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Suppression of autophagy in skeletal muscle uncovers the accumulation of ubiquitinated proteins and their potential role in muscle damage in Pompe disease.
Open accessAbstract
The role of autophagy, a catabolic lysosome-dependent pathway, has recently been recognized in a variety of disorders, including Pompe disease, the genetic deficiency of the glycogen-degrading lysosomal enzyme acid-alpha glucosidase. Accumulation of lysosomal glycogen, presumably transported from the cytoplasm by the autophagic pathway, occurs in multiple tissues, but pathology is most severe in skeletal and cardiac muscle. Skeletal muscle pathology also involves massive autophagic buildup in the core of myofibers. To determine if glycogen reaches the lysosome via autophagy and to ascertain whether autophagic buildup in Pompe disease is a consequence of induction of autophagy and/or reduced turnover due to defective fusion with lysosomes, we generated muscle-specific autophagy-deficient Pompe mice. We have demonstrated that autophagy is not required for glycogen transport to lysosomes in skeletal muscle. We have also found that Pompe disease involves induction of autophagy but manifests as a functional deficiency of autophagy because of impaired autophagosomal-lysosomal fusion. As a result, autophagic substrates, including potentially toxic aggregate-prone ubiquitinated proteins, accumulate in Pompe myofibers and may cause profound muscle damage.
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“Impaired autophagy is known to induce skeletal myofiber degeneration and muscle weakness (Masiero et al., 2009; Raben et al., 2008).”
From Proteasome dysfunction induces muscle growth defects and protein aggregation (2014) · cites this paper as Raben et al., 2008
Experimental — accuracy not yet measuredIn the citing paper
“Likewise, impairment of autophagy by muscle-specific ablation of ATG5 and ATG7 induces accumulation of abnormal mitochondria, induction of oxidative stress, apoptosis, muscle atrophy, weakness, several features of myopathy [230, 231].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [230]
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“Analogously, conditional Atg5 deletion in mouse skeletal muscle leads to accumulation of ubiquitin-positive inclusions and ultrastructural disorganization [478].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [478]
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“Accordingly, the phenotype of mice with muscle-specific inactivation of various genes coding for other autophagy-related proteins, such as Atg5, VPS15, AMPK and mTOR, results in atrophy, weakness and different myopathic features[43-46].”
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Role of Autophagy in Glycogen Breakdown and Its Relevance to Chloroquine Myopathy
Zirin, J. D., Nieuwenhuis, J., & Perrimon, N. (2013) · PLoS Biology · doi:10.1371/journal.pbio.1001708 · Cited by 132
“The only in vivo genetic analysis of the role of these systems during glycogen transport to the lysosome was performed in the mouse model of Pompe disease, where glycogen accumulation in the lysosome was diminished in Atg7deficient GAA KO muscles [12,30,31].”
BackgroundJu, J.-S., Jeon, S.-I., Park, J.-Y., Lee, J.-Y., Lee, S.-C., Cho, K.-J., & Jeong, J.-M. (2016) · The Journal of Physiological Sciences · doi:10.1007/s12576-016-0440-9 · Cited by 125
“knockdown/knockout animals of Atg5 and Atg7, essential autophagy proteins involved in autophagosome formation, also showed the importance of basal autophagy in mitochondrial function in skeletal muscle [36, 37].”
BackgroundDefects of Vps15 in skeletal muscles lead to autophagic vacuolar myopathy and lysosomal disease
Nemazanyy, I., Blaauw, B., Paolini, C., Caillaud, C., Protasi, F., Mueller, A., Proikas‐Cezanne, T., Russell, R. C., Guan, K., Nishino, I., et al. (2013) · EMBO Molecular Medicine · doi:10.1002/emmm.201202057 · Cited by 126
“…block distinct from Atg7 knockout Genetic mouse models carrying muscle specific inactivation of autophagy genes, Atg7 (Masiero et al, 2009) and Atg5 (Raben et al, 2008), highlighted the role of macroautophagy in the to a broader role of Vps15 gene in muscle function than the autophagy genes.”
