• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of applied physiology >AMPK activation attenuates S6K1, 4E-BP1, and eEF2 signaling responses to high-frequency electrically stimulated skeletal muscle contractions
【24h】

AMPK activation attenuates S6K1, 4E-BP1, and eEF2 signaling responses to high-frequency electrically stimulated skeletal muscle contractions

机译：AMPK激活减弱了S6K1、4E-BP1和eEF2信号对高频电刺激骨骼肌收缩的反应

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Regulation of protein translation through Akt and the downstream mammalian target of rapamycin (mTOR) pathway is an important component of the cellular response to hypertrophic stimuli. It has been proposed that 5'AMP-activated protein kinase (AMPK) activation during muscle contraction may limit the hypertrophic response to resistance-type exercise by inhibiting translational signaling. However, experimental manipulation of AMPK activity during such a stimulus has not been attempted. Therefore, we investigated whether AMPK activation can attenuate the downstream signaling response of the Akt/mTOR pathway to electrically stimulated lengthening muscle contractions. Extensor digitorum longus muscles (n = 8/group) were subjected to a 22-min bout of lengthening contractions by high-frequency sciatic nerve electrical stimulation (STIM) in young adult (8 mo) Fischer 344 X Brown Norway male rats. Forty minutes before electrical stimulation, rats were subcutaneously injected with saline or 5-aminoimidazole4-carboxamide-1-4-ribofuranoside (AICAR; 1 mg/g body wt), an AMPK activator. Stimulated and contralateral resting muscles were removed at 0, 20, and 40 min post-STIM, and AMPK, acetyl CoA carboxylase (ACC), Akt, eukaryotic initiation factor 4E-binding protein (4E-BP1), 70-kDa ribosomal protein S6 kinase (S6K1), and eukaryotic elongation factor 2 (eEF2) phosphorylations were assessed by Western blot. AICAR treatment increased (P <= 0.05) post-STIM AMPK (Thr(172)) and ACC phosphorylation (Ser(79/221)), inhibited post-STIM S6K1 (Thr(389)) and 4E-BP1 (gel shift) phosphorylation, and elevated post-STIM eEF2 phosphorylation (Thr(56)). These findings suggest that translational signaling downstream of Akt/mTOR can be inhibited after lengthening contractions when preceded by AMPK activation and that energetic stress may be antagonistic to the hypertrophic translational signaling response to loaded muscle contractions.
机译：通过Akt和下游哺乳动物雷帕霉素（mTOR）途径的靶蛋白调节是细胞对肥厚刺激的重要组成部分。已经提出在肌肉收缩过程中5'AMP激活的蛋白激酶（AMPK）激活可以通过抑制翻译信号传导来限制对抵抗型运动的肥大反应。然而，尚未尝试在这样的刺激过程中实验性地操作AMPK活性。因此，我们调查了AMPK激活是否可以减弱Akt / mTOR通路对电刺激的延长肌肉收缩的下游信号传导反应。用高频坐骨神经电刺激（STIM）对年轻成年（8 mo）Fischer 344 X Brown Norway雄性大鼠的指伸长肌（n = 8 /组）进行22分钟的延长收缩训练。电刺激前四十分钟，给大鼠皮下注射生理盐水或AMPK激活剂5-氨基咪唑4-羧酰胺-1--4-呋喃呋喃糖苷（AICAR; 1 mg / g体重）。在STIM后0、20和40分钟时去除刺激的和对侧的静息肌，并去除AMPK，乙酰辅酶A羧化酶（ACC），Akt，真核起始因子4E结合蛋白（4E-BP1），70 kDa核糖体蛋白S6蛋白质印迹法评估激酶（S6K1）和真核延伸因子2（eEF2）的磷酸化。 AICAR治疗在STIM AMPK（Thr（172））和ACC磷酸化（Ser（79/221））后增加（P <= 0.05），抑制在STIM S6K1（Thr（389））和4E-BP1（凝胶移位）磷酸化和STIM后eEF2磷酸化水平升高（Thr（56））。这些发现表明，在延长收缩后，AMPK激活可抑制Akt / mTOR下游的翻译信号传导，而精力充沛的压力可能会对抗对负载的肌肉收缩的肥大翻译信号反应。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号