Adenylosuccinic acid therapy ameliorates murine Duchenne Muscular Dystrophy.
Adenosine Monophosphate
/ analogs & derivatives
Animals
Calcium
/ analysis
Cell Line, Transformed
Collagen
/ analysis
Drug Evaluation, Preclinical
Electron Transport
/ drug effects
Humans
Lipids
/ analysis
Male
Mice
Mice, Inbred C57BL
Mice, Inbred mdx
Mitochondria, Muscle
/ drug effects
Muscle, Skeletal
/ drug effects
Muscular Dystrophy, Animal
/ drug therapy
Muscular Dystrophy, Duchenne
/ pathology
Myoblasts
/ metabolism
Organelle Biogenesis
Oxygen Consumption
/ drug effects
Superoxides
/ metabolism
Utrophin
/ biosynthesis
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
24 01 2020
24 01 2020
Historique:
received:
15
11
2017
accepted:
30
12
2019
entrez:
26
1
2020
pubmed:
26
1
2020
medline:
21
11
2020
Statut:
epublish
Résumé
Arising from the ablation of the cytoskeletal protein dystrophin, Duchenne Muscular Dystrophy (DMD) is a debilitating and fatal skeletal muscle wasting disease underpinned by metabolic insufficiency. The inability to facilitate adequate energy production may impede calcium (Ca
Identifiants
pubmed: 31980663
doi: 10.1038/s41598-020-57610-w
pii: 10.1038/s41598-020-57610-w
pmc: PMC6981178
doi:
Substances chimiques
Lipids
0
Utrn protein, mouse
0
Utrophin
0
Superoxides
11062-77-4
adenylosuccinate
19240-42-7
Adenosine Monophosphate
415SHH325A
Collagen
9007-34-5
Calcium
SY7Q814VUP
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1125Références
Hoffman, E. P., Brown, R. H. & Kunkel, L. M. Dystrophin: the protein product of the Duchenne muscular dystrophy locus. Cell 51, 919–928 (1987).
pubmed: 3319190
doi: 10.1016/0092-8674(87)90579-4
pmcid: 3319190
Bodensteiner, J. B. & Engel, A. G. Intracellular calcium accumulation in Duchenne dystrophy and other myopathies A study of 567,000 muscle fibers in 114 biopsies. Neurology 28, 439–439 (1978).
pubmed: 76996
doi: 10.1212/WNL.28.5.439
pmcid: 76996
Turner, P. R., Fong, P., Denetclaw, W. F. & Steinhardt, R. A. Increased calcium influx in dystrophic muscle. The Journal of Cell Biology 115, 1701–1712 (1991).
pubmed: 1661733
doi: 10.1083/jcb.115.6.1701
pmcid: 1661733
Alderton, J. M. & Steinhardt, R. A. Calcium influx through calcium leak channels is responsible for the elevated levels of calcium-dependent proteolysis in dystrophic myotubes. Journal of Biological Chemistry 275, 9452–9460 (2000).
pubmed: 10734092
doi: 10.1074/jbc.275.13.9452
pmcid: 10734092
Vandebrouck, C., Martin, D., Colson-Van Schoor, M., Debaix, H. & Gailly, P. Involvement of TRPC in the abnormal calcium influx observed in dystrophic (mdx) mouse skeletal muscle fibers. The Journal of cell biology 158, 1089–1096 (2002).
pubmed: 12235126
pmcid: 2173225
doi: 10.1083/jcb.200203091
Jackson, M. J., Jones, D. A. & Edwards, R. H. Measurements of calcium and other elements in muscle biopsy samples from patients with Duchenne muscular dystrophy. Clinica chimica acta 147, 215–221 (1985).
doi: 10.1016/0009-8981(85)90202-5
Williams, I. A. & Allen, D. G. Intracellular calcium handling in ventricular myocytes from mdx mice. American Journal of Physiology-Heart and Circulatory Physiology 292, H846–H855 (2007).
pubmed: 17012353
doi: 10.1152/ajpheart.00688.2006
pmcid: 17012353
Disatnik, M. H. et al. Evidence of oxidative stress in mdx mouse muscle: Studies of the pre-necrotic state. Journal of the Neurological Sciences 161, 77–84 (1998).
