TY - JOUR
T1 - The involvement of the 67 kDa laminin receptor-mediated modulation of cytoskeleton in the degranulation inhibition induced by epigallocatechin-3-O-gallate
AU - Fujimura, Yoshinori
AU - Umeda, Daisuke
AU - Kiyohara, Yuko
AU - Sunada, Yousuke
AU - Yamada, Koji
AU - Tachibana, Hirofumi
N1 - Funding Information:
This work was supported in part by grants from the Bio-oriented Technology Research Advancement Institution to H.T. We are grateful to Dr. Takeshi Shimomura for helpful discussion. We thank Seiko Tomiyama for technical assistance. The authors thank Perry Seto for proofreading the manuscript.
Copyright:
Copyright 2008 Elsevier B.V., All rights reserved.
PY - 2006/9/22
Y1 - 2006/9/22
N2 - Recently, we have reported that (-)-epigallocatechin-3-O-gallate (EGCG) acts as an inhibitor of degranulation. However, the inhibitory mechanism for degranulation is still poorly understood. Here we show that suppression of exocytosis-related myosin II regulatory light chain phosphorylation and alteration of actin remodeling are involved in the inhibitory effect of EGCG on the calcium ionophore-induced degranulation from human basophilic KU812 cells. Surface plasmon resonance assay also revealed that EGCG binds to the cell surface, and the disruption of lipid rafts resulted in reduction of EGCG's ability. We have previously identified the raft-associated 67 kDa laminin receptor (67LR) as an EGCG receptor on the cell surface. Treatment of the cells with anti-67LR antibody or RNA interference-mediated downregulation of 67LR expression abolished the effects of EGCG. These findings suggest that EGCG-induced inhibition of the degranulation includes the primary binding of EGCG to the cell surface 67LR and subsequent modulation of cytoskeleton.
AB - Recently, we have reported that (-)-epigallocatechin-3-O-gallate (EGCG) acts as an inhibitor of degranulation. However, the inhibitory mechanism for degranulation is still poorly understood. Here we show that suppression of exocytosis-related myosin II regulatory light chain phosphorylation and alteration of actin remodeling are involved in the inhibitory effect of EGCG on the calcium ionophore-induced degranulation from human basophilic KU812 cells. Surface plasmon resonance assay also revealed that EGCG binds to the cell surface, and the disruption of lipid rafts resulted in reduction of EGCG's ability. We have previously identified the raft-associated 67 kDa laminin receptor (67LR) as an EGCG receptor on the cell surface. Treatment of the cells with anti-67LR antibody or RNA interference-mediated downregulation of 67LR expression abolished the effects of EGCG. These findings suggest that EGCG-induced inhibition of the degranulation includes the primary binding of EGCG to the cell surface 67LR and subsequent modulation of cytoskeleton.
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U2 - 10.1016/j.bbrc.2006.07.086
DO - 10.1016/j.bbrc.2006.07.086
M3 - Article
C2 - 16889749
AN - SCOPUS:33746892584
SN - 0006-291X
VL - 348
SP - 524
EP - 531
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -