Mammalian Sperm Acrosomal Enzymes and the Acrosome Reaction

  • L. J. D. Zaneveld
  • C. J. De Jonge

Abstract

The sperm acrosome is an intracellular membrane-limited organelle that surrounds the anterior portion of the nucleus. It consists of an inner acrosomal membrane that is closely associated with the nucleus and is continuous with the outer acrosomal membrane. The acrosomal matrix proper is located between the two membranes. The entire spermatozoon is covered by the plasma membrane. The acrosome has several characteristics in common with the lysosome: it contains a number of enzymes, and the internal milieu is normally acidic. Although all mammals possess an acrosome, significant size and shape variations exist.

Keywords

Seminal Plasma Zona Pellucida Acrosome Reaction Sperm Head Sperm Membrane 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Abla, A., Mroueh, A., and Durr, I. F, 1974, A divalent cation-dependent ATP-ase in human spermatozoa, J. Reprod. Fertil 37: 121–123.PubMedCrossRefGoogle Scholar
  2. Allison, A. C., and Hartree, E. F, 1970, Lysosomal enzymes in the acrosome and their possible role in fertilization, J. Reprod. Fert. 21: 501–515.CrossRefGoogle Scholar
  3. Anderson, R. A., Johnson, S. K., Bielfeld, P, Feathergill, K. A., and Zaneveld, L. J. D., 1990, Characterization and inhibitor sensitivity of human sperm phospholipase A2: evidence against a pivotal involvement of phospholipase A2 in the acrosome reaction, Molec. Reprod. Develop. 27: 305–325.CrossRefGoogle Scholar
  4. Ashraf, M., Peterson, R. N., and Russell, L. D., 1982, Activity and location of cation-dependent ATPases on the plasma membrane of boar spermatozoa, Biochem. Biophys. Res. Commun. 107: 1273–1278.PubMedCrossRefGoogle Scholar
  5. Ashraf, M., Peterson, R. N., and Russell, L. D., 1984, Characterization of (Ca2+ + Mg2+) adenosine triphosphatase activity and calcium transport in boar plasma membrane vesicles and their relation to phosphorylation of plasma membrane proteins, Biol. Reprod. 31: 1061–1071.PubMedCrossRefGoogle Scholar
  6. Austin, C. R., 1985, Sperm maturation in the male and female genital tracts, in: Biology of Fertilization, Vol. 2 ( C. B. Metz and A. Monroy, eds.), Academic Press, New York, pp. 121–155.CrossRefGoogle Scholar
  7. Basuray, R., De Jonge, C. J., Zaneveld, L. J. D., 1990, Evidence for a role of cysteinyl leukotrienes in the fertilization process of mouse and human spermatozoa, J. Androl. 11: 47–51.PubMedGoogle Scholar
  8. Bearer, E. L., and Friend, D. S., 1982, Modification of anionic lipid domains preceding membrane fusion in guinea pig sperm, J. Cell Biol. 92: 604–615.PubMedCrossRefGoogle Scholar
  9. Bedford, J. M., and Cooper, G. W, 1978, Membrane fusion events in the fertilization of vertebrate eggs, in: Membrane Fusion (G. Poste and G. L. Nicolsen, eds.), North Holland, Amsterdam, pp. 65–125.Google Scholar
  10. Bernstein, M. H. and Teichman, R. J., 1973, A chemical procedure for extraction of the acrosomes of mammalian spermatozoa, J. Reprod. Fert. 33: 239–244.CrossRefGoogle Scholar
  11. Berridge, M. J., 1985, The molecular basis of communication within the cell, Sci. Am. 253: 142–152.PubMedCrossRefGoogle Scholar
