The DOI matches its Crossref record; 53 of the 53 references it cites were found in a registry or an index.
PGC-1α protects skeletal muscle from atrophy by suppressing FoxO3 action and atrophy-specific gene transcription
Open accessAbstract
Maintaining muscle size and fiber composition requires contractile activity. Increased activity stimulates expression of the transcriptional coactivator PGC-1α (peroxisome proliferator-activated receptor γ coactivator 1α), which promotes fiber-type switching from glycolytic toward more oxidative fibers. In response to disuse or denervation, but also in fasting and many systemic diseases, muscles undergo marked atrophy through a common set of transcriptional changes. FoxO family transcription factors play a critical role in this loss of cell protein, and when activated, FoxO3 causes expression of the atrophy-related ubiquitin ligases atrogin-1 and MuRF-1 and profound loss of muscle mass. To understand how exercise might retard muscle atrophy, we investigated the possible interplay between PGC-1α and the FoxO family in regulation of muscle size. Rodent muscles showed a large decrease in PGC-1α mRNA during atrophy induced by denervation as well as by cancer cachexia, diabetes, and renal failure. Furthermore, in transgenic mice overexpressing PGC-1α, denervation and fasting caused a much smaller decrease in muscle fiber diameter and a smaller induction of atrogin-1 and MuRF-1 than in control mice. Increased expression of PGC-1α also increased mRNA for several genes involved in energy metabolism whose expression decreases during atrophy. Transfection of PGC-1α into adult fibers reduced the capacity of FoxO3 to cause fiber atrophy and to bind to and transcribe from the atrogin-1 promoter. Thus, the high levels of PGC-1α in dark and exercising muscles can explain their resistance to atrophy, and the rapid fall in PGC-1α during atrophy should enhance the FoxO-dependent loss of muscle mass.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“PPARGC1A, the gene that encodes PGC‐1α, is most well‐known for its role in mitochondrial biogenesis but has been reported to protect muscle mass in the context of muscle atrophy triggered by aging (Yang et al., 2020), chronic heart failure, and various other muscle wasting conditions (Sandri et al., 2006).”
From Autophagy gene expression in skeletal muscle of older individuals is associated with physical performance, muscle volume and mitochondrial function in the study of muscle, mobility and aging ( SOMMA ) (2024) · cites this paper as Sandri et al., 2006
Experimental — accuracy not yet measuredIn the citing paper
“PGC-1α is a transcriptional coactivator that has reduced gene expression in muscles of patients with type 2 diabetes,55 and might have a role in preventing muscle atrophy.53,56”
From Age-related and disease-related muscle loss: The effect of diabetes, obesity, and other diseases (2014) · cites this paper as [53]
In the citing paper
“Myofibre size in skeletal muscle is also reduced in people with type 2 diabetes.53”
From Age-related and disease-related muscle loss: The effect of diabetes, obesity, and other diseases (2014) · cites this paper as [53]
In the citing paper
“First, skeletal muscles are heterogeneous with respect to fiber type and metabolic properties and therefore they vary, often drastically, in their response to the same stimulus.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [2]
In the citing paper
“For instance, slow muscles, such as the soleus, are less sensitive to starvation compared to fast muscles2, while during disuse such as that induced by hind limb suspension, the soleus atrophies faster than glycolytic (fast) muscles3.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [2]
In the citing paper
“For instance, JunB, PGC1α, and PGC1β all inhibit FoxO activity in skeletal muscles2,67,68, while the glucocorticoid receptor and β−catenin synergize with FoxOs to promote muscle wasting69.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [2]
In the citing paper
“With aging, PGC-1α levels dramatically fall in the skeletal muscle [86], while the maintenance of PGC-1α expression preserves muscle mass during sarcopenia, cachexia, denervation, and fasting [85,87].”
From Role of Age-Related Mitochondrial Dysfunction in Sarcopenia (2020) · cites this paper as [85]
In the citing paper
“This phenomenon seems to be mediated by the promotion of mitochondrial turnover and quality control [85,87].”
From Role of Age-Related Mitochondrial Dysfunction in Sarcopenia (2020) · cites this paper as [85]
In the citing paper
“PGC-1α may also prevent muscle atrophy through the regulation of autophagy [85].”
From Role of Age-Related Mitochondrial Dysfunction in Sarcopenia (2020) · cites this paper as [85]
In the citing paper
“Because exercise and ApN share similar signaling pathways [75,76] and the potential of counteracting several facets of this metabolic syndrome, numerous studies attempted to establish relationships between exercise and ApN parameters.”
