Abstract
The subject of the review is on hereditary transthyretin (TTR) amyloidosis which is a genetically transmitted disease that results from a mutation in the gene encoding the plasma TTR protein. TTR is a transport protein for thyroid hormones and vitamin A and is predominantly synthesised in the liver. Although originally regarded as a rare disease, it is now becoming clear that many kindreds exist worldwide. Current knowledge and hypotheses on the biology of TTR, mechanisms of TTR amyloid fibril formation, phenotypic consequences TTR amyloid deposition and pre-clinical models of the disease will be discussed.
Keywords: Amyloidosis, cytotoxicity, fibrillogenesis, familial amyloidotic polyneuropathy, heat shock response, transthyretin (TTR), neurodegenerative diseases, hereditary transthyretin (TTR), plasma TTR protein, hypotheses
Current Medicinal Chemistry
Title:Transthyretin Deposition in Familial Amyloidotic Polyneuropathy
Volume: 19 Issue: 15
Author(s): M. J. Saraiva, J. Magalhaes, N. Ferreira, M. R. Almeida
Affiliation:
Keywords: Amyloidosis, cytotoxicity, fibrillogenesis, familial amyloidotic polyneuropathy, heat shock response, transthyretin (TTR), neurodegenerative diseases, hereditary transthyretin (TTR), plasma TTR protein, hypotheses
Abstract: The subject of the review is on hereditary transthyretin (TTR) amyloidosis which is a genetically transmitted disease that results from a mutation in the gene encoding the plasma TTR protein. TTR is a transport protein for thyroid hormones and vitamin A and is predominantly synthesised in the liver. Although originally regarded as a rare disease, it is now becoming clear that many kindreds exist worldwide. Current knowledge and hypotheses on the biology of TTR, mechanisms of TTR amyloid fibril formation, phenotypic consequences TTR amyloid deposition and pre-clinical models of the disease will be discussed.
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Cite this article as:
M. J. Saraiva, J. Magalhaes, N. Ferreira, M. R. Almeida , Transthyretin Deposition in Familial Amyloidotic Polyneuropathy, Current Medicinal Chemistry 2012; 19 (15) . https://dx.doi.org/10.2174/092986712800269236
DOI https://dx.doi.org/10.2174/092986712800269236 |
Print ISSN 0929-8673 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-533X |
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