pubmed: 9879685
doi: 10.1016/S0022-510X(98)00258-5
pmcid: 9879685
Haycock, J. W., Mac Neil, S., Jones, P., Harris, J. B. & Mantle, D. Oxidative damage to muscle protein in Duchenne muscular dystrophy. Neuroreport 8, 357–361 (1996).
pubmed: 9051810
doi: 10.1097/00001756-199612200-00070
pmcid: 9051810
Dudley, R. W. et al. Sarcolemmal damage in dystrophin deficiency is modulated by synergistic interactions between mechanical and oxidative/nitrosative stresses. The American journal of pathology 168, 1276–1287 (2006).
pubmed: 16565501
pmcid: 1606574
doi: 10.2353/ajpath.2006.050683
Messina, S. et al. Lipid peroxidation inhibition blunts nuclear factor-κB activation, reduces skeletal muscle degeneration, and enhances muscle function in mdx mice. The American journal of pathology 168, 918–926 (2006).
pubmed: 16507907
pmcid: 1606515
doi: 10.2353/ajpath.2006.050673
Allen, D. G., Gervasio, O. L., Yeung, E. W. & Whitehead, N. P. Calcium and the damage pathways in muscular dystrophy This article is one of a selection of papers published in this special issue on Calcium Signaling. Canadian journal of physiology and pharmacology 88, 83–91 (2010).
pubmed: 20237582
doi: 10.1139/Y09-058
pmcid: 20237582
Eagle, M. et al. Survival in Duchenne muscular dystrophy: improvements in life expectancy since 1967 and the impact of home nocturnal ventilation. Neuromuscular Disorders 12, 926–929, https://doi.org/10.1016/S0960-8966(02)00140-2 (2002).
doi: 10.1016/S0960-8966(02)00140-2
pubmed: 12467747
pmcid: 12467747
Timpani, C. A., Hayes, A. & Rybalka, E. Revisiting the dystrophin-ATP connection: How half a century of research still implicates mitochondrial dysfunction in Duchenne Muscular Dystrophy aetiology. Medical Hypotheses 85, 1021–1033 (2015).
pubmed: 26365249
doi: 10.1016/j.mehy.2015.08.015
pmcid: 26365249
Hayes, A. & Williams, D. A. Beneficial effects of voluntary wheel running on the properties of dystrophic mouse muscle. Journal of applied physiology 80, 670–679 (1996).
pubmed: 8929614
doi: 10.1152/jappl.1996.80.2.670
pmcid: 8929614
Onopiuk, M. et al. Mutation in dystrophin-encoding gene affects energy metabolism in mouse myoblasts. Biochemical and Biophysical Research Communications 386, 463–466 (2009).
pubmed: 19527684
doi: 10.1016/j.bbrc.2009.06.053
pmcid: 19527684
Rybalka, E., Timpani, C. A., Cooke, M. B., Williams, A. D. & Hayes, A. Defects in Mitochondrial ATP Synthesis in Dystrophin-Deficient Mdx Skeletal Muscles May Be Caused by Complex I Insufficiency. PloS one 9, e115763 (2014).
pubmed: 25541951
pmcid: 4277356
doi: 10.1371/journal.pone.0115763
McDonald, C. M. et al. Idebenone reduces respiratory complications in patients with Duchenne muscular dystrophy. Neuromuscular Disorders 26, 473–480 (2016).
pubmed: 27238057
doi: 10.1016/j.nmd.2016.05.008
pmcid: 27238057
Rybalka, E., Timpani, C. A., Stathis, C. G., Hayes, A. & Cooke, M. B. Metabogenic and nutriceutical approaches to address energy dysregulation and skeletal muscle wasting in duchenne muscular dystrophy. Nutrients 7, 9734–9767 (2015).
pubmed: 26703720
pmcid: 4690050
doi: 10.3390/nu7125498
Bonsett, C. & Rudman, A. The dystrophin connection—ATP? Medical Hypotheses 38, 139–154 (1992).
pubmed: 1326712
doi: 10.1016/0306-9877(92)90087-S
pmcid: 1326712
Marshall, P., Williams, P. & Goldspink, G. Accumulation of collagen and altered fiber‐type ratios as indicators of abnormal muscle gene expression in the mdx dystrophic mouse. Muscle & nerve 12, 528–537 (1989).
doi: 10.1002/mus.880120703
Akima, H. et al. Relationships of thigh muscle contractile and non-contractile tissue with function, strength, and age in boys with Duchenne muscular dystrophy. Neuromuscular Disorders 22, 16–25 (2012).