From Adiponectin and Its Mimics on Skeletal Muscle: Insulin Sensitizers, Fat Burners, Exercise Mimickers, Muscling Pills … or Everything Together? (2020) · cites this paper as [75]
In the citing paper
“The transcriptional activity of FoxO3 is inhibited, on one hand, by PGC-1α and on the other hand, by the insulin/IGF1 signaling pathway, which also activates protein synthesis [75].”
From Adiponectin and Its Mimics on Skeletal Muscle: Insulin Sensitizers, Fat Burners, Exercise Mimickers, Muscling Pills … or Everything Together? (2020) · cites this paper as [75]
In the citing paper
“Forkhead box O (FoxO) family TF play a critical role in protein breakdown by activating the expression of atrogenes (which include two muscle-specific ubiquitin ligases, atrogin-1 and MuRF1) responsible for profound loss of muscle mass [75].”
From Adiponectin and Its Mimics on Skeletal Muscle: Insulin Sensitizers, Fat Burners, Exercise Mimickers, Muscling Pills … or Everything Together? (2020) · cites this paper as [75]
In the citing paper
“PGC-1α reduces muscle protein degradation by the UPS via blocking nuclear factor κB (NF-κB) and FoxO3 activity (16, 124).”
From Mitochondria initiate and regulate sarcopenia (2017) · cites this paper as [124]
In the citing paper
“Thus, high-level expression of PGC-1 may actually cause accumulation of lipids and/or incomplete oxidation products, leading to reduced insulin sensitivity, as observed in PGC-1␣ transgenic mice (267-269).”
From The role of mitochondria in the pathogenesis of type 2 diabetes (2010) · cites this paper as [269]
In the citing paper
“When PGC-1␣ overexpression is restricted to skeletal muscle but overexpressed throughout development by the use of the creatine kinase gene promoter, very large increases in mitochondrial mass, OXPHOS, and fatty acid oxidation genes are observed (267-269).”
From The role of mitochondria in the pathogenesis of type 2 diabetes (2010) · cites this paper as [269]
In the citing paper
“Despite these effects, insulin sensitivity is normal in PGC-1␣ transgenic mice fed a chow diet and, surprisingly, is reduced during high-fat feeding.”
From The role of mitochondria in the pathogenesis of type 2 diabetes (2010) · cites this paper as [269]
In the citing paper
“In this model, ATP synthesis rate and exercise performance are increased, and fatty acid oxidation is also enhanced.”
From The role of mitochondria in the pathogenesis of type 2 diabetes (2010) · cites this paper as [269]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Calcium's Role in Mechanotransduction during Muscle Development
Damm, T. B., & Egli, M. (2014) · Cellular Physiology and Biochemistry · doi:10.1159/000356667 · Cited by 14,552
Wu, Z., Puigserver, P., Andersson, U., Zhang, C., Adelmant, G., Mootha, V., Troy, A., Cinti, S., Lowell, B., Scarpulla, R. C., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80611-x · Cited by 4,139
Self-citationA Cold-Inducible Coactivator of Nuclear Receptors Linked to Adaptive Thermogenesis
Puigserver, P., Wu, Z., Park, C. W., Graves, R., Wright, M., & Spiegelman, B. M. (1998) · Cell · doi:10.1016/s0092-8674(00)81410-5 · Cited by 3,864
Self-citationIdentification of ubiquitin ligases required for skeletal muscle atrophy.
Bodine, S. C., Latres, E., Baumhueter, S., Lai, V. K.-M., Nunez, L., Clarke, B. A., Poueymirou, W. T., Panaro, F. J., Na, E., Dharmarajan, K., et al. (2001) · Science · doi:10.1126/science.1065874 · Cited by 3,521
Sandri, M., Sandri, C., Gilbert, A., Skurk, C., Calabria, E., Picard, A., Walsh, K., Schiaffino, S., Lecker, S. H., & Goldberg, A. L. (2004) · Cell · doi:10.1016/s0092-8674(04)00400-3 · Cited by 3,012
Self-citationTranscriptional co-activator PGC-1α drives the formation of slow-twitch muscle fibres
Lin, J., Wu, H., Tarr, P. T., Zhang, C.-Y., Wu, Z., Boss, O., Michael, L. F., Puigserver, P., Isotani, E., Olson, E. N., et al. (2002) · Nature · doi:10.1038/nature00904 · Cited by 2,546
Self-citationMetabolic control through the PGC-1 family of transcription coactivators
Lin, J., Handschin, C., & Spiegelman, B. M. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.05.004 · Cited by 2,130
Self-citationStitt, T. N., Drujan, D., Clarke, B. A., Panaro, F., Timofeyva, Y., Kline, W. O., Gonzalez, M., Yancopoulos, G. D., & Glass, D. J. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00211-4 · Cited by 1,964
Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy
Gomes, M. D., Lecker, S. H., Jagoe, R. T., Navon, A., & Goldberg, A. L. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.251541198 · Cited by 1,774
Self-citationMultiple types of skeletal muscle atrophy involve a common program of changes in gene expression
Lecker, S. H., Jagoe, R. T., Gilbert, A., Gomes, M., Baracos, V., Bailey, J., Price, S. R., Mitch, W. E., & Goldberg, A. L. (2004) · The FASEB Journal · doi:10.1096/fj.03-0610com · Cited by 1,539
Self-citation
Flagged first, then by citations
Research works printed but not linked: 7
- JM Sacheck, J-P Hyatt, A Raffaello, RT Jagoe, RR Roy, VR Edgerton, SH Lecker, AL Goldberg FASEB J, in press. (2006).
- G Tiao, M Lieberman, JE Fischer, PO Hasselgren Am J Physiol 272, R849–R856 (1997).
- VE Baracos, C DeVivo, DH Hoyle, AL Goldberg Am J Physiol 268, E996–E1006 (1995).
- 10.1172/JCI200420174 · DOI
- GJ Herbison, MM Jaweed, JF Ditunno Arch Phys Med Rehab 60, 401–404 (1979).
- IC Kettelhut, MT Pepato, RH Migliorini, R Medina, AL Goldberg Braz J Med Biol Res 27, 981–993 (1994).
- SS Wing, AL Goldberg Am J Physiol 264, E668–E676 (1993).
Cited by
Sorted by citations
Items 101–200 of 973
White, J. P., Puppa, M., Sato, S., Gao, S., Price, R. L., Baynes, J., Kostek, M. C., Matesic, L. E., & Carson, J. A. (2012) · Skeletal Muscle · doi:10.1186/2044-5040-2-14 · Cited by 225
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
Brault, J. J., Jespersen, J. G., & Goldberg, A. L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.113092 · Cited by 217
Self-citationSignaling Pathways That Control Muscle Mass
Vainshtein, A., & Sandri, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21134759 · Cited by 222
Self-citationThe effects of obesity on skeletal muscle contractile function
Tallis, J. A., James, R. S., & Seebacher, F. (2018) · Journal of Experimental Biology · doi:10.1242/jeb.163840 · Cited by 235
Lee, D., & Goldberg, A. L. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.489716 · Cited by 211
Self-citationPrevention of liver cancer cachexia-induced cardiac wasting and heart failure
Springer, J., Tschirner, A., Haghikia, A., von Haehling, S., Lal, H., Grzesiak, A., Kaschina, E., Palus, S., Poetsch, M. S., von Websky, K., et al. (2013) · European Heart Journal · doi:10.1093/eurheartj/eht302 · Cited by 211
FOXO-binding partners: it takes two to tango
van der Vos, K. E., & Coffer, P. J. (2008) · Oncogene · doi:10.1038/onc.2008.22 · Cited by 212
Muscle wasting: The gut microbiota as a new therapeutic target?
