Pompe disease: From pathophysiology to therapy and back again

Frontiers in Aging Neuroscience

Volumn 6, Issue JUL, 2014, Pages

  Lim, Jeong A ^a   Li, Lishu ^a   Raben, Nina ^a  

^a NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES   (United States)

Author keywords

Autophagy; Enzyme replacement therapy; Lipofuscin; Lysosome; Pompe disease

Indexed keywords

ALPHA GLUCOSIDASE; GLYCOGEN; GLYCOGEN SYNTHASE; GLYCOGENIN; LIPOFUSCIN; PARVOVIRUS VECTOR; RECOMBINANT GLUCAN 1,4 ALPHA GLUCOSIDASE; SHORT HAIRPIN RNA; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR E3; TRANSCRIPTION FACTOR EB; UNCLASSIFIED DRUG;

AGING; AUTOLYSOSOME; AUTOPHAGY; CLINICAL FEATURE; DISEASE COURSE; DISEASE MODEL; DISORDERS OF MITOCHONDRIAL FUNCTIONS; DRUG MEGADOSE; DRUG SAFETY; EARLY INTERVENTION; ENZYME DEFICIENCY; ENZYME INHIBITION; ENZYME REPLACEMENT; ENZYME SUBSTRATE; EXOCYTOSIS; GENE OVEREXPRESSION; GENE THERAPY; GENETIC MANIPULATION; GLYCOGEN STORAGE DISEASE TYPE 2; HUMAN; HYPERTROPHIC CARDIOMYOPATHY; LYSOSOME; MUSCLE INJURY; MYOPATHY; NONHUMAN; OXIDATIVE STRESS; PATHOPHYSIOLOGY; PATIENT CARE; PHASE 1 CLINICAL TRIAL (TOPIC); PHASE 2 CLINICAL TRIAL (TOPIC); REVIEW; SKELETAL MUSCLE;

EID: 84987673756     PISSN: None     EISSN: 16634365     Source Type: Journal    
DOI: 10.3389/fnagi.2014.00177     Document Type: Review

References (137)

1. Andrews, N. W. (2000). Regulated secretion of conventional lysosomes. Trends Cell Biol. 10, 316-321. doi: 10.1016/s0962-8924(00)01794-3
2. Angelini, C., and Semplicini, C. (2012). Enzyme replacement therapy for Pompe disease. Curr. Neurol. Neurosci. Rep. 12, 70-75. doi: 10.1007/s11910-011-0236-5
3. Appelmans, F., Wattiaux, R., and De Duve, C. (1955). Tissue fractionation studies. 5. The association of acid phosphatase with a special class of cytoplasmic granules in rat liver. Biochem. J. 59, 438-445.
4. Ausems, M. G., Verbiest, J., Hermans, M. P., Kroos, M. A., Beemer, F. A., Wokke, J. H., et al. (1999). Frequency of glycogen storage disease type II in the Netherlands: implications for diagnosis and genetic counselling. Eur. J. Hum. Genet. 7, 713-716. doi: 10.1038/sj.ejhg.5200367
5. Banugaria, S. G., Prater, S. N., Ng, Y. K., Kobori, J. A., Finkel, R. S., Ladda, R. L., et al. (2011). The impact of antibodies on clinical outcomes in diseases treated with therapeutic protein: lessons learned from infantile Pompe disease. Genet. Med. 13, 729-736. doi: 10.1097/gim.0b013e3182174703
6. Bar-Peled, L., and Sabatini, D. M. (2014). Regulation of mTORC1 by amino acids. Trends Cell Biol. 24, 400-406. doi: 10.1016/j.tcb.2014.03.003
7. Becker, J. A., Vlach, J., Raben, N., Nagaraju, K., Adams, E. M., Hermans, M. M., et al. (1998). The African origin of the common mutation in African American patients with glycogen-storage disease type II. Am. J. Hum. Genet. 62, 991-994. doi: 10.1086/301788
8. Berg, T. O., Fengsrud, M., Stromhaug, P. E., Berg, T., and Seglen, P. O. (1998). Isolation and characterization of rat liver amphisomes. Evidence for fusion of autophagosomes with both early and late endosomes. J. Biol. Chem. 273, 21883-21892. doi: 10.1074/jbc.273.34.21883
9. Bijvoet, A. G., Van De Kamp, E. H., Kroos, M. A., Ding, J. H., Yang, B. Z., Visser, P., et al. (1998). Generalized glycogen storage and cardiomegaly in a knockout mouse model of Pompe disease. Hum. Mol. Genet. 7, 53-62. doi: 10.1093/hmg/7.1.53
10. Bischoff, G. (1932). Zum klinischen bild der glykogen-speicherungs-krankheit (glykogenose). Z. Kinderheilkd. 52, 722-726. doi: 10.1007/BF02248461
11. Bjørkøy, G., Lamark, T., Pankiv, S., Overvatn, A., Brech, A., and Johansen, T. (2009). Monitoring autophagic degradation of p62/SQSTM1. Methods Enzymol. 452, 181-197. doi: 10.1016/s0076-6879(08)03612-4
12. Boerkoel, C. F., Exelbert, R., Nicastri, C., Nichols, R. C., Miller, F. W., Plotz, P. H., et al. (1995). Leaky splicing mutation in the acid maltase gene is associated with delayed onset of glycogenosis type II. Am. J. Hum. Genet. 56, 887-897.