  12. Bhalla, V. K., Tillman, W. L., and Williams, W. L., 1973, Presence of 3-aspartyl N-acetyl glucosamine amido hydrolase in mammalian spermatozoa, J. Reprod. Fertil. 34: 137–139.PubMedCrossRefGoogle Scholar
  13. Bhattacharyya, A. K., and Zaneveld, L. J. D., 1982, The sperm head, in: Biochemistry of Mammalian Fertilization ( L. J. D. Zaneveld and R. T. Chatterton, eds.), John Wiley & Sons, New York, pp. 119–151.Google Scholar
  14. Bradford, M. M., McRorie, R. A., and Williams, W. L., 1976, Involvement of esterases in sperm penetration of the corona radiata of the ovum, Biol. Reprod. 15: 102–106.PubMedCrossRefGoogle Scholar
  15. Bradford, M. M., McRorie, R. A., and Williams, W. L., 1976, A role for esterases in the fertilization process, J. Exp. Zool. 197: 297–301.PubMedCrossRefGoogle Scholar
  16. Breitbart, H., Stern, B., and Rubinstein, S., 1983, Calcium transport and Ca2+-ATPase activity in ram spermatozoa plasma membrane vesicles, Biochim. Biophys. Acta 728: 349–355.PubMedCrossRefGoogle Scholar
  17. Chang, M. C., 1984, Meaning of capacitation: A historical perspective, J. Androl. 5: 45–50.PubMedGoogle Scholar
  18. Clegg, E. D., 1983, Mechanisms of mammalian sperm capacitation, in: Mechanism and Control of Animal Fertilization ( J. F. Hartman, ed.), Academic Press, New York, pp. 177–212.Google Scholar
  19. De Jonge, C. J., Mack, S. R., Zaneveld, L. J. D., 1989, Inhibition of the human sperm acrosome reaction by proteinase inhibitors, Gamete Res. 23: 387–397.PubMedCrossRefGoogle Scholar
  20. De Jonge, C. J., Han, H.-L., Lowrie, H., Mack, S. R., Zaneveld, L. J. D., 1991a, Modulation of the human sperm acrosome reaction by effectors of the adenylate cyclase/cyclic AMP second-messenger pathway, J. Exp. Zool. 258: 113–125.PubMedCrossRefGoogle Scholar
  21. De Jonge, C. J., Han, H.-L., Mack, S. R., and Zaneveld, L. J. D., 1991b, Effect of phorbol esters, synthetic diacylglycerols, and a protein kinase C inhibitor on the human sperm acrosome reaction, J. Androl. 12: 62–70.PubMedGoogle Scholar
  22. Dudkiewicz, A. B., 1984, Purification of boar acrosomal arylsulfatase A and possible role in the penetration of cumulus cells, Biol. Reprod. 30: 1005–1014.PubMedCrossRefGoogle Scholar
  23. Farooqui, A. A., and Srivastava, P N., 1980, Isolation of ß-N-acetylhexosamimidase from rabbit semen and its role in fertilization, Biochem. J. 191: 827–834.PubMedGoogle Scholar
  24. Fritz, H., Schleuning W-D., Schiessler, H., Schill, W. B., Wendt, V., and Winkler, G., 1975, Boar, bull and human sperm acrosin–isolation, properties and biological aspects, in: Proteases and Biological Control ( E. Reich, D. Rifkin, and E. Shaw, eds.), Cold Spring Habor Laboratory, New York, pp. 715–735.Google Scholar
  25. Garbers, D. L., and Kopf, G. S., 1980, The regulation of spermatozoa by calcium and cyclic nucleotides, in: Advances in Cyclic Nucleotide Research ( P. Greengard and G. A. Robinson, eds.), Raven Press, New York, pp. 251–305.Google Scholar
  26. Gonzales, L. W., and Meizel, S., 1973, Acid phosphatases of rabbit spermatozoa. II. Partial purification and biochemical characterization of the multiple forms of rabbit spermatozoan acid phosphatase, Biochim. Biophys. Acta 32: 180–194.CrossRefGoogle Scholar
  27. Gordon, M., 1973, Localization of phosphatases activity on the membranes of the mammalian sperm head, J. Exp. Zool. 185: 111–119.PubMedCrossRefGoogle Scholar