Bindels, L. B., & Delzenne, N. M. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.06.021 · Cited by 198
Protein kinase B/Akt: a nexus of growth factor and cytokine signaling in determining muscle mass
Frost, R. A., & Lang, C. H. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00089.2007 · Cited by 200
Ogasawara, R., Fujita, S., Hornberger, T. A., Kitaoka, Y., Makanae, Y., Nakazato, K., & Ishii, N. (2016) · Scientific Reports · doi:10.1038/srep31142 · Cited by 200
FOXO signaling is required for disuse muscle atrophy and is directly regulated by Hsp70
Judge, S. M., DODD, S. L., & Judge, A. R. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00315.2009 · Cited by 202
Brocca, L., Cannavino, J., Coletto, L., Biolo, G., Sandri, M., Bottinelli, R., & Pellegrino, M. A. (2012) · The Journal of Physiology · doi:10.1113/jphysiol.2012.240267 · Cited by 199
Self-citationAbadi, A., Glover, E. I., Isfort, R. J., Raha, S., Safdar, A., Yasuda, N., Kaczor, J. J., Melov, S., Hubbard, A., Qu, X., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006518 · Cited by 189
Bone and muscle loss after spinal cord injury: organ interactions
Qin, W., Bauman, W. A., & Cardozo, C. P. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05806.x · Cited by 194
Acylated and unacylated ghrelin impair skeletal muscle atrophy in mice
Porporato, P. E., Filigheddu, N., Reano, S., Ferrara, M., Angelino, E., Gnocchi, V. F., Prodam, F., Ronchi, G., Fagoonee, S., Fornaro, M., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci39920 · Cited by 194
Exercise-Induced Myokines With Therapeutic Potential for Muscle Wasting
Piccirillo, R. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00287 · Cited by 197
Eisele, P. S., Salatino, S., Sobek, J., Hottiger, M. O., & Handschin, C. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.375253 · Cited by 187
Self-citationVanderVeen, B. N., Fix, D. K., & Carson, J. A. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/3292087 · Cited by 188
Sarcopenia of aging: Underlying cellular mechanisms and protection by calorie restriction
Marzetti, E., Lees, H. A., Wohlgemuth, S. E., & Leeuwenburgh, C. (2009) · BioFactors · doi:10.1002/biof.5 · Cited by 181
Link, W. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-8900-3_1 · Cited by 182
PGC-1α modulates denervation-induced mitophagy in skeletal muscle
Vainshtein, A., Desjardins, E. M., Armani, A., Sandri, M., & Hood, D. A. (2015) · Skeletal Muscle · doi:10.1186/s13395-015-0033-y · Cited by 181
Self-citationRecent progress toward understanding the molecular mechanisms that regulate skeletal muscle mass
Goodman, C. A., Mayhew, D. L., & Hornberger, T. A. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2011.07.013 · Cited by 183
FOXO Transcriptional Factors and Long‐Term Living
Murtaza, G., Khan, A. K., Rashid, R., Muneer, S., Hasan, S. M. F., & Chen, J. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/3494289 · Cited by 182
Inhibition of LTβR signalling activates WNT-induced regeneration in lung
Conlon, T. M., John-Schuster, G., Heide, D., Pfister, D. R., Lehmann, M., Hu, Y., Ertüz, Z., Lopez, M., Ansari, M., Strunz, M., et al. (2020) · Nature · doi:10.1038/s41586-020-2882-8 · Cited by 178
Cruz, S. D., Parone, P. A., Lopes, V. S., Lillo, C., McAlonis‐Downes, M., Lee, S. K., Vetto, A. P., Petrosyan, S., Maršala, M., Murphy, A. N., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.03.019 · Cited by 183
Self-citationExercise-induced hormesis and skeletal muscle health
Ji, L. L., Kang, C., & Zhang, Y. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.02.025 · Cited by 182
Momken, I., Stevens, L., Bergouignan, A., Desplanches, D., Rudwill, F., Chery, I., Zahariev, A., Zahn, S., Stein, T. P., Sebedio, J. L., et al. (2011) · The FASEB Journal · doi:10.1096/fj.10-177295 · Cited by 181
Carson, J. A., & Manolagas, S. C. (2015) · Bone · doi:10.1016/j.bone.2015.04.015 · Cited by 173
PGC-1α buffers ROS-mediated removal of mitochondria during myogenesis
Baldelli, S., Aquilano, K., & Ciriolo, M. R. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.458 · Cited by 175
Kitajima, Y., Yoshioka, K., & Suzuki, N. (2020) · The Journal of Physiological Sciences · doi:10.1186/s12576-020-00768-9 · Cited by 171
