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首页> 外文期刊>EMBO Journal >Deficiency of LKB1 in skeletal muscle prevents AMPK activation and glucose uptake during contraction
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Deficiency of LKB1 in skeletal muscle prevents AMPK activation and glucose uptake during contraction

机译：缺乏骨骼肌LKB1的阻止AMPK活化和葡萄糖吸收收缩

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摘要

Recent studies indicate that the LKB1 tumour suppressor protein kinase is the major 'upstream' activator of the energy sensor AMP-activated protein kinase (AMPK). We have used mice in which LKB1 is expressed at only similar to 10% of the normal levels in muscle and most other tissues, or that lack LKB1 entirely in skeletal muscle. Muscle expressing only 10% of the normal level of LKB1 had significantly reduced phosphorylation and activation of AMPK alpha 2. In LKB1-lacking muscle, the basal activity of the AMPKa2 isoform was greatly reduced and was not increased by the AMP-mimetic agent, 5-aminoimidazole-4-carboxamide riboside (AICAR), by the antidiabetic drug phenformin, or by muscle contraction. Moreover, phosphorylation of acetyl CoA carboxylase-2, a downstream target of AMPK, was profoundly reduced. Glucose uptake stimulated by AICAR or muscle contraction, but not by insulin, was inhibited in the absence of LKB1. Contraction increased the AMP: ATP ratio to a greater extent in LKB1-deficient muscles than in LKB1-expressing muscles. These studies establish the importance of LKB1 in regulating AMPK activity and cellular energy levels in response to contraction and phenformin.
机译：最近的研究表明,LKB1的肿瘤抑制蛋白激酶是主要的“上游”激活的能量传感器活化蛋白激酶(AMPK)。LKB1表示只有10%的相似正常水平在肌肉和其他组织,或者完全缺乏LKB1骨骼肌。肌肉表示只有10%的正常水平LKB1显著降低磷酸化和激活AMPKα2。的基底活动肌肉,AMPKa2同种型大大减少,并不增加了吗AMP-mimetic代理,5-aminoimidazole-4-carboxamide核苷(爱卡),抗糖尿病药苯乙双胍或肌肉收缩。乙酰辅酶a carboxylase-2的磷酸化下游AMPK的目标,是深刻的减少了。肌肉收缩,但不是通过胰岛素抑制在LKB1的缺失。增加了安保:ATP比例在更大程度上在比LKB1-expressing LKB1-deficient肌肉肌肉。LKB1的调控AMPK活性和细胞为了应对收缩和能量水平

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