Abstract
Mature mammalian spermatozoa comprise a relatively homogeneous population of cells. In suspension, their motility provides a readily visualized index of cell viability. Suspensions of spermatozoa are, therefore, convenient and useful systems for studying the reactions of O2 and its partially reduced metabolites which cause cell damage. It has been known for nearly 40 years that high O2 tensions are deleterious to the motility of human sperm (McLeod, 1943). Bull and ram spermatozoa were shown to lose motility on storage at 4°C in concert with loss of phospholipid, particularly plasmalogen, suggesting that this loss was due to lipid peroxidation leading to plasma membrane damage (Jones and Mann, 1973; Mann and Lutwak-Mann, 1981). Since most mammalian sperm contain little or no catalase (Mann, 1964), O2-induced damage to spermatozoa has been attributed to H2O2 (Wales et al., 1959). Another source of O2-induced damage could be the superoxide anion O2: Menella and Jones (1980) demonstrated superoxide dismutase (SOD) activity in spermatozoa from a variety of mammalian species, suggesting that O2 might be produced in these cells. But no documentation of O2 production was provided.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Alvarez, J.G., and Storey, B.T., 1983, Spontaneous lipid peroxidation in rabbit epididymal spermatozoa: its effect on sperm motility, Biol. Reprod., 28: (in press).
Azzi, A., Montecucco, C, and Reichert, C, 1975, The use of acetylated ferricytochrome c for the detection of superoxide radicals produced in biological membranes, Biochem. Biophys. Res. Comm., 65: 597.
Barber, A.A., and Bernheim, F., 1967, Lipid peroxidation: its measurement, occurrence, and significance in animal tissues, Adv. Gerontol. Res., 2: 355.
Bielski, B.H.J., 1978, Re-evaluation of the spectral and kinetic properties of HO2 and O2-free radicals, Phytochem. Phytobiol, 28: 645.
Boveris, A., 1977, Mitochondrial production of superoxide radical and hydrogen peroxide, in: “Tissue Hypoxia and Ischemia”, M. Reivich, R. Coburn, S. Lahiri, and B. Chance, eds., Plenum Press, New York.
Boveris, A., and Chance, B., 1973, The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen, Biochem. J., 134: 707.
Chance, B., Sies, H., and Boveries, A., 1979, Hydroperoxide metabolism in mammalian organs, Physiol. Rev., 59: 527.
Gebicki, J.M., and Bielski, B.H.J., 1981, Comparison of the capacities of the perhydroxyl and superoxide radicals to initiate chain oxidation of linoleic acid, J. Am. Chem. Soc, 103: 703O.
Heffner, L.J., and Storey, B.T., 1982, Cold lability of mouse sperm binding to zona pellucida, J. Exp. Zool., 219: 155.
Holland, M.K., Alvarez, J.G., and Storey, B.T., 1983, Production of superoxide and activity of superoxide dismutase, Biol. Reprod. 28: (in press).
Holland, M.K., and Storey, B.T., 1981, Oxygen metabolism of mammalian spermatozoa. Generation of hydrogen peroxide by rabbit epididymal spermatozoa, Biochem. J., 198: 273.
Jones, R., and Mann, T., 1973, Lipid peroxidation in spermatozoa, Proc. Roy. Soc. London B., 184: 103.
Keyhani, E., and Storey, B.T., 1973, Energy conservation capacity and morphological integrity of mitochondria in hypotonically treated rabbit epididymal spermatozoa, Biochim. Biophys. Acta 305: 557.
Mann, T., 1964, “The Biochemistry of Semen and the Male Reproductive Tract”, pp. 265–292, Methuen and Co., London.
Mann, T., and Lutwak-Mann, C., 1981, “Male Reproductive Function and Semen”, Springer, Berlin/Heidelberg/New York.
Margoliash, E., and Frohwirt, N., 1959, Spectrum of horse heart cytochrome c, Biochem. J., 71: 57O.
McCord, J.M., and Fridovich, I., 1969, Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein), J. Biol. Chem., 244: 6049.
McLaed, J., 1943, The role of oxygen in the metabolism and motility of human spermatozoa, Am. J. Physiol., 138: 512–518.
Mennella, M.R.F., and Jones, 1980, Properties of spermatozoal superoxide dismutase and lack of involvement of superoxide in metalion-catalyzed lipid-peroxidation reactions in semen, Biochem. J., 191: 289.
Storey, B.T., and Kayne, F.J., 1978, Energy metabolism of spermatozoa. VII. Interactions between lactate, pyruvate and malate as oxidative substrates for rabbit sperm mitochondria, Biol. Reprod., 18: 527.
Walling, C.W., 1957, “Free Radicals in Solution”, John Wiley and Sons, New York.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1984 Plenum Press, New York
About this chapter
Cite this chapter
Alvarez, J.G., Holland, M.K., Storey, B.T. (1984). Spontaneous Lipid Peroxidation in Rabbit Spermatozoa: A Useful Model for the Reaction of O2 Metabolites with Single Cells. In: Lübbers, D.W., Acker, H., Leniger-Follert, E., Goldstrick, T.K. (eds) Oxygen Transport to Tissue-V. Advances in Experimental Medicine and Biology, vol 169. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-1188-1_38
Download citation
DOI: https://doi.org/10.1007/978-1-4684-1188-1_38
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-1190-4
Online ISBN: 978-1-4684-1188-1
eBook Packages: Springer Book Archive