Update on mitochondria and muscle aging: All wrong roads lead to sarcopenia

The Hallmarks of Aging

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Mechanisms of mitophagy

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Premature ageing in mice expressing defective mitochondrial DNA polymerase

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Autophagosome formation: core machinery and adaptations

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Tissue-resident macrophages

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FoxO3 Controls Autophagy in Skeletal Muscle In Vivo

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Coordinated reduction of genes of oxidative metabolism in humans with insulin resistance and diabetes: Potential role of <i>PGC1</i> and <i>NRF1</i>

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Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin

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Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A

Züchner, S., Mersiyanova, I. V., Muglia, M., Bissar-Tadmouri, N., Rochelle, J., Dadali, E. L., Zappia, M., Nelis, E., Patitucci, A., Senderek, J., et al. (2004) · Nature Genetics · doi:10.1038/ng1341 · Cited by 1,572 · see citing works

FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells.

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Declining NAD+ Induces a Pseudohypoxic State Disrupting Nuclear-Mitochondrial Communication during Aging

Gomes, A. P., Price, N. L., Ling, A. J. Y., Moslehi, J. J., Montgomery, M. K., Rajman, L., White, J. P., Teodoro, J. S., Wrann, C. D., Hubbard, B. P., et al. (2013) · Cell · doi:10.1016/j.cell.2013.11.037 · Cited by 1,482 · see citing works

Decline in skeletal muscle mitochondrial function with aging in humans

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Autophagy is required to maintain muscle mass.

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Mitochondrial fusion is required for mtDNA stability in skeletal muscle and tolerance of mtDNA mutations

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Metabolic regulation of mitochondrial dynamics

Mishra, P., & Chan, D. C. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201511036 · Cited by 1,096 · see citing works

A mitochondrial specific stress response in mammalian cells

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The cGAS-cGAMP-STING Pathway of Cytosolic DNA Sensing and Signaling

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PGC-1α protects skeletal muscle from atrophy by suppressing FoxO3 action and atrophy-specific gene transcription

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Autophagy deficiency leads to protection from obesity and insulin resistance by inducing Fgf21 as a mitokine

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Oxidative damage to mitochondrial DNA shows marked age-dependent increases in human brain

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A Vesicular Transport Pathway Shuttles Cargo from Mitochondria to Lysosomes

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Mitochondrial Rhomboid PARL Regulates Cytochrome c Release during Apoptosis via OPA1-Dependent Cristae Remodeling

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Sirtuin 3, a New Target of PGC-1α, Plays an Important Role in the Suppression of ROS and Mitochondrial Biogenesis

Kong, X., Wang, R., Xue, Y., Liu, X., Zhang, H., Chen, Y., Fang, F., & Chang, Y. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011707 · Cited by 718 · see citing works

Emerging role of damage-associated molecular patterns derived from mitochondria in inflammation

Krysko, D. V., Agostinis, P., Krysko, O., Garg, A. D., Bachert, C., Lambrecht, B. N., & Vandenabeele, P. (2011) · Trends in Immunology · doi:10.1016/j.it.2011.01.005 · Cited by 680 · see citing works

A PGC-1α isoform induced by resistance training regulates skeletal muscle hypertrophy

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Mitofusin 2 (Mfn2) links mitochondrial and endoplasmic reticulum function with insulin signaling and is essential for normal glucose homeostasis

Sebastián, D., Hernández-Alvarez, M. I., Segalés, J., Sorianello, E., Muñoz, J. P., Sala, D., Waget, A., Liesa, M., Paz, J. C., Gopalacharyulu, P., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1108220109 · Cited by 673 · see citing works

Oxidative capacity and ageing in human muscle

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Mitochondrial fusion, fission and autophagy as a quality control axis: The bioenergetic view

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A pattern of accumulation of a somatic deletion of mitochondrial DNA in aging human tissues.

