Faculty Opinions recommendation of Short-term adenosine monophosphate-activated protein kinase activator 5-aminoimidazole-4-carboxamide-1-β-D-ribofuranoside treatment increases the sirtuin 1 protein expression in skeletal muscle.

During fasting, rapid metabolic adaptations are required to maintain energy homeostasis. This occurs by a coordinated regulation of energy/nutrient-sensing pathways leading to transcriptional activation and repression of specific sets of genes. The aim of the study was to investigate how short-term fasting affects whole body energy homeostasis and skeletal muscle energy/nutrient-sensing pathways and transcriptome in humans. For this purpose, 12 young healthy men were studied during a 24-h fast. Whole body glucose/lipid oxidation rates were determined by indirect calorimetry, and blood and skeletal muscle biopsies were collected and analyzed at baseline and after 10 and 24 h of fasting. As expected, fasting induced a time-dependent decrease in plasma insulin and leptin levels, whereas levels of ketone bodies and free fatty acids increased. This was associated with a metabolic shift from glucose toward lipid oxidation. At the molecular level, activation of the protein kinase B (PKB/Akt) and mammalian target of rapamycin pathways was time-dependently reduced in skeletal muscle during fasting, whereas the AMP-activated protein kinase activity remained unaffected. Furthermore, we report some changes in the phosphorylation and/or content of forkhead protein 1, sirtuin 1, and class IIa histone deacetylase 4, suggesting that these pathways might be involved in the transcriptional adaptation to fasting. Finally, transcriptome profiling identified genes that were significantly regulated by fasting in skeletal muscle at both early and late time points. Collectively, our study provides a comprehensive map of the main energy/nutrient-sensing pathways and transcriptomic changes during short-term adaptation to fasting in human skeletal muscle.

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AMP-Activated Protein Kinase as a Key Trigger for the Disuse-Induced Skeletal Muscle Remodeling

International Journal of Molecular Sciences ◽

10.3390/ijms19113558 ◽

2018 ◽

Vol 19 (11) ◽

pp. 3558 ◽

Cited By ~ 13

Author(s):

Natalia Vilchinskaya ◽

Igor Krivoi ◽

Boris Shenkman

Keyword(s):

Skeletal Muscle ◽

Protein Kinase ◽

Histone Deacetylases ◽

Molecular Mechanisms ◽

Weight Bearing ◽

Mammalian Target Of Rapamycin ◽

Adenosine Monophosphate ◽

Chain Gene ◽

Mtorc1 Signaling ◽

The Impact

Molecular mechanisms that trigger disuse-induced postural muscle atrophy as well as myosin phenotype transformations are poorly studied. This review will summarize the impact of 5′ adenosine monophosphate -activated protein kinase (AMPK) activity on mammalian target of rapamycin complex 1 (mTORC1)-signaling, nuclear-cytoplasmic traffic of class IIa histone deacetylases (HDAC), and myosin heavy chain gene expression in mammalian postural muscles (mainly, soleus muscle) under disuse conditions, i.e., withdrawal of weight-bearing from ankle extensors. Based on the current literature and the authors’ own experimental data, the present review points out that AMPK plays a key role in the regulation of signaling pathways that determine metabolic, structural, and functional alternations in skeletal muscle fibers under disuse.

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Reduced sirtuin 1/adenosine monophosphate‐activated protein kinase in amyotrophic lateral sclerosis patient‐derived mesenchymal stem cells can be restored by resveratrol

Journal of Tissue Engineering and Regenerative Medicine ◽

10.1002/term.2776 ◽

2018 ◽

Cited By ~ 3

Author(s):

Young Chan Yun ◽

Sin‐Gu Jeong ◽

Seung Hyun Kim ◽

Goang‐Won Cho

Keyword(s):

