Affiliation:
1. University Department of Obstetrics and Gynaecology, Jessop Hospital for Women, Leavygreave Road, Sheffield S3 7RE, U.K.
2. Krebs Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, P.O. Box 594, Firth Court, Western Bank, Sheffield S10 2UH, U.K.
3. University Department of Medicine, Wolfson Research Laboratories, Birmingham Women's Hospital, Edgbaston, Birmingham B15 2TG, U.K.
Abstract
Human gamete interaction is of fundamental biological importance, yet the molecular interactions between spermatozoa and the zona pellucida are poorly understood. Surprisingly, the role of the polypeptide backbone of zona pellucida glycoprotein 3 (ZP3), the putative ligand for spermatozoa activation, has been largely overlooked. Purified recombinant human ZP3 was expressed in Escherichia coli as a C-terminal fusion to the dimeric glutathione S-transferase (GST) from Schistosoma japonicum and was shown to induce acrosomal exocytosis in live, capacitated human spermatozoa. The level of exocytosis is comparable with that obtained using purified, glycosylated, recombinant human ZP3 [van Duin, M., Polman, J. E. M., DeBreet, I. T. M., Van Ginneken, K., Bunschoten, H., Grootenhuis, A., Brindle, J. and Aitken, R. J. (1994). Biol Reprod. 51, 607-617]. These data imply that the polypeptide chain of human ZP3 contributes to recognition of spermatozoa during acrosomal exocytosis in vitro.
Subject
Cell Biology,Molecular Biology,Biochemistry
Cited by
38 articles.
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