Literature DB >> 20124121

Reduction of AMP-activated protein kinase alpha2 increases endoplasmic reticulum stress and atherosclerosis in vivo.

Yunzhou Dong1, Miao Zhang, Bin Liang, Zhonglin Xie, Zhengxing Zhao, Sima Asfa, Hyoung Chul Choi, Ming-Hui Zou.   

Abstract

BACKGROUND: Aberrant endoplasmic reticulum (ER) stress is associated with several cardiovascular diseases, including atherosclerosis. The mechanism by which aberrant ER stress develops is poorly understood. This study investigated whether dysfunction of AMP-activated protein kinase (AMPK) causes aberrant ER stress and atherosclerosis in vivo. METHODS AND
RESULTS: Human umbilical vein endothelial cells and mouse aortic endothelial cells from AMPK-deficient mice were used to assess the level of ER stress with Western blotting. Reduction of AMPKalpha2 expression significantly increased the level of ER stress in human umbilical vein endothelial cells. In addition, mouse aortic endothelial cells from AMPKalpha2 knockout (AMPKalpha2(-/-)) mice had higher expression of markers of ER stress and increased levels of intracellular Ca2+. These phenotypes were abolished by adenovirally overexpressing constitutively active AMPK mutants (Ad-AMPK-CA) or by transfecting sarcoendoplasmic reticulum calcium ATPase (SERCA). Inhibition of SERCA induced ER stress in endothelial cells. Furthermore, reduction of AMPKalpha expression suppressed SERCA activity. In addition, SERCA activity was significantly reduced concomitantly with increased oxidation of SERCA in mouse aortic endothelial cells from AMPKalpha2(-/-) mice. Both of these phenotypes were abolished by adenovirally overexpressing Ad-AMPK-CA. Furthermore, Tempol, which restored SERCA activity and decreased oxidized SERCA levels, markedly reduced the level of ER stress in mouse aortic endothelial cells from AMPKalpha2(-/-) mice. Finally, oral administration of tauroursodeoxycholic acid, a chemical chaperone that inhibits ER stress, significantly reduced both ER stress and aortic lesion development in low-density lipoprotein receptor- and AMPKalpha2-deficient mice.
CONCLUSIONS: These results suggest that AMPK functions as a physiological suppressor of ER stress by maintaining SERCA activity and intracellular Ca2+ homeostasis.

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Year:  2010        PMID: 20124121      PMCID: PMC2825900          DOI: 10.1161/CIRCULATIONAHA.109.900928

Source DB:  PubMed          Journal:  Circulation        ISSN: 0009-7322            Impact factor:   29.690


  50 in total

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2.  Hyperglycemia-induced apoptosis in human umbilical vein endothelial cells: inhibition by the AMP-activated protein kinase activation.

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Review 1.  Endoplasmic reticulum stress: a novel mechanism and therapeutic target for cardiovascular diseases.

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Journal:  Acta Pharmacol Sin       Date:  2016-02-01       Impact factor: 6.150

2.  AMP-Activated Protein Kinase Alpha 2 Deletion Induces VSMC Phenotypic Switching and Reduces Features of Atherosclerotic Plaque Stability.

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Review 3.  Mitochondrial ROS and cancer drug resistance: Implications for therapy.

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Journal:  Pharmacol Res       Date:  2015-08-11       Impact factor: 7.658

4.  Cholinergic receptors play a role in the cardioprotective effects of anesthetic preconditioning: Roles of nitric oxide and the CaMKKβ/AMPK pathway.

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7.  Hyperglycemia-Driven Inhibition of AMP-Activated Protein Kinase α2 Induces Diabetic Cardiomyopathy by Promoting Mitochondria-Associated Endoplasmic Reticulum Membranes In Vivo.

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8.  Activation of AMP-activated protein kinase by metformin ablates angiotensin II-induced endoplasmic reticulum stress and hypertension in mice in vivo.

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Review 9.  Role of endoplasmic reticulum stress signalling in diabetic endothelial dysfunction and atherosclerosis.

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10.  Update on vascular endothelial Ca(2+) signalling: A tale of ion channels, pumps and transporters.

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