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A distinct AMP-activated protein kinase phosphorylation site characterizes cardiac hypertrophy induced by l-thyroxine and angiotensin II
Jiang, Sheng-Yang; Xu, Ming; Ma, Xiao-Wei; Xiao, Han; Zhang, You-Yi1
关键词AMP-activated protein kinase angiotensin II cardiac hypertrophy l-thyroxine phosphorylation
刊名CLINICAL AND EXPERIMENTAL PHARMACOLOGY AND PHYSIOLOGY
2010-09-01
DOI10.1111/j.1440-1681.2010.05404.x
37期:9页:919-925
收录类别SCI
文章类型Article
WOS标题词Science & Technology
类目[WOS]Pharmacology & Pharmacy ; Physiology
研究领域[WOS]Pharmacology & Pharmacy ; Physiology
关键词[WOS]MYOSIN HEAVY-CHAIN ; PRESSURE-OVERLOAD HYPERTROPHY ; LEFT-VENTRICULAR HYPERTROPHY ; CARDIOMYOCYTE HYPERTROPHY ; SIGNALING PATHWAY ; MESSENGER-RNA ; AKT ACTIVITY ; RAT HEARTS ; EXPRESSION ; ISOPROTERENOL
英文摘要

P>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 AMPK alpha 2-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 alpha-Ser485/491 and alpha-Thr172 was determined by western blot analysis.

3. In wild-type mice, the phosphorylation of AMPK alpha-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 AMPK alpha-Thr172 was significantly increased by thyroxine, but not AngII, treatment compared with the vehicle control group. Furthermore, knockout of the AMPK alpha 2 subunit abolished phosphorylation at the alpha-Ser485/491 site and significantly suppressed phosphorylation at the alpha-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 alpha-Thr172 may contribute to thyroxine-induced cardiac hypertrophy.

语种英语
WOS记录号WOS:000281219600010
引用统计
被引频次:4[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.bjmu.edu.cn/handle/400002259/67599
专题北京大学第三临床医学院_心血管内科
作者单位1.Peking Univ, Hosp 3, Inst Vasc Med, Beijing 100191, Peoples R China
2.Minist Educ, Key Lab Mol Cardiovasc Sci, Beijing, Peoples R China
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GB/T 7714
Jiang, Sheng-Yang,Xu, Ming,Ma, Xiao-Wei,et al. A distinct AMP-activated protein kinase phosphorylation site characterizes cardiac hypertrophy induced by l-thyroxine and angiotensin II[J]. CLINICAL AND EXPERIMENTAL PHARMACOLOGY AND PHYSIOLOGY,2010,37(9):919-925.
APA Jiang, Sheng-Yang,Xu, Ming,Ma, Xiao-Wei,Xiao, Han,&Zhang, You-Yi.(2010).A distinct AMP-activated protein kinase phosphorylation site characterizes cardiac hypertrophy induced by l-thyroxine and angiotensin II.CLINICAL AND EXPERIMENTAL PHARMACOLOGY AND PHYSIOLOGY,37(9),919-925.
MLA Jiang, Sheng-Yang,et al."A distinct AMP-activated protein kinase phosphorylation site characterizes cardiac hypertrophy induced by l-thyroxine and angiotensin II".CLINICAL AND EXPERIMENTAL PHARMACOLOGY AND PHYSIOLOGY 37.9(2010):919-925.
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