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Running-induced systemic cathepsin B secretion is associated with memory function

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Mitochondrial fission and remodelling contributes to muscle atrophy

Romanello, V., Guadagnin, E., Gomes, L., Roder, I., Sandri, C., Petersen, Y., Milan, G., Masiero, E., Del Piccolo, P., Foretz, M., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.60 · Cited by 596 · see citing works

Endurance Exercise as a Countermeasure for Aging

Lanza, I. R., Short, D. K., Short, K. R., Raghavakaimal, S., Basu, R., Joyner, M. J., McConnell, J. P., & Nair, K. S. (2008) · Diabetes · doi:10.2337/db08-0349 · Cited by 582 · see citing works

Age-Associated Loss of OPA1 in Muscle Impacts Muscle Mass, Metabolic Homeostasis, Systemic Inflammation, and Epithelial Senescence

Tezze, C., Romanello, V., Desbats, M. A., Fadini, G. P., Albiero, M., Favaro, G., Ciciliot, S., Soriano, M. E., Morbidoni, V., Cerqua, C., et al. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.04.021 · Cited by 568 · cited 2× · see citing works

New roles for mitochondrial proteases in health, ageing and disease

Quirós, P. M., Langer, T., & López-Otı́n, C. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3984 · Cited by 546 · see citing works

Autophagy is defective in collagen VI muscular dystrophies, and its reactivation rescues myofiber degeneration

Grumati, P., Coletto, L., Sabatelli, P., Cescon, M., Angelin, A., Bertaggia, E., Blaauw, B., Urciuolo, A., Tiepolo, T., Merlini, L., et al. (2010) · Nature Medicine · doi:10.1038/nm.2247 · Cited by 540 · see citing works

Mitohormesis: Promoting Health and Lifespan by Increased Levels of Reactive Oxygen Species (ROS)

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OPA1 mutations induce mitochondrial DNA instability and optic atrophy 'plus' phenotypes

Amati-Bonneau, P., Valentino, M. L., Reynier, P., Gallardo, M. E., Bornstein, B., Boissiere, A., Campos, Y., Rivera, H., de la Aleja, J. G., Carroccia, R., et al. (2008) · Brain · doi:10.1093/brain/awm298 · Cited by 520 · see citing works

Secretory autophagy

Ponpuak, M., Mandell, M. A., Kimura, T., Chauhan, S., Cleyrat, C., & Deretic, V. P. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2015.04.016 · Cited by 509 · see citing works

Endogenously oxidized mitochondrial DNA induces in vivo and in vitro inflammatory responses

Collins, L. V., Hajizadeh, S., Holme, E., Jonsson, I., & Tarkowski, A. (2004) · Journal of Leukocyte Biology · doi:10.1189/jlb.0703328 · Cited by 504 · see citing works

Oxidized mitochondrial nucleoids released by neutrophils drive type I interferon production in human lupus

Caielli, S., Athale, S., Domic, B., Murat, E., Chandra, M., Banchereau, R., Baisch, J., Phelps, K., Clayton, S., Gong, M., et al. (2016) · Journal of Experimental Medicine · doi:10.1084/jem.20151876 · Cited by 501 · see citing works

Exercise-induced mitochondrial biogenesis begins before the increase in muscle PGC-1α expression.

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The potential of endurance exercise-derived exosomes to treat metabolic diseases

Safdar, A., Saleem, A., & Tarnopolsky, M. A. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2016.76 · Cited by 463 · see citing works

The Opa1-Dependent Mitochondrial Cristae Remodeling Pathway Controls Atrophic, Apoptotic, and Ischemic Tissue Damage

Varanita, T., Soriano, M. E., Romanello, V., Zaglia, T., Quintana-Cabrera, R., Semenzato, M., Menabò, R., Costa, V., Civiletto, G., Pesce, P., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.007 · Cited by 460 · see citing works

Increased Oxidative Damage Is Correlated to Altered Mitochondrial Function in Heterozygous Manganese Superoxide Dismutase Knockout Mice

