Emodin regulates glucose utilization by activating amp-activated protein kinase

Parkyong Song; Jong Hyun Kim; Jaewang Ghim; Jong Hyuk Yoon; Areum Lee; Yonghoon Kwon; Hyunjung Hyun; Hyo Youl Moon; Hueng Sik Choi; Per Olof Berggren; Pann Ghill Suh; Sung Ho Ryu

doi:10.1074/jbc.M112.441477

Emodin regulates glucose utilization by activating amp-activated protein kinase

Parkyong Song, Jong Hyun Kim, Jaewang Ghim, Jong Hyuk Yoon, Areum Lee, Yonghoon Kwon, Hyunjung Hyun, Hyo Youl Moon, Hueng Sik Choi, Per Olof Berggren, Pann Ghill Suh, Sung Ho Ryu

Surgery

Research output: Contribution to journal › Article

42 Scopus citations

Abstract

Background: AMPK activation improves glucose tolerance and insulin sensitivity. Results: Emodin increases glucose uptake in skeletal muscle and lowers blood glucose levels via AMPK activation. Conclusion: Administration of emodin leads to increased glucose tolerance and insulin sensitivity in vivo. Significance: Our results highlight the potential value of emodin as a drug for the treatment of diabetes.

Original language	English (US)
Pages (from-to)	5732-5742
Number of pages	11
Journal	Journal of Biological Chemistry
Volume	288
Issue number	8
DOIs	https://doi.org/10.1074/jbc.M112.441477
State	Published - Feb 22 2013

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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Song, P., Kim, J. H., Ghim, J., Yoon, J. H., Lee, A., Kwon, Y., Hyun, H., Moon, H. Y., Choi, H. S., Berggren, P. O., Suh, P. G., & Ryu, S. H. (2013). Emodin regulates glucose utilization by activating amp-activated protein kinase. Journal of Biological Chemistry, 288(8), 5732-5742. https://doi.org/10.1074/jbc.M112.441477

Emodin regulates glucose utilization by activating amp-activated protein kinase. / Song, Parkyong; Kim, Jong Hyun; Ghim, Jaewang; Yoon, Jong Hyuk; Lee, Areum; Kwon, Yonghoon; Hyun, Hyunjung; Moon, Hyo Youl; Choi, Hueng Sik; Berggren, Per Olof; Suh, Pann Ghill; Ryu, Sung Ho.

In: Journal of Biological Chemistry, Vol. 288, No. 8, 22.02.2013, p. 5732-5742.

Research output: Contribution to journal › Article

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