InfluentialRole of Pro-inflammatory Cytokines in Regulation of Skeletal Muscle Metabolism: A Systematic Review
Sharma, B., & Dabur, R. (2018) · Current Medicinal Chemistry · doi:10.2174/0929867326666181129095309 · Cited by 129
The Role of Autophagy in Skeletal Muscle Diseases
Xia, Q., Huang, X., Huang, J., Zheng, Y., March, M., Li, J., & Wei, Y. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.638983 · Cited by 137
Defects in calcium homeostasis and mitochondria can be reversed in Pompe disease
Lim, J., Li, L., Kakhlon, O., Myerowitz, R., & Raben, N. (2015) · Autophagy · doi:10.1080/15548627.2015.1009779 · Cited by 131
Self-citationThe beneficial role of proteolysis in skeletal muscle growth and stress adaptation
Bell, R. A. V., Al-Khalaf, M. H., & Megeney, L. A. (2016) · Skeletal Muscle · doi:10.1186/s13395-016-0086-6 · Cited by 124
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
“Accordingly, muscle-specific Atg5 knockout mice displayed a similar phenotype [ 40 ].”
BackgroundBasu, S., Rajakaruna, S., Reyes, B. A. S., Bockstaele, E. V., & Menko, A. S. (2014) · Autophagy · doi:10.4161/auto.28768 · Cited by 117
“Most of our knowledge of how autophagy functions in regulating cell differentiation is based on tissue specific knockouts of autophagy-related genes.(7,13,14) Little is known about the signaling mechanisms that initiate autophagy-dependent differentiation pathways.”
BackgroundAutophagy and mitochondria in Pompe disease: Nothing is so new as what has long been forgotten
Raben, N., Wong, A., Ralston, E., & Myerowitz, R. (2012) · American Journal of Medical Genetics Part C Seminars in Medical Genetics · doi:10.1002/ajmg.c.31317 · Cited by 120
“Indeed, the levels of potentially toxic ubiquitinated proteins that can form insoluble aggregates are significantly elevated in Pompe skeletal muscle, suggesting that the recycling process is inefficient [Raben et al., 2008].”
BackgroundSelf-citationSebori, R., Kuno, A., Hosoda, R., Hayashi, T., & Horio, Y. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/9179270 · Cited by 114
“In addition, the muscle-specific knockout of Atg5 or Atg7 results in muscle atrophy, dysfunction, and myopathy [21, 22].”
BackgroundThe role of autophagy in the pathogenesis of glycogen storage disease type II (GSDII)
Nascimbeni, A. C., Fanin, M., Masiero, E., Angelini, C. I., & Sandri, M. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.52 · Cited by 106
“However, genetic suppression of autophagy in skeletal muscles significantly reduced the glycogen burden in GAA-KO mice(10) but did not improve clinical signs such as kyphosis, muscle wasting and decreased life span.(11) Our recent data show that inhibiting autophagy specifically in muscle tissue causes muscle weakness…”
The PKB/FOXO switch in aging and cancer
Kloet, D. E. A., & Burgering, B. M. T. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.04.003 · Cited by 106
Yamada, E., Bastie, C. C., Koga, H., Wang, Y., Cuervo, A. M., & Pessin, J. E. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.03.014 · Cited by 103
“In this regard, deficiency of skeletal muscle macroautophagy (acid a-glucosidase as seen in Pompe KO mice) results in marked skeletal muscle atrophy in glycolytic fibers but with less of an effect in oxidative fibers (Raben et al., 2008).”
BackgroundFritzen, A. M., Madsen, A. B., Kleinert, M., Treebak, J. T., Lundsgaard, A., Jensen, T. E., Richter, E. A., Wojtaszewski, J. F. P., Kiens, B., & Frøsig, C. (2015) · The Journal of Physiology · doi:10.1113/jp271405 · Cited by 103
“…is essential for cell differentiation, development and survival (Levine & Kroemer, 2008), and in skeletal muscle knockout of various proteins linked to autophagy leads to dysregulation of muscle metabolism and function (Raben et al. 2008; Masiero et al. 2009; Grumati et al. 2010; He et al. 2012).”
BackgroundThe Interplay between Mitochondrial Morphology and Myomitokines in Aging Sarcopenia
Romanello, V. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms22010091 · Cited by 101
Induction of autophagy improves hepatic lipid metabolism in glucose-6-phosphatase deficiency
Farah, B. L., Landau, D. J., Sinha, R. A., Brooks, E. D., Wu, Y., Fung, S. Y. S., Tanaka, T., Hirayama, M., Bay, B., Koeberl, D. D., et al. (2015) · Journal of Hepatology · doi:10.1016/j.jhep.2015.10.008 · Cited by 99
“Constitutively active AMPK plasmid (pEBG-AMPK a1[1‐312], Addgene plasmid 27632) was a gift from Dr.”