pubmed: 21807516
doi: 10.1016/j.nmd.2011.06.750
pmcid: 21807516
Kim, H. K. et al. T2 Mapping in Duchenne Muscular Dystrophy: Distribution of Disease Activity and Correlation with Clinical Assessments 1. Radiology 255, 899–908 (2010).
pubmed: 20501727
doi: 10.1148/radiol.10091547
pmcid: 20501727
Gooding, J. R. et al. Adenylosuccinate Is an Insulin Secretagogue Derived from Glucose-Induced Purine Metabolism. Cell reports 13, 157–167 (2015).
pubmed: 26411681
pmcid: 4598307
doi: 10.1016/j.celrep.2015.08.072
Glesby, M. J., Rosenmann, E., Nylen, E. G. & Wrogemann, K. Serum CK, calcium, magnesium, and oxidative phosphorylation in mdx mouse muscular dystrophy. Muscle & Nerve 11, 852–856 (1988).
doi: 10.1002/mus.880110809
Kuznetsov, A. V. et al. Impaired mitochondrial oxidative phosphorylation in skeletal muscle of the dystrophin-deficient mdx mouse. Molecular and cellular biochemistry 183, 87–96 (1998).
pubmed: 9655182
doi: 10.1023/A:1006868130002
pmcid: 9655182
Martens, M., Jankulovska, L., Neymark, M. & Lee, C. Impaired substrate utilization in mitochondria from strain 129 dystrophic mice. Biochimica et Biophysica Acta (BBA)-Bioenergetics 589, 190–200 (1980).
doi: 10.1016/0005-2728(80)90037-7
Bhattacharya, S. K., Johnson, P. L. & Thakar, J. H. Reversal of impaired oxidative phosphorylation and calcium overloading in the in vitro cardiac mitochondria of CHF-146 dystrophic hamsters with hereditary muscular dystrophy. Journal of the Neurological Sciences 120, 180–186 (1993).
pubmed: 8138808
doi: 10.1016/0022-510X(93)90271-Y
pmcid: 8138808
Faist, V., König, J., Höger, H. & Elmadfa, I. Decreased mitochondrial oxygen consumption and antioxidant enzyme activities in skeletal muscle of dystrophic mice after low-intensity exercise. Annals of nutrition and metabolism 45, 58–66 (2001).
pubmed: 11359030
doi: 10.1159/000046707
pmcid: 11359030
Olson, E., Vignos, P., Woodlock, J. & Perry, T. Oxidative phosphorylation of skeletal muscle in human muscular dystrophy. J. Lab. Clin. Med. 71, 23l (1968).
Griffin, J. et al. Metabolic Profiling of Genetic Disorders: A Multitissue
pubmed: 11373073
doi: 10.1006/abio.2001.5096
Chen, W.-C., Huang, W.-C., Chiu, C.-C., Chang, Y.-K. & Huang, C.-C. Whey protein improves exercise performance and biochemical profiles in trained mice. Medicine and science in sports and exercise 46, 1517 (2014).
pubmed: 24504433
pmcid: 4186725
doi: 10.1249/MSS.0000000000000272
Shavlakadze, T., White, J., Hoh, J. F., Rosenthal, N. & Grounds, M. D. Targeted expression of insulin-like growth factor-I reduces early myofiber necrosis in dystrophic mdx mice. Molecular Therapy 10, 829–843 (2004).
pubmed: 15509501
doi: 10.1016/j.ymthe.2004.07.026
Sheehan, D. C. & Hrapchak, B. B. Theory and practice of histotechnology. (Cv Mosby, 1980).
Timpani, C. A. et al. Attempting to Compensate for Reduced Neuronal Nitric Oxide Synthase Protein with Nitrate Supplementation Cannot Overcome Metabolic Dysfunction but Rather Has Detrimental Effects in Dystrophin-Deficient mdx Muscle. Neurotherapeutics, 1–18 (2016).
Sorensen, J. C. et al. BGP-15 protects against Oxaliplatin-induced skeletal myopathy and mitochondrial reactive oxygen species production in mice. Frontiers in Pharmacology 8 (2017).
