Mol. Hum. Reprod. Advance Access published online on October 29, 2004
Molecular Human Reproduction, doi:10.1093/molehr/gah122
© 2004 by Oxford University Press
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1 Instituto de Biología y Medicina Experimental--CONICET, Buenos Aires, C1428ADN, Argentina
* To whom correspondence should be addressed. Glycoproteins and lectin-like proteins mediate sperm-zona pellucida interaction. The present study analysed the participation of carbohydrates in the different stages of sperm interaction with the zona pellucida in hamster, by determining the effects of different monosaccharides. N-acetylglucosamine (GlcNAc, 1 mM) reduced sperm ability to bind to the zona pellucida. Surprisingly, spontaneous acrosome reaction (AR) was also inhibited by this sugar. In order to analyse the effect of GlcNAc on sperm-zona pellucida binding, independent of its effect on the AR, strontium (Sr) was used as a calcium (Ca) replacement in the sperm capacitation and co-incubation medium. Sr seemed to be able to replace Ca for sperm capacitation, at least when measured as the ability to bind to the zona pellucida, and undergo AR when Ca is provided. Moreover, sperm-zona pellucida binding could also take place in a Sr-modified medium. When binding assays were carried out in the Sr medium, GlcNAc also produced an inhibitory effect. This could be reproduced when sperm, but not oocytes, were pre-incubated with the monosaccharide. IVF assays were also carried out to analyse the participation of GlcNAc in the different steps of sperm-oocyte interaction. Taken together, the results support the involvement of the GlcNAc residues of the zona pellucida in the early steps of the interaction with sperm. *These authors contributed equally to this paper.
Revised September 28, 2004
Accepted October 4, 2004
Article
Analysis of the participation of N-acetylglucosamine in the different steps of sperm-zona pellucida interaction in hamster
Patricia V. Miranda, E-mail: pmiranda{at}dna.uba.ar
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K. Zitta, E. V. Wertheimer, and P. V. Miranda Sperm N-acetylglucosaminidase is involved in primary binding to the zona pellucida Mol. Hum. Reprod., September 1, 2006; 12(9): 557 - 563. [Abstract] [Full Text] [PDF] |
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