Epitope mapping of antibodies against TDP-43 and detection of protease-resistant fragments of pathological TDP-43 in amyotrophic lateral sclerosis and frontotemporal lobar degeneration

Biochemical and Biophysical Research Communications

Volumn 417, Issue 1, 2012, Pages 116-121

  Tsuji, Hiroshi ^a,b   Nonaka, Takashi ^a   Yamashita, Makiko ^a   Masuda Suzukake, Masami ^a   Kametani, Fuyuki ^a   Akiyama, Haruhiko ^a   Mann, David M A ^c   Tamaoka, Akira ^b   Hasegawa, Masato ^a  

^a TOKYO METROPOLITAN INSTITUTE OF MEDICAL SCIENCE   (Japan)

^b UNIVERSITY OF TSUKUBA   (Japan)

^c UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

Aggregation; Alpha synuclein; ALS; FTLD; Tau

Indexed keywords

ARGININE; ASPARTIC ACID; EPITOPE; GLUTAMIC ACID; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 60019 2 IG; POLYCLONAL ANTIBODY; POLYCLONAL ANTIBODY 10782 2 AP; TAR DNA BINDING PROTEIN; UNCLASSIFIED DRUG;

AMYOTROPHIC LATERAL SCLEROSIS; ANTIGEN ANTIBODY REACTION; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME STRUCTURE; EPITOPE MAPPING; FRONTOTEMPORAL DEMENTIA; HUMAN; HUMAN CELL; IMMUNOBLOTTING; PRIORITY JOURNAL; PROTEASE RESISTANT FRAGMENT; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; TDP 43 PROTEINOPATHY;

AMINO ACID SEQUENCE; AMYOTROPHIC LATERAL SCLEROSIS; ANIMALS; ANTIBODIES; ANTIBODIES, MONOCLONAL; BRAIN; BRAIN CHEMISTRY; DNA-BINDING PROTEINS; EPITOPE MAPPING; FRONTOTEMPORAL LOBAR DEGENERATION; HUMANS; MICE; MOLECULAR SEQUENCE DATA; PEPTIDE HYDROLASES;

ANIMALIA;

EID: 84855809818     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.11.066     Document Type: Article

References (32)