Timpani, C. A. et al. Attempting to compensate for reduced neuronal nitric oxide synthase protein with nitrate supplementation cannot overcome metabolic dysfunction but rather Has detrimental effects in dystrophin-deficient mdx muscle. Neurotherapeutics 14, 429–446 (2017).
pubmed: 27921261
doi: 10.1007/s13311-016-0494-7
pmcid: 27921261
Brooks, S. V. & Faulkner, J. A. Contractile properties of skeletal muscles from young, adult and aged mice. The Journal of physiology 404, 71–82 (1988).
pubmed: 3253447
pmcid: 1190815
doi: 10.1113/jphysiol.1988.sp017279
Schuh, R. A., Jackson, K. C., Khairallah, R. J., Ward, C. W. & Spangenburg, E. E. Measuring mitochondrial respiration in intact single muscle fibers. American Journal of Physiology - Regulatory, Integrative and Comparative Physiology 302, R712–R719, https://doi.org/10.1152/ajpregu.00229.2011 (2012).
doi: 10.1152/ajpregu.00229.2011
pubmed: 22160545
pmcid: 22160545
Welinder, C. & Ekblad, L. Coomassie Staining as Loading Control in Western Blot Analysis. Journal of Proteome Research 10, 1416–1419, https://doi.org/10.1021/pr1011476 (2011).
doi: 10.1021/pr1011476
pubmed: 21186791
pmcid: 21186791
Vigelsø Hansen, A., Andersen, N. B. & Dela, F. The relationship between skeletal muscle mitochondrial citrate synthase activity and whole body oxygen uptake adaptations in response to exercise training. International journal of physiology, pathophysiology and pharmacology 6, 84–101 (2014).
Srere, P. [1] Citrate synthase:[EC 4.1. 3.7. Citrate oxaloacetate-lyase (CoA-acetylating)]. Methods in enzymology 13, 3–11 (1969).
doi: 10.1016/0076-6879(69)13005-0
Lowry, O. & Passonneau, J. (New York: Academic Press, 1972).
Stathis, C. G., Carey, M. F., Hayes, A., Garnham, A. P. & Snow, R. J. Sprint training reduces urinary purine loss following intense exercise in humans. Applied physiology, nutrition, and metabolism 31, 702–708 (2006).
pubmed: 17213884
doi: 10.1139/h06-074
pmcid: 17213884
Bonsett, C., Rudman, A. & Elliott, A. Y. Intracellular lipid in pseudohypertrophic muscular dystrophy tissue culture. J. Indiana State Med. Assoc. 72, 184–187 (1979).
pubmed: 217934
pmcid: 217934
Reichmann, H., Hoppeler, H., Mathieu-Costello, O., Von Bergen, F. & Pette, D. Biochemical and ultrastructural changes of skeletal muscle mitochondria after chronic electrical stimulation in rabbits. Pflügers Archiv 404, 1–9 (1985).
pubmed: 4011395
doi: 10.1007/BF00581484
pmcid: 4011395
Larsen, S. et al. Biomarkers of mitochondrial content in skeletal muscle of healthy young human subjects. The Journal of physiology 590, 3349–3360 (2012).
pubmed: 22586215
pmcid: 3459047
doi: 10.1113/jphysiol.2012.230185
Suárez-Rivero, J. M. et al. Mitochondrial Dynamics in Mitochondrial Diseases. Diseases 5, 1 (2016).
pmcid: 5456341
doi: 10.3390/diseases5010001
Armstrong, R. & Phelps, R. Muscle fiber type composition of the rat hindlimb. American Journal of Anatomy 171, 259–272 (1984).
pubmed: 6517030
doi: 10.1002/aja.1001710303
pmcid: 6517030
Pickett-Gies, C. A., Carlsen, R. C., Anderson, L. J., Angelos, K. L. & Walsh, D. A. Characterization of the isolated rat flexor digitorum brevis for the study of skeletal muscle phosphorylase kinase phosphorylation. Journal of Biological Chemistry 262, 3227–3238 (1987).
pubmed: 3029105
pmcid: 3029105
Burkholder, T. J., Fingado, B., Baron, S. & Lieber, R. L. Relationship between muscle fiber types and sizes and muscle architectural properties in the mouse hindlimb. Journal of Morphology 221, 177–190 (1994).