13. Brunk, U. T., and Terman, A. (2002). Lipofuscin: mechanisms of age-related accumulation and influence on cell function. Free Radic. Biol. Med. 33, 611-619. doi: 10.1016/s0891-5849(02)00959-0
14. Byrne, B. J., Falk, D. J., Pacak, C. A., Nayak, S., Herzog, R. W., Elder, M. E., et al. (2011). Pompe disease gene therapy. Hum. Mol. Genet. 20, R61-R68. doi: 10.1093/hmg/ddr174
15. Cameron, J. M., Levandovskiy, V., Mackay, N., Utgikar, R., Ackerley, C., Chiasson, D., et al. (2009). Identification of a novel mutation in GYS1 (muscle-specific glycogen synthase) resulting in sudden cardiac death, that is diagnosable from skin fibroblasts. Mol. Genet. Metab. 98, 378-382. doi: 10.1016/j.ymgme.2009.07.012
16. Chakrapani, A., Vellodi, A., Robinson, P., Jones, S., and Wraith, J. E. (2010). Treatment of infantile Pompe disease with alglucosidase alpha: the UK experience. J. Inherit. Metab. Dis. 33, 747-750. doi: 10.1007/s10545-010-9206-3
17. Chien, Y. H., Chiang, S. C., Zhang, X. K., Keutzer, J., Lee, N. C., Huang, A. C., et al. (2008). Early detection of Pompe disease by newborn screening is feasible: results from the Taiwan screening program. Pediatrics 122, e39-e45. doi: 10.1542/peds.2007-2222
18. Chien, Y. H., Hwu, W. L., and Lee, N. C. (2013). Pompe disease: early diagnosis and early treatment make a difference. Pediatr. Neonatol. 54, 219-227. doi: 10.1016/j.pedneo.2013.03.009
19. Chien, Y. H., Lee, N. C., Thurberg, B. L., Chiang, S. C., Zhang, X. K., Keutzer, J., et al. (2009). Pompe disease in infants: improving the prognosis by newborn screening and early treatment. Pediatrics 124, e1116-e1125. doi: 10.1542/peds.2008-3667
20. Cori, G. T. (1954). Enzymes and glycogen structure in glycogenosis. Osterr. Z. Kinderheilkd. Kinderfuersorge 10, 38-42.
21. de Filippi, P., Ravaglia, S., Bembi, B., Costa, A., Moglia, A., Piccolo, G., et al. (2010). The angiotensin-converting enzyme insertion/deletion polymorphism modifies the clinical outcome in patients with Pompe disease. Genet. Med. 12, 206-211. doi: 10.1097/gim.0b013e3181d2900e
22. Demetriades, C., Doumpas, N., and Teleman, A. A. (2014). Regulation of TORC1 in response to amino acid starvation via lysosomal recruitment of TSC2. Cell 156, 786-799. doi: 10.1016/j.cell.2014.01.024
23. Douillard-Guilloux, G., Raben, N., Takikita, S., Batista, L., Caillaud, C., and Richard, E. (2008). Modulation of glycogen synthesis by RNA interference: towards a new therapeutic approach for glycogenosis type II. Hum. Mol. Genet. 17, 3876-3886. doi: 10.1093/hmg/ddn290
24. Douillard-Guilloux, G., Raben, N., Takikita, S., Ferry, A., Vignaud, A., Guillet-Deniau, I., et al. (2010). Restoration of muscle functionality by genetic suppression of glycogen synthesis in a murine model of Pompe disease. Hum. Mol. Genet. 19, 684-696. doi: 10.1093/hmg/ddp535
25. Drost, M. R., Hesselink, R. P., Oomens, C. W., and Van Der Vusse, G. J. (2005). Effects of non-contractile inclusions on mechanical performance of skeletal muscle. J. Biomech. 38, 1035-1043. doi: 10.1016/j.jbiomech.2004.05.040
26. Efeyan, A., Zoncu, R., Chang, S., Gumper, I., Snitkin, H., Wolfson, R. L., et al. (2013). Regulation of mTORC1 by the Rag GTPases is necessary for neonatal autophagy and survival. Nature 493, 679-683. doi: 10.1038/nature11745
27. Engel, A. G. (1970). Acid maltase deficiency in adults: studies in four cases of a syndrome which may mimic muscular dystrophy or other myopathies. Brain 93, 599-616. doi: 10.1093/brain/93.3.599
28. Feeney, E. J., Austin, S., Chien, Y. H., Mandel, H., Schoser, B., Prater, S., et al. (2014). The value of muscle biopsies in Pompe disease: identifying lipofuscin inclusions in juvenile-and adult-onset patients. Acta Neuropathol. Commun. 2, 2-17. doi: 10.1186/2051-5960-2-2
29. Feeney, E. J., Spampanato, C., Puertollano, R., Ballabio, A., Parenti, G., and Raben, N. (2013). What else is in store for autophagy? Exocytosis of autolysosomes as a mechanism of TFEB-mediated cellular clearance in Pompe disease. Autophagy 9, 1117-1118. doi: 10.4161/auto.24920
30. Filosto, M., Todeschini, A., Cotelli, M. S., Vielmi, V., Rinaldi, F., Rota, S., et al. (2013). Non-muscle involvement in late-onset glycogenosis II. Acta Myol. 32, 91-94.
