IBYME   02675
INSTITUTO DE BIOLOGIA Y MEDICINA EXPERIMENTAL
Unidad Ejecutora - UE
artículos
Título:
Sperm N-acetylglucosaminidase is involved in primary binding to the zona pellucida
Autor/es:
KARINA ZITTA; EVA WERTHEIMER; PATRICIA V. MIRANDA
Revista:
MOLECULAR HUMAN REPRODUCTION.
Editorial:
Oxford Journals
Referencias:
Lugar: Oxford; Año: 2006 vol. 12 p. 557 - 563
ISSN:
1360-9947
Resumen:
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 since it has been involved in ZP
binding and penetration, and polyspermy block. In the present study the
involvement of NAG during sperm interaction with the zona pellucida (ZP) was
analyzed. 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 in vitro
fertilization (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-egg 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.