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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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Antibody-Mediated Enzyme Therapeutics and Applications in Glycogen Storage Diseases
Zhou, Z., Austin, G. L., Shaffer, R., Armstrong, D., & Gentry, M. S. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.08.005 · Cited by 40
Defective expression of ATG4D abrogates autophagy and promotes growth in human uterine fibroids
Andaloussi, A. E., Habib, S., Soylemes, G., Laknaur, A., Elhusseini, H., Al-Hendy, A. A., & Ismail, N. (2017) · Cell Death Discovery · doi:10.1038/cddiscovery.2017.41 · Cited by 39
Mitochondrial breakdown in skeletal muscle and the emerging role of the lysosomes
Triolo, M., & Hood, D. A. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.11.004 · Cited by 39
Chung, L.-H., Liu, S., Huang, S., Salter, D. M., Lee, H., & Hsu, Y. (2020) · Aging · doi:10.18632/aging.103896 · Cited by 42
“deletion of the autophagy-related genes Atg5 or Atg7 results in skeletal muscle atrophy accompanied by accumulation of p62 [19, 20].”
BackgroundThree-dimensional tissue-engineered human skeletal muscle model of Pompe disease
Wang, J., Zhou, C. J., Khodabukus, A., Tran, S., Han, S.-O., Carlson, A. L., Madden, L. R., Kishnani, P. S., Koeberl, D. D., & Bursac, N. (2021) · Communications Biology · doi:10.1038/s42003-021-02059-4 · Cited by 45
Deletion of ATG5 Shows a Role of Autophagy in Salivary Homeostatic Control
Morgan-Bathke, M. E., Lin, H. H., Chibly, A. M., Zhang, W., Sun, X., Chen, C.-H., Flodby, P., Borok, Z., Wu, R., Arnett, D. G., et al. (2013) · Journal of Dental Research · doi:10.1177/0022034513499350 · Cited by 40
“Based on previous conditional knockouts of models of autophagy in a variety of tissues (Nakai et al., 2007; Raben et al., 2008), it is clear that autophagy is involved in diverse physiological and pathological processes with immense relevance in human development, diseases, and aging.”
BackgroundImpairment of autophagosome-lysosome fusion contributes to chronic ethanol-induced liver injury
Cho, H., Choi, J.-W., & Lee, S. (2014) · Alcohol · doi:10.1016/j.alcohol.2014.08.006 · Cited by 38
“Indeed, in Pompe disease, impaired autophagic flux leads to accumulation of ubiquitinated proteins and subsequently causes profound muscle damage (Raben et al., 2008).”
BackgroundDisrupted autophagy undermines skeletal muscle adaptation and integrity
Jokl, E. J., & Blanco, G. (2016) · Mammalian Genome · doi:10.1007/s00335-016-9659-2 · Cited by 38
“This accumulation of autophagic material at the core of the fibres is due to impaired autophagosome lysosome fusion, although induction of autophagy may also contribute (Raben et al. 2008).”
Lipin‐1 regulates Bnip3–mediated mitophagy in glycolytic muscle
Alshudukhi, A. A., Zhu, J., Huang, D., Jama, A., Smith, J. D., Wang, Q. J., Esser, K. A., & Ren, H. (2018) · The FASEB Journal · doi:10.1096/fj.201800374 · Cited by 37
Banduseela, V. C., Chen, Y., Kultima, H. G., Norman, H. S., Aare, S., Radell, P. J., Eriksson, L. I., Hoffman, E. P., & Larsson, L. (2013) · Physiological Genomics · doi:10.1152/physiolgenomics.00141.2012 · Cited by 36
Zaal, K. J. M., Reid, E., Mousavi, K., Zhang, T., Mehta, A., Bugnard, E., Sartorelli, V., & Ralston, E. (2011) · PLoS ONE · doi:10.1371/journal.pone.0029057 · Cited by 37
“The Golgi complex organization is also altered during mitosis [12,13,14], in apoptotic cells [15], in diseases such as Amyotrophic Lateral Sclerosis [16,17], and in animal models of diseases such as Duchenne Muscular Dystrophy [18,19,20] and Pompe Disease [21,22,23].”
BackgroundSelf-citationRecent advances in mitochondrial turnover during chronic muscle disuse
Tryon, L. D., Vainshtein, A., Memme, J. M., Crilly, M. J., & Hood, D. A. (2014) · Integrative Medicine Research · doi:10.1016/j.imr.2014.09.001 · Cited by 33
Exercise prevents impaired autophagy and proteostasis in a model of neurogenic myopathy
Campos, J. C., Baehr, L. M., Gomes, K. M. S., Bechara, L. R. G., Voltarelli, V. A., Bozi, L. H. M., Ribeiro, M. A. C., Ferreira, N. D., Moreira, J. B. N., Brum, P. C., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-30365-1 · Cited by 32
Jiang, D., Chen, K., Lu, X., Gao, H., Qin, Z., & Lin, F. (2013) · Acta Pharmacologica Sinica · doi:10.1038/aps.2013.144 · Cited by 32
Silva, K. A. S., Ghiarone, T., Schreiber, K. L., Grant, D. G., White, T., Frisard, M. I., Sukhanov, S., Chandrasekar, B., Delafontaine, P., & Yoshida, T. (2019) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00898.2018 · Cited by 32
“In fact, persistent reduction in autophagic activity compromising skeletal muscle has been reported in several genetic muscle disorders such as collagen VI muscular dystrophy, Pompe disease, and Danon disease (23, 34, 40, 47, 57).”
BackgroundPicca, A., Lozanoska‐Ochser, B., Calvani, R., Coelho‐Júnior, H. J., Leewenburgh, C., & Marzetti, E. (2023) · Experimental Gerontology · doi:10.1016/j.exger.2023.112204 · Cited by 30
Autophagy is altered in skeletal and cardiac muscle of spontaneously hypertensive rats
Bloemberg, D., McDonald, E. J., Dulay, D., & Quadrilatero, J. (2013) · Acta Physiologica · doi:10.1111/apha.12178 · Cited by 30
Gene Therapy for Pompe Disease: The Time is now
Colella, P., & Mingozzi, F. (2019) · Human Gene Therapy · doi:10.1089/hum.2019.109 · Cited by 31
“…(1) whole-body glycogen accumulation (including cardiac muscle, skeletal muscle, and CNS) 16,66 ; (2) impaired autophagic flux in skeletal muscle 40,71 ; (3) motor neuron loss, neuroinflammation, and neuromuscular junction defects 7,17,67 ; (4) cardiac hypertrophy and cardiac dysfunction 72 ; (5)…”
InfluentialKey considerations for investigating and interpreting autophagy in skeletal muscle
Rahman, F. A., Baechler, B. L., & Quadrilatero, J. (2024) · Autophagy · doi:10.1080/15548627.2024.2373676 · Cited by 31
“Furthermore, mouse models of Pompe’s disease exhibit augmented LC3-I and LC3-II in the SOL and WG [31].”
InfluentialBiomedical Implications of Autophagy in Macromolecule Storage Disorders
Palhegyi, A. M., Seranova, E., Dimova, S., Hoque, S., & Sarkar, S. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00179 · Cited by 30
“Accumulation of autophagosomes and autophagy substrates as well as vacuolization, enlarged lysosomes and improper lysosomal acidification were found in the myotubes of patients and primary myoblasts of Gaa-deficient mice (Fukuda et al., 2006b; Raben et al., 2008; Takikita et al., 2009; Nascimbeni et al., 2012); implic…”
BackgroundSIRT1: A Novel Target for the Treatment of Muscular Dystrophies
Kuno, A., & Horio, Y. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/6714686 · Cited by 29
Shibu, M. A., Hung, T.-H., Chiang, W., & Lin, W. (2018) · Journal of Medicinal Food · doi:10.1089/jmf.2017.3941 · Cited by 29
“36,37 Consistent with previous reports, our results show excessive apoptosis with respect to elevation in the levels of proapoptotic proteins and reduction in the antiapoptotic proteins; however, it can be significantly ameliorated when treated with low, moderate, and high levels of VHVV.”
Preclinical Research in Glycogen Storage Diseases: A Comprehensive Review of Current Animal Models
Almodóvar-Payá, A., Villarreal‐Salazar, M., de Luna, N., Nogales‐Gadea, G., Real‐Martínez, A., Andreu, A. L., Martín, M. A., Arenas, J., Lucía, A., Vissing, J., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249621 · Cited by 28
“No AD-6neo/6neo Not reported [183,184] No AD2-6neo/6neo Not reported [185]”
BackgroundMethodInfluentialMyotubularin-related phosphatase 5 is a critical determinant of autophagy in neurons
Chua, J. P., Bedi, K., Paulsen, M. T., Ljungman, M. E., Tank, E. M. H., Kim, E. S., McBride, J. P., Colon, J., Ward, M. E., Weisman, L. S., et al. (2022) · Current Biology · doi:10.1016/j.cub.2022.04.053 · Cited by 28
Autophagy: Can it become a potential therapeutic target? (Review)
Naomoto (2010) · International Journal of Molecular Medicine · doi:10.3892/ijmm_00000369 · Cited by 28
Aerobic training as an adjunctive therapy to enzyme replacement in Pompe disease
Nilsson, M. I., Samjoo, I. A., Hettinga, B. P., Koeberl, D. D., Zhang, H., Hawke, T. J., Nissar, A. A., Ali, T., Brandt, L., Ansari, M. U., et al. (2012) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2012.09.010 · Cited by 28
“As previously demonstrated [10,60,61], we found that Pompe mice exhibited higher expression of Beclin-1 and LC3B compared to wild-type littermates (Figs.”
BackgroundResultAge-Related Maintenance of the Autophagy-Lysosomal System Is Dependent on Skeletal Muscle Type
Fernando, R., Castro, J. P., Flore, T., Deubel, S., Grune, T., & Ott, C. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/4908162 · Cited by 27
“demonstrated, bymeans ofmuscle-specificAtg5 inactivation inmice, an impairment of autophagy process, by the inhibition of LC3-II conversion [37].”
BackgroundIrimia, J. M., Tagliabracci, V. S., Meyer, C. M., Segvich, D. M., DePaoli-Roach, A. A., & Roach, P. J. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.673897 · Cited by 28
“The mechanism by which glycogen is transferred to lysosomes is not well understood but likely involves autophagy or an autophagy-like pathway (1, 3).”
BackgroundXu, S., Galperin, M. M., Melvin, G. M., Horowits, R., Raben, N., Plötz, P. H., & Yu, L. C. (2010) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01253.2009 · Cited by 27
“Procedure for isolation, fixation, and immunostaining of single fibers is described elsewhere (21).”
Self-citationPizon, V., Rybina, S., Gerbal, F., Delort, F., Vicart, P., Baldacci, G., & Karsenti, E. (2013) · PLoS ONE · doi:10.1371/journal.pone.0076140 · Cited by 27
Activation of autophagy is required for muscle homeostasis during physical exercise
Nair, U., & Klionsky, D. J. (2011) · Autophagy · doi:10.4161/auto.7.12.18315 · Cited by 28
“Muscular atrophy observed in mice with muscle-specific knockout of the autophagy genes Atg5 or Atg7 reinforces the role of autophagy in skeletal muscle homeostasis.(3,4) Mutations in any of the three genes that encode collagen VI, one of the major skeletal muscle extracellular matrix proteins, result in Bethlem myopat…”
BackgroundYi, H., Fredrickson, K., Das, S., Kishnani, P. S., & Sun, B. (2013) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2013.05.004 · Cited by 26
“InGAA-KOmice, autophagy was dramatically induced in both slow- and fast-twitch skeletal muscles [16].”
BackgroundFarah, B. L., Yen, P. M., & Koeberl, D. D. (2019) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2019.11.005 · Cited by 26
“Besides increases in the number of dysfunctional autophagosomes and lysosomes, there also is an increase in large protein aggregates that contain SQSTM1/p62 that likely contributes to the deterioration in function and cell death in skeletal muscle in GSDII patients [108].”
BackgroundColella, P., Sellier, P., Gómez, M. J., Biferi, M. G., Tanniou, G., Guerchet, N., Cohen-Tannoudji, M., Moya‐Nilges, M., van Wittenberghe, L., Danièle, N., et al. (2020) · EBioMedicine · doi:10.1016/j.ebiom.2020.103052 · Cited by 26
Quantitative evaluation of skeletal muscle defects in second harmonic generation images
Liu, W., Ralston, E., & Raben, N. (2013) · Journal of Biomedical Optics · doi:10.1117/1.jbo.18.2.026005 · Cited by 25
Self-citationAn integrative correlation of myopathology, phenotype and genotype in late onset Pompe disease
Kulessa, M., Weyer-Menkhoff, I., Viergutz, L., Kornblum, C., Claeys, K. G., Schneider, I., Plöckinger, U., Young, P., Boentert, M., Vielhaber, S., et al. (2019) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12580 · Cited by 25
Emerging role of mitophagy in myoblast differentiation and skeletal muscle remodeling
Rahman, F. A., & Quadrilatero, J. (2021) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2021.11.026 · Cited by 25
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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