1. Ayala Y.M., Misteli T., Baralle F.E. TDP-43 regulates retinoblastoma protein phosphorylation through the repression of cyclin-dependent kinase 6 expression. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:3785-3789.
2. Ayala Y.M., Pagani F., Baralle F.E. TDP43 depletion rescues aberrant CFTR exon 9 skipping. FEBS Lett. 2006, 580:1339-1344.
3. Buratti E., Baralle F.E. Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease. Front. Biosci. 2008, 13:867-878.
4. Ou S.H., Wu F., Harrich D., et al. Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs. J. Virol. 1995, 69:3584-3596.
5. Wang I.F., Reddy N.M., Shen C.K. Higher order arrangement of the eukaryotic nuclear bodies. Proc. Natl. Acad. Sci. U.S.A. 2002, 99:13583-13588.
6. Arai T., Hasegawa M., Akiyama H., et al. TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Biochem. Biophys. Res. Commun. 2006, 351:602-611.
7. Neumann M., Sampathu D.M., Kwong L.K., et al. Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 2006, 314:130-133.
8. Arai T., Mackenzie I.R., Hasegawa M., et al. Phosphorylated TDP-43 in Alzheimer's disease and dementia with Lewy bodies. Acta Neuropathol. (Berl) 2009, 117:125-136.
9. Hasegawa M., Arai T., Akiyama H., et al. TDP-43 is deposited in the Guam parkinsonism-dementia complex brains. Brain 2007, 130:1386-1394.
10. Tan C.F., Yamada M., Toyoshima Y., et al. Selective occurrence of TDP-43-immunoreactive inclusions in the lower motor neurons in Machado-Joseph disease. Acta Neuropathol. (Berl) 2009, 118:553-560.
11. Toyoshima Y., Tanaka H., Shimohata M., et al. Spinocerebellar ataxia type 2 (SCA2) is associated with TDP-43 pathology. Acta Neuropathol. (Berl) 2011, 122:375-378.
12. Yokota O., Davidson Y., Bigio E.H., et al. Phosphorylated TDP-43 pathology and hippocampal sclerosis in progressive supranuclear palsy. Acta Neuropathol. (Berl) 2010, 120:55-66.
13. Kabashi E., Valdmanis P.N., Dion P., et al. TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis. Nat. Genet. 2008, 40:572-574.
14. Sreedharan J., Blair I.P., Tripathi V.B., et al. TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis. Science 2008, 319:1668-1672.
15. Tamaoka A., Arai M., Itokawa M., et al. TDP-43 M337V mutation in familial amyotrophic lateral sclerosis in Japan. Intern. Med. 2010, 49:331-334.
16. Mackenzie I.R., Rademakers R., Neumann M. TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia. Lancet Neurol. 2010, 9:995-1007.
17. Hasegawa M., Arai T., Nonaka T., et al. Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Ann. Neurol. 2008, 64:60-70.
18. Mackenzie I.R., Bigio E.H., Ince P.G., et al. Pathological TDP-43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with SOD1 mutations. Ann. Neurol. 2007, 61:427-434.
19. Neumann M., Kwong L.K., Truax A.C., et al. TDP-43-positive white matter pathology in frontotemporal lobar degeneration with ubiquitin-positive inclusions. J. Neuropathol. Exp. Neurol. 2007, 66:177-183.
20. Zhang H., Tan C.F., Mori F., et al. TDP-43-immunoreactive neuronal and glial inclusions in the neostriatum in amyotrophic lateral sclerosis with and without dementia. Acta Neuropathol. (Berl) 2008, 115:115-122.
21. Neumann M., Mackenzie I.R., Cairns N.J., et al. TDP-43 in the ubiquitin pathology of frontotemporal dementia with VCP gene mutations. J. Neuropathol. Exp. Neurol. 2007, 66:152-157.
22. Zhang H.X., Tanji K., Mori F., et al. Epitope mapping of 2E2-D3, a monoclonal antibody directed against human TDP-43. Neurosci. Lett. 2008, 434:170-174.
23. Nonaka T., Kametani F., Arai T., et al. Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43. Hum. Mol. Genet. 2009, 18:3353-3364.
24. Nonaka T., Arai T., Buratti E., et al. Phosphorylated and ubiquitinated TDP-43 pathological inclusions in ALS and FTLD-U are recapitulated in SH-SY5Y cells. FEBS Lett. 2009, 583:394-400.
25. Nishimoto Y., Ito D., Yagi T., et al. Characterization of alternative isoforms and inclusion body of the TAR DNA-binding protein-43. J. Biol. Chem. 2010, 285:608-619.
26. Buratti E., Baralle F.E. Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9. J. Biol. Chem. 2001, 276:36337-36343.
27. Wils H., Kleinberger G., Janssens J., et al. TDP-43 transgenic mice develop spastic paralysis and neuronal inclusions characteristic of ALS and frontotemporal lobar degeneration. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:3858-3863.
28. Igaz L.M., Kwong L.K., Chen-Plotkin A., et al. Expression of TDP-43 C-terminal Fragments in Vitro Recapitulates Pathological Features of TDP-43 Proteinopathies. J. Biol. Chem. 2009, 284:8516-8524.
29. Hasegawa M., Nonaka T., Tsuji H., et al. Molecular Dissection of TDP-43 Proteinopathies. J. Mol. Neurosci. 2011, 45:480-485.
30. Collinge J., Sidle K.C., Meads J., et al. Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD. Nature 1996, 383:685-690.
31. Miake H., Mizusawa H., Iwatsubo T., et al. Biochemical characterization of the core structure of alpha-synuclein filaments. J. Biol. Chem. 2002, 277:19213-19219.
32. Novak M., Kabat J., Wischik C.M. Molecular characterization of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament. EMBO J. 1993, 12:365-370.