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Interactions between a decapacitation factor and mouse spermatozoa appear to involve fucose residues and a GPI‐anchored receptor
Author(s) -
Fraser Lynn R.
Publication year - 1998
Publication title -
molecular reproduction and development
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.745
H-Index - 105
eISSN - 1098-2795
pISSN - 1040-452X
DOI - 10.1002/(sici)1098-2795(199810)51:2<193::aid-mrd9>3.0.co;2-l
Subject(s) - fucose , capacitation , biology , receptor , biochemistry , endogeny , microbiology and biotechnology , glycoprotein , in vitro
Epididymal mouse spermatozoa have a surface‐associated decapacitation factor (DF) that can be removed precociously by centrifugation, resulting in acceleration of capacitation and increased fertilizing ability. Addition of exogenous DF to capacitated suspensions inhibits fertilizing ability and reverses capacitation in acrosome‐intact cells. DF appears to regulate a Ca 2+ ‐ATPase, located primarily in the postacrosomal region. The present investigations of DF↮spermatozoon interaction indicate that DF can be removed from uncapacitated cells by treatment with phosphatidylinositol‐specific phospholipase C (PIC), suggesting the involvement of a glycosylphosphatidylinositol (GPI) moiety. However, exogenous DF cannot reassociate with PIC‐treated spermatozoa, suggesting that DF may bind to spermatozoa via a GPI‐anchored receptor. DF binding appears to involve fucose residues, since depletion of endogenous DF followed by brief exposure to fucose (0.1–10 mM) prevented DF reassociation with cells. Furthermore, 5 mM fucose could displace DF from uncapacitated cells, accelerating capacitation and resulting in a higher proportion of fertilized oocytes, with increased polyspermy, than obtained with untreated controls. FITC‐labelled fucosylated BSA bound specifically to the postacrosomal region, binding being inhibited by both excess fucose and crude DF. UEA I, a lectin with specificity for fucose residues, bound to the postacrosomal region of cells preincubated in fucose but not crude DF, and blocked DF binding to DF‐depleted cells. These results are consistent with the DF binding, via fucose residues, to a GPI‐anchored receptor. Fucose binding sites are in the same region where Ca 2+ ‐ATPase, the enzyme regulated by DF, has been localized; these results support the hypothesis that DF modulates capacitation by regulating enzyme activity and hence the intracellular Ca 2+ concentration. Mol. Reprod. Dev. 51:193–202, 1998. © 1998 Wiley‐Liss, Inc.