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Gene Review

ACR  -  acrosin

Bos taurus

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Disease relevance of ACR


High impact information on ACR


Biological context of ACR

  • Mapping of the gene encoding bovine preproacrosin (ACR) to chromosome BTA 5 region q35 [5].
  • We propose that the OMC regulates proacrosin release during the acrosome reaction and maintains elevated acrosin concentrations at the site of sperm-egg interaction [6].
  • Two-dimensional polyacrylamide gel electrophoresis revealed that the 42- and 41-kDa proteases were distinguished from acrosin by the isoelectric point and immunoreactivity with affinity-purified antibody against an oligopeptide corresponding to the N-terminal amino acid sequence of mouse proacrosin [7].
  • Evidence is presented that the acrosin light chain is connected via two disulfide bridges to the heavy chain which contains about 320 amino acids including the active-site residues of the proteinase [8].
  • It turned out that proacrosin/acrosin activity is first demonstrable in haploid spermatids, increases during spermiohistogenesis in the testis, and remains nearly constant in epididymal and ejaculated spermatozoa [9].

Anatomical context of ACR


Associations of ACR with chemical compounds

  • The proportion of sperm with active acrosin were determined using the biotinylated isocoumarin serine protease inhibitor, Bi-Aca-Aca-OMe-IC (BIC) [13].
  • A fraction of acrosomal proteins dispersed during calcium ionophore A23187-induced acrosome reaction was prepared from cauda epididymal sperm of wild-type and acrosin-deficient mice, rat, and hamster [7].
  • Caltrin I may play an important role in the control of sperm functions such as Ca(2+) influx in the acrosome reaction and activation of acrosin and other serine-proteases at the proper site and proper time to ensure successful fertilization [14].
  • This effect of heparin was time- and dose-dependent and was increased by the presence of the acrosin inhibitor benzamidine [15].
  • Acrosin (EC, the major proteinase of mammalian spermatozoa, has been demonstrated to be a two-chain glycoprotein with an Mr-4200 light chain covalently attached to an Mr-37000 heavy chain [8].

Other interactions of ACR

  • Cleavage specificity of boar acrosin on polypeptide substrates, ribonuclease and insulin B-chain [16].
  • Histones H2a, H2b, H3, and H4 associated with DNA are relatively resistant to acrosin [17].

Analytical, diagnostic and therapeutic context of ACR

  • 3. The standard procedure permits titrations of 20-100pmol of acrosin, i.e. amounts normally taken for conventional rate assays, and with these amounts the impurities present in crude enzme fractions did not interfere [4].
  • Significant differences (p < 0.05) were found among bulls in the proportion of sperm with activable proacrosin/acrosin both before and after cryopreservation [13].
  • The activable proacrosin/acrosin levels in bovine sperm were examined using fluorescent staining and flow cytometry [13].
  • It is concluded that, although active immunization with acrosin had no significant effect on fertility, the antibody titer produced may be a factor [10].
  • Twelve females received intradermal injections of purified acrosin in Freund's complete adjuvant followed by a booster injection 6 weeks later [10].


  1. Inhibition of hamster sperm acrosomal enzyme by gossypol is closely associated with the decrease in fertilization capacity. Yuan, Y.Y., Shi, Q.X. Contraception. (2000) [Pubmed]
  2. Stimulation of high-affinity GTPase by trypsin and trypsin-like proteinases in membranes of human platelets. Jakobs, K.H., Aktories, K. Biochem. J. (1988) [Pubmed]
  3. Studies on ram acrosin. Isolation from spermatozoa, activation by cations and organic solvents, and influence of cations on its reaction with inhibitors. Brown, C.R., Andani, Z., Hartree, E.F. Biochem. J. (1975) [Pubmed]
  4. Studies on ram acrosin. Fluorimetric titratiion of operational molarity with 4-methylumbelliferyl p-guanidinobenzoate. Brown, C.R., Andani, Z., Hartree, E.F. Biochem. J. (1975) [Pubmed]
  5. Mapping of the gene encoding bovine preproacrosin (ACR) to chromosome BTA 5 region q35. Friedl, R., Adham, I.M., Rottmann, O.J. Mamm. Genome (1994) [Pubmed]
  6. Proacrosin-acrosomal matrix binding interactions in ejaculated bovine spermatozoa. NagDas, S.K., Winfrey, V.P., Olson, G.E. Biol. Reprod. (1996) [Pubmed]
  7. Difference of acrosomal serine protease system between mouse and other rodent sperm. Yamagata, K., Honda, A., Kashiwabara, S.I., Baba, T. Dev. Genet. (1999) [Pubmed]
  8. Boar acrosin is a two-chain molecule. Isolation and primary structure of the light chain; homology with the pro-part of other serine proteinases. Fock-Nüzel, R., Lottspeich, F., Henschen, A., Müller-Esterl, W. Eur. J. Biochem. (1984) [Pubmed]
  9. Proacrosin/acrosin activity during spermiohistogenesis of the bull. Mansouri, A., Phi-van, L., Geithe, H.P., Engel, W. Differentiation (1983) [Pubmed]
  10. Active immunization of female rabbits with purified rabbit acrosin and effect on fertility. Syner, F.N., Kuras, R., Moghissi, K.S. Fertil. Steril. (1979) [Pubmed]
  11. Inhibition of human and bovine sperm acrosin by divalent metal ions. Possible role of zinc as a regulator of acrosin activity. Steven, F.S., Griffin, M.M., Chantler, E.N. Int. J. Androl. (1982) [Pubmed]
  12. Immunolocalization of proacrosin/acrosin in bovine sperm and sperm penetration through the zona pellucida. De los Reyes, M., Barros, C. Anim. Reprod. Sci. (2000) [Pubmed]
  13. Determination of activable proacrosin/acrosin in bovine sperm using an irreversible isocoumarin serine protease inhibitor. Palencia, D.D., Garner, D.L., Hudig, D., Holcombe, D.W., Burner, C.A., Redelman, D., Fernandez, G.C., Abuelyaman, A.S., Kam, C.M., Powers, J.C. Biol. Reprod. (1996) [Pubmed]
  14. Trypsin/acrosin inhibitor activity of rat and guinea pig caltrin proteins. Structural and functional studies. Winnica, D.E., Novella, M.L., Dematteis, A., Coronel, C.E. Biol. Reprod. (2000) [Pubmed]
  15. Effect of heparin on the expression of calmodulin-binding proteins in bull spermatozoa. Leclerc, P., Langlais, J., Lambert, R.D., Sirard, M.A., Chafouleas, J.G. J. Reprod. Fertil. (1989) [Pubmed]
  16. Cleavage specificity of boar acrosin on polypeptide substrates, ribonuclease and insulin B-chain. Schiessler, H., Schleuning, W.D., Fritz, H. Hoppe-Seyler's Z. Physiol. Chem. (1975) [Pubmed]
  17. Dispersion of mammalian sperm chromatin during fertilization: an in vitro study. Marushige, Y., Marushige, K. Biochim. Biophys. Acta (1978) [Pubmed]
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