31. Fujimoto, S., Manabe, Y., Fujii, D., Kozai, Y., Matsuzono, K., Takahashi, Y., et al. (2013). A novel mutation of the GAA gene in a patient with adult-onset Pompe disease lacking a disease-specific pathology. Intern. Med. 52, 2461-2464. doi: 10.2169/internalmedicine.52.0311
32. Fukuda, T., Ahearn, M., Roberts, A., Mattaliano, R. J., Zaal, K., Ralston, E., et al. (2006). Autophagy and mistargeting of therapeutic enzyme in skeletal muscle in Pompe disease. Mol. Ther. 14, 831-839. doi: 10.1016/j.ymthe.2006.08.009
33. Griffin, J. L. (1984a). Infantile acid maltase deficiency. I. Muscle fiber destruction after lysosomal rupture4. Virchows Arch. B Cell Pathol. Incl. Mol. Pathol. 45, 23-36. doi: 10.1007/bf02889849
34. Griffin, J. L. (1984b). Infantile acid maltase deficiency. II. Muscle fiber hypertrophy and the ultrastructure of end-stage fibers3. Virchows Arch. B Cell Pathol. Incl. Mol. Pathol. 45, 37-50. doi: 10.1007/bf02889850
35. Güngör, D., and Reuser, A. J. (2013). How to describe the clinical spectrum in Pompe disease. Am. J. Med. Genet. A 161A, 399-400. doi: 10.1002/ajmg.a.35662
36. He, C., and Klionsky, D. J. (2009). Regulation mechanisms and signaling pathways of autophagy. Annu. Rev. Genet. 43, 67-93. doi: 10.1146/annurev-genet-102808-114910
37. Hermans, M. M., De Graaff, E., Kroos, M. A., Mohkamsing, S., Eussen, B. J., Joosse, M., et al. (1994). The effect of a single base pair deletion (delta T525) and a C1634T missense mutation (pro545leu) on the expression of lysosomal alpha-glucosidase in patients with glycogen storage disease type II. Hum. Mol. Genet. 3, 2213-2218. doi: 10.1093/hmg/3.12.2213
38. Hermans, M. M., Wisselaar, H. A., Kroos, M. A., Oostra, B. A., and Reuser, A. J. (1993). Human lysosomal alpha-glucosidase: functional characterization of the glycosylation sites. Biochem. J. 289, 681-686.
39. Hers, H. G. (1963). Alpha-glucosidase deficiency in generalize glycogen storage disease (Pompe's disease). Biochem. J. 86, 11-16.
40. Herzog, A., Hartung, R., Reuser, A. J., Hermanns, P., Runz, H., Karabul, N., et al. (2012). A cross-sectional single-centre study on the spectrum of Pompe disease, German patients: molecular analysis of the GAA gene, manifestation and genotype-phenotype correlations. Orphanet J. Rare Dis. 7:35. doi: 10.1186/1750-1172-7-35
41. Hesselink, R. P., Wagenmakers, A. J., Drost, M. R., and Van Der Vusse, G. J. (2003). Lysosomal dysfunction in muscle with special reference to glycogen storage disease type II. Biochim. Biophys. Acta 1637, 164-170. doi: 10.1016/s0925-4439(02)00229-6
42. Hirschhorn, R., and Huie, M. L. (1999). Frequency of mutations for glycogen storage disease type II in different populations: the delta525T and deltaexon 18 mutations are not generally "common" in white populations. J. Med. Genet. 36, 85-86.
43. Hirschhorn, R., and Reuser, A. J. (2001). "Glycogen storage disease type II: acid alpha-glucosidase (acid maltase) deficiency, " in The Metabolic and Molecular Basis of Inherited Disease, eds C. R. Scriver, A. Beaudet, W. S. Sly and D. Valle (New York, NY: McGraw-Hill), 3389-3420.
44. Hoefsloot, L. H., Hoogeveen-Westerveld, M., Kroos, M. A., Van Beeumen, J., Reuser, A. J., and Oostra, B. A. (1988). Primary structure and processing of lysosomal alpha-glucosidase; homology with the intestinal sucrase-isomaltase complex. EMBO J. 7, 1697-1704.
45. Hoefsloot, L. H., Hoogeveen-Westerveld, M., Reuser, A. J., and Oostra, B. A. (1990). Characterization of the human lysosomal alpha-glucosidase gene. Biochem. J. 272, 493-497.
46. Höhn, A., Jung, T., and Grune, T. (2014). Pathophysiological importance of aggregated damaged proteins. Free Radic. Biol. Med. 71C, 70-89. doi: 10.1016/j.freeradbiomed.2014.02.028
47. Höhn, A., Sittig, A., Jung, T., Grimm, S., and Grune, T. (2012). Lipofuscin is formed independently of macroautophagy and lysosomal activity in stress-induced prematurely senescent human fibroblasts. Free Radic. Biol. Med. 53, 1760-1769. doi: 10.1016/j.freeradbiomed.2012.08.591
48. Hollak, C. E., and Wijburg, F. A. (2014). Treatment of lysosomal storage disorders: successes and challenges. J. Inherit. Metab. Dis. doi: 10.1007/s10545-014-9718-3. [Epub ahead of print].
49. Huie, M. L., Chen, A. S., Tsujino, S., Shanske, S., Dimauro, S., Engel, A. G., et al. (1994). Aberrant splicing in adult onset glycogen storage disease type II (GSDII): molecular identification of an IVS1 (+13T→G) mutation in a majority of patients and a novel IVS10 (-1GT→CT) mutation. Hum. Mol. Genet. 3, 2231-2236. doi: 10.1093/hmg/3.12.2231
50. Jay, V., Christodoulou, J., Mercer-Connolly, A., and Mcinnes, R. R. (1992). "Reducing body"-like inclusions in skeletal muscle in childhood-onset acid maltase deficiency. Acta Neuropathol. 85, 111-115. doi: 10.1007/bf00304641
51. Jat, P. S., Noble, M. D., Ataliotis, P., Tanaka, Y., Yannoutsos, N., Larsen, L., et al. (1991). Direct derivation of conditionally immortal cell lines from an H-2Kb-tsA58 transgenic mouse. Proc. Natl. Acad. Sci. U S A 88, 5096-5100. doi: 10.1073/pnas.88.12.5096
52. Kabeya, Y., Mizushima, N., Ueno, T., Yamamoto, A., Kirisako, T., Noda, T., et al. (2000). LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing. EMBO J. 19, 5720-5728. doi: 10.1093/emboj/19.21.5720
53. Kaushik, S., Bandyopadhyay, U., Sridhar, S., Kiffin, R., Martinez-Vicente, M., Kon, M., et al. (2011). Chaperone-mediated autophagy at a glance. J. Cell Sci. 124, 495-499. doi: 10.1242/jcs.073874
54. Kikuchi, T., Yang, H. W., Pennybacker, M., Ichihara, N., Mizutani, M., Van Hove, J. L., et al. (1998). Clinical and metabolic correction of pompe disease by enzyme therapy in acid maltase-deficient quail. J. Clin. Invest. 101, 827-833. doi: 10.1172/jci1722
55. Kishnani, P. S., Corzo, D., Nicolino, M., Byrne, B., Mandel, H., Hwu, W. L., et al. (2007). Recombinant human acid [alpha]-glucosidase: major clinical benefits in infantile-onset Pompe disease. Neurology 68, 99-109. doi: 10.1212/01.wnl.0000251268.41188.04
56. Kishnani, P. S., Hwu, W. L., Mandel, H., Nicolino, M., Yong, F., and Corzo, D. (2006). A retrospective, multinational, multicenter study on the natural history of infantile-onset Pompe disease. J. Pediatr. 148, 671-676. doi: 10.1016/j.jpeds.2005.11.033
57. Klionsky, D. J. (2007). Autophagy: from phenomenology to molecular understanding in less than a decade. Nat. Rev. Mol. Cell Biol. 8, 931-937. doi: 10.1038/nrm2245
58. Koeberl, D. D., Austin, S., Case, L. E., Smith, E. C., Buckley, A. F., Young, S. P., et al. (2014). Adjunctive albuterol enhances the response to enzyme replacement therapy in late-onset Pompe disease. FASEB J. 28, 2171-2176. doi: 10.1096/fj.13-241893
59. Kollberg, G., Tulinius, M., Gilljam, T., Ostman-Smith, I., Forsander, G., Jotorp, P., et al. (2007). Cardiomyopathy and exercise intolerance in muscle glycogen storage disease 0. N. Engl. J. Med. 357, 1507-1514. doi: 10.1056/nejmoa066691
60. Komatsu, M., Waguri, S., Koike, M., Sou, Y. S., Ueno, T., Hara, T., et al. (2007). Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice. Cell 131, 1149-1163. doi: 10.1016/j.cell.2007.10.035
61. Kornfeld, S. (1992). Structure and function of the mannose 6-phosphate/insulinlike growth factor II receptors. Annu. Rev. Biochem. 61, 307-330. doi: 10.1146/annurev.biochem.61.1.307
62. Kotoulas, O. B., Kalamidas, S. A., and Kondomerkos, D. J. (2006). Glycogen autophagy in glucose homeostasis. Pathol. Res. Pract. 202, 631-638. doi: 10.1016/j.prp.2006.04.001
63. Kroos, M., Hoogeveen-Westerveld, M., Van Der Ploeg, A., and Reuser, A. J. (2012). The genotype-phenotype correlation in Pompe disease. Am. J. Med. Genet. C Semin. Med. Genet. 160, 59-68. doi: 10.1002/ajmg.c.31318
64. Kuo, W. L., Hirschhorn, R., Huie, M. L., and Hirschhorn, K. (1996). Localization and ordering of acid alpha-glucosidase (GAA) and thymidine kinase (TK1) by fluorescence in situ hybridization. Hum. Genet. 97, 404-406. doi: 10.1007/bf02185782
65. Lewandowska, E., Wierzba-Bobrowicz, T., Rola, R., Modzelewska, J., Stepien, T., Lugowska, A., et al. (2008). Pathology of skeletal muscle cells in adult-onset glycogenosis type II (Pompe disease): ultrastructural study. Folia Neuropathol. 46, 123-133.