Adaptive plasticity of autophagic proteins to denervation in aging skeletal muscle
O'Leary, M. F., Vainshtein, A., Iqbal, S., Ostojic, O., & Hood, D. A. (2013) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00240.2012 · Cited by 165
Hori, Y. S., Kuno, A., Hosoda, R., Tanno, M., Miura, T., Shimamoto, K., & Horio, Y. (2011) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.111.183210 · Cited by 169
Coordinate activation of autophagy and the proteasome pathway by FoxO transcription factor
Zhao, J., Brault, J. J., Schild, A., & Goldberg, A. L. (2008) · Autophagy · doi:10.4161/auto.5633 · Cited by 164
Self-citationUnravelling the mechanisms regulating muscle mitochondrial biogenesis
Hood, D. A., Tryon, L. D., Carter, H. N., Kim, Y., & Chen, C. C. W. (2016) · Biochemical Journal · doi:10.1042/bcj20160009 · Cited by 159
JunB transcription factor maintains skeletal muscle mass and promotes hypertrophy
Raffaello, A., Milan, G., Masiero, E., Carnio, S., Lee, D., Lanfranchi, G., Goldberg, A. L., & Sandri, M. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201001136 · Cited by 156
Self-citationMuscle oxidative capacity during IL-6-dependent cancer cachexia
White, J. P., Baltgalvis, K. A., Puppa, M., Sato, S., Baynes, J., & Carson, J. A. (2010) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00300.2010 · Cited by 174
Myotoxicity of statins: Mechanism of action
du Souich, P., Roederer, G. O., & Dufour, R. (2017) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2017.02.029 · Cited by 168
Durieux, A., Amirouche, A., Banzet, S., Koulmann, N., Bonnefoy, R., Pasdeloup, M., Mouret, C., Bigard, X. A., Peinnequin, A., & Freyssenet, D. G. (2007) · Endocrinology · doi:10.1210/en.2006-1500 · Cited by 162
Aging Affects the Transcriptional Regulation of Human Skeletal Muscle Disuse Atrophy
Suetta, C., Frandsen, U., Jensen, L., Jensen, M. M., Jespersen, J. G., Hvid, L. G., Bayer, M. L., Petersson, S. J., Schrøder, H. D., Andersen, J. L., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0051238 · Cited by 164
Impact of Aging and Exercise on Mitochondrial Quality Control in Skeletal Muscle
Kim, Y., Triolo, M., & Hood, D. A. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/3165396 · Cited by 166
Involvement of MicroRNAs in the Regulation of Muscle Wasting during Catabolic Conditions
Soares, R., Cagnin, S., Chemello, F., Silvestrin, M., Musarò, A., Pittà, C. D., Lanfranchi, G., & Sandri, M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.561845 · Cited by 157
Self-citationMitochondria initiate and regulate sarcopenia
Alway, S. E., Mohamed, J. S., & Myers, M. J. (2017) · Exercise and Sport Sciences Reviews · doi:10.1249/jes.0000000000000101 · Cited by 153
“Furthermore, PGC-1α reduces muscle protein degradation by the UPS via blocking nuclear factor κB and FoxO3 activity (16,124).”
BackgroundDifferential response of skeletal muscles to mTORC1 signaling during atrophy and hypertrophy
Bentzinger, C. F., Lin, S., Romanino, K., Castets, P., Guridi, M., Summermatter, S., Handschin, C., Tintignac, L. A., Hall, M. N., & Rüegg, M. A. (2013) · Skeletal Muscle · doi:10.1186/2044-5040-3-6 · Cited by 153
Self-citationPuig-Vilanova, E., Rodriguez, D. A., Lloreta, J., Ausin, P., Pascual-Guardia, S., Broquetas, J., Roca, J., Gea, J., & Barreiro, E. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.11.006 · Cited by 167
You, J., Anderson, G. B., Dooley, M. S., & Hornberger, T. A. (2015) · Disease Models & Mechanisms · doi:10.1242/dmm.019414 · Cited by 154
Mitochondria and PGC-1α in Aging and Age-Associated Diseases
Wenz, T. (2011) · Journal of Aging Research · doi:10.4061/2011/810619 · Cited by 152
Cellular and molecular events controlling skeletal muscle mass in response to altered use
Favier, F. B., Benoit, H., & Freyssenet, D. G. (2008) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-007-0423-z · Cited by 156
Jackson, J. R., Ryan, M. J., & Alway, S. E. (2011) · The Journals of Gerontology Series A · doi:10.1093/gerona/glr047 · Cited by 149
PGC-1α regulates a HIF2α-dependent switch in skeletal muscle fiber types
