Cross-linking of Thy-1 glycoproteins or high-affinity IgE receptors induces mast cell activation via different mechanisms
Language English Country Great Britain, England Media print
Document type Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.
PubMed
7902332
PubMed Central
PMC1422128
Knihovny.cz E-resources
- MeSH
- Antigens, Surface immunology MeSH
- Thy-1 Antigens MeSH
- Cholera Toxin immunology MeSH
- Dexamethasone immunology MeSH
- Phosphoric Diester Hydrolases immunology MeSH
- Phosphoinositide Phospholipase C MeSH
- Phosphorylation MeSH
- Rats MeSH
- Phosphatidylinositol Diacylglycerol-Lyase MeSH
- Mast Cells immunology MeSH
- Membrane Glycoproteins immunology MeSH
- Antibodies, Monoclonal immunology MeSH
- Cross-Linking Reagents MeSH
- Receptors, Fc immunology MeSH
- Receptors, IgE immunology MeSH
- Tyrosine immunology 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
- Cholera Toxin MeSH
- Dexamethasone MeSH
- Phosphoric Diester Hydrolases MeSH
- Phosphoinositide Phospholipase C MeSH
- Phosphatidylinositol Diacylglycerol-Lyase MeSH
- Membrane Glycoproteins MeSH
- Antibodies, Monoclonal MeSH
- Cross-Linking Reagents MeSH
- Receptors, Fc MeSH
- Receptors, IgE MeSH
- Tyrosine MeSH
Rat peritoneal and pleural mast cells and rat basophilic leukemia cells, RBL-2H3, have been previously shown to be activated by Thy-1-specific monoclonal antibodies (mAb). In the present study we investigated the mechanism of Thy-1-mediated activation and compared it with activation induced by cross-linking of the high-affinity IgE receptor. Binding of an IgG Thy-1 x 1-specific mAb, MRCOX7 (OX7), to RBL-2H3 cells and mast cells, and activation of RBL-2H3 by the OX7 were abrogated by pretreatment of the cells with phosphatidyl inositol-specific phospholipase C (PI-PLC). The F(ab')2 fragment of OX7, in contrast to the Fab' fragment, induced cell activation as well as intact OX7 mAb. Cells sensitized with IgE exhibited an increased responsiveness to anti-Thy-1 antibodies suggesting formation of functional complexes of IgE receptor/IgE/Thy-1/anti-Thy-1. Pretreatment of RBL-2H3 cells with cholera toxin potentiated activation induced by IgE+antigen (Ag) and IgE+OX7, but had no effect on activation induced by OX7 antibody alone. Similarly, dexamethasone had no effect on OX7-induced activation but inhibited IgE+Ag- and IgE+OX7-induced activation. Analysis of phosphotyrosine-containing proteins in RBL-2H3 cell lysates revealed that IgE+Ag and IgE+OX7 induced a marked increase in tyrosine phosphorylation of several proteins that were not tyrosine phosphorylated in cells exposed to OX7 mAb alone. Similar results were obtained when RBL-2H3-derived cells, expressing transfected mouse Thy-1.2, were activated with Thy-1.2-specific IgM antibody. The combined data suggest that Thy-1-specific antibodies activate cells by a mechanism that is different from activation induced by cross-linking of high-affinity IgE receptor.
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Thy-1-mediated activation of rat mast cells: the role of Thy-1 membrane microdomains