66. Lieberman, A. P., Puertollano, R., Raben, N., Slaugenhaupt, S., Walkley, S. U., and Ballabio, A. (2012). Autophagy in lysosomal storage disorders. Autophagy 8, 719-730. doi: 10.4161/auto.19469
67. Lin, J., Wu, H., Tarr, P. T., Zhang, C. Y., Wu, Z., Boss, O., et al. (2002). Transcriptional co-activator PGC-1 alpha drives the formation of slow-twitch muscle fibres. Nature 418, 797-801. doi: 10.1038/nature00904
68. Maga, J. A., Zhou, J., Kambampati, R., Peng, S., Wang, X., Bohnsack, R. N., et al. (2013). Glycosylation-independent lysosomal targeting of acid alpha-glucosidase enhances muscle glycogen clearance in Pompe mice. J. Biol. Chem. 288, 1428-1438. doi: 10.1074/jbc.M112.438663
69. Martina, J. A., Chen, Y., Gucek, M., and Puertollano, R. (2012). MTORC1 functions as a transcriptional regulator of autophagy by preventing nuclear transport of TFEB. Autophagy 8, 903-914. doi: 10.4161/auto.19653
70. Martina, J. A., Diab, H. I., Li, H., and Puertollano, R. (2014a). Novel roles for the MiTF/TFE family of transcription factors in organelle biogenesis, nutrient sensing and energy homeostasis. Cell. Mol. Life Sci. 71, 2483-2497. doi: 10.1007/s00018-014-1565-8
71. Martina, J. A., Diab, H. I., Lishu, L., Jeong-A, L., Patange, S., Raben, N., et al. (2014b). The nutrient-responsive transcription factor TFE3 promotes autophagy, lysosomal biogenesis and clearance of cellular debris. Sci. Signal. 7:ra9. doi: 10.1126/scisignal.2004754
72. Martiniuk, F., Chen, A., Mack, A., Arvanitopoulos, E., Chen, Y., Rom, W. N., et al. (1998). Carrier frequency for glycogen storage disease type II in New York and estimates of affected individuals born with the disease. Am. J. Med. Genet. 79, 69-72. doi: 10.1002/(sici)1096-8628(19980827)79:1<69::aid-ajmg16>3.0.co;2-k
73. Martiniuk, F., Mehler, M., Tzall, S., Meredith, G., and Hirschhorn, R. (1990). Sequence of the cDNA and 5'-flanking region for human acid alpha-glucosidase, detection of an intron in the 5' untranslated leader sequence, definition of 18-bp polymorphisms and differences with previous cDNA and amino acid sequences. DNA Cell Biol. 9, 85-94. doi: 10.1089/dna.1990.9.85
74. Masiero, E., Agatea, L., Mammucari, C., Blaauw, B., Loro, E., Komatsu, M., et al. (2009). Autophagy is required to maintain muscle mass. Cell Metab. 10, 507-515. doi: 10.1016/j.cmet.2009.10.008
75. Masiero, E., and Sandri, M. (2010). Autophagy inhibition induces atrophy and myopathy in adult skeletal muscles. Autophagy 6, 307-309. doi: 10.4161/auto.6.2.11137
76. Mechtler, T. P., Stary, S., Metz, T. F., De Jesus, V. R., Greber-Platzer, S., Pollak, A., et al. (2012). Neonatal screening for lysosomal storage disorders: feasibility and incidence from a nationwide study in Austria. Lancet 379, 335-341. doi: 10.1016/S0140-6736(11)61266-X
77. Medina, D. L., Fraldi, A., Bouche, V., Annunziata, F., Mansueto, G., Spampanato, C., et al. (2011). Transcriptional activation of lysosomal exocytosis promotes cellular clearance. Dev. Cell 21, 421-430. doi: 10.1016/j.devcel.2011.07.016
78. Menon, S., Dibble, C. C., Talbott, G., Hoxhaj, G., Valvezan, A. J., Takahashi, H., et al. (2014). Spatial control of the TSC complex integrates insulin and nutrient regulation of mTORC1 at the lysosome. Cell 156, 771-785. doi: 10.1016/j.cell.2013.11.049
79. Mizushima, N., Yoshimori, T., and Levine, B. (2010). Methods in mammalian autophagy research. Cell 140, 313-326. doi: 10.1016/j.cell.2010.01.028
80. Moreland, R. J., Jin, X., Zhang, X. K., Decker, R. W., Albee, K. L., Lee, K. L., et al. (2005). Lysosomal acid alpha-glucosidase consists of four different peptides processed from a single chain precursor. J. Biol. Chem. 280, 6780-6791. doi: 10.1074/jbc.m404008200
81. Nascimbeni, A. C., Fanin, M., Masiero, E., Angelini, C., and Sandri, M. (2012a). Impaired autophagy contributes to muscle atrophy in glycogen storage disease type II patients. Autophagy 8, 1697-1700. doi: 10.4161/auto.21691
82. Nascimbeni, A. C., Fanin, M., Masiero, E., Angelini, C., and Sandri, M. (2012b). The role of autophagy in the pathogenesis of glycogen storage disease type II (GSDII). Cell Death Differ. 19, 1698-1708. doi: 10.1038/cdd.2012.52
