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  • PMID: 24896092 was deleted because it is a duplicate of PMID: 25482120
Nucleus. 2014 Jul-Aug;5(4):311-7. doi: 10.4161/nucl.29404.

Pathology and function of nuclear amyloid. Protein homeostasis matters.

Author information

1
a IUF - Leibniz Research Institute for Environmental Medicine at Heinrich-Heine-University; Duesseldorf, Germany.

Abstract

In aging societies increasing cases of neurodegenerative protein deposit diseases urge for the identification of the underlying mechanisms. Expectations are that in 2050 the percentage of population over age 60 is 42% in Japan, 34% in China, and 27% in the US. The cell nucleus is a major target of amyloid-like protein fibrillation in a variety of disorders that are characterized by widespread aggregation of proteins with instable homopolymeric amino acid repeats, ubiquitin, and other proteinaceous components. Additionally, accumulation of insoluble, SDS-resistant proteins has been identified as an intrinsic property of organismal aging. This review collects current knowledge about the composition and function of insoluble, nuclear protein inclusions from the protein homeostasis perspective. It discusses the occurrence and role of nuclear amyloid in the diseased as well as the healthy cell. Features of nuclear inclusions such as protein composition and locally active protein degradation may predict neural fitness and survival in a variety of health or disease settings.

KEYWORDS:

Congo red; Huntington disease; aging; amyloid; fibrillation; neurodegeneration; nuclear inclusions; nucleus; polyQ; prion disease; protein aggregation

PMID:
25482120
PMCID:
PMC4152345
DOI:
10.4161/nucl.29404
[Indexed for MEDLINE]

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