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Molecular Human Reproduction, Vol. 6, No. 8, 699-706, August 2000
© 2000 European Society of Human Reproduction and Embryology

Embryo development

Evidence for the participation of ß-hexosaminidase in human sperm–zona pellucida interaction in vitro

Patricia V. Miranda1,4, Fernanda González-Echeverría2, Jorge A. Blaquier2, Don J. Mahuran3 and Jorge G. Tezón1

1 Instituto de Biología y Medicina Experimental (CONICET), Buenos Aires, 2 Fertilab, Buenos Aires, Argentina and 3 Research Institute, Hospital for Sick Children, Toronto, Ontario, Canada

Abstract

Mammalian sperm–zona pellucida (ZP) interaction is mediated by sperm lectin-like proteins and ZP glycoproteins. We have previously reported the participation of binding sites for N-acetylglucosamine (GlcNAc) residues in human sperm function, including sperm interaction with the ZP. Additionally, previous results from our laboratory suggested that some of these events may be mediated by the glycosidase N-acetylglucosaminidase (ß-hexosaminidase, Hex, in mammals). In this study, we report the possible participation of Hex in human sperm–ZP interaction. Human recombinant Hex (hrHex) was obtained by expression in a stable transfected CHO cell line. When the recombinant enzyme was present during hemizona (HZ) assays, the number of sperm bound per HZ was significantly reduced. The same result was obtained when HZ were preincubated with hrHex. Additionally, the presence of a Hex-specific substrate during the HZ assay produced the same inhibitory effect. These results suggest the participation of a sperm Hex in the interaction with human ZP in vitro.

ß-hexosaminidase/fertilization/spermatozoa/sperm-zona binding/zona pellucida

Notes

4 To whom correspondence should be addressed at: Instituto de Biología y Medicina Experimental, Vuelta de Obligado 2490, (1428) Buenos Aires, Argentina. E-mail: pmiranda{at}dna.uba.ar


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