83. Neufeld, E. F., and Fratantoni, J. C. (1970). Inborn errors of mucopolysaccharide metabolism. Science 169, 141-146. doi: 10.1126/science.169.3941.141
84. Nicolino, M., Byrne, B., Wraith, J. E., Leslie, N., Mandel, H., Freyer, D. R., et al. (2009). Clinical outcomes after long-term treatment with alglucosidase alfa in infants and children with advanced Pompe disease. Genet. Med. 11, 210-219. doi: 10.1097/GIM.0b013e31819d0996
85. Pankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J. A., Outzen, H., et al. (2007). p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy. J. Biol. Chem. 282, 24131-24145. doi: 10.1074/jbc.m702824200
86. Pederson, B. A., Chen, H., Schroeder, J. M., Shou, W., Depaoli-Roach, A. A., and Roach, P. J. (2004). Abnormal cardiac development in the absence of heart glycogen. Mol. Cell. Biol. 24, 7179-7187. doi: 10.1128/mcb.24.16.7179-7187.2004
87. Porto, C., Cardone, M., Fontana, F., Rossi, B., Tuzzi, M. R., Tarallo, A., et al. (2009). The pharmacological chaperone N-butyldeoxynojirimycin enhances enzyme replacement therapy in Pompe disease fibroblasts. Mol. Ther. 17, 964-971. doi: 10.1038/mt.2009.53
88. Porto, C., Ferrara, M. C., Meli, M., Acampora, E., Avolio, V., Rosa, M., et al. (2012). Pharmacological enhancement of alpha-glucosidase by the allosteric chaperone N-acetylcysteine. Mol. Ther. 20, 2201-2211. doi: 10.1038/mt.2012.152
89. Prater, S. N., Banugaria, S. G., Dearmey, S. M., Botha, E. G., Stege, E. M., Case, L. E., et al. (2012). The emerging phenotype of long-term survivors with infantile Pompe disease. Genet. Med. 14, 800-810. doi: 10.1038/gim.2012.44
90. Prater, S. N., Patel, T. T., Buckley, A. F., Mandel, H., Vlodavski, E., Banugaria, S. G., et al. (2013). Skeletal muscle pathology of infantile Pompe disease during long-term enzyme replacement therapy. Orphanet J. Rare Dis. 8:90. doi: 10.1186/1750-1172-8-90. [Epub ahead of print].
91. Putschar, M. (1932). Uber angeborene Glykogenspeicher-Krankheit des herzens. Beitr. Pathol. Anat. Allg. Pathol. 90:222.
92. Raben, N., Fukuda, T., Gilbert, A. L., De Jong, D., Thurberg, B. L., Mattaliano, R. J., et al. (2005). Replacing acid alpha-glucosidase in Pompe disease: recombinant and transgenic enzymes are equipotent, but neither completely clears glycogen from type II muscle fibers. Mol. Ther. 11, 48-56. doi: 10.1016/j.ymthe.2004.09.017
93. Raben, N., Hill, V., Shea, L., Takikita, S., Baum, R., Mizushima, N., et al. (2008). Suppression of autophagy in skeletal muscle uncovers the accumulation of ubiquitinated proteins and their potential role in muscle damage in Pompe disease. Hum. Mol. Genet. 17, 3897-3908. doi: 10.1093/hmg/ddn292
94. Raben, N., Nagaraju, K., Lee, E., Kessler, P., Byrne, B., Lee, L., et al. (1998). Targeted disruption of the acid alpha-glucosidase gene in mice causes an illness with critical features of both infantile and adult human glycogen storage disease type II. J. Biol. Chem. 273, 19086-19092. doi: 10.1074/jbc.273.30.19086
95. Raben, N., Nichols, R. C., Martiniuk, F., and Plotz, P. H. (1996). A model of mRNA splicing in adult lysosomal storage disease (glycogenosis type II). Hum. Mol. Genet. 5, 995-1000. doi: 10.1093/hmg/5.7.995
96. Raben, N., Ralston, E., Chien, Y. H., Baum, R., Schreiner, C., Hwu, W. L., et al. (2010a). Differences in the predominance of lysosomal and autophagic pathologies between infants and adults with Pompe disease: implications for therapy. Mol. Genet. Metab. 101, 324-331. doi: 10.1016/j.ymgme.2010.08.001
97. Raben, N., Roberts, A., and Plotz, P. H. (2007a). Role of autophagy in the pathogenesis of Pompe disease. Acta Myol. 26, 45-48.
98. Raben, N., Schreiner, C., Baum, R., Takikita, S., Xu, S., Xie, T., et al. (2010b). Suppression of autophagy permits successful enzyme replacement therapy in a lysosomal storage disorder-murine Pompe disease. Autophagy 6, 1078-1089. doi: 10.4161/auto.6.8.13378
99. Raben, N., Shea, L., Hill, V., and Plotz, P. (2009). Monitoring autophagy in lysosomal storage disorders. Methods Enzymol. 453, 417-449. doi: 10.1016/S0076-6879(08)04021-4
100. Raben, N., Takikita, S., Pittis, M. G., Bembi, B., Marie, S. K. N., Roberts, A., et al. (2007b). Deconstructing Pompe disease by analyzing single muscle fibers. Autophagy 3, 546-552.
