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      Resveratrol Improves Muscle Atrophy by Modulating Mitochondrial Quality Control in STZ‐Induced Diabetic Mice

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          Abstract

          Scope

          In this study, we aim to determine the effects of resveratrol (RSV) on muscle atrophy in streptozocin‐induced diabetic mice and to explore mitochondrial quality control (MQC) as a possible mechanism.

          Methods and results

          The experimental mice were fed either a control diet or an identical diet containing 0.04% RSV for 8 weeks. Examinations were subsequently carried out, including the effects of RSV on muscle atrophy and muscle function, as well as on the signaling pathways related to protein degradation and MQC processes. The results show that RSV supplementation improves muscle atrophy and muscle function, attenuates the increase in ubiquitin and muscle RING‐finger protein‐1 (MuRF‐1), and simultaneously attenuates LC3‐II and cleaved caspase‐3 in the skeletal muscle of diabetic mice. Moreover, RSV treatment of diabetic mice results in an increase in mitochondrial biogenesis and inhibition of the activation of mitophagy in skeletal muscle. RSV also protects skeletal muscle against excess mitochondrial fusion and fission in the diabetic mice.

          Conclusion

          The results suggest that RSV ameliorates diabetes‐induced skeletal muscle atrophy by modulating MQC.

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          Autophagy in skeletal muscle.

          Marco Sandri (2010)
          Muscle mass represents 40-50% of the human body and, in mammals, is one of the most important sites for the control of metabolism. Moreover, during catabolic conditions, muscle proteins are mobilized to sustain gluconeogenesis in the liver and to provide alternative energy substrates for organs. However, excessive protein degradation in the skeletal muscle is detrimental for the economy of the body and it can lead to death. The ubiquitin-proteasome and autophagy-lysosome systems are the major proteolytic pathways of the cell and are coordinately activated in atrophying muscles. However, the role and regulation of the autophagic pathway in skeletal muscle is still largely unknown. This review will focus on autophagy and discuss its beneficial or detrimental role for the maintenance of muscle mass. Copyright 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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            IL-6 regulation on skeletal muscle mitochondrial remodeling during cancer cachexia in the ApcMin/+ mouse

            James P. White, Melissa J. Puppa, Shuichi Sato … (2012)
            Background Muscle protein turnover regulation during cancer cachexia is being rapidly defined, and skeletal muscle mitochondria function appears coupled to processes regulating muscle wasting. Skeletal muscle oxidative capacity and the expression of proteins regulating mitochondrial biogenesis and dynamics are disrupted in severely cachectic Apc Min/+ mice. It has not been determined if these changes occur at the onset of cachexia and are necessary for the progression of muscle wasting. Exercise and anti-cytokine therapies have proven effective in preventing cachexia development in tumor bearing mice, while their effect on mitochondrial content, biogenesis and dynamics is not well understood. The purposes of this study were to 1) determine IL-6 regulation on mitochondrial remodeling/dysfunction during the progression of cancer cachexia and 2) to determine if exercise training can attenuate mitochondrial dysfunction and the induction of proteolytic pathways during IL-6 induced cancer cachexia. Methods Apc Min/+ mice were examined during the progression of cachexia, after systemic interleukin (IL)-6r antibody treatment, or after IL-6 over-expression with or without exercise. Direct effects of IL-6 on mitochondrial remodeling were examined in cultured C2C12 myoblasts. Results Mitochondrial content was not reduced during the initial development of cachexia, while muscle PGC-1α and fusion (Mfn1, Mfn2) protein expression was repressed. With progressive weight loss mitochondrial content decreased, PGC-1α and fusion proteins were further suppressed, and fission protein (FIS1) was induced. IL-6 receptor antibody administration after the onset of cachexia improved mitochondrial content, PGC-1α, Mfn1/Mfn2 and FIS1 protein expression. IL-6 over-expression in pre-cachectic mice accelerated body weight loss and muscle wasting, without reducing mitochondrial content, while PGC-1α and Mfn1/Mfn2 protein expression was suppressed and FIS1 protein expression induced. Exercise normalized these IL-6 induced effects. C2C12 myotubes administered IL-6 had increased FIS1 protein expression, increased oxidative stress, and reduced PGC-1α gene expression without altered mitochondrial protein expression. Conclusions Altered expression of proteins regulating mitochondrial biogenesis and fusion are early events in the initiation of cachexia regulated by IL-6, which precede the loss of muscle mitochondrial content. Furthermore, IL-6 induced mitochondrial remodeling and proteolysis can be rescued with moderate exercise training even in the presence of high circulating IL-6 levels.
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              Dysregulation of Mitochondrial Quality Control Processes Contribute to Sarcopenia in a Mouse Model of Premature Aging

