Molecular Human Reproduction, Vol 4, 1136-1144, Copyright © 1998 by Oxford University Press
IA Brewis, R Clayton, CE Browes, M Martin, CL Barratt, DP Hornby and HD Moore
Protein tyrosine phosphorylation and induction of the acrosome reaction
(AR) in non-capacitated and capacitated human spermatozoa was investigated
in response to recombinant human zona pellucida glycoprotein (rhZP3)
produced by Chinese hamster ovary cells transfected with a plasmid
containing human ZP3 cDNA. rhZP3-containing medium promoted the AR in a
high proportion of capacitated spermatozoa (48.6 +/- 3.2%; P < 0.01)
compared with control (no rhZP3) samples (14.8 +/- 2.1%). However,
rhZP3-containing medium did not cause increased acrosomal exocytosis in
non-capacitated spermatozoa (16.8 +/- 3.0%). Induction of the AR was
associated with increased tyrosine phosphorylation of a 95 +/- 5 kDa
epitope only in capacitated spermatozoa. A dose-dependent increase in the
protein phosphorylation of a 95 kDa epitope in response to rhZP3 was
detected by [gamma-32P]- ATP labelling of detergent-solubilized sperm
proteins. When spermatozoa were co-incubated with monoclonal antibody 97.25
(mAb 97.25) recognizing a 95 kDa tyrosine kinase epitope, there was no
rhZP3 induction of tyrosine phosphorylation of the 95 kDa protein. Such co-
incubation also markedly inhibited the AR (23.9 +/- 3.1%). These results
support the model that initial interaction of the fertilizing spermatozoon
with ZP3 involves the tyrosine phosphorylation of a 95 kDa tyrosine kinase
protein and that this requires capacitation.
JOURNAL ARTICLE
Tyrosine phosphorylation of a 95 kDa protein and induction of the acrosome reaction in human spermatozoa by recombinant human zona pellucida glycoprotein 3
Department of Molecular Biology and Biotechnology, The University of Sheffield, UK.
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