Skip Navigation


Mol. Hum. Reprod. Advance Access originally published online on July 7, 2006
Molecular Human Reproduction 2006 12(9):557-563; doi:10.1093/molehr/gal059
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow All Versions of this Article:
12/9/557    most recent
gal059v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (3)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Zitta, K.
Right arrow Articles by Miranda, P. V.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zitta, K.
Right arrow Articles by Miranda, P. V.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2006. Published by Oxford University Press on behalf of the European Society of Human Reproduction and Embryology. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org

Sperm N-acetylglucosaminidase is involved in primary binding to the zona pellucida

Karina Zitta, Eva V. Wertheimer and Patricia V. Miranda1

Instituto de Biología y Medicina Experimental, CONICET, Buenos Aires, Argentina

1 To whom correspondence should be addressed at: Instituto de Biologia y Medicina Experimental, Vuelta de Obligado 2490, (C1428ADN) Buenos Aires, Argentina. E-mail: pmiranda{at}dna.uba.ar

The glycosidase-recognizing N-acetylglucosamine terminal residue, N-acetylglucosaminidase (NAG), has been repetitively implicated in fertilization. Nevertheless, its role in the multiple steps comprising this process is a matter of debate because it has been involved in zona pellucida (ZP) binding and penetration and polyspermy block. In this study, the involvement of NAG during sperm interaction with the ZP was analysed. Soluble ZP was able to inhibit sperm NAG activity, suggesting that it can be recognized as a ligand by this enzyme. Sperm–ZP binding assays were carried out under conditions where acrosome reaction (AR) could not take place (salt-stored oocytes and a modified medium where Ca2+ was replaced by Sr2+). Different NAG-specific reagents—an inhibitor (2-acetamido-2-deoxy-D-glucono-1,5-lactone), a substrate (p-nitrophenyl-N-acetylglucosaminide) and an anti-NAG antibody—were able to impair sperm binding to the ZP when present during these assays. The lactone was also able to inhibit oocyte penetration during IVF assays, although not when present after primary binding had taken place. This result was not related to the interference of lactone with AR or zona penetrability. Exogenous NAG also inhibited sperm–oocyte interaction when present during binding and IVF assays or used for oocyte pre-incubation. These results suggest the participation of NAG in sperm primary binding to the ZP.

Key words: N-acetylglucosaminidase/primary binding/sperm/zona binding


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.