TY - JOUR
T1 - Lipid raft-associated catechin suppresses the FcεRI expression by inhibiting phosphorylation of the extracellular signal-regulated kinase1/2
AU - Fujimura, Yoshinori
AU - Tachibana, Hirofumi
AU - Yamada, Koji
N1 - Funding Information:
This work was supported in part by Grants from the Program for Promotion of Basic Research Activities for Innovative Biosciences (to H.T.). The first author was supported by a fellowship from the Research Fellowships of the Japan Society for the Promotion of Science for Young Scientists. The authors thank Perry Seto for proofreading the manuscript.
PY - 2004/1/2
Y1 - 2004/1/2
N2 - The major green tea catechin, (-)-epigallocatechin-3-O-gallate (EGCG), has a suppressive effect on the expression of the high-affinity IgE receptor FcεRI, which is key molecule in the IgE-mediated allergic reactions. Here we show that EGCG binds to the cell surface and highly associates with plasma membrane microdomains, lipid rafts, on the human basophilic KU812 cells. The disruption of these lipid rafts caused a reduction of the amount of raft-associated EGCG and the FcεRI-suppressive effect of EGCG. We also found that EGCG has an ability to inhibit the phosphorylation of the extracellular signal-regulated kinase1/2 (ERK1/2) and that the ERK1/2 specific inhibitor also reduced FcεRI expression. Moreover, the inhibitory effect elicited by EGCG on ERK1/2 was prevented by disruption of rafts. Thus, these results suggest that the interaction between EGCG and the lipid rafts is important for EGCG's ability to downregulate FcεRI expression, and ERK1/2 may be involved in this suppression signal.
AB - The major green tea catechin, (-)-epigallocatechin-3-O-gallate (EGCG), has a suppressive effect on the expression of the high-affinity IgE receptor FcεRI, which is key molecule in the IgE-mediated allergic reactions. Here we show that EGCG binds to the cell surface and highly associates with plasma membrane microdomains, lipid rafts, on the human basophilic KU812 cells. The disruption of these lipid rafts caused a reduction of the amount of raft-associated EGCG and the FcεRI-suppressive effect of EGCG. We also found that EGCG has an ability to inhibit the phosphorylation of the extracellular signal-regulated kinase1/2 (ERK1/2) and that the ERK1/2 specific inhibitor also reduced FcεRI expression. Moreover, the inhibitory effect elicited by EGCG on ERK1/2 was prevented by disruption of rafts. Thus, these results suggest that the interaction between EGCG and the lipid rafts is important for EGCG's ability to downregulate FcεRI expression, and ERK1/2 may be involved in this suppression signal.
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U2 - 10.1016/S0014-5793(03)01432-7
DO - 10.1016/S0014-5793(03)01432-7
M3 - Article
C2 - 14706851
AN - SCOPUS:0346094387
VL - 556
SP - 204
EP - 210
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 1-3
ER -