101. Saftig, P., and Klumperman, J. (2009). Lysosome biogenesis and lysosomal membrane proteins: trafficking meets function. Nat. Rev. Mol. Cell Biol. 10, 623-635. doi: 10.1038/nrm2745
102. Sardiello, M., Palmieri, M., Di Ronza, A., Medina, D. L., Valenza, M., Gennarino, V. A., et al. (2009). A gene network regulating lysosomal biogenesis and function. Science 325, 473-477. doi: 10.1126/science.1174447
103. Schiaffino, S., and Hanzlikova, V. (1972). Autophagic degradation of glycogen in skeletal muscles of the newborn rat. J. Cell Biol. 52, 41-51. doi: 10.1083/jcb.52.1.41
104. Schiaffino, S., Mammucari, C., and Sandri, M. (2008). The role of autophagy in neonatal tissues: just a response to amino acid starvation? Autophagy 4, 727-730.
105. Schoser, B., Hill, V., and Raben, N. (2008). Therapeutic approaches in glycogen storage disease type II/Pompe disease. Neurotherapeutics 5, 569-578. doi: 10.1016/j.nurt.2008.08.009
106. Schoser, B. G., Muller-Hocker, J., Horvath, R., Gempel, K., Pongratz, D., Lochmuller, H., et al. (2007). Adult-onset glycogen storage disease type 2: clinico-pathological phenotype revisited. Neuropathol. Appl. Neurobiol. 33, 544-559. doi: 10.1111/j.1365-2990.2007.00839.x
107. Schuller, A., Wenninger, S., Strigl-Pill, N., and Schoser, B. (2012). Toward deconstructing the phenotype of late-onset Pompe disease. Am. J. Med. Genet. C Semin. Med. Genet. 160C, 80-88. doi: 10.1002/ajmg.c.31322
108. Seppala, E. H., Reuser, A. J., and Lohi, H. (2013). A nonsense mutation in the acid alpha-glucosidase gene causes Pompe disease in Finnish and Swedish Lapphunds. PLoS One 8:e56825. doi: 10.1371/journal.pone.0056825
109. Settembre, C., and Ballabio, A. (2011). TFEB regulates autophagy: an integrated coordination of cellular degradation and recycling processes. Autophagy 7, 1379-1381. doi: 10.4161/auto.7.11.17166
110. Settembre, C., and Ballabio, A. (2014). Lysosomal adaptation: how the lysosome responds to external cues. Cold Spring Harb. Perspect. Biol. 6:a016907. doi: 10.1101/cshperspect.a016907
111. Settembre, C., Di Malta, C., Polito, V. A., Garcia Arencibia, M., Vetrini, F., Erdin, S., et al. (2011). TFEB links autophagy to lysosomal biogenesis. Science 332, 1429-1433. doi: 10.1126/science.1204592
112. Settembre, C., Zoncu, R., Medina, D. L., Vetrini, F., Erdin, S., Huynh, T., et al. (2012). A lysosome-to-nucleus signalling mechanism senses and regulates the lysosome via mTOR and TFEB. EMBO J. 31, 1095-1108. doi: 10.1038/emboj.2012.32
113. Sharma, M. C., Schultze, C., Von Moers, A., Stoltenburg-Didinger, G., Shin, Y. S., Podskarbi, T., et al. (2005). Delayed or late-onset type II glycogenosis with globular inclusions. Acta Neuropathol. 110, 151-157. doi: 10.1007/s00401-005-1026-4
114. Shea, L., and Raben, N. (2009). Autophagy in skeletal muscle: implications for Pompe disease. Int. J. Clin. Pharmacol. Ther. 47(Suppl. 1), S42-S47. doi: 10.5414/cpp47042
115. Shieh, J. J., and Lin, C. Y. (1998). Frequent mutation in Chinese patients with infantile type of GSD II in Taiwan: evidence for a founder effect. Hum. Mutat. 11, 306-312. doi: 10.1002/(sici)1098-1004(1998)11:4<306::aid-humu8>3.3.co;2-j
116. Slonim, A. E., Bulone, L., Ritz, S., Goldberg, T., Chen, A., and Martiniuk, F. (2000). Identification of two subtypes of infantile acid maltase deficiency. J. Pediatr. 137, 283-285. doi: 10.1067/mpd.2000.107112
117. Smith, B. K., Collins, S. W., Conlon, T. J., Mah, C. S., Lawson, L. A., Martin, A. D., et al. (2013). Phase I/II trial of adeno-associated virus-mediated alpha-glucosidase gene therapy to the diaphragm for chronic respiratory failure in Pompe disease: initial safety and ventilatory outcomes. Hum. Gene Ther. 24, 630-640. doi: 10.1089/hum.2012.250
118. Spampanato, C., Feeney, E., Li, L., Cardone, M., Lim, J. A., Annunziata, F., et al. (2013). Transcription factor EB (TFEB) is a new therapeutic target for Pompe disease. EMBO Mol. Med. 5, 691-706. doi: 10.1002/emmm.201202176
119. Strothotte, S., Strigl-Pill, N., Grunert, B., Kornblum, C., Eger, K., Wessig, C., et al. (2010). Enzyme replacement therapy with alglucosidase alfa in 44 patients with late-onset glycogen storage disease type 2: 12-month results of an observational clinical trial. J. Neurol. 257, 91-97. doi: 10.1007/s00415-009-5275-3
