Seishin Shinkeigaku Zasshi. 2011;113(6):574-83.

[A new dementia group caused by TDP-43 abnormality].

Seishin shinkeigaku zasshi = Psychiatria et neurologia Japonica

[Article in Japanese]
Tetsuaki Arai, Masato Hosokawa, Masato Hasegawa, Haruhiko Akiyama, Takashi Asada

PMID: 21815469

Abstract

The TAR DNA-binding protein Mr 43 kDa (TDP-43) is a major component of the tau-negative and ubiquitin-positive inclusions that characterize amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration, which is now referred to as FTLD-TDP. Concurrent TDP-43 pathology has been reported in a variety of other neurodegenerative disorders such as Alzheimer's disease, forming a group of TDP-43 proteinopathies. Accumulated TDP-43 is characterized by phosphorylation and fragmentation. There is a close relationship between the pathological subtypes of FTLD-TDP and the immunoblot pattern of the C-terminal fragments of phosphorylated TDP-43. These results suggest that proteolytic processing of accumulated TDP-43 may play an important role in the pathological process. Understanding the mechanism of phosphorylation and truncation of TDP-43, and aggregate formation, may be crucial to clarifying the pathogenesis of TDP-43 proteinopathy and for developing useful therapies.

Substances

• DNA-Binding Proteins

MeSH terms

• DNA-Binding Proteins / metabolism
• Humans
• TDP-43 Proteinopathies / genetics
• TDP-43 Proteinopathies / metabolism

Publication Types

• English Abstract
• Journal Article
• Review