Iron deficiency attenuates protein synthesis stimulated by branched-chain amino acids and insulin in myotubes

化学 生物化学 胰岛素 氨基酸 骨骼肌 内科学 内分泌学 蛋白质生物合成 亮氨酸 肌发生 葡萄糖摄取 胰岛素受体
作者
Kazuhiko Higashida,Sachika Inoue,Naoya Nakai
出处
期刊:Biochemical and Biophysical Research Communications [Elsevier]
卷期号:531 (2): 112-117 被引量:5
标识
DOI:10.1016/j.bbrc.2020.07.041
摘要

Iron deficiency anemia indicates poor nutrition and is a public health problem. Iron deficiency is also associated with muscle weakness. However, the intracellular mechanisms by which iron deficiency induces muscle weakness are obscure. The purpose of the present study was to evaluate the effect of iron deficiency on protein synthesis in basal and branched-amino acids (BCAA)- and insulin-stimulated state in muscle cells. Differentiated C2C12 myotubes were incubated with an iron chelator, deferoxamine mesylate, and then stimulated with BCAA or insulin to activate protein synthesis. This iron deprivation resulted in a significant reduction in the abundance of iron-containing proteins, such as the mitochondrial complex 1 subunit protein, compared to control cells, but not of protein that does not contain iron, such as citrate synthase. Proteins involved in glucose utilization, such as glucose transpoter-1, hexokinase and AMP-activated protein kinase (AMPK), were upregulated under iron deficiency. Additionally, rates of BCAA- and insulin-stimulated protein synthesis, measured by puromycin incorporation, were lower in iron-deficient myotubes than in control cells. We suggest that low iron availability attenuates BCAA- and insulin-stimulated protein synthesis, possibly via activation of AMPK in myotubes. The present findings advance the understanding of the importance of iron to skeletal muscle protein synthesis and, thus, may contribute to the prevention of sarcopenia and frailty.
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