Irisin, a Novel Myokine, Regulates Glucose Uptake in Skeletal Muscle Cells via AMPK (original) (raw)

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Hye Jeong Lee ,

1Department of Anatomy (H.J.L., J.O.L., N.K., J.K.K., H.I.K., Y.W.L., S.J.K., S.H.P., H.S.K.), Korea University College of Medicine, Seoul, Korea 136-705

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Jung Ok Lee ,

1Department of Anatomy (H.J.L., J.O.L., N.K., J.K.K., H.I.K., Y.W.L., S.J.K., S.H.P., H.S.K.), Korea University College of Medicine, Seoul, Korea 136-705

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Nami Kim ,

1Department of Anatomy (H.J.L., J.O.L., N.K., J.K.K., H.I.K., Y.W.L., S.J.K., S.H.P., H.S.K.), Korea University College of Medicine, Seoul, Korea 136-705

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Joong Kwan Kim ,

1Department of Anatomy (H.J.L., J.O.L., N.K., J.K.K., H.I.K., Y.W.L., S.J.K., S.H.P., H.S.K.), Korea University College of Medicine, Seoul, Korea 136-705

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Hyung Ip Kim ,

1Department of Anatomy (H.J.L., J.O.L., N.K., J.K.K., H.I.K., Y.W.L., S.J.K., S.H.P., H.S.K.), Korea University College of Medicine, Seoul, Korea 136-705

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Yong Woo Lee ,

1Department of Anatomy (H.J.L., J.O.L., N.K., J.K.K., H.I.K., Y.W.L., S.J.K., S.H.P., H.S.K.), Korea University College of Medicine, Seoul, Korea 136-705

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Su Jin Kim ,

1Department of Anatomy (H.J.L., J.O.L., N.K., J.K.K., H.I.K., Y.W.L., S.J.K., S.H.P., H.S.K.), Korea University College of Medicine, Seoul, Korea 136-705

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Jong-Il Choi ,

2Division of Cardiology (J.-I.C.), Department of Internal Medicine, Korea University Medical Center, Seoul, Korea

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Yoonji Oh ,

3College of Nursing (Y.O.), Korea University, Seoul, Korea 136-705

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Jeong Hyun Kim

4College of Pre-Pharm·Med (J.H.K.), DukSung Women's University, Seoul, Korea 132-714

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Received:

05 November 2014

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Hye Jeong Lee, Jung Ok Lee, Nami Kim, Joong Kwan Kim, Hyung Ip Kim, Yong Woo Lee, Su Jin Kim, Jong-Il Choi, Yoonji Oh, Jeong Hyun Kim, Suyeon- Hwang, Sun Hwa Park, Hyeon Soo Kim, Irisin, a Novel Myokine, Regulates Glucose Uptake in Skeletal Muscle Cells via AMPK, Molecular Endocrinology, Volume 29, Issue 6, 1 June 2015, Pages 873–881, https://doi.org/10.1210/me.2014-1353
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Abstract

Irisin is a novel myokine produced by skeletal muscle. However, its metabolic role is poorly understood. In the present study, irisin induced glucose uptake in differentiated skeletal muscle cells. It increased AMP-activated protein kinase (AMPK) phosphorylation and the inhibition of AMPK blocked glucose uptake. It also increased reactive oxygen species (ROS) generation. N-acetyl cysteine, a ROS scavenger, blocked irisin-induced AMPK phosphorylation. Moreover, irisin activated p38 MAPK in an AMPK-dependent manner. The inhibition and knockdown of p38 MAPK blocked irisin-induced glucose uptake. A colorimetric absorbance assay showed that irisin stimulated the translocation of glucose transporter type 4 to the plasma membrane and that this effect was suppressed in cells pretreated with a p38 MAPK inhibitor or p38 MAPK small interfering RNA. In primary cultured myoblast cells, irisin increased the concentration of intracellular calcium. STO-609, a calcium/calmodulin-dependent protein kinase kinase inhibitor, blocked irisin-induced AMPK phosphorylation, implying that calcium is involved in irisin-mediated signaling. Our results suggest that irisin plays an important role in glucose metabolism via the ROS-mediated AMPK pathway in skeletal muscle cells.

Copyright © 2015 by the Endocrine Society

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