Irisin, a Novel Myokine, Regulates Glucose Uptake in Skeletal Muscle Cells via AMPK
| Autor: | Suyeon Hwang, Jung Ok Lee, Jeong Hyun Kim, Jong Il Choi, Sun Hwa Park, Yong Woo Lee, Hyeon Soo Kim, Nami Kim, Hye Jeong Lee, Su Jin Kim, Hyung Ip Kim, Joong Kwan Kim, Yoonji Oh |
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| Rok vydání: | 2015 |
| Předmět: |
Glucose uptake
AMP-Activated Protein Kinases p38 Mitogen-Activated Protein Kinases Myoblasts Endocrinology AMP-activated protein kinase Myokine medicine Animals Myocyte Muscle Skeletal Protein kinase A Molecular Biology Cells Cultured Original Research Glucose Transporter Type 4 biology Glucose transporter Skeletal muscle AMPK Cell Differentiation General Medicine Fibronectins Rats Cell biology Enzyme Activation Protein Transport Glucose medicine.anatomical_structure biology.protein Reactive Oxygen Species Signal Transduction |
| Zdroj: | Molecular Endocrinology. 29:873-881 |
| ISSN: | 1944-9917 0888-8809 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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