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Brief Note : Proacrosin-acrosin activity in capacitated and acrosome reacted sperm from cryopreserved bovine semen

M. I. ROSATTI, M. T. BECONI, M. CÓRDOBA
Area of Biochemistry, School of Veterinary Sciences, University of Buenos Aires, Argentina
Address correspondence to: Dra. Martha T. Beconi. Area de Química Biológica. Facultad de Ciencias Veterinarias, UBA. Chorroarín 280, (1427) Buenos Aires, ARGENTINA. E-mail: Quimbiol@fvet.uba.ar

BIOCELL 2004, 28(3), 311-316. https://doi.org/10.32604/biocell.2004.28.311

Abstract

Acrosin activity is associated with normal fertility in human and bovine spermatozoa. The aim of the study was to determine the variation of the enzyme activity in the proacrosin-acrosin system in capacitated and acrosome reacted cryopreserved bovine sperm. Enzyme activity was assessed spectrophotometrically using N-α-benzoyl-DL-arginine p-nitroanilide (BAPNA) as specific substrate for acrosin at pH 8. Capacitation with heparin and quercitin failed to induce conversion of proacrosin to acrosin. An increase in acrosin activity produced by the presence of progesterone, in a dose-dependent manner, was related with the induction of true acrosome reaction. The total level of acrosin activity registered showed that 96% of acrosin of capacitated sperm samples and control is present in the zymogen form. Moreover, progesterone is capable of duplicating the level of active enzyme, indicating that enzyme activity changes are related to acrosome reaction, suggesting that only a minor proportion of the total of proacrosin-acrosin system is required in the exocytotic process on cryopreserved bovine sperm.

Keywords

bovine sperm, proacrosin-acrosin, heparin, quercitin, progesterone

Cite This Article

I., M. (2004). Brief Note : Proacrosin-acrosin activity in capacitated and acrosome reacted sperm from cryopreserved bovine semen. BIOCELL, 28(3), 311–316.

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This work is licensed under a Creative Commons Attribution 4.0 International License , which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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