pubmed: 7932768
doi: 10.1002/jmor.1052210207
pmcid: 7932768
Kuznetsov, A. V. et al. Striking Differences Between the Kinetics of Regulation of Respiration by ADP in Slow‐Twitch and Fast‐Twitch Muscles In Vivo. European Journal of Biochemistry 241, 909–915 (1996).
pubmed: 8944782
doi: 10.1111/j.1432-1033.1996.00909.x
pmcid: 8944782
Sahlin, K. & Broberg, S. Adenine nucleotide depletion in human muscle during exercise: causality and significance of AMP deamination. International journal of sports medicine 11, S62–S67 (1990).
pubmed: 2361781
doi: 10.1055/s-2007-1024856
pmcid: 2361781
Mihaylova, M. M. & Shaw, R. J. The AMP-activated protein kinase (AMPK) signaling pathway coordinates cell growth, autophagy, & metabolism. Nature cell biology 13, 1016 (2011).
pubmed: 21892142
pmcid: 3249400
doi: 10.1038/ncb2329
Matsumura, K., Ervasti, J. M., Ohlendieck, K., Kahl, S. D. & Campbell, K. P. Association of dystrophin-related protein with dystrophin-associated proteins in mdx mouse muscle. Nature 360, 588–591 (1992).
pubmed: 1461282
doi: 10.1038/360588a0
pmcid: 1461282
Ljubicic, V. et al. Chronic AMPK activation evokes the slow, oxidative myogenic program and triggers beneficial adaptations in mdx mouse skeletal muscle. Human molecular genetics, ddr265 (2011).
Buyse, G. M. et al. Efficacy of idebenone on respiratory function in patients with Duchenne muscular dystrophy not using glucocorticoids (DELOS): a double-blind randomised placebo-controlled phase 3 trial. The Lancet 385, 1748–1757 (2015).
doi: 10.1016/S0140-6736(15)60025-3
Mastaglia, F. & Kakulas, B. Regeneration in Duchenne muscular dystrophy: a histological and histochemical study. Brain 92, 809–818 (1969).
pubmed: 5364011
doi: 10.1093/brain/92.4.809
pmcid: 5364011
Pastoret, C. & Sebille, A. Mdx mice show progressive weakness and muscle deterioration with age. Journal of the neurological sciences 129, 97–105 (1995).
pubmed: 7608742
doi: 10.1016/0022-510X(94)00276-T
pmcid: 7608742
Arpan, I. et al. T2 mapping provides multiple approaches for the characterization of muscle involvement in neuromuscular diseases: a cross‐sectional study of lower leg muscles in 5–15‐year‐old boys with Duchenne muscular dystrophy. NMR in biomedicine 26, 320–328 (2013).
pubmed: 23044995
doi: 10.1002/nbm.2851
pmcid: 23044995
Wren, T. A., Bluml, S., Tseng-Ong, L. & Gilsanz, V. Three-point technique of fat quantification of muscle tissue as a marker of disease progression in Duchenne muscular dystrophy: preliminary study. American Journal of Roentgenology 190, W8-W12 (2008).
Cros, D., Harnden, P., Pellissier, J. & Serratrice, G. Muscle hypertrophy in Duchenne muscular dystrophy. Journal of neurology 236, 43–47 (1989).
pubmed: 2915226
doi: 10.1007/BF00314217
pmcid: 2915226
Willcocks, R. et al. Longitudinal measurements of MRI-T 2 in boys with Duchenne muscular dystrophy: Effects of age and disease progression. Neuromuscular Disorders 24, 393–401 (2014).
pubmed: 24491484
doi: 10.1016/j.nmd.2013.12.012
pmcid: 24491484
Vohra, R. S. et al. Magnetic resonance assessment of hypertrophic and pseudo-hypertrophic changes in lower leg muscles of boys with Duchenne muscular dystrophy and their relationship to functional measurements. PloS one 10, e0128915 (2015).
pubmed: 26103164
pmcid: 4477876
doi: 10.1371/journal.pone.0128915
Coulton, G. R., Morgan, J. E., Partridge, T. A. & Sloper, J. C. The mdx mouse skeletal muscle myopathy: I. A histological, morphometric and biochemical investigation. Neuropathology and Applied Neurobiology 14, 53–70, https://doi.org/10.1111/j.1365-2990.1988.tb00866.x (1988).
doi: 10.1111/j.1365-2990.1988.tb00866.x
pubmed: 2967442
pmcid: 2967442
Bonsett, C. & Rudman, A. Duchenne’s muscular dystrophy: a tissue culture perspective. Indiana medicine: the journal of the Indiana State Medical Association 77, 446 (1984).
