IMR Press / FBL / Volume 13 / Issue 17 / DOI: 10.2741/3185

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Article
Structural changes of the zona pellucida during fertilization and embryo development
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1 Laboratory of Electron Microscopy “Pietro M. Motta”, Department of Anatomy, University of Rome “La Sapienza”, Via A. Borelli, 50, 00161 - Rome, Italy
2 Monash Institute of Medical Research (MIMR), Monash University, Victoria 3800, Australia

*Author to whom correspondence should be addressed.

 

Front. Biosci. (Landmark Ed) 2008, 13(17), 6730–6751; https://doi.org/10.2741/3185
Published: 1 May 2008
Abstract

The zona pellucida (ZP) is a unique extracellular coat surrounding the maturing oocyte, during ovulation, fertilization, and early embryo development. It is formed by three/four glycoproteins. Ultrastructural data obtained with transmission (TEM) and scanning electron microscopy (SEM) were compared with molecular data on the glycoproteins network from ovulation to blastocyst formation. Molecular models are quite different to the morphology obtained with TEM, which shows a microfibrillar architecture, or with SEM, which shows a spongy or smooth surface. The saponin-ruthenium red-osmium tetroxide-thiocarbohydrazide technique allows to show the ZP real microfilamentous structure and the related functional changes. These results support an ultrastructural supramolecular model, more similar and comparable to molecular models related with the glycoprotein network. A detailed mapping of single mammalian ZP proteins and their relationship within the supramolecular architecture of the zona matrix would clearly supply insights into the molecular basis of sperm-egg recognition. Differences in ZP glycoproteins among mammals do not affect structural morphology; further studies are needed to clarify the relationships between ultrastructural and molecular organizations.

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