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Journal of Histochemistry and Cytochemistry, Vol. 48, 1705-1716, December 2000, Copyright © 2000, The Histochemical Society, Inc.

ARTICLE

Distinct Aggregation of ß- and {gamma}-Chains of the High-affinity IgE Receptor on Cross-Linking

Koichi Asaia, Kazushi Fujimotob,c,e, Masashi Harazakia, Takashi Kusunokia, Seigo Korematsua, Chizuka Ideb, Chisei Rad, and Susumu Hosoia
a Department of Pediatrics and Developmental Medicine, Graduate School of Medicine, Kyoto University
b Department of Anatomy, Faculty of Medicine, Kyoto University
c Laboratory for Neural Architecture, Brain Science Institute, The Institute of Physical and Chemical Research (Riken)
d Department of Immunology, Juntendo University School of Medicine, Tokyo, Japan
e CREST Japan Science and Technology Corporation, Tokyo, Japan

Correspondence to: Kazushi Fujimoto, Section of Physiological Anatomy, Fukui Prefectural U. Faculty of Nursing and Welfare, 4-1-1 Kenjojima, Matsuoka-cho, Yoshida-gun, Fukui 910-1195, Japan. E-mail: fujimoto@fpu.ac.jp

The high-affinity IgE receptor (Fc{epsilon}RI) on mast cells and basophils consists of a ligand-binding {alpha}-chain and two kinds of signaling chains, a ß-chain and disulfide-linked homodimeric {gamma}-chains. Crosslinking by multivalent antigen results in the aggregation of the bound IgE/{alpha}-chain complexes at the cell surface, triggering cell activation, and subsequent internalization through coated pits. However, the precise topographical alterations of the signaling ß- and {gamma}-chains during stimulation remain unclarified despite their importance in ligand binding/signaling coupling. Here we describe the dynamics of Fc{epsilon}RI subunit distribution in rat basophilic leukemia cells during stimulation as revealed by immunofluorescence and immunogold electron microscopy. Immunolocalization of ß- and {gamma}-chains was homogeneously distributed on the cell surfaces before stimulation, while crosslinking with multivalent antigen, which elicited optimal degranulation, caused a distinct aggregation of these signaling chains on the cell membrane. Moreover, only {gamma}- but not ß-chains were aggregated during the stimulation that evoked suboptimal secretion. These findings suggest that high-affinity IgE receptor ß- and {gamma}-chains do not co-aggregate but for the most part form homogenous aggregates of ß-chains or {gamma}-chains after crosslinking.

(J Histochem Cytochem 48:1705–1715, 2000)

Key Words: mast cells/basophils, Fc receptors, immunogold electron microscopy


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