  28. Gordon, M., and Barnett, R. H., 1967, Fine structural localization of phosphatases in rat and guinea pig, Exp. Cell Res. 48: 395–412.PubMedCrossRefGoogle Scholar
  29. Gottlieb, W, and Meizel, S., 1987, Biochemical studies of metalloendoproteinase activity in the spermatozoa of three mammalian species, J. Androl. 8: 14–24.PubMedGoogle Scholar
  30. Green, D. P. L., 1978, The mechanism of the acrosome reaction, in: Development in Mammals, Vol. 3 ( M. J. Johnson, ed.), North Holland, New York, pp. 65–80.Google Scholar
  31. Guerette, P, Langlais, J., Antaki, P, Chapdelaine, A., and Roberts, K.D., 1988, Activation of phospholipase A2 of human spermatozoa by proteases, Gamete Res. 19: 203–214.PubMedCrossRefGoogle Scholar
  32. Hinrichsen-Kohane, A. C., Hinrichsen, M. J., and Schill, W. B., 1984, Molecular events leading to fertilization—a review, Andrologia 16: 321–341.PubMedCrossRefGoogle Scholar
  33. Hoskins, D. D., and Casillas, E. R., 1975, Hormones, second messengers and the mammalian spermatozoon, in: Advances in Sex Hormone Research ( R. H. Singal and J. A. Thomas, eds.), University Park Press, Baltimore, pp. 283–321.Google Scholar
  34. Johnson, R. A., Jakobs, K. H., and Schultz, G., 1985, Extraction of the adenylate cyclase-activating factor of bovine sperm and its identification as a trypsin-like proteinase, J. Biol. Chem. 260: 114–121.PubMedGoogle Scholar
  35. Joyce, C., Jeyendran, R. S., and Zaneveld, L. J. D., 1985, Release, extraction, and stability of hyaluronidase associated with human spermatozoa. Comparisons with the rabbit, J. Androl. 6: 152–161.PubMedGoogle Scholar
  36. Khar, A., and Anand, S. R., 1977, Studies on the glycosidases of semen, Purification and properties of ß-N-acetylglucosaminidase from bull sperm, Biochim. Biophys. Acta 483: 141–151.PubMedCrossRefGoogle Scholar
  37. Kipping, D., 1970, Zur Kenntnis der sauren Phosphomonoesterase der menschlichen Spermatozoen, Klinische Wochenschr. 48: 1127–1128.CrossRefGoogle Scholar
  38. Kopf, G. S., 1988, Regulation of sperm function by guanine nucleotide-binding regulatory proteins (G-proteins), in: Meiotic Inhibition: Molecular Control of Meiosis ( F. P Hazeltine and F L. First, eds.), Alan R. Liss, New York, pp. 357–386.Google Scholar
  39. Kopf, G. S., and Vacquier, V. D., 1985, Characteristics of a calcium-modulated adenylate cyclase from abalone spermatozoa. Biol. Reprod. 33: 1094–1104.PubMedCrossRefGoogle Scholar
  40. Langlais, J., and Roberts, K. D., 1985, A molecular membrane model of sperm capacitation and the acrosome reaction of mammalian spermatozoa, Gamete Res. 12: 183–224.CrossRefGoogle Scholar
  41. Lee, M. A., Kopf, G. S., and Storey, B. T., 1987, Effects of phorbol esters and a diacylglycerol on the mouse sperm acrosome reaction induced by the zona pellucida, Biol. Reprod. 36: 617–627.PubMedCrossRefGoogle Scholar
  42. Lessley, B. A., and Garner, D. L., 1984, Identification and preliminary characterization of two distinct bovine seminal Pz-peptidases, Biol. Reprod. 31: 353–369.PubMedCrossRefGoogle Scholar
  43. Llanos, M. N., Lui, C. W, and Meizel, S., 1982, Studies of phospholipase A2 related to the hamster sperm acrosome reaction, J. Exp. Zool. 221: 107–117.PubMedCrossRefGoogle Scholar
