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Electrical pulse stimulation induces GLUT4 translocation in a Rac‐Akt‐dependent manner in C2C12 myotubes
Author(s) -
Hu Fang,
Li Nana,
Li Zhu,
Zhang Chang,
Yue Yingying,
Liu Qian,
Chen Liming,
Bilan Philip J.,
Niu Wenyan
Publication year - 2018
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12982
Subject(s) - glut4 , protein kinase b , myogenesis , phosphorylation , glucose uptake , skeletal muscle , chemistry , microbiology and biotechnology , stimulation , chromosomal translocation , myocyte , biochemistry , biology , insulin , endocrinology , gene
Muscle contraction increases skeletal muscle glucose uptake, but the underlying mechanisms are not fully elucidated. While important for insulin‐stimulated glucose uptake, the role of Akt in contraction‐stimulated muscle glucose uptake is controversial. In our study, C2C12 skeletal muscle myotubes were contracted by electrical pulse stimulation (EPS). We found that EPS leads to Akt phosphorylation on sites S473 and T308 in a time‐dependent manner. The Akt inhibitor MK2206 partly reduces EPS‐stimulated GLUT4 translocation without affecting EPS‐stimulated AMPK phosphorylation. EPS activates Rac1 GTP‐binding, and EPS‐stimulated GLUT4 translocation is partly inhibited by Rac1 inhibitor II and siRac1. Interestingly, both Rac1 inhibitor II and siRac1 inhibit EPS‐stimulated Akt phosphorylation on sites S473 and T308. Our findings implicate a Rac1‐Akt signaling pathway in EPS‐stimulated GLUT4 translocation in C2C12 myotubes.