Rasbach, K. A., Gupta, R. K., Ruas, J. L., Wu, J., Naseri, E., Estall, J. L., & Spiegelman, B. M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016089107 · Cited by 147
Self-citationMuRF1/TRIM63, Master Regulator of Muscle Mass
Peris-Moreno, D., Taillandier, D., & Polge, C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186663 · Cited by 144
Myricanol rescues dexamethasone-induced muscle dysfunction Via a sirtuin 1-dependent mechanism
Shen, S., Liao, Q., Liu, J., Pan, R., Lee, S. M., & Lin, L. (2019) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12393 · Cited by 142
Talbert, E. E., Smuder, A. J., Min, K., Kwon, O. S., Szeto, H. H., & Powers, S. K. (2013) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00471.2013 · Cited by 143
Mechanisms of muscle growth and atrophy in mammals and Drosophila
Piccirillo, R., Demontis, F., Perrimon, N., & Goldberg, A. L. (2013) · Developmental Dynamics · doi:10.1002/dvdy.24036 · Cited by 147
Self-citationStressed out: the skeletal muscle ryanodine receptor as a target of stress
Bellinger, A. M., Mongillo, M., & Marks, A. R. (2008) · Journal of Clinical Investigation · doi:10.1172/jci34006 · Cited by 138
Busquets, S., Toledo, M., Orpí, M., Massa, D., Porta, M. M., Capdevila, E., Padilla, N., Frailis, V., López-Soriano, F. J., Han, H. Q., et al. (2011) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-011-0049-z · Cited by 141
Experimental Models of Sarcopenia: Bridging Molecular Mechanism and Therapeutic Strategy
Mankhong, S., Kim, S., Moon, S., Kwak, H., Park, D., & Kang, J. (2020) · Cells · doi:10.3390/cells9061385 · Cited by 150
Smad3 Induces Atrogin-1, Inhibits mTOR and Protein Synthesis, and Promotes Muscle Atrophy In Vivo
Goodman, C. A., McNally, R. M., Hoffmann, F. M., & Hornberger, T. A. (2013) · Molecular Endocrinology · doi:10.1210/me.2013-1194 · Cited by 152
Dyle, M. C., Ebert, S. M., Cook, D. P., Kunkel, S. D., Fox, D. K., Bongers, K. S., Bullard, S. A., Dierdorff, J. M., & Adams, C. M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.556241 · Cited by 138
Sato, A. Y., Richardson, D., Cregor, M. D., Davis, H. M., Au, E. D., McAndrews, K., Zimmers, T. A., Organ, J. M., Peacock, M., Plotkin, L. I., et al. (2017) · Endocrinology · doi:10.1210/en.2016-1779 · Cited by 144
Yeo, D., Kang, C., Gomez-Cabrera, M. C., Vina, J., & Ji, L. L. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.10.456 · Cited by 137
Metallothionein Prevents High-Fat Diet–Induced Cardiac Contractile Dysfunction
Dong, F., Li, Q., Sreejayan, N., Nunn, J. M., & Ren, J. T. (2007) · Diabetes · doi:10.2337/db06-1596 · Cited by 136
Sáinz, N., Rodríguez, A., Catalán, V., Becerril, S., Ramírez, B., Gómez-Ambrosi, J., & Frühbeck, G. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006808 · Cited by 135
Exercise and nutritional interventions for improving aging muscle health
Forbes, S. C., Little, J. P., & Candow, D. G. (2012) · Endocrine · doi:10.1007/s12020-012-9676-1 · Cited by 136
Protein breakdown in cancer cachexia
Sandri, M. (2016) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2015.11.002 · Cited by 134
Self-citationCurrent understanding of sarcopenia: possible candidates modulating muscle mass
Sakuma, K., Aoi, W., & Yamaguchi, A. (2014) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-014-1527-x · Cited by 133
The Transcription Factor ATF4 Promotes Skeletal Myofiber Atrophy during Fasting
Ebert, S. M., Monteys, A. M., Fox, D. K., Bongers, K. S., Shields, B. E., Malmberg, S. E., Davidson, B. L., Suneja, M., & Adams, C. M. (2010) · Molecular Endocrinology · doi:10.1210/me.2009-0345 · Cited by 130
Chalkiadaki, A., Igarashi, M., Nasamu, A. S., Knezevic, J., & Guarente, L. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004490 · Cited by 126
Derbré, F., Gómez‐Cabrera, M. C., Nascimento, A. L. R., Sanchis‐Gomar, F., Martinez-Bello, V. E., Tresguerres, J. A. F., Fuentes, T., Gratas‐Delamarche, A., Monsalve, M., & Viña, J. (2011) · AGE · doi:10.1007/s11357-011-9264-y · Cited by 135
Recent advances in the biology and therapy of muscle wasting
Glass, D. J., & Roubenoff, R. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05809.x · Cited by 130