Rayavarapu, S. et al. Identification of disease specific pathways using in vivo SILAC proteomics in dystrophin deficient mdx mouse. Molecular & cellular proteomics: MCP 12, 1061–1073, https://doi.org/10.1074/mcp.M112.023127 (2013).
doi: 10.1074/mcp.M112.023127
Dreyfus, J.-C., Schapira, G. & Schapira, F. Biochemical study of muscle in progressive muscular dystrophy. J. Clin. Invest. 33, 794–797 (1954).
pubmed: 13163170
pmcid: 438512
doi: 10.1172/JCI102950
Di Mauro, S., Angelini, C. & Catani, C. Enzymes of the glycogen cycle and glycolysis in various human neuromuscular disorders. J. Neurol. Neurosurg. Psychiat. 30, 411–415 (1967).
pubmed: 4228900
doi: 10.1136/jnnp.30.5.411
pmcid: 4228900
Hess, J. Phosphorylase activity and glycogen, glucose-6-phosphate, and lactic acid content of human skeletal muscle in various myopathies. J. Lab. Clin. Med. 66, 452–463 (1965).
pubmed: 4378663
Chi, M. M. Y. et al. Effect of Duchenne muscular dystrophy on enzymes of energy metabolism in individual muscle fibers. Metabolism 36, 761–767, https://doi.org/10.1016/0026-0495(87)90113-2 (1987).
doi: 10.1016/0026-0495(87)90113-2
pubmed: 3600288
Stapleton, D. I. et al. Dysfunctional Muscle and Liver Glycogen Metabolism in mdx Dystrophic Mice. PLoS One 9, e91514, https://doi.org/10.1371/journal.pone.0091514 (2014).
doi: 10.1371/journal.pone.0091514
pubmed: 24626262
pmcid: 3953428
Ronzoni, E., Berg, L. & Landau, W. Enzyme studies in progressive muscular dystrophy. Res. Publ. Ass. nerv. ment. Dis. 38, 721–729 (1960).
Ellis, D. Intermediary metabolism of muscle in Duchenne muscular dystrophy. British Medical Bulletin 36, 165–172 (1980).
pubmed: 7020844
doi: 10.1093/oxfordjournals.bmb.a071633
Petell, J. K., Marshall, N. A. & Lebherz, H. G. Content and synthesis of several abundant glycolytic enzymes in skeletal muscles of normal and dystrophic mice. International Journal of Biochemistry 16, 61–67 (1984).
pubmed: 6698288
doi: 10.1016/0020-711X(84)90051-X
Engel, A. In Myology (eds Engel, A. G. & Banker, B. Q.) 1185–1240 (McGraw-Hill, 1986).
Chen, Y. W., Zhao, P., Borup, R. & Hoffman, E. P. Expression profiling in the muscular dystrophies: identification of novel aspects of molecular pathophysiology. J. Cell. Biol. 151, 1321–1336 (2000).
pubmed: 11121445
pmcid: 2190600
doi: 10.1083/jcb.151.6.1321
Carberry, S., Brinkmeier, H., Zhang, Y., Winkler, C. K. & Ohlendieck, K. Comparative proteomic profiling of soleus, extensor digitorum longus, flexor digitorum brevis and interosseus muscles from the mdx mouse model of Duchenne muscular dystrophy. International Journal of Molecular Medicine (2013).
Ionǎşescu, V., Luca, N. & Vuia, O. Respiratory control and oxidative phosphorylation in the dystrophic muscle. Acta Neurologica Scandinavica 43, 564–572 (1967).
pubmed: 6083363
doi: 10.1111/j.1600-0404.1967.tb05551.x
Nylen, E. G. & Wrogemann, K. Mitochondrial calcium content and oxidative phosphorylation in heart and skeletal muscle of dystrophic mice. Experimental neurology 80, 69–80 (1983).
pubmed: 6832274
doi: 10.1016/0014-4886(83)90007-9
pmcid: 6832274
Chinet, A., Even, P. & Decrouy, A. Dystrophin-dependent efficiency of metabolic pathways in mouse skeletal muscles. Cellular and Molecular Life Sciences 50, 602–605 (1994).
