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J. Biol. Chem., Vol. 278, Issue 15, 13570-13577, April 11, 2003
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From the Previous studies showed that zona binding
inhibitory factor-1 (ZIF-1) was the glycoprotein mainly responsible for
the spermatozoa zona binding inhibitory activity of human
follicular fluid. ZIF-1 has a number of properties similar to
glycodelin-A. A binding kinetics experiment in the present study
demonstrated the presence of two binding sites of ZIF-1 on human
spermatozoa. These binding sites were saturable, reversible, and bound
to 125I-ZIF-1 in a time-, concentration-, and
temperature-dependent manner. Glycodelin-A shared one
common binding site with ZIF-1 on spermatozoa, and it could displace
only 70% of the 125I-ZIF-1 bound on human spermatozoa.
ZIF-1 and glycodelin-A formed complexes with the soluble extract of
human spermatozoa. Coincubation of solubilized zona pellucida proteins
reduced the binding of ZIF-1 to two complexes of the extract,
suggesting that the ZIF-1 binding sites and zona pellucida protein
receptors on human spermatozoa were closely related. ZIF-1, but not
glycodelin-A, significantly suppressed progesterone-induced acrosome
reaction of human spermatozoa. The carbohydrate moieties derived from
ZIF-1 reduced the binding of native ZIF-1 on human spermatozoa as well
as the zona binding inhibitory activity of the glycoprotein, although
the intensity of the effects are lower when compared with the native
protein. These effects are not due to the action of the molecules on
the motility, viability, and acrosomal status of the treated
spermatozoa. Deglycosylated ZIF-1 had no inhibitory effect on both
ZIF-1 binding and zona binding capacity of spermatozoa. We concluded
that the carbohydrate part of ZIF-1 was critical for the functioning of the glycoprotein.
Binding of Zona Binding Inhibitory Factor-1 (ZIF-1) from Human
Follicular Fluid on Spermatozoa*
,, and¶
Department of Obstetrics and Gynaecology,
University of Hong Kong, Queen Mary Hospital, Hong Kong, Special
Administrative Region China and the § Department of
Obstetrics and Gynecology, University Central Hospital, Helsinki
FIN-00290, Finland
*
This work was supported by the Research Grant Council, Hong
Kong (Grants HKU7188/99 M and HKU7261/01M), University of Hong Kong,
Helsinki University Central Hospital Research Funds, Federation of the
Finnish Life and Pension Insurance Companies, the Cancer Society of
Finland, the Academy of Finland, and University of Helsinki.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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