  44. McDonald, J. K., and Kadhodayen, S., 1988, Cathespin L—a latent proteinase in guinea pig sperm, Biochem. Biophys. Res. Commun. 151: 827–835.PubMedCrossRefGoogle Scholar
  45. McRorie, R. A., and Williams, W L., 1974, Biochemistry of mammalian fertilization, Annu. Rev. Biochem. 43: 777–798.PubMedCrossRefGoogle Scholar
  46. McRorie, R. A., Turner, R. B., Bradford, M. M., and Williams, W. L., 1976, Acrolysin, the aminoproteinase catalyzing the initial conversion of proacrosin to acrosin in mammalian fertilization, Biochem. Biophys. Res. Commun. 71: 492–498.PubMedCrossRefGoogle Scholar
  47. Meizel, S., 1978, The mammalian sperm acrosome reaction, a biochemical approach, in: Development in Mammals (M. H. Johnson, ed.), North Holland, Amsterdam, pp. 1–64.Google Scholar
  48. Meizel, S., 1984, The importance of hydrolytic enzymes to an exocytotic event, the mammalian sperm acrosome reaction, Biol. Rev. 59: 125–157.PubMedCrossRefGoogle Scholar
  49. Meizel, S., 1985, Molecules that initiate or help stimulate the acrosome reaction by their interaction with the mammalian sperm surface, Am. J. Anat. 174: 285–302.PubMedCrossRefGoogle Scholar
  50. Meizel, S., Boggs, D., and Cotham, J., 1971, Electrophoretic studies of esterases of bull spermatozoa, cytoplasmic droplets and seminal plasma, J. Histochem. Cytochem. 19: 226–231.PubMedCrossRefGoogle Scholar
  51. Monks, N. J., Stein, D. M., and Fraser, L. R., 1986, Adenylate cyclase activity of mouse sperm during capacitation in vitro; effect of calcium and a GTP analogue. Int. J. Androl. 9: 67–76.PubMedCrossRefGoogle Scholar
  52. Monroy, A., and Rosati, F., 1983, A comparative analysis of sperm–egg interaction, Gamete Res. 7: 85–102.CrossRefGoogle Scholar
  53. Morton, D. B., 1977, The occurrence and function of proteolytic enzymes in the reproductive tract of mammals, in: Proteinases in Mammalian Cells and Tissues (A. J. Barret, ed.), North Holland, Amsterdam, pp. 445–500.Google Scholar
  54. Mrsny, R. J., and Meizel, S., 1985, Inhibition of hamster sperm Na+, K+-ATPase activity by taurine and hypotaurine, Life Sci. 36: 271–275.PubMedCrossRefGoogle Scholar
  55. Nishizuka, Y., 1986, Studies and perspectives of protein kinase C. Science 233: 305–312.PubMedCrossRefGoogle Scholar
  56. Parrish, R. E, and Polakoski, K. L., 1979, Mammalian sperm proacrosin–acrosin system, Int. J. Biochem. 10: 391–395.PubMedCrossRefGoogle Scholar
  57. Peterson, R. N., Hunt, W. P, and Saxena, N., 1987, Role of spermatozoa membranes in sperm capacitation and oocyte recognition, CRC Crit. Rev. Anat. Sci. 1: 1–14.Google Scholar
  58. Polakoski, K. L., and Siegel, M. S., 1986, The proacrosin–acrosin system, in: Andrology, Male Fertility and Sterility ( J. D. Paulson, A. Nigro-Vilar, E. Lucena, and L. Martin, eds.), Academic Press, New York, pp. 359–375.Google Scholar
  59. Polakoski, K. L., and Zaneveld, L. J. D., 1976, Proacrosin, in: Methods in Enzymology, Vol. LV, Proteolytic Enzymes, Part B ( L. Lorand, ed.), Academic Press, New York. pp. 325–331.Google Scholar
  60. Qian, Z.-U., Tsai, Y-H., Steinberger, A., Lu, M., Greenfield, A. R. L., and Haddox, M. K., 1985, Localization of ornithine decarboxylase in rat testicular cells and epididymal spermatozoa, Biol. Reprod. 33: 1189–1195.PubMedCrossRefGoogle Scholar
