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Int. J. Mol. Sci. 2015, 16(7), 16288-16299; doi:10.3390/ijms160716288

3-O-Acyl-epicatechins Increase Glucose Uptake Activity and GLUT4 Translocation through Activation of PI3K Signaling in Skeletal Muscle Cells

1
Department of Agrobioscience, Graduate School of Agricultural Science, Kobe University, Nada-ku, Kobe, Hyogo 657-8501, Japan
2
National Agriculture and Food Research Organization, National Food Research Institute, Tsukuba, Ibaraki 305-8642, Japan
3
Department of Food Science, Institute of Health Biosciences, University of Tokushima Graduate School, Kuramoto, Tokushima 770-8503, Japan
4
Laboratory of Food and Nutritional Sciences, Faculty of Nutrition, Kobe Gakuin University, Nishi-ku, Kobe, Hyogo 651-2180, Japan
5
Graduate School of Agriculture, Shinshu University, Minamiminowa-mura, Kamiina-gun, Nagano 399-4598, Japan
*
Author to whom correspondence should be addressed.
Academic Editor: Vladimír Křen
Received: 26 May 2015 / Revised: 25 June 2015 / Accepted: 14 July 2015 / Published: 17 July 2015
(This article belongs to the Section Biochemistry, Molecular and Cellular Biology)
View Full-Text   |   Download PDF [1029 KB, uploaded 17 July 2015]   |  

Abstract

Tea catechins promote glucose uptake in skeletal muscle cells. In this study, we investigated whether the addition of an acyl group to the C-3 position of catechins to generate 3-O-acyl-catechins promoted glucose uptake in L6 myotubes. 3-O-Myristoyl-(−)-epicatechin (EC-C14) and 3-O-palmitoyl-(−)-epicatechin (EC-C16) promoted glucose uptake and translocation of glucose transporter (GLUT) 4 in the cells. The effect of 3-O-acyl-(−)-epicatechins was stronger than that of (−)-epicatechin (EC), whereas neither 3-O-myristoyl-(+)-catechin (C-C14) nor 3-O-palmitoyl-(+)catechin (C-C16) promoted glucose uptake or GLUT4 translocation as well as (+)-catechin (C). We further investigated an affinity of catechins and 3-O-acyl-catechins to the lipid bilayer membrane by using surface plasma resonance analysis. Maximum binding amounts of EC-C16 and C-C16 to the lipid bilayer clearly increased compared with that of (−)-EC and (+)-C, respectively. We also examined the mechanism of GLUT4 translocation and found EC-C14 and EC-C16 induced the phosphorylation of PI3K, but did not affect phosphorylation of Akt or IR. In conclusion, the addition of an acyl group to the C-3 position of (−)-EC increases its affinity for the lipid bilayer membrane and promotes GLUT4 translocation through PI3K-dependent pathways in L6 myotubes. View Full-Text
Keywords: acyl catechin; glucose transporter 4; skeletal muscle; insulin signaling pathway acyl catechin; glucose transporter 4; skeletal muscle; insulin signaling pathway
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Ueda-Wakagi, M.; Mukai, R.; Fuse, N.; Mizushina, Y.; Ashida, H. 3-O-Acyl-epicatechins Increase Glucose Uptake Activity and GLUT4 Translocation through Activation of PI3K Signaling in Skeletal Muscle Cells. Int. J. Mol. Sci. 2015, 16, 16288-16299.

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