Differential influence of recombinant non-glycosylated and glycosylated glycodelin on human sperm function: comparative studies with hamster spermatozoa
B. Dutta et al., Differential influence of recombinant non-glycosylated and glycosylated glycodelin on human sperm function: comparative studies with hamster spermatozoa, REPROD FERT, 13(2-3), 2001, pp. 111-118
Glycodelin, also known as placental protein 14, has been implicated in endo
metriosis-related infertility. To determine the role of glycodelin and its
glycosylated state, the influence of recombinant nonglycosylated-glycodelin
(nongly-glycodelin) and glycosylated-glycodelin (gly-glycodelin) on human
sperm function was evaluated. Whereas there was a significant (P <0.001) in
crease in the capacitation of nongly-glycodelin-treated spermatozoa compare
d with untreated controls (28.8 +/- 1.0% v. 21 +/- 1.5% respectively), trea
tment of spermatozoa with gly-glycodelin markedly (P <0.001) inhibited capa
citation (10.7 +/- 0.3%); acrosome reaction (AR) remained unaltered in all
treatments. In a zona-free hamster egg penetration assay, the egg penetrati
on index was higher (P <0.001) with nongly-glycodelin-treated spermatozoa (
3.4 +/- 0.3) than with gly-glycodelin-treated spermatozoa (0.4 +/- 0.1) and
untreated spermatozoa (1.6 +/- 0.2). A similar influence of glycodelin on
capacitation was observed with hamster spermatozoa. However, the AR rate wa
s higher (P <0.01) in nongly-glycodelin-treated spermatozoa (39.4 +/- 1.6%)
than in either gly-glycodelin-treated spermatozoa (19.3 +/- 2.0%) or untre
ated controls (30.0 +/- 1.2%). Moreover, the in vitro fertilization rate wa
s significantly (P <0.01) higher with nongly-glycodelin treated-spermatozoa
compared with untreated spermatozoa (77.5 +/- 2.3% v. 52.9 +/- 4.3%) and g
ly-glycodelin-treated spermatozoa (38.3 +/- 6.5%; P <0.05). These results i
ndicate that whereas nongly-glycodelin improves, gly-glycodelin inhibits, c
apacitation and fertilization potential of human and hamster spermatozoa, a
nd that the glycosylation status of glycodelin deter-mines its influence on
sperm function.