Wolfberries potentiate mitophagy and enhance mitochondrial biogenesis leading to prevention of hepatic steatosis in obese mice: The role of AMP-activated protein kinase α2 subunit

2014 ◽  
Vol 58 (5) ◽  
pp. 1005-1015 ◽  
Author(s):  
Dingbo Lin ◽  
Hui He ◽  
Hua Ji ◽  
Jordan Willis ◽  
Lloyd Willard ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Hepatic Steatosis ◽  
Mitochondrial Biogenesis ◽  
Obese Mice ◽  
Amp Activated Protein Kinase

scholarly journals Critical role of AMP-activated protein kinase in the balance between mitophagy and mitochondrial biogenesis in MELAS disease

2015 ◽  
Vol 1852 (11) ◽  
pp. 2535-2553 ◽  
Author(s):  
Juan Garrido-Maraver ◽  
Marina Villanueva Paz ◽  
Mario D. Cordero ◽  
Juan Bautista-Lorite ◽  
Manuel Oropesa-Ávila ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Mitochondrial Biogenesis ◽  
Critical Role ◽  
Amp Activated Protein Kinase

scholarly journals The role of AMP-activated protein kinase in quercetin-induced apoptosis of HL-60 cells

2014 ◽  
Vol 46 (5) ◽  
pp. 394-400 ◽  
Author(s):  
J. Xiao ◽  
G. Niu ◽  
S. Yin ◽  
S. Xie ◽  
Y. Li ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Induced Apoptosis ◽  
Amp Activated Protein Kinase

Role of the AMP-activated protein kinase in regulating fatty acid metabolism during exerciseThis paper is one of a selection of papers published in this Special Issue, entitled 14th International Biochemistry of Exercise Conference – Muscles as Molecular and Metabolic Machines, and has undergone the Journal’s usual peer review process.

2009 ◽  
Vol 34 (3) ◽  
pp. 315-322 ◽  
Author(s):  
Gregory R. Steinberg
Keyword(s):  
Skeletal Muscle ◽  
Fatty Acids ◽  
Adipose Tissue ◽  
Fatty Acid ◽  
Protein Kinase ◽  
Fatty Acid Metabolism ◽  
Acid Metabolism ◽  
Moderate Intensity ◽  
Amp Activated Protein Kinase

During moderate-intensity exercise, fatty acids are the predominant substrate for working skeletal muscle. The release of fatty acids from adipose tissue stores, combined with the ability of skeletal muscle to actively fine tune the gradient between fatty acid and carbohydrate metabolism, depending on substrate availability and energetic demands, requires a coordinated system of metabolic control. Over the past decade, since the discovery that AMP-activated protein kinase (AMPK) was increased in accordance with exercise intensity, there has been significant interest in the proposed role of this ancient stress-sensing kinase as a critical integrative switch controlling metabolic responses during exercise. In this review, studies examining the role of AMPK as a regulator of fatty acid metabolism in both adipose tissue and skeletal muscle during exercise will be discussed. Exercise induces activation of AMPK in adipocytes and regulates triglyceride hydrolysis and esterfication through phosphorylation of hormone sensitive lipase (HSL) and glycerol-3-phosphate acyl-transferase, respectively. In skeletal muscle, exercise-induced activation of AMPK is associated with increases in fatty acid uptake, phosphorylation of HSL, and increased fatty acid oxidation, which is thought to occur via the acetyl-CoA carboxylase-malony-CoA-CPT-1 signalling axis. Despite the importance of AMPK in regulating fatty acid metabolism under resting conditions, recent evidence from transgenic models of AMPK deficiency suggest that alternative signalling pathways may also be important for the control of fatty acid metabolism during exercise.

The emerging role of AMP-activated protein kinase in cholestatic liver diseases

2017 ◽  
Vol 125 ◽  
pp. 105-113 ◽  
Author(s):  
Xiaojiaoyang Li ◽  
Runping Liu ◽  
Luyong Zhang ◽  
Zhenzhou Jiang
Keyword(s):  
Protein Kinase ◽  
Liver Diseases ◽  
Amp Activated Protein Kinase

scholarly journals Beneficial Role of Erythrocyte Adenosine A2B Receptor–Mediated AMP-Activated Protein Kinase Activation in High-Altitude Hypoxia

Circulation ◽  
2016 ◽  
Vol 134 (5) ◽  
pp. 405-421 ◽  
Author(s):  
Hong Liu ◽  
Yujin Zhang ◽  
Hongyu Wu ◽  
Angelo D’Alessandro ◽  
Gennady G. Yegutkin ◽  
...  
Keyword(s):  
Protein Kinase ◽  
High Altitude ◽  
Altitude Hypoxia ◽  
Kinase Activation ◽  
Beneficial Role ◽  
Protein Kinase Activation ◽  
A2b Receptor ◽  
Amp Activated Protein Kinase ◽  
Adenosine A2b

scholarly journals Role of Binding and Nucleoside Diphosphate Kinase A (NDPK‐A) in the Regulation of CFTR by AMP‐Activated Protein Kinase (AMPK)

2012 ◽  
Vol 26 (S1) ◽  
Author(s):  
J Darwin King ◽  
Jeffrey Lee ◽  
Claudia E. Rieman ◽  
Anil Mehta ◽  
Richmond Muimo ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Nucleoside Diphosphate Kinase ◽  
Amp Activated Protein Kinase ◽  
Kinase A

scholarly journals Characterization of the Role of AMP-Activated Protein Kinase in the Regulation of Glucose-Activated Gene Expression Using Constitutively Active and Dominant Negative Forms of the Kinase

2000 ◽  
Vol 20 (18) ◽  
pp. 6704-6711 ◽  
Author(s):  
Angela Woods ◽  
Dalila Azzout-Marniche ◽  
Marc Foretz ◽  
Silvie C. Stein ◽  
Patricia Lemarchand ◽  
...  
Keyword(s):  
Gene Expression ◽  
Protein Kinase ◽  
Fatty Acid Synthase ◽  
Physiological Role ◽  
Rat Hepatocytes ◽  
Dominant Negative ◽  
Ampk Activity ◽  
Amp Activated Protein Kinase ◽  
Constitutively Active

ABSTRACT In the liver, glucose induces the expression of a number of genes involved in glucose and lipid metabolism, e.g., those encoding L-type pyruvate kinase and fatty acid synthase. Recent evidence has indicated a role for the AMP-activated protein kinase (AMPK) in the inhibition of glucose-activated gene expression in hepatocytes. It remains unclear, however, whether AMPK is involved in the glucose induction of these genes. In order to study further the role of AMPK in regulating gene expression, we have generated two mutant forms of AMPK. One of these (α1312) acts as a constitutively active kinase, while the other (α1DN) acts as a dominant negative inhibitor of endogenous AMPK. We have used adenovirus-mediated gene transfer to express these mutants in primary rat hepatocytes in culture in order to determine their effect on AMPK activity and the transcription of glucose-activated genes. Expression of α1312 increased AMPK activity in hepatocytes and blocked completely the induction of a number of glucose-activated genes in response to 25 mM glucose. This effect is similar to that observed following activation of AMPK by 5-amino-imidazolecarboxamide riboside. Expression of α1DN markedly inhibited both basal and stimulated activity of endogenous AMPK but had no effect on the transcription of glucose-activated genes. Our results suggest that AMPK is involved in the inhibition of glucose-activated gene expression but not in the induction pathway. This study demonstrates that the two mutants we have described will provide valuable tools for studying the wider physiological role of AMPK.

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