doi: 10.1007/BF01921731
Cao, A., Macciotta, A., Fiorelli, G., Mannucci, P. & Idéo, G. Chromatographic and electrophoretic pattern of lactate and malate dehydrogenase in normal human adult and foetal muscle and in muscle of patients affected by Duchenne muscular dystrophy. Enzymologia biologica et clinica 7, 156–166 (1965).
doi: 10.1159/000457301
Akiba, T., Hiragi, K. & Tuboi, S. Intracellular distribution of fumarase in various animals. Journal of biochemistry 96, 189–195 (1984).
pubmed: 6333419
doi: 10.1093/oxfordjournals.jbchem.a134812
pmcid: 6333419
Lee, S. et al. Mitochondrial fission and fusion mediators, hFis1 and OPA1, modulate cellular senescence. Journal of Biological Chemistry 282, 22977–22983 (2007).
pubmed: 17545159
doi: 10.1074/jbc.M700679200
pmcid: 17545159
Willems, P. H., Rossignol, R., Dieteren, C. E., Murphy, M. P. & Koopman, W. J. Redox homeostasis and mitochondrial dynamics. Cell metabolism 22, 207–218 (2015).
pubmed: 26166745
doi: 10.1016/j.cmet.2015.06.006
pmcid: 26166745
Khairallah, R. J. et al. Microtubules underlie dysfunction in duchenne muscular dystrophy. Science signaling 5 (2012).
pubmed: 22871609
doi: 10.1126/scisignal.2002829
pmcid: 22871609
Austin, L. et al. Potential oxyradical damage and energy status in individual muscle fibres from degenerating muscle diseases. Neuromuscular Disorders 2, 27–33 (1992).
pubmed: 1525555
doi: 10.1016/0960-8966(92)90023-Y
pmcid: 1525555
Pinto, R. & Bartley, W. The effect of age and sex on glutathione reductase and glutathione peroxidase activities and on aerobic glutathione oxidation in rat liver homogenates. Biochemical Journal 112, 109–115 (1969).
pubmed: 4388243
pmcid: 1187646
doi: 10.1042/bj1120109
Laplante, A., Vincent, G., Poirier, M. & Des Rosiers, C. Effects and metabolism of fumarate in the perfused rat heart. A 13C mass isotopomer study. American Journal of Physiology-Endocrinology And Metabolism 272, E74–E82 (1997).
doi: 10.1152/ajpendo.1997.272.1.E74
Raimundo, N., Baysal, B. E. & Shadel, G. S. Revisiting the TCA cycle: signaling to tumor formation. Trends in molecular medicine 17, 641–649 (2011).
pubmed: 21764377
pmcid: 3205302
doi: 10.1016/j.molmed.2011.06.001
Sharma, U., Atri, S., Sharma, M., Sarkar, C. & Jagannathan, N. Skeletal muscle metabolism in Duchenne muscular dystrophy (DMD): an in-vitro proton NMR spectroscopy study. Magnetic resonance imaging 21, 145–153 (2003).
pubmed: 12670601
doi: 10.1016/S0730-725X(02)00646-X
pmcid: 12670601
Lin, C. H. H. A. S. K. Fatty acid oxidation by skeletal muscle mitochondria in Duchenne muscular dystrophy. Life Sci. II 11, 355–362 (1972).
pubmed: 4656512
doi: 10.1016/0024-3205(72)90075-6
pmcid: 4656512
Shumate, J. B., Carroll, J. E., Brooke, M. H. & Choksi, R. M. Palmitate oxidation in human muscle: comparison to CPT and carnitine. Muscle & nerve 5, 226–231 (1982).
doi: 10.1002/mus.880050309
Carroll, J. E., Norris, B. J. & Brooke, M. H. Defective [U-14 C] palmitic acid oxidation in Duchenne muscular dystrophy. Neurology 35, 96–97 (1985).
pubmed: 3966007
doi: 10.1212/WNL.35.1.96
pmcid: 3966007
Kang, C., Goodman, C. A., Hornberger, T. A. & Ji, L. L. PGC-1α overexpression by in vivo transfection attenuates mitochondrial deterioration of skeletal muscle caused by immobilization. The FASEB Journal 29, 4092–4106 (2015).
pubmed: 26178167
pmcid: 4566942
doi: 10.1096/fj.14-266619