BackgroundRag GTPases are cardioprotective by regulating lysosomal function
Kim, Y. C., Park, H. W., Sciarretta, S., Mo, J., Jewell, J. L., Russell, R. C., Wu, X., Sadoshima, J., & Guan, K. (2014) · Nature Communications · doi:10.1038/ncomms5241 · Cited by 94
“Accumulation of ubiquitinated proteins is also observed in lysosomal storage diseases including a mouse model of Pompe disease 14, 41 .”
Lesmana, R., Sinha, R. A., Singh, B. K., Zhou, J., Ohba, K., Wu, Y., Yau, W. W. Y., Bay, B., & Yen, P. M. (2015) · Endocrinology · doi:10.1210/en.2015-1632 · Cited by 97
Defective Autophagy and mTORC1 Signaling in Myotubularin Null Mice
Fetalvero, K. M., Yu, Y., Goetschkes, M., Liang, G., Valdez, R. A., Gould, T., Triantafellow, E., Bergling, S., Loureiro, J., Eash, J., et al. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01075-12 · Cited by 96
“Musclespecific deletion of Atg5 or Atg7 results in muscle atrophy and a decrease in muscle strength (8, 9).”
BackgroundAutophagy, nutrition and immunology
Cuervo, A. M., & Macián, F. (2011) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2011.09.001 · Cited by 98
“In this respect, macroautophagy and microautophagy have been shown capable of breaking down glycogen (Kotoulas et al. 2006; Raben et al. 2008) (Fig.”
BackgroundModulation of mTOR signaling as a strategy for the treatment of Pompe disease
Lim, J., Li, L., Shirihai, O. S., Trudeau, K. M., Puertollano, R., & Raben, N. (2017) · EMBO Molecular Medicine · doi:10.15252/emmm.201606547 · Cited by 97
“In agreement with our previous data on fiber size of the tibialis anterior and psoas muscles (Raben et al, 2008; Takikita et al, 2010), GAA-KO gastrocnemius fibers were atrophic [cross-sectional area (CSA) = 736 12 lm2] compared to the WT [CSA = 1051 14 lm2].”
ResultSelf-citationVainshtein, A., Grumati, P., Sandri, M., & Bonaldo, P. (2014) · Journal of Molecular Medicine · doi:10.1007/s00109-013-1096-z · Cited by 88
“Generation of Atg5 and Atg7 muscle-specific knockout mice confirmed the physiological importance of this system in muscle mass maintenance [26, 27].”
BackgroundHerzog, A., Hartung, R., Reuser, A. J. J., Hermanns, P., Runz, H., Karabul, N., Gökce, S., Pohlenz, J., Kampmann, C., Lampe, C., et al. (2012) · Orphanet Journal of Rare Diseases · doi:10.1186/1750-1172-7-35 · Cited by 89
“Variation can also be envisaged to develop on the basis of qualitative and quantitative differences in the autophagy pathway that influence the lysosomal glycogen deposition [45].”
BackgroundThe Role of IGF-1 Signaling in Skeletal Muscle Atrophy
Timmer, L. T., Hoogaars, W. M. H., & Jaspers, R. T. (2018) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-1435-3_6 · Cited by 90
Bhatnagar, S., Mittal, A., Gupta, S. K., & Kumar, A. (2011) · Journal of Cellular Physiology · doi:10.1002/jcp.22821 · Cited by 90
“Autophagosome formation and elevated expression of several genes of this pathway have been observed in skeletal muscle of mice in response to starvation and denervation (Mammucari et al., 2007; Zhao et al., 2007; Romanello et al., 2010).”
BackgroundAutophagy in Skeletal Muscle Homeostasis and in Muscular Dystrophies
Grumati, P., & Bonaldo, P. (2012) · Cells · doi:10.3390/cells1030325 · Cited by 96
Raval, K. K., Tao, R., White, B. E., de Lange, W. J., Koonce, C. H., Yu, J., Kishnani, P. S., Thomson, J. A., Mosher, D. F., Ralphe, J. C., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.628628 · Cited by 86
“Pompe skeletal muscle has accumulations of autophagosomes and ubiquitinated protein aggregates, indicating that the lysosomes are not digesting intracellular materials at a sufficient rate (11).”
