Hostname: page-component-586b7cd67f-t7fkt Total loading time: 0 Render date: 2024-11-26T08:38:05.397Z Has data issue: false hasContentIssue false
  • English
  • Français

Acrosin activity in spermatozoa from sterile t6/tw32 and fertile control mice

Published online by Cambridge University Press:  14 April 2009

Ram Devi Mittal ,
Geraldine Wileman  and
Nina Hillman
Ram Devi Mittal
Affiliation:
Department of Biology, Temple University, Philadelphia, PA 19122
Geraldine Wileman
Affiliation:
Department of Biology, Temple University, Philadelphia, PA 19122
Nina Hillman*
Affiliation:
Department of Biology, Temple University, Philadelphia, PA 19122
*
*Corresponding author.
Rights & Permissions [Opens in a new window]

Summary

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

Spermatozoa from sterile t6/tw32 and control fertile + / +, T/tw32, T/t6 mice were compared for their abilities to hydrolyse protein matrices and for their levels of acrosin activity. The data show that the immature and mature gametes from both the experimental and control males hydrolyse protein matrices. The quantitative acrosin assays show, however, that the mature gametes from the intercomplement males have significantly less total acrosin activity than any of the control groups of gametes. These findings suggest that this reduced acrosin activity is an additional phenotypic expression of the intercomplement genotype which results in male sterility.

Type
Research Article
Information
Genetics Research , Volume 54 , Issue 2 , October 1989 , pp. 143 - 148
Copyright
Copyright © Cambridge University Press 1989