  61. Ribbes, H., Plantavid, M., Bennet, P. J., Chap, H., and Douste-Blazy, L., 1987, Phospholipase C from human sperm specific for phosphoinositides, Biochim. Biophys. Acta 919: 245–254.PubMedCrossRefGoogle Scholar
  62. Rogers, B. J., and Bentwood, B. J., 1982, Capacitation, acrosome reaction and fertilization, in: Biochemistry of Mammalian Fertilization ( L. J. D. Zaneveld and R. T. Chatterton, eds.), John Wiley & Sons, New York, pp. 203–230.Google Scholar
  63. Saling, P M., 1991, How the egg regulates sperm function during gamete interaction: facts and fantasies, Biol. Reprod. 44: 246–251.PubMedCrossRefGoogle Scholar
  64. Schollmeier, J. E., 1986, Identification of calpain II in porcine sperm, Biol. Reprod. 34: 721–731.CrossRefGoogle Scholar
  65. Seiguer, A. C., and Castro, A. E., 1972, Electron microscope demonstration of arylsulfatase activity during acrosome formation in the rat, Biol. Reprod. 7: 31–42.PubMedGoogle Scholar
  66. Shapiro, B. M., Schackmann, R. W, Tomber, R. M., and Kazazoglau, T., 1985, Coupled ionic and enzymatic regulation of sperm behavior, Curr. Top. Cell Regul. 26: 97–113.PubMedGoogle Scholar
  67. Shur, B. D., and Hall, N. G., 1982, Sperm surface galactosyltransferase activities during in vitro capacitation, J. Cell Biol. 95: 567–673PubMedCrossRefGoogle Scholar
  68. Shur, B. D., and Neely, C. A., 1988, Plasma membrane association, purification and partial characterization of mouse sperm 31,4-galactosyltransferase, J. Biol. Chem. 263: 17706–17714.PubMedGoogle Scholar
  69. Siegel, M. S., Bechtold, D. S., Willard, J. L., and Polakoski, K. L., 1987, Partial purification and characterization of human sperminogen, Biol. Reprod. 36: 1063–1068.PubMedCrossRefGoogle Scholar
  70. Singer, R., Barnet, M., Allalouf, D., Schwartzman, S., Sagiv, M., Landau, B., Segenreich, E., and Servadio, C., 1980, Some properties of acid and alkaline phosphatase in seminal fluid and isolated sperm, Arch. Androl. 5: 195–199.PubMedCrossRefGoogle Scholar
  71. Srivastava, P. N., and Abou-Issa, H., 1977, Purification and properties of rabbit spermatozoa) acrosomal neuraminidase, Biochem. J. 161: 193–200.PubMedGoogle Scholar
  72. Srivastava, P. N., and Ninjoor, V, 1982, Isolation of rabbit testicular cathepsin D and its role in the activation of proacrosin, Biochem. Biophys. Res. Commun. 109: 63–69.PubMedCrossRefGoogle Scholar
  73. Stambaugh, R., 1978, Enzymatic and morphological events in mammalian fertilization, Gamete Res. 1: 65–85.CrossRefGoogle Scholar
  74. Talbot, P., and Dicarlantonio, G., 1985, Cytochemical localization of dipeptidyl peptidase II (DPP-II) in mature guinea pig sperm, J. Histochem. Cytochem. 33: 1169–1172.PubMedCrossRefGoogle Scholar
  75. Teichman, R. J., and Bernstein, M. H., 1971, Fine structure localization of acid phosphatase in rabbit and bull sperm heads, J. Reprod. Fert. 27: 243–248.CrossRefGoogle Scholar
  76. Tesarik, J., 1986, From the cellular to the molecular dimension: The actual challenge for human fertilization research, Gamete Res. 13: 47–89.CrossRefGoogle Scholar
  77. Thakkar, J. K., East, J., Seyler, D., and Francson, R. C., 1983, Surface-active phospholipase A2 in mouse spermatozoa, Biochim. Biophys. Acta 754: 44–50.PubMedCrossRefGoogle Scholar
