A Comparison of Mammalian Sperm Membranes
Mammalian spermatozoa exhibit considerable species differences in their size and shape, yet they all possess the same set of cellular organelles assembled on a common architectural theme. The polarized spermatozoon is partitioned into distinct segments or domains, distinguished by specific subsets of the cellular organelles (Eddy, 1988; Fawcett, 1975). These include the acrosomal and postacrosomal segments of the head, followed by the connecting piece, midpiece, principal piece, and end piece segments of the flagellum. During fertilization, different segments perform specific functions in generating motility, in binding the zona pellucida, in penetrating the egg coats, and in fusing with the egg plasma membrane (Wassarman, 1987; Yanagimachi, 1988). The sperm plasma membrane plays a central role in regulating these functions, and it varies in structure and molecular composition in the different domains. In this chapter we discuss domain-specific properties of the plasma membrane and address mechanisms that may maintain their unique properties.
KeywordsZona Pellucida Acrosome Reaction Epididymal Spermatozoon Mouse Sperm Intramembranous Particle
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- Eddy, E. M., 1988, The spermatozoon, in: The Physiology of Reproduction, Vol. 1 ( E. Knobil and J. D. Neill, eds.), Raven Press, New York, pp. 27–68.Google Scholar
- Endo, Y., Lee, M. A., and Kopf, G. S., 1988, Characterization of an islet-activating protein-sensitive site in mouse sperm that is involved in the zona pellucida-induced acrosome reaction, De,. Biol. 129: 12–24.Google Scholar
- Fournier-Delpech, S., Hamamah, S., Tananis-Anthony,C., Courot, M., and Orgebin-Crist, M.-C., 1984, Hormonal regulation of zona-binding ability and fertilizing ability of rat epididymal spermatozoa, Gamete Res. 9: 21–30.Google Scholar
- Friend, D. S., 1977, The organization of the spermatozoa) membrane, in: Immunobiology of Gametes ( M. Edidin and M. H. Johnson, eds.), Cambridge University Press, Cambridge, pp. 5–30.Google Scholar
- Friend, D. S., 1984, Membrane organization and differentiation in the guinea pig spermatozoon, in: Ultrastructure of Reproduction J. Van Blerkom and P. M. Motta, eds.), Martinus Nijhoff, Boston, pp. 75–85.Google Scholar
- Leyton, L., and Saling, P., 1989b, 95kd sperm proteins bind ZP3 and serve as tyrosine kinase substrates in response to zona binding, Cell 57: 1123–1130.Google Scholar
- Olson, G. E., Winfrey, V. P., and Flaherty, S. P, 1990, Membrane-cytoskeleton interactions in the sperm acrosome, in: Gamete Physiology ( R. Asch, J. Balmaceda, and J. Johnston, eds.), Serono Symposia, Newport Beach, California, pp. 109–118.Google Scholar
- San Agustin, J. T., Hughes, P, and Lardy, H. A., 1987, Properties and function of caltrin, the calcium-transport inhibitor of bull seminal plasma, FASEB J. 1: 60–66.Google Scholar
- Suzuki, F., and Nagano, T., 19806, Morphological relationship between the plasma membrane and the microtubules in the end piece of the boar spermatozoa, J. Electron Microsc. 29: 190–192.Google Scholar
- Yanagimachi, R., 1988, Mammalian fertilization, in: The Physiology of Reproduction, Vol. 1 ( E. Knobil and J. D. Neill, eds.), Raven Press, New York, pp. 135–186.Google Scholar