Garcia, M. M., Guéant‐Rodriguez, R., Pooya, S., Brachet, P., Alberto, J., Jeannesson, É., Maskali, F., Guéguen, N., Marie, P., Lacolley, P. J., et al. (2011) · The Journal of Pathology · doi:10.1002/path.2881 · Cited by 127
Forkhead Box, Class O Transcription Factors in Brain: Regulation and Behavioral Manifestation
Polter, A. M., Yang, S., Zmijewska, A. A., van Groen, T., Paik, J.-H., DePinho, R. A., Peng, S. L., Jope, R. S., & Li, X. (2008) · Biological Psychiatry · doi:10.1016/j.biopsych.2008.08.005 · Cited by 128
PGC-1α is Dispensable for Exercise-Induced Mitochondrial Biogenesis in Skeletal Muscle
Rowe, G. C., El‐Khoury, R., Patten, I. S., Rustin, P., & Arany, Z. P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041817 · Cited by 132
Self-citationMitochondrial dysfunction and skeletal muscle atrophy: Causes, mechanisms, and treatment strategies
Kubat, G. B., Bouhamida, E., Ülger, Ö., Türkel, İ., Pedriali, G., Ramaccini, D., Ekinci, Ö., Özerkliğ, B., Atalay, Ö., Patergnani, S., et al. (2023) · Mitochondrion · doi:10.1016/j.mito.2023.07.003 · Cited by 134
Muscle wasting and interleukin-6-induced atrogin-I expression in the cachectic Apc Min/+ mouse
Baltgalvis, K. A., Berger, F. G., Peña, M. M. O., Davis, J. M., White, J. P., & Carson, J. A. (2008) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-008-0574-6 · Cited by 129
Tang, K., Wagner, P. D., & Breen, E. C. (2010) · Journal of Cellular Physiology · doi:10.1002/jcp.21955 · Cited by 125
“…of PGC-1a may be mediated by a combination of both a loss of VEGF-dependent capillaries supplying oxygen to the muscle and altered regulation of genes important for mitochondrial biogenesis, type IIa fiber preservation and prevention of muscle atrophy (Sandri et al., 2006; Handschin et al., 2007).”
BackgroundGuigni, B. A., Callahan, D. M., Tourville, T. W., Miller, M. S., Fiske, B. R., Voigt, T. B., Korwin-Mihavics, B. R., Anathy, V., Dittus, K. L., & Toth, M. J. (2018) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00002.2018 · Cited by 125
Forkhead Box O Signaling Pathway in Skeletal Muscle Atrophy
Chen, K., Gao, P., Li, Z., Dai, A., Yang, M. W. O., Chen, S., Su, J., Deng, Z., & Li, L. (2022) · American Journal Of Pathology · doi:10.1016/j.ajpath.2022.09.003 · Cited by 129
The many roles of PGC-1α in muscle — recent developments
Chan, M. C., & Arany, Z. P. (2014) · Metabolism · doi:10.1016/j.metabol.2014.01.006 · Cited by 127
Self-citationMolecular Adaptations to Aerobic Exercise Training in Skeletal Muscle of Older Women
Konopka, A. R., Douglass, M. D., Kaminsky, L. A., Jemioło, B., Trappe, T. A., Trappe, S. W., & Harber, M. P. (2010) · The Journals of Gerontology Series A · doi:10.1093/gerona/glq109 · Cited by 134
Lokireddy, S., Mouly, V., Butler-Browne, G. S., Gluckman, P. D., Sharma, M., Kambadur, R., & McFarlane, C. (2011) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00114.2011 · Cited by 126
PGC-1 coactivators in the cardiovascular system
Patten, I. S., & Arany, Z. P. (2011) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2011.09.007 · Cited by 125
Self-citationBiological basis and treatment of frailty and sarcopenia
Sato, R., Vatic, M., da Fonseca, G. W. P., Anker, S. D., & von Haehling, S. (2024) · Cardiovascular Research · doi:10.1093/cvr/cvae073 · Cited by 130
Mitochondrial Biogenesis and Fragmentation as Regulators of Muscle Protein Degradation
Romanello, V., & Sandri, M. (2010) · Current Hypertension Reports · doi:10.1007/s11906-010-0157-8 · Cited by 123
Self-citationMitochondrial Biogenesis in Health and Disease. Molecular and Therapeutic Approaches
Sanchis‐Gomar, F., García‐Giménez, J. L., Gómez‐Cabrera, M. C., & Pallardó, F. V. (2014) · Current Pharmaceutical Design · doi:10.2174/1381612820666140306095106 · Cited by 120
Metabolic benefits of resistance training and fast glycolytic skeletal muscle
LeBrasseur, N. K., Walsh, K. X., & Arany, Z. P. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00512.2010 · Cited by 123
Self-citationRelationship between Human Aging Muscle and Oxidative System Pathway
Doria, E., Buonocore, D., Focarelli, A., & Marzatico, F. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/830257 · Cited by 127
Update on mitochondria and muscle aging: All wrong roads lead to sarcopenia