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Mitochondrial DNA–Deletion Mutations Accumulate Intracellularly to Detrimental Levels in Aged Human Skeletal Muscle Fibers

Bua, E., Johnson, J., Herbst, A., Delong, B., McKenzie, D., Salamat, S., & Aiken, J. M. (2006) · The American Journal of Human Genetics · doi:10.1086/507132 · Cited by 442 · see citing works

Sarcopenia: An overview

on behalf of the SPRINTT Consortium, Marzetti, E., Calvani, R., Tosato, M., Cesari, M., Di Bari, M., Cherubini, A., Collamati, A., D’Angelo, E., Pahor, M., et al. (2017) · Aging Clinical and Experimental Research · doi:10.1007/s40520-016-0704-5 · Cited by 438 · see citing works

Mitochondrial function and apoptotic susceptibility in aging skeletal muscle

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Mitochondrial quality control and muscle mass maintenance.

Romanello, V., & Sandri, M. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2015.00422 · Cited by 434 · see citing works

Autophagy Impairment in Muscle Induces Neuromuscular Junction Degeneration and Precocious Aging

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Biological consequences of free radical-damaged DNA bases1,2 1Guest Editor: Miral Dizdaroglu 2This article is part of a series of reviews on “Oxidative DNA Damage and Repair.” The full list of papers may be found on the homepage of the journal.

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Circulating mitochondrial DNA increases with age and is a familiar trait: Implications for “inflamm-aging”

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Mfn2 deficiency links age‐related sarcopenia and impaired autophagy to activation of an adaptive mitophagy pathway

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The impact of aging on mitochondrial function and biogenesis pathways in skeletal muscle of sedentary high- and low-functioning elderly individuals

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Mitochondrial DNA deletion mutations colocalize with segmental electron transport system abnormalities, muscle fiber atrophy, fiber splitting, and oxidative damage in sarcopenia

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Expression of <i>Mfn2</i>, the Charcot-Marie-Tooth Neuropathy Type 2A Gene, in Human Skeletal Muscle

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Effects of Aging on Mitochondrial DNA Copy Number and Cytochromec Oxidase Gene Expression in Rat Skeletal Muscle, Liver, and Heart

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Rapamycin Reverses Elevated mTORC1 Signaling in Lamin A/C–Deficient Mice, Rescues Cardiac and Skeletal Muscle Function, and Extends Survival

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Evidence for a Mitochondrial Regulatory Pathway Defined by Peroxisome Proliferator–Activated Receptor-γ Coactivator-1α, Estrogen-Related Receptor-α, and Mitofusin 2

Soriano, F. X., Liesa, M., Bach, D., Chan, D. C., Palacín, M., & Zorzano, A. (2006) · Diabetes · doi:10.2337/db05-0509 · Cited by 343 · cited 8× · see citing works

Distribution of different fibre types in human skeletal muscles

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Mitochondrial pathways in sarcopenia of aging and disuse muscle atrophy

Calvani, R., Joseph, A.-M., Adhihetty, P. J., Miccheli, A., Bossola, M., Leeuwenburgh, C., Bernabei, R., & Marzetti, E. (2013) · bchm · doi:10.1515/hsz-2012-0247 · Cited by 328 · see citing works

A Stress-Responsive System for Mitochondrial Protein Degradation

Heo, J.-M., Livnat-Levanon, N., Taylor, E. B., Jones, K. T., Dephoure, N., Ring, J., Xie, J., Brodsky, J. L., Madeo, F., Gygi, S. P., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.021 · Cited by 304 · see citing works

Sustained Activation of mTORC1 in Skeletal Muscle Inhibits Constitutive and Starvation-Induced Autophagy and Causes a Severe, Late-Onset Myopathy

Castets, P., Lin, S., Rion, N., Di Fulvio, S., Romanino, K., Guridi, M., Frank, S., Tintignac, L. A., Sinnreich, M., & Rüegg, M. A. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.03.015 · Cited by 302 · see citing works

