A new cellular model of pathological TDP-43: The neurotoxicity of stably expressed CTF25 of TDP-43 depends on the proteasome

Neuroscience

Volumn 281, Issue , 2014, Pages 88-98

  Liu, Y ^a   Duan, W ^a,b,c   Guo, Y ^a,b,c   Li, Z ^a,b,c   Han, H ^a   Zhang, S ^a   Yuan, P ^a   Li, C ^a,b,c  

^a HEBEI MEDICAL UNIVERSITY   (China)

^b Institute of Cardiocerebrovascular Disease   (China)

^c Neurological Laboratory of Hebei Province   (China)

Author keywords

Amyotrophic lateral sclerosis; TDP 43; The CTF25 of TDP 43

Indexed keywords

PROTEASOME; TAR DNA BINDING PROTEIN; DNA BINDING PROTEIN; TDP-43 PROTEIN, HUMAN;

ARTICLE; AUTOPHAGY; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ELECTRON MICROSCOPY; ENZYME ACTIVITY; FLOW CYTOMETRY; LIPID PEROXIDATION; MITOCHONDRION SWELLING; NEUROPATHOLOGY; NEUROTOXICITY; OXIDATIVE STRESS; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN FUNCTION; SIGNAL TRANSDUCTION; STABLE EXPRESSION; AMYOTROPHIC LATERAL SCLEROSIS; CELL LINE; HUMAN; METABOLISM;

AMYOTROPHIC LATERAL SCLEROSIS; CELL LINE; DNA-BINDING PROTEINS; HUMANS; PROTEASOME ENDOPEPTIDASE COMPLEX;

EID: 84908070723     PISSN: 03064522     EISSN: 18737544     Source Type: Journal    
DOI: 10.1016/j.neuroscience.2014.09.043     Document Type: Article

References (36)

