 119–128.
Maier, I. and Müller, D. G. (1986) Sexual pheromones in algae. Biol. Bull. 170, 145–175.
Olson, J. H., Xiang, X., Ziegert, T., et al. (2001) Allurin, a 21-kDa sperm chemoattractant from Xenopus egg jelly, is related to mammalian sperm-binding proteins. Proc. Natl. Acad. Sci. USA 98, 11,205–11,210.
Cosson, J., Carré, D., and Cosson, M. P. (1986) Sperm chemotaxis in siphonophores: identification and biochemical properties of the attractant. Cell Motil. Cytoskeleton 6, 225–228.
Punnett, T., Miller, R. L., and Yoo, B.-H. (1992) Partial purification and some chemical properties of the sperm chemoattractant from the forcipulate starfish Pycnopodia helianthoides (Brandt, 1835). J. Exp. Zool. 262, 87–96.
Coll, J. C., Bowden, B. F., Meehan, G. V., et al. (1994) Chemical aspects of mass spawning in corals. I. Sperm-attractant molecules in the eggs of the scleractinian coral Montipora digitata. Mar. Biol. 118, 177–182.
Yoshida, M., Murata, M., Inaba, K., and Morisawa, M. (2002) A chemoattractant for ascidian spermatozoa is a sulfated steroid. Proc. Natl. Acad. Sci. USA 99, 14,831–14,836.
Cosson, M. P., Carré, D., and Cosson, J. (1984) Sperm chemotaxis in siphonophores. II. Calcium-dependent asymmetrical movement of spermatozoa induced by attractant. J. Cell Sci. 68, 163–181.
Miller, R. L. (1966) Chemotaxis during fertilization in the hydroid Campanularia. J. Exp. Zool. 162, 23–44.
Miller, R. L. and Brokaw, C. J. (1970) Chemotactic turning behaviour of Tubularia spermatozoa. J. Exp. Biol. 52, 699–706.
Brokaw, C. J. (1974) Calcium and fragellar response during the chemotaxis of bracken spermatozoids. J. Cell. Physiol. 83, 151–158.
Cosson, M. P., Carré, D., Cosson, J., et al. (1983) Calcium mediates sperm chemotaxis in siphonophores. J. Submicrosc. Cytol. 15, 89–93.
Singh, S., Lowe, D. G., Thorpe, D. S., et al. (1988) Membrane guanylate cyclase is a cell-surface receptor with homology to protein kinases. Nature 334, 708–712.
Cook, S. P., Brokaw, C. J., Muller, C. H., and Babcock, D. F. (1994) Sperm chemotaxis: egg peptides control cytosolic calcium to regulate flagellar responses. Dev. Biol. 165, 10–19.
Ren, D., Navarro, B., Perez, G., et al. (2001) A sperm ion channel required for sperm motility and male fertility. Nature 413, 603–609.
Quill, T. A., Ren, D., Clapham, D. E., and Garbers, D. L. (2001) A voltage-gated ion channel expressed specifically in spermatozoa. Proc. Natl. Acad. Sci. USA 98, 12,527–12,531.
Brokaw, C. J., Josslin, R., and Bobrow, L. (1974) Calcium ion regulation of flagellar beat symmetry in reactivated sea urchin spermatozoa. Biochem. Biophys. Res. Commun. 58, 795–800.
Brokaw, C. J. (1979) Calcium-induced asymmetrical beating of triton-demembranated sea urchin sperm flagella. J. Cell Biol. 82, 401–411.
Brokaw, C. J. and Nagayama, S. (1985) Modulation of the asymmetry of sea urchin sperm flagellar bending by calmodulin. J. Cell Biol. 100, 1875–1883.
Izumi, H., Márian, T., Inaba, K., Oka, Y., and Morisawa, M. (1999) Membrane hyperpolarization by sperm-activating and-attracting factor increases cAMP level and activates sperm motility in the ascidian Ciona intestinalis. Dev. Biol. 213, 246–256.
Nomura, M., Inaba, K., and Morisawa, M. (2000) Cyclic AMP-and calmodulin-dependent phosphorylation of 21 and 26 kDa proteins in axoneme is a prerequisite for SAAF-induced motile activation in ascidian spermatozoa. Dev. Growth Differ. 42, 129–138.
Yoshida, M., Ishikawa, M., Izumi, H., De Santis, R., and Morisawa, M. (2003) Store-operated calcium channel regulates the chemotactic behavior of ascidian sperm. Proc. Natl. Acad. Sci. USA 100, 149–154.
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© 2004 Humana Press Inc., Totowa, NJ
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Yoshida, M. (2004). Fertilization and Sperm Chemotaxis in Ascidians. In: Schatten, H. (eds) Germ Cell Protocols. Methods in Molecular Biology™, vol 253. Humana Press. https://doi.org/10.1385/1-59259-744-0:013
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DOI: https://doi.org/10.1385/1-59259-744-0:013
Publisher Name: Humana Press
Print ISBN: 978-1-58829-121-9
Online ISBN: 978-1-59259-744-4
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