Metabolic reprogramming, caloric restriction and aging

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Reactive oxygen in skeletal muscle. III. Contractility of unfatigued muscle

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Mitochondrial DNA nucleoid structure

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Increased superoxide in vivo accelerates age‐associated muscle atrophy through mitochondrial dysfunction and neuromuscular junction degeneration

Jang, Y. C., Lustgarten, M. S., Liu, Y., Müller, F. L., Bhattacharya, A., Liang, H., Salmon, A. B., Brooks, S. V., Larkin, L. M., Hayworth, C. R., et al. (2009) · The FASEB Journal · doi:10.1096/fj.09-146308 · Cited by 290 · see citing works

Regulation of mitochondrial biogenesis through TFAM–mitochondrial DNA interactions

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Total Skeletal Muscle PGC-1 Deficiency Uncouples Mitochondrial Derangements from Fiber Type Determination and Insulin Sensitivity

Zechner, C., Lai, L., Zechner, J. F., Geng, T., Yan, Z., Rumsey, J. W., Collia, D., Chen, Z., Wozniak, D. F., Leone, T. C., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.11.008 · Cited by 274 · cited 5× · see citing works

Mitochondrial DNA Mutations Induce Mitochondrial Dysfunction, Apoptosis and Sarcopenia in Skeletal Muscle of Mitochondrial DNA Mutator Mice

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Autophagy as a new therapeutic target in Duchenne muscular dystrophy

De Palma, C., Morisi, F., Cheli, S., Pambianco, S., Cappello, V, Vezzoli, M., Rovere-Querini, P., Moggio, M., Ripolone, M., Francolini, M., et al. (2012) · Cell Death &amp; Disease · doi:10.1038/cddis.2012.159 · Cited by 269 · see citing works

The Effect of Aging on Human Skeletal Muscle Mitochondrial and Intramyocellular Lipid Ultrastructure

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Pharmacological Inhibition of poly(ADP-ribose) polymerases improves fitness and mitochondrial function in skeletal muscle

Pirinen, E., Cantó, C., Jo, Y. S., Morato, L., Zhang, H., Menzies, K. J., Williams, E. G., Mouchiroud, L., Moullan, N., Hagberg, C., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.04.002 · Cited by 254 · cited 1× · see citing works

AMPK Activation of Muscle Autophagy Prevents Fasting-Induced Hypoglycemia and Myopathy during Aging

Bujak, A. L., Crane, J. D., Lally, J., Ford, R. J., Kang, S. J., Rebalka, I. A., Green, A. E., Kemp, B. E., Hawke, T. J., Schertzer, J. D., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.016 · Cited by 252 · see citing works

Free radical theory of aging: Consequences of mitochondrial aging

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Mitochondrial oxidative stress in mice lacking the glutathione peroxidase-1 gene

Esposito, L. A., Kokoszka, J. E., Waymire, K. G., Cottrell, B., MacGregor, G. R., & Wallace, D. C. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00161-1 · Cited by 228 · see citing works

Chaperone–protease networks in mitochondrial protein homeostasis

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Peroxisome Proliferator-activated Receptor γ Coactivator 1α or 1β Overexpression Inhibits Muscle Protein Degradation, Induction of Ubiquitin Ligases, and Disuse Atrophy

Brault, J. J., Jespersen, J. G., & Goldberg, A. L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.113092 · Cited by 217 · see citing works

Aberrant mitochondrial homeostasis in the skeletal muscle of sedentary older adults

Safdar, A., Hamadeh, M. J., Kaczor, J. J., Raha, S., deBeer, J., & Tarnopolsky, M. A. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010778 · Cited by 217 · see citing works

Mice Deficient in Both Mn Superoxide Dismutase and Glutathione Peroxidase-1 Have Increased Oxidative Damage and a Greater Incidence of Pathology but No Reduction in Longevity

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