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Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis
M. Neumann ,
D. M. Sampathu ,
L. K. Kwong ,
A. C. Truax ,
M. C. Micsenyi ,
T. T. Chou ,
J. Bruce ,
T. Schuck ,
M. Grossman ,
C. M. Clark ,
L. F. McCluskey ,
B. L. Miller ,
E. Masliah ,
I. R. Mackenzie ,
H. Feldman ,
W. Feiden ,
H. A. Kretzschmar ,
J. Q. Trojanowski ,
V. M.-Y. Lee
October 06 2006
October 06 2006
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Abstract
Ubiquitin-positive, tau- and alpha-synuclein-negative inclusions are hallmarks of
frontotemporal lobar degeneration with ubiquitin-positive inclusions and amyotrophic
lateral sclerosis. Although the identity of the ubiquitinated protein specific to
either disorder was unknown, we showed that TDP-43 is the major disease protein in
both disorders. Pathologic TDP-43 was hyper-phosphorylated, ubiquitinated, and cleaved
to generate C-terminal fragments and was recovered only from affected central nervous
system regions, including hippocampus, neocortex, and spinal cord. TDP-43 represents
the common pathologic substrate linking these neurodegenerative disorders.