120. Sukigara, S., Liang, W. C., Komaki, H., Fukuda, T., Miyamoto, T., Saito, T., et al. (2012). Muscle glycogen storage disease 0 presenting recurrent syncope with weakness and myalgia. Neuromuscul. Disord. 22, 162-165. doi: 10.1016/j.nmd.2011.08.008
121. Takikita, S., Schreiner, C., Baum, R., Xie, T., Ralston, E., Plotz, P. H., et al. (2010). Fiber type conversion by PGC-1alpha activates lysosomal and autophagosomal biogenesis in both unaffected and Pompe skeletal muscle. PLoS One 5:e15239. doi: 10.1371/journal.pone.0015239
122. Terman, A., and Brunk, U. T. (2006). Oxidative stress, accumulation of biological 'garbage' and aging. Antioxid. Redox Signal. 8, 197-204. doi: 10.1089/ars.2006.8.197
123. Terman, A., Gustafsson, B., and Brunk, U. T. (2006). The lysosomal-mitochondrial axis theory of postmitotic aging and cell death. Chem. Biol. Interact. 163, 29-37. doi: 10.1016/j.cbi.2006.04.013
124. Terman, A., Kurz, T., Navratil, M., Arriaga, E. A., and Brunk, U. T. (2010). Mitochondrial turnover and aging of long-lived postmitotic cells: the mitochondrial-lysosomal axis theory of aging. Antioxid. Redox Signal. 12, 503-535. doi: 10.1089/ars.2009.2598
125. Thurberg, B. L., Lynch, M. C., Vaccaro, C., Afonso, K., Tsai, A. C., Bossen, E., et al. (2006). Characterization of pre-and post-treatment pathology after enzyme replacement therapy for pompe disease. Lab. Invest. 86, 1208-1220. doi: 10.1038/labinvest.3700484
126. Tiels, P., Baranova, E., Piens, K., De Visscher, C., Pynaert, G., Nerinckx, W., et al. (2012). A bacterial glycosidase enables mannose-6-phosphate modification and improved cellular uptake of yeast-produced recombinant human lysosomal enzymes. Nat. Biotechnol. 30, 1225-1231. doi: 10.1038/nbt.2427
127. Tsuburaya, R. S., Monma, K., Oya, Y., Nakayama, T., Fukuda, T., Sugie, H., et al. (2012). Acid phosphatase-positive globular inclusions is a good diagnostic marker for two patients with adult-onset Pompe disease lacking disease specific pathology. Neuromuscul. Disord. 22, 389-393. doi: 10.1016/j.nmd.2011.11.003
128. van den Hout, H. M., Hop, W., van Diggelen, O. P., Smeitink, J. A., Smit, G. P., Poll-The, B. T., et al. (2003). The natural course of infantile Pompe's disease: 20 original cases compared with 133 cases from the literature. Pediatrics 112, 332-340. doi: 10.1542/peds.112.2.332
129. Van den Hout, J. M., Kamphoven, J. H., Winkel, L. P., Arts, W. F., De Klerk, J. B., Loonen, M. C., et al. (2004). Long-term intravenous treatment of Pompe disease with recombinant human alpha-glucosidase from milk. Pediatrics 113, e448-e457. doi: 10.1542/peds.113.5.e448
130. Van der Ploeg, A. T., Clemens, P. R., Corzo, D., Escolar, D. M., Florence, J., Groeneveld, G. J., et al. (2010). A randomized study of alglucosidase alfa in late-onset Pompe's disease. N. Engl. J. Med. 362, 1396-1406. doi: 10.1056/NEJMoa0909859
131. Walkley, S. U. (2008). "Pathogenesis of CNS disease in lysosomal storage disorders, " in 10th International Symposium on Mucopolysaccharide and Related Diseases (Vancouver, Canada).
132. Wisselaar, H. A., Kroos, M. A., Hermans, M. M., van Beeumen, J., and Reuser, A. J. (1993). Structural and functional changes of lysosomal acid alpha-glucosidase during intracellular transport and maturation. J. Biol. Chem. 268, 2223-2231.
133. Wu, J. J., Quijano, C., Chen, E., Liu, H., Cao, L., Fergusson, M. M., et al. (2009). Mitochondrial dysfunction and oxidative stress mediate the physiological impairment induced by the disruption of autophagy. Aging (Albany NY) 1, 425-437.
134. Xu, F., Ding, E., Liao, S. X., Migone, F., Dai, J., Schneider, A., et al. (2004). Improved efficacy of gene therapy approaches for Pompe disease using a new, immune-deficient GSD-II mouse model. Gene Ther. 11, 1590-1598. doi: 10.1038/sj.gt.3302314
135. Yang, Z., and Klionsky, D. J. (2010). Mammalian autophagy: core molecular machinery and signaling regulation. Curr. Opin. Cell Biol. 22, 124-131. doi: 10.1016/j.ceb.2009.11.014
136. Zhu, Y., Jiang, J. L., Gumlaw, N. K., Zhang, J., Bercury, S. D., Ziegler, R. J., et al. (2009). Glycoengineered acid alpha-glucosidase with improved efficacy at correcting the metabolic aberrations and motor function deficits in a mouse model of Pompe disease. Mol. Ther. 17, 954-963. doi: 10.1038/mt.2009.37
137. Zoncu, R., Bar-Peled, L., Efeyan, A., Wang, S., Sancak, Y., and Sabatini, D. M. (2011). mTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H(+)-ATPase. Science 334, 678-683. doi: 10.1126/science.1207056