References

Bennett, D. & Dunn, L. C. (1967). Studies of effects of t-alleles in the house mouse on spermatozoa. I. Male sterility effects. Journal of Reproduction and Fertility 13, 421–428.CrossRefGoogle ScholarPubMed
Bhattacharyya, A. K., Goodpasture, J. C. & Zaneveld, L. J. D. (1979). Acrosin of mouse spermatozoa. American Journal of Physiology 237, E40–E44.Google ScholarPubMed
Brackett, B. G., Hall, J. L. & Oh, Y. (1978). In vitro fertilizing ability of testicular, epididymal, and ejaculated rabbit spermatozoa. Fertility and Sterility 29, 571–582.CrossRefGoogle ScholarPubMed
Brown, C. R. (1983). Purification of mouse sperm acrosin, its activation from proacrosin and effect on homologous egg investments. Journal of Reproduction and Fertility 69, 289–295.CrossRefGoogle ScholarPubMed
Brown, C. R. & Harrison, R. A. P. (1978). The activation of proacrosin in spermatozoa from ram, bull and boar. Biochimica et Biophysica Acta 526, 202–217.CrossRefGoogle ScholarPubMed
Bryson, V. (1944). Spermatogenesis and fertility in Mus musculus as affected by factors at the T locus. Journal of Morphology 74, 131–185.CrossRefGoogle Scholar
Chesley, P. (1935). Development of the short-tailed mutant in the house mouse. Journal of Experimental Zoology 70, 429–459.CrossRefGoogle Scholar
Fraser, L. R. (1982). p-Aminobenzamidine, an acrosin inhibitor, inhibits mouse sperm penetration of the zona pellucida but not the acrosome reaction. Journal of Reproduction and Fertility 65, 185–194.CrossRefGoogle Scholar
Fraser, L. R. & Drury, L. M. (1975). The relationship between sperm concentration and fertilization in vitro of mouse eggs. Biology of Reproduction 13, 513–518.CrossRefGoogle ScholarPubMed
Gaddum-Rosse, P. & Blandau, R. J. (1972). Comparative studies on the proteolysis of fixed gelatin membranes by mammalian sperm acrosomes. American Journal of Anatomy 134, 133–143.CrossRefGoogle ScholarPubMed
Garner, D. L. & Easton, M. P. (1977). Immunofluorescent localization of acrosin in mammalian spermatozoa. Journal of Experimental Zoology 200, 157–162.CrossRefGoogle ScholarPubMed
Georgiev, G. Kh. (1983). The acrosome - protein composition and function. Soviet Journal of Developmental Biology 14, 185–191.Google ScholarPubMed
Goodpasture, J. C., Reddy, J. M. & Zaneveld, L. J. D. (1981). Acrosin, proacrosin, and acrosin inhibitor of guinea pig spermatozoa capacitated and acrosomereacted in vitro. Biology of Reproduction 25, 44–55.CrossRefGoogle ScholarPubMed
Green, D. P. L. (1978). The activation of proteolysis in the acrosome reaction of guinea-pig sperm. Journal of Cell Science 32, 153–164.CrossRefGoogle ScholarPubMed
Green, D. P. L. & Hockaday, A. R. (1978). The histochemical localization of acrosin in guinea-pig sperm after the acrosome reaction. Journal of Cell Science 32, 177–184.CrossRefGoogle ScholarPubMed
Harrison, R. A. P., Fléchon, J.-E. & Brown, C. R. (1982). The localization of acrosin and proacrosin in ram spermatozoa. Journal of Reproduction and Fertility 66, 349–358.CrossRefGoogle Scholar
Hartree, E. F. & Srivastava, P. N. (1965). The chemical composition of the acrosomes of ram spermatozoa. Journal of Reproduction and Fertility 9, 47–61.CrossRefGoogle ScholarPubMed
Katz, D. F. & deMestre, N. J. (1985). Thrust generation by mammalian spermatozoa against the zona pellucida. Biophysical Journal 47, 123a abstr. 154.Google Scholar
Lyon, M. F. (1986). Male sterility of the mouse t-complex is due to homozygosity of the distorter genes. Cell 44. 357–363.CrossRefGoogle ScholarPubMed
Lyon, M. F. (1987). Distorter genes of the mouse t-complex impair male fertility when heterozygous. Genetical Research 49, 57–60.CrossRefGoogle ScholarPubMed
Mack, S., Bhattacharyya, A. K., Joyce, C., van der Ven, H. & Zaneveld, L. J. D. (1983). Acrosomal enzymes of human spermatozoa before and after in vitro capacitation. Biology of Reproduction 28, 1032–1042.CrossRefGoogle ScholarPubMed
McGrath, J. & Hillman, N. (1980 a). Sterility in mutant (tLx/tLy) male mice. III. In vitro fertilization. Journal of Embryology and Experimental Morphology 59. 49–58.Google ScholarPubMed
McGrath, J. & Hillman, N. (1980 b). The in vitro transmission frequency of the t 6 allele. Nature 283, 479–481.CrossRefGoogle ScholarPubMed
McRorie, R. A. & Williams, W. L. (1974). Biochemistry of mammalian fertilization. Annual Review of Biochemistry 43, 777–803.CrossRefGoogle ScholarPubMed
Morton, D. B. (1975). Acrosomal enzymes: immunochemical localization of acrosin and hyaluronidase in ram spermatozoa. Journal of Reproduction and Fertility 45, 375–378.CrossRefGoogle ScholarPubMed
Müller-Esterl, W. & Fritz, H. (1981). Sperm acrosin. Methods in Enzymology 80, 621–632.CrossRefGoogle ScholarPubMed
Nadijcka, M. & Hillman, N. (1974). Ultrastructural studies of the mouse blastocyst substages. Journal of Embryology and Experimental Morphology 32, 675–695.Google ScholarPubMed
Penn, A., Gledhill, B. L. & Darżynkiewicz, Z. (1972). Modification of the gelatin substrate procedure for demonstration of acrosomal proteolytic activity. Journal of Histochemistry and Cytochemistry 20, 499–506.CrossRefGoogle ScholarPubMed
Phi-Van, L., Müller-Esterl, W., Flörke, S., Schmid, M. & Engel, W. (1983). Proacrosin and the differentiation of the spermatozoa. Biology of Reproduction 29, 479–486.CrossRefGoogle ScholarPubMed
Polakoski, K. L. & McRorie, R. A. (1973). Boar acrosin. II. Classification, inhibition and specificity studies of a proteinase from sperm acrosomes. Journal of Biological Chemistry 248, 8183–8188.CrossRefGoogle ScholarPubMed
Polakoski, K. L., Zahler, W. L. & Paulson, J. D. (1977). Demonstration of proacrosin and quantitation of acrosin in ejaculated human spermatozoa. Fertility and Sterility 28, 668–670.CrossRefGoogle ScholarPubMed
Richardson, K. C., Jarett, L. & Finke, E. H. (1960). Embedding in epoxy resin for ultrathin sectioning in electron microscopy. Stain Technology 35, 313–323.CrossRefGoogle ScholarPubMed
Schwert, G. W. & Takenaka, Y. (1955). A spectro-photometric determination of trypsin and chymotrypsin. Biochimica et Biophysica Acta 16, 570–575.CrossRefGoogle Scholar
Stambaugh, R., Brackett, B. C. & Mastronianni, L. (1969). Inhibition of in vitro fertilization of rabbit ova by trypsin inhibitors. Biology of Reproduction 1, 223–227.CrossRefGoogle ScholarPubMed
Stambaugh, R. & Buckley, J. (1969). Identification and subcellular localization of the enzymes effecting penetration of the zona pellucida by rabbit spermatozoa. Journal of Reproduction and Fertility 19, 423–432.CrossRefGoogle ScholarPubMed
Whitaker, J. R. & Bender, H. E. (1965). Kinetics of papain-catalyzed hydrolysis of α-N-benzoyl-L-arginine ethyl ester and α-N-benzoyl-L-argininamide. Journal of the American Chemical Society 87, 2728–2737.CrossRefGoogle ScholarPubMed
Wolf, D. P., Inoue, M. & Stark, R. A. (1976). Penetration of zona free mouse ova. Biology of Reproduction 15, 213–221.CrossRefGoogle ScholarPubMed
Zaneveld, L. J. D., Robertson, R. T., Kessler, M. & Williams, W. L. (1971). Inhibition of fertilization in vivo by pancreatic and seminal plasma trypsin inhibitors. Journal of Reproduction and Fertility 25, 387–392.CrossRefGoogle ScholarPubMed
Zaneveld, L. J. D., Robertson, R. T. & Williams, W. L. (1970). Synthetic enzyme inhibitors as antifertility agents. FEBS Letters 11, 345–349.CrossRefGoogle Scholar