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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 Small
Familial 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 Journal

Volume

274

Issue

7

Pagination

1637-1650

ISSN

1742-464X

Department/School

Menzies Institute for Medical Research

Publisher

Wiley-Blackwell Publishing Ltd.

Place of publication

United Kingdom

Repository Status

  • Restricted

Socio-economic Objectives

Clinical health not elsewhere classified

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