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Transthyretin and familial amyloidotic polyneuropathy: Recent progress in understanding the molecular mechanism of neurodegeneration
journal contribution
posted on 2023-05-17, 01:40 authored by Hou, X, Aguilar, MI, David SmallDavid SmallFamilial amyloidotic polyneuropathy (FAP) is an inherited autosomal dominant disease that is commonly caused by accumulation of deposits of transthyretin (TTR) amyloid around peripheral nerves. The only effective treatment for FAP is liver transplantation. However, recent studies on TTR aggregation provide clues to the mechanism of the molecular pathogenesis of FAP and suggest new avenues for therapeutic intervention. It is increasingly recognized that there are common features of a number of protein-misfolding diseases that can lead to neurodegeneration. As for other amyloidogenic proteins, the most toxic forms of aggregated TTR are likely to be the low-molecular-mass diffusible species, and there is increasing evidence that this toxicity is mediated by disturbances in calcium homeostasis. This article reviews what is already known about the mechanism of TTR aggregation in FAP and describes how recent discoveries in other areas of amyloid research, particularly Alzheimer's disease, provide clues to the molecular pathogenesis of FAP.
History
Publication title
The F E B S JournalVolume
274Issue
7Pagination
1637-1650ISSN
1742-464XDepartment/School
Menzies Institute for Medical ResearchPublisher
Wiley-Blackwell Publishing Ltd.Place of publication
United KingdomRepository Status
- Restricted