Thy-1 glycoprotein and src-like protein-tyrosine kinase p53/p56lyn are associated in large detergent-resistant complexes in rat basophilic leukemia cells
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.
PubMed
7682713
PubMed Central
PMC46351
DOI
10.1073/pnas.90.8.3611
Knihovny.cz E-resources
- MeSH
- Leukemia, Basophilic, Acute MeSH
- Antigens, Surface isolation & purification metabolism MeSH
- Thy-1 Antigens MeSH
- CSK Tyrosine-Protein Kinase MeSH
- Electrophoresis, Polyacrylamide Gel MeSH
- Phosphoric Diester Hydrolases MeSH
- Chromatography, Gel MeSH
- Immunoblotting MeSH
- Rats MeSH
- Phosphatidylinositol Diacylglycerol-Lyase MeSH
- Macromolecular Substances MeSH
- Membrane Glycoproteins isolation & purification metabolism MeSH
- Molecular Weight MeSH
- Antibodies, Monoclonal MeSH
- Tumor Cells, Cultured MeSH
- Proto-Oncogene Proteins pp60(c-src) isolation & purification metabolism MeSH
- Receptors, IgE metabolism MeSH
- src-Family Kinases * MeSH
- Protein-Tyrosine Kinases isolation & purification metabolism MeSH
- Animals MeSH
- Check Tag
- Rats MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Research Support, U.S. Gov't, P.H.S. MeSH
- Names of Substances
- Antigens, Surface MeSH
- Thy-1 Antigens MeSH
- CSK Tyrosine-Protein Kinase MeSH
- Phosphoric Diester Hydrolases MeSH
- Phosphatidylinositol Diacylglycerol-Lyase MeSH
- lyn protein-tyrosine kinase MeSH Browser
- Macromolecular Substances MeSH
- Membrane Glycoproteins MeSH
- Antibodies, Monoclonal MeSH
- Proto-Oncogene Proteins pp60(c-src) MeSH
- Receptors, IgE MeSH
- src-Family Kinases * MeSH
- Protein-Tyrosine Kinases MeSH
Thy-1 is a surface glycoprotein that is attached to the plasma membrane by a glycosyl-phosphatidyl-inositol anchor. Crosslinking of Thy-1 in rat mast cells and basophilic leukemia cells (RBL-2H3) induces cell activation including histamine release and tyrosine phosphorylation of several proteins. Here we show that glycosyl-phosphatidylinositol-linked Thy-1 forms noncovalent complexes with src-related protein-tyrosine kinase p53/p56lyn and other protein-tyrosine kinases and/or their substrates. These complexes are resistant to solubilization by a nonionic detergent, sedimentable at 200,000 x g, and very large ( > 10 MDa) as determined by gel chromatography. Activation of RBL-2H3 cells by crosslinking of the high-affinity IgE receptors resulted in decreased recovery of the complexes. The combined data indicate the existence of large detergent-resistant domains in the surface membrane of mast cells that may play an important role in their activation.
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