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dc.creatorMoreno,Ricardo D
dc.creatorLaserre A,Andrea
dc.creatorBarros,Claudio
dc.date2011-01-01
dc.date.accessioned2019-05-02T21:22:00Z
dc.date.available2019-05-02T21:22:00Z
dc.identifierhttps://scielo.conicyt.cl/scielo.php?script=sci_arttext&pid=S0716-97602011000200006
dc.identifier.urihttp://revistaschilenas.uchile.cl/handle/2250/82122
dc.descriptionThe 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.
dc.formattext/html
dc.languageen
dc.publisherSociedad de Biología de Chile
dc.relation10.4067/S0716-97602011000200006
dc.rightsinfo:eu-repo/semantics/openAccess
dc.sourceBiological Research v.44 n.2 2011
dc.subjectFertilization
dc.subjectacrosin
dc.subjectacrosome
dc.subjectzona pellucida
dc.subjectsperm
dc.titleProtease activity involvement in the passage of mammalian sperm through the zona pellucida


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