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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
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pubmed:dateCreated |
1999-3-12
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Egg Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/zona pellucida glycoproteins
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1360-9947
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1136-44
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9872364-Acrosome Reaction,
pubmed-meshheading:9872364-Animals,
pubmed-meshheading:9872364-Antibodies, Monoclonal,
pubmed-meshheading:9872364-Blotting, Western,
pubmed-meshheading:9872364-Cricetinae,
pubmed-meshheading:9872364-Dose-Response Relationship, Drug,
pubmed-meshheading:9872364-Egg Proteins,
pubmed-meshheading:9872364-Epitopes,
pubmed-meshheading:9872364-Humans,
pubmed-meshheading:9872364-Male,
pubmed-meshheading:9872364-Membrane Glycoproteins,
pubmed-meshheading:9872364-Phosphorylation,
pubmed-meshheading:9872364-Receptors, Cell Surface,
pubmed-meshheading:9872364-Recombinant Proteins,
pubmed-meshheading:9872364-Spermatozoa,
pubmed-meshheading:9872364-Tyrosine,
pubmed-meshheading:9872364-Zona Pellucida
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pubmed:year |
1998
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pubmed:articleTitle |
Tyrosine phosphorylation of a 95 kDa protein and induction of the acrosome reaction in human spermatozoa by recombinant human zona pellucida glycoprotein 3.
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pubmed:affiliation |
Department of Molecular Biology and Biotechnology, The University of Sheffield, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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