BackgroundImproved efficacy of a next-generation ERT in murine Pompe disease
Xu, S., Lun, Y., Frascella, M., Garcia, A., Soska, R., Nair, A., Ponery, A. S., Schilling, A. E., Feng, J., Tuske, S. J., et al. (2019) · JCI Insight · doi:10.1172/jci.insight.125358 · Cited by 92
“significant fiber size reduction was observed in quadriceps from Gaa-KO mice compared with age-matched WT animals, consistent with our previous data in other muscle groups (56, 79, 80).”
BackgroundResultSelf-citationMolecular machinery of macroautophagy and its deregulation in diseases
Wong, A. S. L., Cheung, Z. H., & Ip, N. Y. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.07.005 · Cited by 95
“In addition, impaired autophagosome maturation is implicated in Pompe disease pathology [145], with the disease pathology alleviated in macroautophagy-deficient mice following therapy [146].”
BackgroundRole of AMPK in regulation of LC3 lipidation as a marker of autophagy in skeletal muscle
Fritzen, A. M., Frøsig, C., Jeppesen, J. F., Jensen, T. E., Lundsgaard, A., Serup, A. K., Schjerling, P., Proud, C. G., Richter, E. A., & Kiens, B. (2016) · Cellular Signalling · doi:10.1016/j.cellsig.2016.03.005 · Cited by 86
Kou, X., Li, J., Liu, X., Yang, X., Fan, J., & Chen, N. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2017.03.070 · Cited by 81
Hollywood, J. A., Przepiorski, A. J., D’Souza, R. F., Sreebhavan, S., Wolvetang, E. J., Harrison, P. T., Davidson, A. J., & Holm, T. M. (2020) · Journal of the American Society of Nephrology · doi:10.1681/asn.2019070712 · Cited by 79
Lee, H. S., Daniels, B. H., Salas, E., Bollen, A. W., Debnath, J., & Margeta, M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0036221 · Cited by 78
“This linear pattern of staining may be related to the linear intermyofibrillar organization of microtubules (along which autophagosomes propagate) [19], and likely corresponds to the centrally-located zone of autophagic buildup that was detected in autophagy-deficient (ATG52/2) murine skeletal muscle [32].”
Background
Metadata
- Authors
- Raben, N., Hill, V., Shea, L., Takikita, S., Baum, R., Mizushima, N., Ralston, E., & Plotz, P.
- Affiliations
- National Institutes of Health (US)
- Tokyo Medical and Dental University (JP)
- Corresponding author
- Raben, N.
- Venue
- Human Molecular Genetics
- Publisher
- Oxford University Press (OUP)
- Published
- 2008-09-04
- Volume
- 17
- Issue
- 24
- Pages
- 3897-3908
- ISSN
- 0964-6906 (ISSN-L)
- 1460-2083
- PMC
- PMC2638578
- OpenAlex
- W2136000647
- Cited by
- 352
- References
- 61
- Citations by year
- 2026: 14 · 2025: 10 · 2024: 15 · 2023: 19 · 2022: 21 · 2021: 21 · 2020: 16 · 2019: 18 · 2018: 17 · 2017: 23 · 2016: 18 · 2015: 26 · 2014: 25 · 2013: 21 · 2012: 33
- FWCI
- 12.22
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Human Molecular Genetics (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- York University
- Institut National de la Santé et de la Recherche Médicale
- National Institutes of Health
- National Institute of Neurological Disorders and Stroke
- National Institute of Arthritis and Musculoskeletal and Skin Diseases
- Topics
- Health Sciences › Medicine › Genetics (clinical) › Lysosomal Storage Disorders Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Glycogen Storage Diseases and Myoclonus
- Keywords
- Pompe disease, autophagy, skeletal muscle, acid alpha-glucosidase deficiency, lysosomal glycogen accumulation, ubiquitinated proteins, protein aggregation, muscle damage
- MeSH terms
- alpha-Glucosidases, Animals, Autophagy, Female, Glycogen Storage Disease Type II, Male, Mice, Transgenic, Muscular Diseases, Proteins, Mice, Knockout, Muscle, Skeletal, Mice, Ubiquitination
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