1. Arai T., Hasegawa M., Akiyama H., Ikeda K., Nonaka T., Mori H., Mann D., Tsuchiya K., Yoshida M., Hashizume Y., 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.
2. 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.
3. Blokhuis A.M., Groen E.J., Koppers M., van den Berg L.H., Pasterkamp R.J. Protein aggregation in amyotrophic lateral sclerosis. Acta Neuropathol 2013, 125(6):777-794.
4. Bose J.K., Wang I.F., Hung L., Tarn W.Y., Shen C.K. TDP-43 overexpression enhances exon 7 inclusion during the survival of motor neuron pre-mRNA splicing. J Biol Chem 2008, 283:28852-28859.
5. Bose J.K., Huang C.C., Shen C.K. Regulation of autophagy by neuropathological protein TDP-43. J Biol Chem 2011, 286(52):44441-44448.
6. Brady O.A., Meng P., Zheng Y., Mao Y., Hu F. Regulation of TDP-43 aggregation by phosphorylation and p62/SQSTM1. J Neurochem 2011, 116(2):248-259.
7. Caccamo A., Majumder S., Deng J.J., Bai Y., Thornton F.B., Oddo S. Rapamycin rescues TDP-43 mislocalization and the associated low molecular mass neurofilament instability. J Biol Chem 2009, 284(40):27416-27424.
8. Caccamo A., Majumder S., Oddo S. Cognitive decline typical of frontotemporal lobar degeneration in transgenic mice expressing the 25-kDa C-terminal fragment of TDP-43. Am J Pathol 2012, 180(1):293-302.
9. Caccamo A., Medina D.X., Oddo S. Glucocorticoids exacerbate cognitive deficits in TD-F25 transgenic mice via a glutathione-mediated mechanism: implications for aging, stress and TDP-43 proteinopathies. J Neurosci 2013, 33(3):906-913.
10. Cashman N.R., Durham H.D., Blusztajn J.K., Oda K., Tabira T., Shaw I.T., Dahrouge S., Antel J.P. Neuroblastomaspinal cord (NSC) hybrid cell lines resemble developing motor neurons. Dev Dyn 1992, 194:209-221.
11. Cecarini V., Bonfili L., Cuccioloni M., Mozzicafreddo M., Rossi G., Keller J.N., Angeletti M., Eleuteri A.M. Wild type and mutant amyloid precursor proteins influence downstream effects of proteasome and autophagy inhibition. Biochim Biophys Acta 2014, 1842(2):127-134.
12. Chen S., Zhang X., Song L., Le W. Autophagy dysregulation in amyotrophic lateral sclerosis. Brain Pathol 2012 Jan, 22(1):110-116.
13. Cherra S.J., Dagda R.K., Chu C.T. Review: autophagy and neurodegeneration: survival at a cost?. Neuropathol Appl Neurobiol 2010, 36(2):125-132.
14. Dayton R.D., Gitcho M.A., Orchard E.A., Wilson J.D., Wang D.B., Cain C.D., Johnson J.A., Zhang Y.J., Petrucelli L., Mathis J.M., Klein R.L. Selective forelimb impairment in rats expressing a pathological TDP-43 25kDa C-terminal fragment to mimic amyotrophic lateral sclerosis. Mol Ther 2013 Jul, 21(7):1324-1334.
15. Deretic V. Autophagy in infection. Curr Opin Cell Biol 2010, 22(2):252-262.
16. Duan W., Li X., Shi J., Guo Y., Li Z., Li C. Mutant TDP-43 induces oxidative injury in motor neuron-like cell. Neuroscience 2010, 169:1621-1629.
17. García M.L., Fernández A., Solas M.T. Mitochondria, motor neurons and aging. J Neurol Sci 2013, 330(1-2):18-26.
18. Hershko A., Ciechanover A. The ubiquitin system. Annu Rev Biochem 1998, 67:425-479.
19. Hong K., Li Y., Duan W., Guo Y., Jiang H., Li W., Li C. Full-length TDP-43 and its C-terminal fragments activate mitophagy in NSC34 cell line. Neurosci Lett 2012, 530(2):144-149.
20. Igaz L.M., Kwong L.K., Chen-Plotkin A., Winton M.J., Unger T.L., Xu Y., Neumann M., Trojanowski J.Q., Lee V.M. Expression of TDP-43 C-terminal fragments in vitro recapitulates pathological features of TDP-43 proteinopathies. J Biol Chem 2009, 284:8516-8524.
21. Iguchi Y., Katsuno M., Niwa J., Yamada S., Sone J., Waza M., Adachi H., Tanaka F., Nagata K., Arimura N., Watanabe T., Kaibuchi K., Sobue G. TDP-43 depletion induces neuronal cell damage through dysregulation of Rho family GTPases. J Biol Chem 2009, 284:22059-22066.
22. Jara J.H., Frank D.D., Ozdinler P.H. Could dysregulation of UPS be a common underlying mechanism for cancer and neurodegeneration? Lessons from UCHL1. Cell Biochem Biophys 2013, 67(1):45-53.
23. Li Y.R., King O.D., Shorter J., Gitler A.D. Stressgranules as crucibles of ALS pathogenesis. J Cell Biol 2013, 201(3):361-372.
24. Mizushima N., Levine B., Cuervo A.M., Klionsky D.J. Autophagy fights disease through cellular self-digestion. Nature 2008, 451(7182):1069-1075.
25. Neumann M., Sampathu D.M., Kwong L.K., Truax A.C., Micsenyi M.C., Chou T.T., Bruce J., Schuck T., Grossman M., Clark C.M., McCluskey L.F., Miller B.L., Masliah E., Mackenzie I.R., Feldman H., Feiden W., Kretzschmar H.A., Trojanowski J.Q., Lee V.M. Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 2006, 314:130-133.
26. Pratt A.J., Getzoff E.D., Perry J.J. Amyotrophic lateral sclerosis: update and new developments. Degener Neurol Neuromuscul Dis 2012, 2:1-14.
27. Sarkar S., Korolchuk V.I., Renna M., Imarisio S., Fleming A., Williams A., Garcia-Arencibia M., Rose C., Luo S., Underwood B.R., Kroemer G., O'Kane C.J., Rubinsztein D.C. Complex inhibitory effects of nitric oxide on autophagy. Mol Cell 2011, 43(1):19-32.
28. Sreedharan J., Blair I.P., Tripathi V.B., Hu X., Vance C., Rogelj B., Ackerley S., Durnall J.C., Williams K.L., Buratti E., Baralle F., de Belleroche J., Mitchell J.D., Leigh P.N., Al-Chalabi A., Miller C.C., Nicholson G., Shaw C.E. TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis. Science 2008, 319:1668-1672.
29. Tashiro Y., Urushitani M., Inoue H., Koike M., Uchiyama Y., Komatsu M., Tanaka K., Yamazaki M., Abe M., Misawa H., Sakimura K., Ito H., Takahashi R. Motor neuron-specific disruption of proteasomes, but not autophagy, replicates amyotrophic lateral sclerosis. J Biol Chem 2012, 287(51):42984-42994.
30. Ułamek-Kozioł M., Furmaga-Jabłońska W., Januszewski S., Brzozowska J., Sciślewska M., Jabłoński M., Pluta R. Neuronal autophagy: self-eating or self-cannibalism in Alzheimer's disease. Neurochem Res 2013, 38(9):1769-1773.
31. Urushitani M., Sato T., Bamba H., Hisa Y., Tooyama I. Synergistic effect between proteasome and autophagosome in the clearance of polyubiquitinated TDP-43. J Neurosci Res 2010, 88(4):784-797.
32. Wang X., Fan H., Ying Z., Li B., Wang H., Wang G. Degradation of TDP-43 and its pathogenic form by autophagy and the ubiquitin-proteasome system. Neurosci Lett 2010, 469(1):112-116.
33. Wang I.F., Guo B.S., Liu Y.C., Wu C.C., Yang C.H., Tsai K.J., Shen C.K. Autophagy activators rescue and alleviate pathogenesis of a mouse model with proteinopathies of the TAR DNA-binding protein 43. Proc Natl Acad Sci U S A 2012, 109(37):15024-15029.
34. Wils H., Kleinberger G., Janssens J., Pereson S., Joris G., Cuijt I., Smits V., Groote C.C., Van Broeckhoven C., Kumar-Singh S. TDP-43 transgenic mice develop spastic paralysis and neuronal inclusions characteristic of ALS and frontotemporal lobar degeneration. Proc. Natl Acad. Sci. USA 2010, 107(8):3858-3863.
35. Wu L.S., Cheng W.C., Hou S.C., Yan Y.T., Jiang S.T., Shen C.K. TDP-43, a neuro-pathosignature factor, is essential for early mouse embryogenesis. Genesis 2010, 48:56-62.
36. Zhang Y.J., Xu Y.F., Cook C., Gendron T.F., Roettges P., Link C.D., Lin W.L., Tong J., Castanedes-Casey M., Ash P., Gass J., Rangachari V., Buratti E., Baralle F., Golde T.E., Dickson D.W., Petrucelli L. Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity. Proc Natl Acad Sci U S A 2009, 106:7607-7612.