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Transthyretin and familial amyloidotic polyneuropathy: Recent progress in understanding the molecular mechanism of neurodegeneration

Citation

Hou, X and Aguilar, MI and Small, DH, Transthyretin and familial amyloidotic polyneuropathy: Recent progress in understanding the molecular mechanism of neurodegeneration, The F E B S Journal, 274, (7) pp. 1637-1650. ISSN 1742-464X (2007) [Refereed Article]

DOI: doi:10.1111/j.1742-4658.2007.05712.x

Abstract

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.

Item Details

Item Type:Refereed Article
Research Division:Medical and Health Sciences
Research Group:Neurosciences
Research Field:Neurosciences not elsewhere classified
Objective Division:Health
Objective Group:Clinical Health (Organs, Diseases and Abnormal Conditions)
Objective Field:Neurodegenerative Disorders Related to Ageing
Author:Small, DH (Professor David Small)
ID Code:61393
Year Published:2007
Web of Science® Times Cited:104
Deposited By:Menzies Institute for Medical Research
Deposited On:2010-03-03
Last Modified:2010-06-04
Downloads:0

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