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- W2076982480 abstract "Previous studies in our laboratory established that the symmetrical bivalent ligand, N,N‘-bis[[ε-(2,4-dinitrophenyl)amino]caproyl]-l-tyrosyl]-l-cystine ((DCT)2-cys), stably cross-links anti-2,4-dinitrophenyl-immunoglobulin E (IgE) bound to high affinity receptors FcεRI on the surface of RBL-2H3 cells, forming mostly cyclic dimers containing two IgE-FcεRI and two (DCT)2-cys (Posner et al. (1995) J. Immunol. 155, 3601−3609). These cyclic dimers do not trigger Ca2+ or degranulation responses under a variety of conditions. However, we find that the linearly cross-linked IgE-FcεRI formed at higher concentrations of (DCT)2-cys do trigger degranulation in the presence of cytochalasin D, an inhibitor of actin polymerization. We further investigated stimulation by (DCT)2-cys of the earliest known events in the functional response, i.e., tyrosine phosphorylation of the β and γ subunits of FcεRI. At the higher (DCT)2-cys concentrations corresponding to linear dimers and maximal degranulation, tyrosine phosphorylation of both β and γ are observed. At lower (DCT)2-cys concentrations where cross-linking is maximal and cyclic dimers are overwhelmingly dominant, only γ tyrosine phosphorylation is observed. Cytochalasin D does not affect these phosphorylation patterns, but instead appears to enhance coupling to downstream signaling events. Phosphorylation of Syk occurs at the higher (DCT)2-cys concentrations in parallel with β phosphorylation but does not occur in its absence at the lower (DCT)2-cys concentrations. These results suggest that cyclic dimers of IgE-FcεRI are sterically restricted such that they stimulate tyrosine phosphorylation of γ but not β, and this is not sufficient for Syk binding and/or activation." @default.
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- W2076982480 date "1997-02-01" @default.
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- W2076982480 title "Altered Patterns of Tyrosine Phosphorylation and Syk Activation for Sterically Restricted Cyclic Dimers of IgE-FcεRI" @default.
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- W2076982480 doi "https://doi.org/10.1021/bi9619839" @default.
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