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vol.44 issue2Acrosin release and acrosin activity during incubation in capacitating media using fresh and frozen-thawed dog spermModulation of spermatozoon acrosome reaction author indexsubject indexarticles search
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Biological Research

Print version ISSN 0716-9760

Abstract

MORENO, Ricardo D; LASERRE A, Andrea  and  BARROS, Claudio. Protease activity involvement in the passage of mammalian sperm through the zona pellucida. Biol. Res. [online]. 2011, vol.44, n.2, pp.145-150. ISSN 0716-9760.  http://dx.doi.org/10.4067/S0716-97602011000200006.

The interaction between acrosome-reacted sperm and zona pellucida proteins is not yet fully understood. Serine protease acrosin and its zymogen proacrosin have been proposed to fulfill this function due to their capacity to bind zona pellucida glycoproteins. However, the molecular mechanism underlying this interaction has been merely speculative. Here we show that fucoidan (a sulfated polysaccharide) and solubilized zona pellucida glycoproteins, but not soybean trypsin inhibitor, are able to detach bound spermatozoa, which suggests that live sperm binds to the zona pellucida in a non-enzymatical way. Interestingly, mild proteolytic digestion with acrosin or trypsin does not modify the structure of the zona pellucida, but rather results in fewer spermatozoa binding to the zona. These results agree with a model where the active site of acrosin digests the zona pellucida and binds through the polysulfate-binding domain through a three-dimensional zona structure rather than a single ligand.

Keywords : Fertilization; acrosin; acrosome; zona pellucida; sperm.

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