Isolated inclusion body myopathy caused by a multisystem proteinopathy-linked hnRNPA1 mutation

Neurology: Genetics

Volumn 1, Issue 3, 2015, Pages

  Izumi, Rumiko ^a   Warita, Hitoshi ^a   Niihori, Tetsuya ^a   Takahashi, Toshiaki ^b   Tateyama, Maki ^a,c   Suzuki, Naoki ^a   Nishiyama, Ayumi ^a   Shirota, Matsuyuki ^a,d   Funayama, Ryo ^a   Nakayama, Keiko ^a   Mitsuhashi, Satomi ^a   Nishino, Ichizo ^d   Aoki, Yoko ^a   Aoki, Masashi ^a  

^a TOHOKU UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

^b National Hospital Organization Sendai Nishitaga Hospital   (Japan)

^c National Hospital Organization Iwate Hospital   (Japan)

^d NATIONAL INSTITUTE OF MENTAL HEALTH   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE; CALCIUM; PROTEIN P97; RNA BINDING PROTEIN; UBIQUITIN; VALOSIN CONTAINING PROTEIN;

ADULT; ALKALINE PHOSPHATASE BLOOD LEVEL; AMYOTROPHIC LATERAL SCLEROSIS; ARTICLE; AUTOPHAGOSOME; BONE DISEASE; BONE MALFORMATION; BONE PAIN; CALCIUM BLOOD LEVEL; CLINICAL ARTICLE; CLINICAL FEATURE; COGNITIVE DEFECT; CONTROLLED STUDY; DISEASE ASSOCIATION; DISEASE COURSE; FEMALE; GENE; GENE SEQUENCE; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A1 GENE; HUMAN; IMMUNOHISTOCHEMISTRY; ISOLATED INCLUSION BODY MYOPATHY; MALE; MIDDLE AGED; MISSENSE MUTATION; MOTONEURON; MOTOR UNIT POTENTIAL; MUSCLE BIOPSY; MUSCLE DISEASE; MUSCLE WEAKNESS; MYOPATHY; NEUROGENIC INFLAMMATION; NEUROLOGIC EXAMINATION; PRIORITY JOURNAL; TDP 43 PROTEINOPATHY;

EID: 84987760964     PISSN: None     EISSN: 23767839     Source Type: Journal    
DOI: 10.1212/NXG.0000000000000023     Document Type: Article

References (37)

