| pubmed-article:1281543 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1281543 | lifeskim:mentions | umls-concept:C0025914 | lld:lifeskim |
| pubmed-article:1281543 | lifeskim:mentions | umls-concept:C0026809 | lld:lifeskim |
| pubmed-article:1281543 | lifeskim:mentions | umls-concept:C0037868 | lld:lifeskim |
| pubmed-article:1281543 | lifeskim:mentions | umls-concept:C0033681 | lld:lifeskim |
| pubmed-article:1281543 | lifeskim:mentions | umls-concept:C0037853 | lld:lifeskim |
| pubmed-article:1281543 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:1281543 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:1281543 | pubmed:dateCreated | 1993-1-19 | lld:pubmed |
| pubmed-article:1281543 | pubmed:abstractText | A 95-kDa mouse sperm protein has been previously identified as a putative receptor involved in the sperm-egg interactions that lead to fertilization. The ligand for this receptor is the zona pellucida glycoprotein ZP3. This constituent of the oocyte-specific extracellular matrix mediates not only sperm binding to the zona but also triggers acrosomal exocytosis. The latter, also termed the acrosome reaction, is a key regulatory event upon which fertilization is absolutely dependent. Previously, we showed that the 95-kDa protein that binds ZP3 is a substrate for tyrosine kinase, and its phosphotyrosine content increases after sperm-zona pellucida binding. Here, we show the presence of protein tyrosine kinase activity in sperm plasma membranes and in electroeluted 95-kDa protein. The tyrosine kinase activity of the isolated protein is stimulated by solubilized zona pellucida and inhibited by tyrphostin RG-50864, a membrane-permeable tyrosine kinase inhibitor. Furthermore, tyrphostin inhibits zona-triggered acrosomal exocytosis in a dose-dependent manner. These findings indicate that the 95-kDa protein participates in a critical regulatory event of gamete interaction; moreover, our experiments suggest that sperm protein tyrosine kinase may be an excellent target for the control of fertility. | lld:pubmed |
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| pubmed-article:1281543 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1281543 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1281543 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1281543 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1281543 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1281543 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:1281543 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:1281543 | pubmed:author | pubmed-author:SalingP MPM | lld:pubmed |
| pubmed-article:1281543 | pubmed:author | pubmed-author:BunchDD | lld:pubmed |
| pubmed-article:1281543 | pubmed:author | pubmed-author:LeytonLL | lld:pubmed |
| pubmed-article:1281543 | pubmed:author | pubmed-author:LeGuenPP | lld:pubmed |
| pubmed-article:1281543 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1281543 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:1281543 | pubmed:volume | 89 | lld:pubmed |
| pubmed-article:1281543 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1281543 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1281543 | pubmed:pagination | 11692-5 | lld:pubmed |
| pubmed-article:1281543 | pubmed:dateRevised | 2010-9-7 | lld:pubmed |
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| pubmed-article:1281543 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1281543 | pubmed:articleTitle | Regulation of mouse gamete interaction by a sperm tyrosine kinase. | lld:pubmed |
| pubmed-article:1281543 | pubmed:affiliation | Department of Obstetrics and Gynecology, Duke University Medical Center, Durham, NC 27710. | lld:pubmed |
| pubmed-article:1281543 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1281543 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1281543 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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