Musclin Inhibits Insulin Activation of Akt/Protein Kinase B in Rat Skeletal Muscle

Author:

Liu Y1,Huo X2,Pang XF3,Zong ZH4,Meng X1,Liu GL1

Affiliation:

1. Department of Endocrinology, China Medical University, Shenyang, Liaoning, China

2. Department of General Surgery 3, China Medical University, Shenyang, Liaoning, China

3. Department of Cardiology, The First Hospital, China Medical University, Shenyang, Liaoning, China

4. Department of Biochemistry and Molecular Biology, China Medical University, Shenyang, Liaoning, China

Abstract

Musclin is a muscle-derived secretory peptide that induces insulin resistance in vitro We studied the effect of musclin (0.5 μg/ml) on insulin-stimulated glucose uptake in rat skeletal muscles and also the effect of rosiglitazone (0.4 μg/ml). Pre-incubation of muscles with musclin resulted in decreased insulin-stimulated glucose uptake. Musclin also reduced expression of peroxisome proliferator-activated receptor γ (PPARγ) and liver X receptor α (LXRα) mRNAs, although expression of glucose transporter 4 mRNA was unaltered. Rosiglitazone attenuated the effects of musclin on glucose uptake and PPARγ and LXRα mRNA expression. Western blotting demonstrated that activation of protein kinase B (Akt/PKB) in the insulin-signalling cascade was decreased by musclin but corrected by rosiglitazone. These findings suggest that musclin-induced impairment of insulin-stimulated glucose uptake in skeletal muscle is related to Akt/PKB inhibition and might be modulated by PPARγ/LXRα.

Publisher

SAGE Publications

Subject

Biochemistry (medical),Cell Biology,Biochemistry,General Medicine

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