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Sci Rep. 2016 Sep 7;6:32556. doi: 10.1038/srep32556.

The C-terminal region of OVGP1 remodels the zona pellucida and modifies fertility parameters.

Author information

1
Department of Cell Biology and Histology, School of Medicine, University of Murcia, Campus Mare Nostrum and IMIB-Arrixaca, Murcia, Spain.
2
Department of Biosciences and Nutrition &Center for Innovative Medicine, Karolinska Institutet, Huddinge, Sweden.
3
Department of Physiology, Faculty of Veterinary, University of Murcia, Campus Mare Nostrum and IMIB-Arrixaca, Murcia, Spain.

Abstract

OVGP1 is the major non-serum glycoprotein in the oviduct fluid at the time of fertilization and early embryo development. Its activity differs among species. Here, we show that the C-terminal region of recombinant OVGP1 regulates its binding to the extracellular zona pellucida and affects its activity during fertilization. While porcine OVGP1 penetrates two-thirds of the thickness of the zona pellucida, shorter OVGP1 glycoproteins, including rabbit OVGP1, are restricted to the outer one-third of the zona matrix. Deletion of the C-terminal region reduces the ability of the glycoprotein to penetrate through the zona pellucida and prevents OVGP1 endocytosis. This affects the structure of the zona matrix and increases its resistance to protease digestion. However, only full-length porcine OVGP1 is able to increase the efficiency rate of in vitro fertilization. Thus, our findings document that the presence or absence of conserved regions in the C-terminus of OVGP1 modify its association with the zona pellucida that affects matrix structure and renders the zona matrix permissive to sperm penetration and OVGP1 endocytosis into the egg.

PMID:
27601270
PMCID:
PMC5013273
DOI:
10.1038/srep32556
[Indexed for MEDLINE]
Free PMC Article

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