Journal
JOURNAL OF MEDICINAL FOOD
Volume 11, Issue 3, Pages 429-434Publisher
MARY ANN LIEBERT, INC
DOI: 10.1089/jmf.2007.0107
Keywords
AMP-activated protein kinase; epigallocatechin gallate; glucose uptake; phosphatidylinositol 3-kinase; skeletal muscle
Funding
- Korea Research Institute of Bioscience Biotechnology
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The effect of epigallocatechin gallate (EGCG) on glucose uptake was studied in L6 rat skeletal muscle cells. Glucose uptake assay revealed that EGCG increased glucose uptake >70% compared to control. EGCG-stimulated glucose uptake was blocked by LY294002, an inhibitor of phosphatidylinositol (PI) 3-kinase, which is a major regulatory molecule in glucose uptake pathways. However, AMP-activated protein kinase (AMPK), which is another Crucial mediator in independent glucose uptake pathways, did not inhibit EGCG-stimulated glucose uptake by SB203585, a specific inhibitor of the AMPK downstream mediator, p38 mitogen-activated protein kinase (MAPK). We also found that EGCG increased the phosphorylation level of protein kinase B and PI 3-kinase activity, when assessed by PI 3-kinase assay, whereas no increase in the phosphorylation level of AMPK and p38 MAPK was observed. Taken together, these results Suggest that EGCG might stimulate glucose uptake, not AMPK-mediated but PI 3-kinase-mediated, in skeletal muscle cells, thereby contributing to glucose homeostasis.
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