Stem Cells ◽

Amyotrophic Lateral Sclerosis ◽

Mesenchymal Stem Cells ◽

Protein Kinase ◽

Amyotrophic Lateral Sclerosis Patient ◽

Adenosine Monophosphate ◽

Sirtuin 1 ◽

Lateral Sclerosis

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Genistein promotes insulin action through adenosine monophosphate–activated protein kinase activation and p70 ribosomal protein S6 kinase 1 inhibition in the skeletal muscle of mice fed a high energy diet

Nutrition Research ◽

10.1016/j.nutres.2012.06.002 ◽

2012 ◽

Vol 32 (8) ◽

pp. 617-625 ◽

Cited By ~ 23

Author(s):

Elumalai Arunkumar ◽

Carani Venkatraman Anuradha

Keyword(s):

Skeletal Muscle ◽

Protein Kinase ◽

Ribosomal Protein ◽

Insulin Action ◽

Adenosine Monophosphate ◽

High Energy ◽

S6 Kinase ◽

Kinase Activation ◽

Ribosomal Protein S6 ◽

Protein Kinase Activation

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Separation of regulatory and catalytic subunits of the cyclic 3′, 5′-adenosine monophosphate-dependent protein kinase(s) of rabbit skeletal muscle

Biochemical and Biophysical Research Communications ◽

10.1016/0006-291x(71)90086-6 ◽

1971 ◽

Vol 42 (2) ◽

pp. 187-194 ◽

Cited By ~ 206

Author(s):

E.M. Reimann ◽

C.O. Brostrom ◽

J.D. Corbin ◽

C.A. King ◽

E.G. Krebs

Keyword(s):

Skeletal Muscle ◽

Protein Kinase ◽

Adenosine Monophosphate ◽

Rabbit Skeletal Muscle ◽

Dependent Protein Kinase ◽

Catalytic Subunits ◽

Dependent Protein

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Angiotensin II inhibits glucose uptake of skeletal muscle via the adenosine monophosphate-activated protein kinase pathway

Journal of the American Society of Hypertension ◽

10.1016/j.jash.2007.04.007 ◽

2007 ◽

Vol 1 (4) ◽

pp. 251-255 ◽

Cited By ~ 8

Author(s):

Yasuyuki Shinshi ◽

Katsuhiro Higashiura ◽

Daisuke Yoshida ◽

Nobuhiko Togashi ◽

Hideaki Yoshida ◽

...

Keyword(s):

Skeletal Muscle ◽

Angiotensin Ii ◽

Protein Kinase ◽

Glucose Uptake ◽

Adenosine Monophosphate ◽

Kinase Pathway

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Thyroid Hormone Stimulation of Autophagy Is Essential for Mitochondrial Biogenesis and Activity in Skeletal Muscle

Endocrinology ◽

10.1210/en.2015-1632 ◽

2016 ◽

Vol 157 (1) ◽

pp. 23-38 ◽

Cited By ~ 41

Author(s):

Ronny Lesmana ◽

Rohit A. Sinha ◽

Brijesh K. Singh ◽

Jin Zhou ◽

Kenji Ohba ◽

...

Keyword(s):