1. Watts GD, Wymer J, Kovach MJ, et al. Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosincontaining protein. Nat Genet 2004;36:377-381.
2. Kim HJ, Kim NC, Wang YD, et al. Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Nature 2013;495:467-473.
3. Bucelli RC, Arhzaouy K, Pestronk A, et al. SQSTM1 splice site mutation in distal myopathy with rimmed vacuoles. Neurology 2015;85:665-674.
4. Senderek J, Garvey SM, Krieger M, et al. Autosomaldominant distal myopathy associated with a recurrent missense mutation in the gene encoding the nuclear matrix protein, matrin 3. Am J Hum Genet 2009;84:511-518.
5. Johnson JO, Pioro EP, Boehringer A, et al. Mutations in the Matrin 3 gene cause familial amyotrophic lateral sclerosis. Nat Neurosci 2014;17:664-666.
6. Benatar M, Wuu J, Fernandez C, et al. Motor neuron involvement in multisystem proteinopathy: implications for ALS. Neurology 2013;80:1874-1880.
7. Seelen M, Visser AE, Overste DJ, et al. No mutations in hnRNPA1 and hnRNPA2B1 in Dutch patients with amyotrophic lateral sclerosis, frontotemporal dementia, and inclusion body myopathy. Neurobiol Aging 2014;35:1956. e1959-e1911.
8. Le Ber I, Van Bortel I, Nicolas G, et al. hnRNPA2B1 and hnRNPA1 mutations are rare in patients with "multisystem proteinopathy" and frontotemporal lobar degeneration phenotypes. Neurobiol Aging 2014;35:934. e935-e936.
9. Calini D, Corrado L, Del Bo R, et al. Analysis of hnRNPA1, A2/B1, and A3 genes in patients with amyotrophic lateral sclerosis. Neurobiol Aging 2013;34:2695. e2611-e2692.
10. Mizuno H, Warita H, Aoki M, Itoyama Y. Accumulation of chondroitin sulfate proteoglycans in the microenvironment of spinal motor neurons in amyotrophic lateral sclerosis transgenic rats. J Neurosci Res 2008;86:2512-2523.
11. Tateyama M, Fujihara K, Itoyama Y. Dendritic cells in muscle lesions of sarcoidosis. Hum Pathol 2011;42:340-346.
12. Li H, Durbin R. Fast and accurate short read alignment with Burrows-Wheeler transform. Bioinformatics 2009;25:1754-1760.
13. McKenna A, Hanna M, Banks E, et al. The Genome Analysis Toolkit: a MapReduce framework for analyzing next-generation DNA sequencing data. Genome Res 2010;20:1297-1303.
14. Wang K, Li M, Hakonarson H. ANNOVAR: functional annotation of genetic variants from high-throughput sequencing data. Nucleic Acids Res 2010;38:e164.
15. Suzuki N, Aoki M, Mizuno H, et al. Late-onset distal myopathy with rimmed vacuoles without mutation in the GNE or dysferlin genes. Muscle Nerve 2005;32:812-814.
16. Darin N, Kyllerman M, Wahlstrom J, Martinsson T, Oldfors A. Autosomal dominant myopathy with congenital joint contractures, ophthalmoplegia, and rimmed vacuoles. Ann Neurol 1998;44:242-248.
17. Hauser MA, Horrigan SK, Salmikangas P, et al. Myotilin is mutated in limb girdle muscular dystrophy 1A. Hum Mol Genet 2000;9:2141-2147.
18. Horowitz SH, Schmalbruch H. Autosomal dominant distal myopathy with desmin storage: a clinicopathologic and electrophysiologic study of a large kinship. Muscle Nerve 1994;17:151-160.
19. Vicart P, Caron A, Guicheney P, et al. A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy. Nat Genet 1998;20:92-95.
20. Udd B, Partanen J, Halonen P, et al. Tibial muscular dystrophy. Late adult-onset distal myopathy in 66 Finnish patients. Arch Neurol 1993;50:604-608.
21. Brais B, Bouchard JP, Xie YG, et al. Short GCG expansions in the PABP2 gene cause oculopharyngeal muscular dystrophy. Nat Genet 1998;18:164-167.
22. Kottlors M, Moske-Eick O, Huebner A, et al. Late-onset autosomal dominant limb girdle muscular dystrophy and Paget's disease of bone unlinked to the VCP gene locus. J Neurol Sci 2010;291:79-85.
23. Kimonis VE, Mehta SG, Fulchiero EC, et al. Clinical studies in familial VCP myopathy associated with Paget disease of bone and frontotemporal dementia. Am J Med Genet A 2008;146A:745-757.
24. Weihl CC, Pestronk A, Kimonis VE. Valosin-containing protein disease: inclusion body myopathy with Paget's disease of the bone and fronto-temporal dementia. Neuromuscul Disord 2009;19:308-315.
25. Matsumoto G, Wada K, Okuno M, Kurosawa M, Nukina N. Serine 403 phosphorylation of p62/SQSTM1 regulates selective autophagic clearance of ubiquitinated proteins. Mol Cell 2011;44:279-289.
26. Pinkus JL, Amato AA, Taylor JP, Greenberg SA. Abnormal distribution of heterogeneous nuclear ribonucleoproteins in sporadic inclusion body myositis. Neuromuscul Disord 2014;24:611-616.
27. Yamashita S, Kimura E, Tawara N, et al. Optineurin is potentially associated with TDP-43 and involved in the pathogenesis of inclusion body myositis. Neuropathol Appl Neurobiol 2013;39:406-416.
28. Buratti E, Brindisi A, Giombi M, Tisminetzky S, Ayala YM, Baralle FE. TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail: an important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing. J Biol Chem 2005;280:37572-37584.
29. Shorter J, Taylor JP. Disease mutations in the prion-like domains of hnRNPA1 and hnRNPA2/B1 introduce potent steric zippers that drive excess RNP granule assembly. Rare Dis 2013;1:e25200.
30. Buchan JR, Kolaitis RM, Taylor JP, Parker R. Eukaryotic stress granules are cleared by autophagy and Cdc48/VCP function. Cell 2013;153:1461-1474.
31. Cacciottolo M, Nogalska A, D'Agostino C, Engel WK, Askanas V. Dysferlin is a newly identified binding partner of AbPP and it co-aggregates with amyloid-b42 within sporadic inclusion-body myositis (s-IBM) muscle fibers. Acta Neuropathol 2013;126:781-783.
32. Mehta SG, Khare M, Ramani R, et al. Genotype-phenotype studies of VCP-associated inclusion body myopathy with Paget disease of bone and/or frontotemporal dementia. Clin Genet 2013;83:422-431.
33. Shi Z, Hayashi YK, Mitsuhashi S, et al. Characterization of the Asian myopathy patients with VCP mutations. Eur J Neurol 2012;19:501-509.
34. Takata S, Hashimoto J, Nakatsuka K, et al. Guidelines for diagnosis and management of Paget's disease of bone in Japan. J Bone Miner Metab 2006;24:359-367.
35. Hackman P, Sarparanta J, Lehtinen S, et al. Welander distal myopathy is caused by a mutation in the RNA-binding protein TIA1. Ann Neurol 2013;73:500-509.
36. Klar J, Sobol M, Melberg A, et al. Welander distal myopathy caused by an ancient founder mutation in TIA1 associated with perturbed splicing. Hum Mutat 2013;34:572-577.
37. Vieira NM, Naslavsky MS, Licinio L, et al. A defect in the RNA-processing protein HNRPDL causes limb-girdle muscular dystrophy 1G (LGMD1G). Hum Mol Genet 2014;23:4103-4110.