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Titolo:
Transthyretin amyloidosis: a tale of weak interactions
Autore:
Saraiva, MJM;
Indirizzi:
Univ Porto, Inst Mol & Cellular Biol, Amyloid Unit, P-4150 Porto, PortugalUniv Porto Porto Portugal P-4150 l, Amyloid Unit, P-4150 Porto, Portugal Univ Porto, Inst Ciencias Biomed, P-4150 Porto, Portugal Univ Porto Porto Portugal P-4150 Ciencias Biomed, P-4150 Porto, Portugal
Titolo Testata:
FEBS LETTERS
fascicolo: 2-3, volume: 498, anno: 2001,
pagine: 201 - 203
SICI:
0014-5793(20010608)498:2-3<201:TAATOW>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
VARIANT; 4'-IODO-4'-DEOXYDOXORUBICIN; FIBRILS;
Keywords:
transthyretin; amyloid; familial amyloidotic polyneuropathy; thyroxine; iododoxorubicin;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
19
Recensione:
Indirizzi per estratti:
Indirizzo: Saraiva, MJM Univ Porto, Inst Mol & Cellular Biol, Amyloid Unit, R Campo Alegre 823, P-4150 Porto, Portugal Univ Porto R Campo Alegre 823 Porto Portugal P-4150 Portugal
Citazione:
M.J.M. Saraiva, "Transthyretin amyloidosis: a tale of weak interactions", FEBS LETTER, 498(2-3), 2001, pp. 201-203

Abstract

Over 70 transthyretin (TTR) mutations have been associated with hereditaryamyloidoses, which are all autosomal dominant disorders with adult age of onset. TTR is the main constituent of amyloid that deposits preferentially in peripheral nerve giving rise to familial amyloid polyneuropathy (FAP), or in the heart leading to familial amyloid cardiomyopathy. Since the beginning of this decade the central question of these types of amyloidoses has been why TTR is an amyloidogenic protein with clinically heterogeneous pathogenic consequences. As a result of amino acid substitutions, conformationalchanges occur in the molecule, leading to weaker subunit interactions of the tetrameric structure as revealed by X-ray studies of some amyloidogenic mutants. Modified soluble tetramers exposing cryptic epitopes seem to circulate in FAP patients as evidenced by antibody probes recognizing specifically TTR amyloid fibrils, but what triggers dissociation into monomeric and oligomeric intermediates of amyloid fibrils is largely unknown. Avoiding tetramer dissociation and disrupting amyloid fibrils are possible avenues of therapeutic intervention based on current molecular knowledge of TTR amyloidogenesis and fibril structure. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B,V, Ail rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/03/20 alle ore 23:29:11