Picca, A., Calvani, R., Bossola, M., Allocca, E., Menghi, A., Pesce, V., Lezza, A. M. S., Bernabei, R., Landi, F., & Marzetti, E. (2018) · Biological Chemistry · doi:10.1515/hsz-2017-0331 · Cited by 116
Oxidative stress: Biomarkers and novel therapeutic pathways
Maiese, K., Chong, Z. Z., Hou, J., & Shang, Y. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.01.004 · Cited by 117
Sestrins are evolutionarily conserved mediators of exercise benefits
Kim, M., Sujkowski, A. L., Namkoong, S., Gu, B., Cobb, T., Kim, B. Y., Kowalsky, A. H., Cho, C., Semple, I. A., Ro, S., et al. (2020) · Nature Communications · doi:10.1038/s41467-019-13442-5 · Cited by 119
Summermatter, S., Baum, O., Santos, G., Hoppeler, H. H., & Handschin, C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.145995 · Cited by 115
Self-citationLeick, L., Lyngby, S. S., Wojtaszewski, J. F. P., & Pilegaard, H. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.01.011 · Cited by 121
Duscha, B. D., Schulze, P. C., Robbins, J. L., & Forman, D. E. (2007) · Heart Failure Reviews · doi:10.1007/s10741-007-9056-8 · Cited by 114
Posttranslational modifications control FoxO3 activity during denervation
Bertaggia, E., Coletto, L., & Sandri, M. (2012) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00142.2011 · Cited by 114
Self-citationCho, Y., Hazen, B. C., Russell, A. P., & Kralli, A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.489674 · Cited by 117
Molecular Mechanisms of Muscle Plasticity with Exercise
Hoppeler, H. H., Baum, O., Lurman, G. J., & Mueller, M. (2011) · Comprehensive physiology · doi:10.1002/cphy.c100042 · Cited by 131
Guo, A., Li, K., Tian, H., Fan, Z., Chen, Q., Yang, Y., Yu, J., Wu, Y., & Xiao, Q. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16448 · Cited by 118
Altered regulation of the PINK1 locus: a link between type 2 diabetes and neurodegeneration?
Scheele, C., Nielsen, A. R., Walden, T. B., Sewell, D. A., Fischer, C. P., Brogan, R. J., Petrovic, N., Larsson, O., Tesch, P. A., Wennmalm, K., et al. (2007) · The FASEB Journal · doi:10.1096/fj.07-8520com · Cited by 110
Monsalve, M., & Olmos, Y. (2011) · Current Drug Targets · doi:10.2174/138945011796150307 · Cited by 113
Molecular Mechanisms and Treatment Options for Muscle Wasting Diseases
Rüegg, M. A., & Glass, D. J. (2011) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010510-100537 · Cited by 114
Metadata
- Authors
- Sandri, M., Lin, J., Handschin, C., Yang, W., Arany, Z. P., Lecker, S. H., Goldberg, A. L., & Spiegelman, B. M.
- Affiliations
- Harvard University (US)
- Beth Israel Deaconess Medical Center (US)
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2006-10-31
- Volume
- 103
- Issue
- 44
- Pages
- 16260-16265
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC1637570
- OpenAlex
- W1977548231
- Cited by
- 974
- References
- 53
- Citations by year
- 2026: 20 · 2025: 38 · 2024: 44 · 2023: 51 · 2022: 56 · 2021: 42 · 2020: 66 · 2019: 64 · 2018: 54 · 2017: 40 · 2016: 51 · 2015: 57 · 2014: 65 · 2013: 68 · 2012: 52
- FWCI
- 13.20
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- edoc (University of Basel) (submittedVersion)
- Digital Access to Scholarship at Harvard (DASH) (Harvard University) (submittedVersion, cc-by)
- edoc (University of Basel)
- Funders
- Muscular Dystrophy Association
- Compagnia di San Paolo
- National Institutes of Health (DK6230701)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01-DK-6230701, R01DK062307, R56DK054477, P30DK040561)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- PGC-1α, skeletal muscle atrophy, FOXO3, atrogin-1, MuRF1, ubiquitin ligase, denervation, cancer cachexia, diabetes mellitus, renal failure, fasting, physical activity, muscle fiber diameter, energy metabolism, transcriptional coactivator, muscle fiber type shift
- MeSH terms
- Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha, Animals, Gene Expression Regulation, Mice, Transgenic, Muscular Atrophy, Nerve Tissue Proteins, Transcription Factors, Transcription, Genetic, Biomarkers, Trans-Activators, Muscle, Skeletal, Mice, Forkhead Transcription Factors
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review