Hostname: page-component-586b7cd67f-rdxmf Total loading time: 0 Render date: 2024-11-22T22:31:11.599Z Has data issue: false hasContentIssue false

Hereditary transthyretin amyloidosis: molecular basis and therapeutical strategies

Published online by Cambridge University Press:  13 February 2004

Maria João Mascarenhas Saraiva
Affiliation:
Amyloid Unit, Institute for Cellular and Molecular Biology and Instituto de Ciências Biomédicas Abel Salazar, University of Porto, R. Campo Alegre, 823. 4150-180 Porto, Portugal.

Abstract

Transthyretin (TTR) is a transport protein for thyroid hormones and vitamin A and might have an important role in the nervous system. However, TTR can undergo a conformational change and form amyloid fibrils, in both acquired and hereditary forms of systemic amyloidosis. More than 80 TTR mutations have been associated with autosomal dominant amyloidosis, usually presenting with peripheral and autonomic neuropathy and/or cardiomyopathy. Major areas of research in TTR amyloidosis include: molecular mechanisms leading to fibril formation; mechanisms of fibril-induced cell death; modulators of phenotypic expression of the disease; and therapeutic strategies.

Type
Review Article
Copyright
© Cambridge University Press 2002

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)