Skeletal Muscle ◽

Thyroid Hormone ◽

Protein Kinase ◽

Mitochondrial Biogenesis ◽

Mitochondrial Protein ◽

Adenosine Monophosphate ◽

Mitochondrial Activity ◽

Dependent Manner ◽

In Vivo Models ◽

Stimulation Of

Abstract Thyroid hormone (TH) and autophagy share similar functions in regulating skeletal muscle growth, regeneration, and differentiation. Although TH recently has been shown to increase autophagy in liver, the regulation and role of autophagy by this hormone in skeletal muscle is not known. Here, using both in vitro and in vivo models, we demonstrated that TH induces autophagy in a dose- and time-dependent manner in skeletal muscle. TH induction of autophagy involved reactive oxygen species (ROS) stimulation of 5′adenosine monophosphate-activated protein kinase (AMPK)-Mammalian target of rapamycin (mTOR)- Unc-51-like kinase 1 (Ulk1) signaling. TH also increased mRNA and protein expression of key autophagy genes, microtubule-associated protein light chain 3 (LC3), Sequestosome 1 (p62), and Ulk1, as well as genes that modulated autophagy and Forkhead box O (FOXO) 1/3a. TH increased mitochondrial protein synthesis and number as well as basal mitochondrial O2 consumption, ATP turnover, and maximal respiratory capacity. Surprisingly, mitochondrial activity and biogenesis were blunted when autophagy was blocked in muscle cells by Autophagy-related gene (Atg)5 short hairpin RNA (shRNA). Induction of ROS and 5′adenosine monophosphate-activated protein kinase (AMPK) by TH played a significant role in the up-regulation of Peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PPARGC1A), the key regulator of mitochondrial synthesis. In summary, our findings showed that TH-mediated autophagy was essential for stimulation of mitochondrial biogenesis and activity in skeletal muscle. Moreover, autophagy and mitochondrial biogenesis were coupled in skeletal muscle via TH induction of mitochondrial activity and ROS generation.

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Roles of adenosine monophosphate–activated protein kinase in skeletal muscle: fatty acid oxidation, glucose transport, and gene regulation

Current Opinion in Endocrinology & Diabetes ◽

10.1097/00060793-200108000-00003 ◽

2001 ◽

Vol 8 (4) ◽

pp. 180-185 ◽

Cited By ~ 2

Author(s):

William W. Winder

Keyword(s):

Skeletal Muscle ◽

Gene Regulation ◽

Fatty Acid ◽

Protein Kinase ◽

Glucose Transport ◽

Fatty Acid Oxidation ◽

Adenosine Monophosphate ◽

Acid Oxidation

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The Effects of Testosterone Deprivation and Supplementation on Proteasomal and Autophagy Activity in the Skeletal Muscle of the Male Mouse: Differential Effects on High-Androgen Responder and Low-Androgen Responder Muscle Groups

Endocrinology ◽

10.1210/en.2013-1004 ◽

2013 ◽

Vol 154 (12) ◽

pp. 4594-4606 ◽

Cited By ~ 35

Author(s):

Carlo Serra ◽

Nicolae Lucian Sandor ◽

Hyeran Jang ◽

Daniel Lee ◽

Gianluca Toraldo ◽

...

Keyword(s):

Skeletal Muscle ◽

Protein Kinase ◽

Enzymatic Activity ◽

Levator Ani ◽

Androgen Deprivation ◽

Levator Ani Muscle ◽

Short Term ◽

Triceps Muscle ◽

Amp Activated Protein Kinase

Men with prostate cancer who receive androgen deprivation therapy show profound skeletal muscle loss. We hypothesized that the androgen deficiency activates not only the ubiquitin-proteasome systems but also the autophagy and affects key aspects of the molecular cross talk between protein synthesis and degradation. Here, 2-month-old male mice were castrated and treated with either testosterone (T) propionate or vehicle for 7 days (short term) or 43 days (long term), and with and without hydroxyflutamide. Castrated mice showed rapid and profound atrophy of the levator ani muscle (high androgen responder) at short term and lesser atrophy of the triceps muscle (low androgen responder) at long term. Levator ani and triceps muscles of castrated mice showed increased level of autophagy markers and lysosome enzymatic activity; only the levator ani showed increased proteasomal enzymatic activity. The levator ani muscle of the castrated mice showed increased level and activation of forkhead box protein O3A, the inhibition of mechanistic target of rapamicyn, and the activation of tuberous sclerosis complex protein 2 and 5′-AMP-activated protein kinase. Similar results were obtained in the triceps muscle of castrated mice. T rescued the loss of muscle mass after orchiectomy and inhibited lysosome and proteasome pathways dose dependently and in a seemingly IGF-I-dependent manner. Hydroxyflutamide attenuated the effect of T in the levator ani muscle of castrated mice. In conclusion, androgen deprivation in adult mice induces muscle atrophy associated with proteasomal and lysosomal activity. T optimizes muscle protein balance by modulating the equilibrium between mechanistic target of rapamicyn and 5′-AMP-activated protein kinase pathways.

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