Valosine containing protein is a substrate of cAMP-activated boar sperm tyrosine kinase
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
12237953
DOI
10.1002/mrd.10156
Knihovny.cz E-resources
- MeSH
- Adenosine Triphosphatases MeSH
- Electrophoresis, Polyacrylamide Gel MeSH
- Phosphorylation MeSH
- Molecular Sequence Data MeSH
- Swine MeSH
- Valosin Containing Protein MeSH
- Cell Cycle Proteins genetics metabolism MeSH
- Amino Acid Sequence MeSH
- Spermatozoa enzymology MeSH
- Protein-Tyrosine Kinases metabolism MeSH
- Animals MeSH
- Check Tag
- Male MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Adenosine Triphosphatases MeSH
- Valosin Containing Protein MeSH
- Cell Cycle Proteins MeSH
- Protein-Tyrosine Kinases MeSH
Previously we reported that treatment of boar sperm with cAMP-elevating drugs induces tyrosine phosphorylation of a triton-insoluble 93 kDa protein (p93). We have isolated p93 by preparative SDS electrophoresis and blotting from urea-extracted boar sperm and identified it as a valosine containing protein (VCP) by mass spectrometry and microsequencing. With the use of antibodies to VCP and phosphotyrosine (pY) we found that both p93 and VCP are poorly extractable with triton and are solubilized in > 6 M urea. Furthermore, VCP and p93 overlap on one and two dimensional (1 and 2D) electrophoretic gels, supporting the identity of p93 as a tyrosine-phosphorylated population of VCP. According to immunofluorescence, VCP is localized along the entire sperm tail, in the posterior ring, distal equatorial segment, and postacrosome. In addition, 9-12% sperm contained VCP in the acrosome. The cAMP-elevating treatment did not alter VCP localization but induced tail tyrosine phosphorylation in 15% sperm cells. In those sperm, VCP and pY colocalized in connecting piece and posterior ring.
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