  78. Thakkar, J. K., East, J., and Francson, R. C., 1984, Modulation of phospholipase A2 activity associated with human sperm membranes by divalent cations and calcium antagonists, Biol. Reprod. 30: 679–686.PubMedCrossRefGoogle Scholar
  79. Usui, N., and Yanagimachi, R., 1986, Cytochemical localization of membrane-bound Mgt+-dependent ATPase activity in guinea pig sperm head before and during the acrosome reaction, Gamete Res. 13: 271–280.CrossRefGoogle Scholar
  80. Vijayasarathy, S., Shivaji, S., and Balaram, P., 1980, Plasma membrane bound Cat+-ATPase activity in bull sperm, FEBS Lett. 114: 45–49.PubMedCrossRefGoogle Scholar
  81. Waibel, R., Granet, R., Ficsor, G., and Ginsberg, L., 1985, Caproyl esterase from rat testis: purification and action on cumulus cells, Gamete Res. 12: 75–84.CrossRefGoogle Scholar
  82. Wasserman, P. M., 1987, Early events in mammalian fertilization, Annu. Rev. Cell Biol. 3: 109–142.CrossRefGoogle Scholar
  83. Working, P. K., and Meizel, S., 1982, Preliminary characterization of a MG2+-ATPase in hamster sperm head membranes, Biochem. Biophys. Res. Commun. 104: 1060–1065.PubMedCrossRefGoogle Scholar
  84. Yang, C.-H., and Srivastava, P N., 1974, Separation and properties of hyaluronidase from ram sperm acrosomes, J. Reprod. Fertil. 37: 17–25.PubMedCrossRefGoogle Scholar
  85. Yang, C.-H., and Srivastava, P. N., 1975, Purification and properties of hyaluronidase from bull sperm, J. Biol. Chem. 250: 79–83.PubMedGoogle Scholar
  86. Yanigmachi, R., 1988, Mammalian fertilization, in: The Physiology of Reproduction ( E. Knobil and J. Neill, eds.), Raven Press, New York, pp. 135–185.Google Scholar
  87. Yotsumoto, H., Sato, S., and Shibuya, M., 1984, Localization of angiotension converting enzyme (dipeptidyl carboxypeptidase) in swine sperm by immunofluorescence, Life Sci. 35: 1257–1261.PubMedCrossRefGoogle Scholar
  88. Zaneveld, L. J. D., and Polakoski, K. L., 1976, Biochemistry of human spermatozoa, in: Human Semen and Fertility Regulation in Men ( E. S. E. Haffez, ed.), C. V. Mosby, St. Louis, pp. 167–175.Google Scholar
  89. Zaneveld, L. J. D., and Williams, W. L., 1970, A sperm enzyme that disperses the corona radiata and its inhibition by decapacitation factor, Biol. Reprod. 2: 363–368.PubMedCrossRefGoogle Scholar
  90. Zaneveld, L. J. D., Polakoski, K. L., and Schumacher, G. F. B., 1973, Properties of acrosomal hyaluronidase from bull spermatozoa, J. Biol. Chem. 248: 564–570.PubMedGoogle Scholar
  91. Zaneveld, L. J. D., Polakoski, K. L., and Shumacher, G. F. B., 1975, The proteolytic enzyme systems of mammalian genital tract secretions and spermatozoa, in: Proteases and Biological Control ( E. Reich, D. Rifkin, and E. Shaws, eds.), Cold Spring Harbor Laboratory, New York, pp. 683–706.Google Scholar
  92. Zaneveld, L. J. D., De Jonge, C. J., Anderson, R. A., and Mack, S. R., 1991, Human sperm capacitation and the acrosome reaction, Hum. Reprod. (In press).Google Scholar

Copyright information

© Springer Science+Business Media New York 1991

Authors and Affiliations

  • L. J. D. Zaneveld
    • 1
  • C. J. De Jonge
    • 2
  1. 1.Department of Obstetrics and Gynecology, and Department of BiochemistryRush University, Rush-Presbyterian-St. Luke’s Medical CenterChicagoUSA
  2. 2.Department of Obstetrics and GynecologyRush University, Rush-Presbyterian-St. Luke’s Medical CenterChicagoUSA

Personalised recommendations