Additional corresponding author: Yiu-Kay Lai, E-mail: firstname.lastname@example.org
Rutin potentiates insulin receptor kinase to enhance insulin-dependent glucose transporter 4 translocation
Article first published online: 24 FEB 2014
© 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Molecular Nutrition & Food Research
Volume 58, Issue 6, pages 1168–1176, June 2014
How to Cite
Hsu, C.-Y., Shih, H.-Y., Chia, Y.-C., Lee, C.-H., Ashida, H., Lai, Y.-K. and Weng, C.-F. (2014), Rutin potentiates insulin receptor kinase to enhance insulin-dependent glucose transporter 4 translocation. Mol. Nutr. Food Res., 58: 1168–1176. doi: 10.1002/mnfr.201300691
- Issue published online: 5 JUN 2014
- Article first published online: 24 FEB 2014
- Manuscript Accepted: 5 DEC 2013
- Manuscript Revised: 3 DEC 2013
- Manuscript Received: 20 SEP 2013
- National Science Council. Grant Numbers: 99-2923-B-259-002-MY3, 99-2311-B-259-001-MY3
- Glucose transporter 4;
- Insulin receptor kinase;
- Insulin resistance;
- Toona sinensis Roem
We investigated whether rutin, a flavonoid isolated from Toona sinensis Roem, has the ability to enhance insulin-dependent receptor kinase (IRK) activity and glucose transporter 4 (GLUT4) translocation in differentiated myotubes. We also tested the effects of rutin treatment in insulin-resistant mice using an oral glucose tolerance test (OGTT).
Methods and results
Rutin potentiated insulin receptor kinase (IRK) phosphorylation when IRK autophosphorylation was triggered by insulin in differentiated myotubes. Co-treatment of cells with rutin and insulin attenuated S961-mediated inhibition of insulin-dependent GLUT4 translocation. In S961-treated C57BL/6 mice, an in vivo model of insulin resistance and type 2 diabetes, rutin treatment showed a normoglycemic effect in the OGTT.
This study shows evidence that rutin may serve as a potential agent for glycemic control through enhancement of IRK activity, thereby inducing the insulin signaling pathway causing increased GLUT4 translocation and increased glucose uptake.