              Anna-Maria Joseph, Peter J. Adhihetty, Nicholas R. Wawrzyniak … (2013)
              Mitochondrial DNA (mtDNA) mutations lead to decrements in mitochondrial function and accelerated rates of these mutations has been linked to skeletal muscle loss (sarcopenia). The purpose of this study was to investigate the effect of mtDNA mutations on mitochondrial quality control processes in skeletal muscle from animals (young; 3–6 months and older; 8–15 months) expressing a proofreading-deficient version of mtDNA polymerase gamma (PolG). This progeroid aging model exhibits elevated mtDNA mutation rates, mitochondrial dysfunction, and a premature aging phenotype that includes sarcopenia. We found increased expression of the mitochondrial biogenesis regulator peroxisome proliferator-activated receptor gamma coactivator-1α (PGC-1α) and its target proteins, nuclear respiratory factor 1 (NRF-1) and mitochondrial transcription factor A (Tfam) in PolG animals compared to wild-type (WT) (P<0.05). Muscle from older PolG animals displayed higher mitochondrial fission protein 1 (Fis1) concurrent with greater induction of autophagy, as indicated by changes in Atg5 and p62 protein content (P<0.05). Additionally, levels of the Tom22 import protein were higher in PolG animals when compared to WT (P<0.05). In contrast, muscle from normally-aged animals exhibited a distinctly different expression profile compared to PolG animals. Older WT animals appeared to have higher fusion (greater Mfn1/Mfn2, and lower Fis1) and lower autophagy (Beclin-1 and p62) compared to young WT suggesting that autophagy is impaired in aging muscle. In conclusion, muscle from mtDNA mutator mice display higher mitochondrial fission and autophagy levels that likely contribute to the sarcopenic phenotype observed in premature aging and this differs from the response observed in normally-aged muscle.
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                Author and article information

                Contributors
                Dongtao Wang: 95401864@qq.com
                Shunmin Li: shunminli@126.com
                Journal
                Journal ID (nlm-ta): Mol Nutr Food Res
                Journal ID (iso-abbrev): Mol Nutr Food Res
                Journal ID (doi): 10.1002/(ISSN)1613-4133
                Journal ID (publisher-id): MNFR
                Title: Molecular Nutrition & Food Research
                Publisher: John Wiley and Sons Inc. (Hoboken )
                ISSN (Print): 1613-4125
                ISSN (Electronic): 1613-4133
                Publication date (Electronic): 23 April 2018
                Publication date (Print): May 2018
                Volume: 62
                Issue: 9 ( doiID: 10.1002/mnfr.v62.9 )
                Electronic Location Identifier: 1700941
                Affiliations
                [ 1 ] Department of Traditional Chinese Medicine Shenzhen Hospital Southern Medical University Shenzhen Guangdong 518000 China
                [ 2 ] Department of Nephrology Shenzhen Traditional Chinese Medicine Hospital Guangzhou University of Chinese Medicine Shenzhen Guangdong 518033 China
                [ 3 ] Department of Nephrology Ruikang Affiliated Hospital Guangxi University of Chinese Medicine Nanning 530011 China
                [ 4 ] Department of Pharmacology Guangdong Key Laboratory for R&D of Natural Drug Guangdong Medical College Zhanjiang 524023 China
                Author notes
                [*] [* ] Correspondence:

                Dr. Dongtao Wang

                E‐mail: 95401864@ 123456qq.com

                Dr. Shunmin Li

                E‐mail: shunminli@ 123456126.com

                Article
                Publisher ID: MNFR3204
                DOI: 10.1002/mnfr.201700941
                PMC ID: 6001753
                PubMed ID: 29578301
                SO-VID: 0582051c-c3d2-4e32-90c0-6f0f30cc6936
                Copyright © © 2018 The Authors. Published by WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim.
                License:

                This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

                History
                Date received : 13 November 2017
                Date revision received : 10 March 2018
                Page count
                Figures: 9, Tables: 1, Pages: 11, Words: 7240
                Funding
                Funded by: National Natural Science Foundation of China
                Award ID: 81503398
                Award ID: 81373565
                Funded by: China Postdoctoral Science Foundation
                Award ID: 2015M582372
                Funded by: Natural Science Foundation of Guangxi Province
                Award ID: 2015GXNSFBA139171
                Award ID: 2016GXNSFAA380005
                Funded by: Shenzhen Science and Technology Project
                Award ID: JCYJ20160428175036148
                Award ID: JSGG20141017103353178
                Funded by: Health and Family Planning Commission of Shenzhen Municipality
                Award ID: 201605013
                Funded by: Science and Technology Planning Project of Guangdong Province
                Award ID: 2016A020226032
                Award ID: 2017A020213008
                Categories
                Subject: Research Article
                Subject: Research Articles
                Custom metadata
                source-schema-version-number 2.0
                component-id mnfr3204
                cover-date May 2018
                details-of-publishers-convertor Converter:WILEY_ML3GV2_TO_NLMPMC version:version=5.4.1.1 mode:remove_FC converted:14.06.2018

                ScienceOpen disciplines: Nutrition & Dietetics
                Keywords: atrophy,diabetes,mitochondria,resveratrol,skeletal muscle
                Data availability:
                ScienceOpen disciplines: Nutrition & Dietetics
                Keywords: atrophy, diabetes, mitochondria, resveratrol, skeletal muscle

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