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      The Role of AMPK in the Regulation of Skeletal Muscle Size, Hypertrophy, and Regeneration

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      Publication date (Electronic):
      Journal: International Journal of Molecular Sciences
      Publisher: MDPI
      Keywords: AMPK, LKB1, autophagy, proteasome, hypertrophy, atrophy, skeletal muscle, AICAR, mTOR, protein synthesis

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          Abstract

          AMPK (5’-adenosine monophosphate-activated protein kinase) is heavily involved in skeletal muscle metabolic control through its regulation of many downstream targets. Because of their effects on anabolic and catabolic cellular processes, AMPK plays an important role in the control of skeletal muscle development and growth. In this review, the effects of AMPK signaling, and those of its upstream activator, liver kinase B1 (LKB1), on skeletal muscle growth and atrophy are reviewed. The effect of AMPK activity on satellite cell-mediated muscle growth and regeneration after injury is also reviewed. Together, the current data indicate that AMPK does play an important role in regulating muscle mass and regeneration, with AMPKα1 playing a prominent role in stimulating anabolism and in regulating satellite cell dynamics during regeneration, and AMPKα2 playing a potentially more important role in regulating muscle degradation during atrophy.

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          Mammalian Autophagy: How Does It Work?

          Carla F Bento, Maurizio Renna, Ghita Ghislat … (2016)
          Autophagy is a conserved intracellular pathway that delivers cytoplasmic contents to lysosomes for degradation via double-membrane autophagosomes. Autophagy substrates include organelles such as mitochondria, aggregate-prone proteins that cause neurodegeneration and various pathogens. Thus, this pathway appears to be relevant to the pathogenesis of diverse diseases, and its modulation may have therapeutic value. Here, we focus on the cell and molecular biology of mammalian autophagy and review the key proteins that regulate the process by discussing their roles and how these may be modulated by posttranslational modifications. We consider the membrane-trafficking events that impact autophagy and the questions relating to the sources of autophagosome membrane(s). Finally, we discuss data from structural studies and some of the insights these have provided.
          Article 0 comments Cited 316 times – based on 0 reviews     Review now
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            Mitochondrial fission and remodelling contributes to muscle atrophy.

            Vanina Romanello, Eleonora Guadagnin, Ligia F Gomes … (2010)
            Mitochondria are crucial organelles in the production of energy and in the control of signalling cascades. A machinery of pro-fusion and fission proteins regulates their morphology and subcellular localization. In muscle this results in an orderly pattern of intermyofibrillar and subsarcolemmal mitochondria. Muscular atrophy is a genetically controlled process involving the activation of the autophagy-lysosome and the ubiquitin-proteasome systems. Whether and how the mitochondria are involved in muscular atrophy is unknown. Here, we show that the mitochondria are removed through autophagy system and that changes in mitochondrial network occur in atrophying muscles. Expression of the fission machinery is per se sufficient to cause muscle wasting in adult animals, by triggering organelle dysfunction and AMPK activation. Conversely, inhibition of the mitochondrial fission inhibits muscle loss during fasting and after FoxO3 overexpression. Mitochondrial-dependent muscle atrophy requires AMPK activation as inhibition of AMPK restores muscle size in myofibres with altered mitochondria. Thus, disruption of the mitochondrial network is an essential amplificatory loop of the muscular atrophy programme.
            Article 0 comments Cited 241 times – based on 0 reviews     Review now
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              Glucose restriction inhibits skeletal myoblast differentiation by activating SIRT1 through AMPK-mediated regulation of Nampt.

              Marcella Fulco, Yana Cen, Po Zhao … (2008)
              It is intuitive to speculate that nutrient availability may influence differentiation of mammalian cells. Nonetheless, a comprehensive complement of the molecular determinants involved in this process has not been elucidated yet. Here, we have investigated how nutrients (glucose) affect skeletal myogenesis. Glucose restriction (GR) impaired differentiation of skeletal myoblasts and was associated with activation of the AMP-activated protein kinase (AMPK). Activated AMPK was required to promote GR-induced transcription of the NAD+ biosynthetic enzyme Nampt. Indeed, GR augmented the Nampt activity, which consequently modified the intracellular [NAD+]:[NADH] ratio and nicotinamide levels, and mediated inhibition of skeletal myogenesis. Skeletal myoblasts derived from SIRT1+/- heterozygous mice were resistant to the effects of either GR or AMPK activation. These experiments reveal that AMPK, Nampt, and SIRT1 are the molecular components of a functional signaling pathway that allows skeletal muscle cells to sense and react to nutrient availability.
              Article 0 comments Cited 229 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (nlm-ta): Int J Mol Sci
                Journal ID (iso-abbrev): Int J Mol Sci
                Journal ID (publisher-id): ijms
                Title: International Journal of Molecular Sciences
                Publisher: MDPI
                ISSN (Electronic): 1422-0067
                Publication date (Electronic): 11 October 2018
                Publication date Collection: October 2018
                Volume: 19
                Issue: 10
                Electronic Location Identifier: 3125
                Affiliations
                Department of Physiology & Developmental Biology, Brigham Young University, Provo, UT 84602, USA; david_thomson@ 123456byu.edu ; Tel.: +1-801-422-8709
                Article
                Publisher ID: ijms-19-03125
                DOI: 10.3390/ijms19103125
                PMC ID: 6212977
                PubMed ID: 30314396
                SO-VID: f03c94f7-dc0c-4dda-9bf3-01d9dcedca43
                Copyright © © 2018 by the author.
                License:

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 28 September 2018
                Date accepted : 09 October 2018
                Categories
                Subject: Review

                ScienceOpen disciplines: Molecular biology
                Keywords: ampk,lkb1,autophagy,proteasome,hypertrophy,atrophy,skeletal muscle,aicar,mtor,protein synthesis
                Data availability:
                ScienceOpen disciplines: Molecular biology
                Keywords: ampk, lkb1, autophagy, proteasome, hypertrophy, atrophy, skeletal muscle, aicar, mtor, protein synthesis

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