XB-ART-2894
Biochem Biophys Res Commun
2004 Nov 12;3242:648-54. doi: 10.1016/j.bbrc.2004.09.099.
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Proteolysis of Xenopus laevis egg envelope ZPA triggers envelope hardening.
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The egg envelope of most animal eggs is modified following fertilization, resulting in the prevention of polyspermy and hardening of the egg envelope. In frogs and mammals a prominent feature of envelope modification is N-terminal proteolysis of the envelope glycoprotein ZPA. We have purified the ZPA protease from Xenopus laevis eggs and characterized it as a zinc metalloprotease. Proteolysis of isolated egg envelopes by the isolated protease resulted in envelope hardening. The N-terminal peptide fragment of ZPA remained disulfide bond linked to the ZPA glycoprotein moiety following proteolysis. We propose a mechanism for egg envelope hardening involving ZPA proteolysis by an egg metalloprotease as a triggering event followed by induction of global conformational changes in egg envelope glycoproteins.
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Species referenced: Xenopus laevis
Genes referenced: zp2