Thy-1 glycoprotein and src-like protein-tyrosine kinase p53/p56lyn are associated in large detergent-resistant complexes in rat basophilic leukemia cells
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, práce podpořená grantem, Research Support, U.S. Gov't, P.H.S.
PubMed
7682713
PubMed Central
PMC46351
DOI
10.1073/pnas.90.8.3611
Knihovny.cz E-zdroje
- MeSH
- akutní bazofilní leukemie MeSH
- antigeny povrchové izolace a purifikace metabolismus MeSH
- antigeny Thy-1 MeSH
- C-terminální Src kinasa MeSH
- elektroforéza v polyakrylamidovém gelu MeSH
- fosfodiesterasy MeSH
- gelová chromatografie MeSH
- imunoblotting MeSH
- krysa rodu Rattus MeSH
- lyasa fosfatidylinositoldiacylglycerolu MeSH
- makromolekulární látky MeSH
- membránové glykoproteiny izolace a purifikace metabolismus MeSH
- molekulová hmotnost MeSH
- monoklonální protilátky MeSH
- nádorové buňky kultivované MeSH
- protoonkogenní proteiny pp60(c-src) izolace a purifikace metabolismus MeSH
- receptory IgE metabolismus MeSH
- skupina kinas odvozených od src-genu * MeSH
- tyrosinkinasy izolace a purifikace metabolismus MeSH
- zvířata MeSH
- Check Tag
- krysa rodu Rattus MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Research Support, U.S. Gov't, P.H.S. MeSH
- Názvy látek
- antigeny povrchové MeSH
- antigeny Thy-1 MeSH
- C-terminální Src kinasa MeSH
- fosfodiesterasy MeSH
- lyasa fosfatidylinositoldiacylglycerolu MeSH
- lyn protein-tyrosine kinase MeSH Prohlížeč
- makromolekulární látky MeSH
- membránové glykoproteiny MeSH
- monoklonální protilátky MeSH
- protoonkogenní proteiny pp60(c-src) MeSH
- receptory IgE MeSH
- skupina kinas odvozených od src-genu * MeSH
- tyrosinkinasy 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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