Health & Environmental Research Online (HERO)


Print Feedback Export to File
6791927 
Journal Article 
IgE stabilizes its high affinity receptor (Fc epsilon RI) on mast cells in vitro and ex vivo: The mechanism of IgE-mediated Fc epsilon RI up-regulation and its physiological meaning 
Kubo, S; Matsuoka, K; Taya, C; Kitamura, F; Yonekawa, H; Karasuyama, H; , 
2001 
SPRINGER-VERLAG TOKYO 
TOKYO 
183-188 
WOS:000170202000023 
The interaction of IgE with the high affinity receptor for immunoglobulin E (designated Fc epsilon RI) is central to IgE dependent anaphylaxis. Cross-linking of Fc epsilon RI initiates an intracellular signal transduction cascade that triggers the release of mediators of the allergic response. Surface Fc epsilon RI levels of mast cells and basophils are regulated by I-E. There is a correlation between the number of Fc epsilon RI and the severity of effector responses. Ligand-mediated Fc epsilon RI up-regulation should be one of the key mechanisms to control I-E response. Here we study the major mechanism by which IgE mediates Fc epsilon RI up-regulation. Intracellular protein transport inhibitor Brefeldin A (BFA) inhibited I-E-mediated Fc epsilon RI up-regulation. In the presence of BFA, IgE-free Fc epsilon RI disappeared from cell surface rapidly, whereas I-E-bound Fc epsilon RI were lost ver slowly. Total amount of new Fc epsilon RI expression did not depend on total number of I.-E-bound Fc epsilon RI. In human Fc epsilon RI alpha transgenic mice, human IgE enhanced expression of human FceRI, but mouse Fc epsilon RI levels were the same as before addition of human IgE. These suggest that stabilization of Fc epsilon RI by IgE is the major mechanism of IgE-mediated Fc epsilon RI up-regulation. 
Cooper, MD; Takai, T; Ravetch, JV; 
4-431-70297-0 
CREST International Symposium on Immunoglobulin-like Receptors 
SENDAI, JAPAN