Get access

A distinct AMP-activated protein kinase phosphorylation site characterizes cardiac hypertrophy induced by l-thyroxine and angiotensin II

Authors

  • Sheng-Yang Jiang,

    Search for more papers by this author
    • Present address: Department of Cardiology, The 3rd People’s Hospital of Wuxi, Wuxi, Jiangsu, China.

  • Ming Xu,

    1. Institute of Vascular Medicine, Peking University Third Hospital and Key Laboratory of Molecular Cardiovascular Science, Ministry of Education, Beijing, China
    Search for more papers by this author
  • Xiao-Wei Ma,

    1. Institute of Vascular Medicine, Peking University Third Hospital and Key Laboratory of Molecular Cardiovascular Science, Ministry of Education, Beijing, China
    Search for more papers by this author
  • Han Xiao,

    1. Institute of Vascular Medicine, Peking University Third Hospital and Key Laboratory of Molecular Cardiovascular Science, Ministry of Education, Beijing, China
    Search for more papers by this author
  • You-Yi Zhang

    1. Institute of Vascular Medicine, Peking University Third Hospital and Key Laboratory of Molecular Cardiovascular Science, Ministry of Education, Beijing, China
    Search for more papers by this author

You-Yi Zhang, Institute of Vascular Medicine, Peking University Third Hospital, Beijing 100191, China. Email: zhangyy@bjmu.edu.cn

Summary

1. The purpose of the present study was to evaluate differences in the AMP-activated protein kinase (AMPK) phosphorylation sites in cardiac hypertrophy induced by l-thyroxine and angiotensin (Ang) II.

2. Cardiac hypertrophy was induced in wild-type and AMPKα2-knockout mice by treatment with 1 mg/kg, i.p., thyroxine or 1.44 mg/kg per day AngII for 14 days. The phenotype of the hypertrophy was evaluated using echocardiographic measurments and histological analyses. The phosphorylation of AMPK at α-Ser485/491 and α-Thr172 was determined by western blot analysis.

3. In wild-type mice, the phosphorylation of AMPKα-Ser485/491 was significantly elevated in the AngII-treated group, but not in the thyroxine-reated group, compared with the vehicle control group. In contrast, the phosphorylation of AMPKα-Thr172 was significantly increased by thyroxine, but not AngII, treatment compared with the vehicle control group. Furthermore, knockout of the AMPKα2 subunit abolished phosphorylation at the α-Ser485/491 site and significantly suppressed phosphorylation at the α-Thr172 site, resulting in alleviation of thyroxine- but not AngII-induced hypertrophy.

4. In conclusion, l-thyroxine and AngII induce the phosphorylation of distinct sites of AMPK in cardiac hypertrophy. Phosphorylation of AMPK α-Thr172 may contribute to thyroxine-induced cardiac hypertrophy.

Ancillary