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TDP-43 Proteinopathies: Neurodegenerative Protein Misfolding Diseases without AmyloidosisKwong L.K.a · Uryu K.a · Trojanowski J.Q.a, b · Lee V.M.-Y.a, b
aCenter for Neurodegenerative Disease Research, Department of Pathology and Laboratory Medicine, and bInstitute on Aging, University of Pennsylvania School of Medicine, Philadelphia, Pa., USA Corresponding Author
Virginia M.-Y. Lee, PhD, Center for Neurodegenerative Disease Research
Department of Pathology and Laboratory Medicine
University of Pennsylvania School of Medicine, HUP, Maloney 3rd Floor
36th and Spruce Streets, Philadelphia, PA 19104-4283 (USA)
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In this review, we summarize recent advances in understanding frontotemporal lobar degeneration (FTLD), amyotrophic lateral sclerosis (ALS) and related neurodegenerative disorders that are collectively known as TDP-43 proteinopathies, since transactive response DNA-binding protein 43 (TDP-43) was recently shown to be the major component of the ubiquitinated inclusions that are their pathological hallmarks. TDP-43 proteinopathies are distinct from most other neurodegenerative disorders because TDP-43 inclusions are not amyloid deposits. Besides TDP-43-positive inclusions, both sporadic and familial forms of FTLD and ALS have the pathologic TDP-43 signature of abnormal hyperphosphorylation, ubiquitination and C-terminal fragments in affected brain and spinal cord, suggesting that they share a common mechanism of pathogenesis. Thus, these findings support the concept that FTLD and ALS represent a clinicopathologic spectrum of one disease, that is, TDP-43 proteinopathy.
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