Formation of a mast cell synapse: Fc epsilon RI membrane dynamics upon binding mobile or immobilized ligands on surfaces.
Formation of a mast cell synapse: Fc epsilon RI membrane dynamics upon binding mobile or immobilized ligands on surfaces.
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DOI:
10.4049/jimmunol.0903071
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发表时间:
2010-02-01
期刊:
影响因子:
--
通讯作者:
Timlin JA
中科院分区:
文献类型:
--
作者:
Carroll-Portillo A;Spendier K;Pfeiffer J;Griffiths G;Li H;Lidke KA;Oliver JM;Lidke DS;Thomas JL;Wilson BS;Timlin JA
High affinity IgE receptors (FcεRI) on mast cells form a “synapse” when presented with mobile, bilayer incorporated antigen. Here, we show that receptor reorganization within the contacting mast cell membrane is markedly different upon binding of mobile and immobilized ligands. Rat basophilic leukemia mast cells (RBL-2H3) primed with fluorescent anti-DNP IgE were engaged by surfaces presenting either bilayer-incorporated, monovalent DNP-lipid (mobile ligand) or chemically crosslinked, multivalent DNP (immobilized ligand). Total internal reflection fluorescence imaging and electron microscopy methods were used to visualize receptor reorganization at the contact site. The spatial relationships of FcεRI to other cellular components at the synapse, such as actin, cholesterol and LAT, were also analyzed. Stimulation of mast cells with immobilized polyvalent ligand resulted in typical levels of degranulation. Remarkably, degranulation also followed interaction of mast cells with bilayers presenting mobile, monovalent ligand. Receptors engaged with mobile ligand coalesce into large, cholesterol-rich clusters that occupy the central portion of the contacting membrane. These data indicate that FcεRI crosslinking is not an obligatory step in triggering mast cell signaling and suggest that dense populations of mobile receptors are capable of initiating low level degranulation upon ligand recognition.
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DOI:
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发表时间:
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影响因子:
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