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Titolo:
Capture of a dimeric intermediate during transthyretin amyloid formation
Autore:
Olofsson, A; Ippel, HJ; Baranov, V; Horstedt, P; Wijmenga, S; Lundgren, E;
Indirizzi:
Umea Univ, Dept Cell & Mol Biol, S-90187 Umea, Sweden Umea Univ Umea Sweden S-90187 Dept Cell & Mol Biol, S-90187 Umea, Sweden Umea Univ, Dept Immunol, S-90187 Umea, Sweden Umea Univ Umea Sweden S-90187 a Univ, Dept Immunol, S-90187 Umea, Sweden Umea Univ, Dept Med Biosci, S-90187 Umea, Sweden Umea Univ Umea Sweden S-90187 niv, Dept Med Biosci, S-90187 Umea, Sweden Umea Univ, Dept Med Biophys, S-90187 Umea, Sweden Umea Univ Umea Sweden S-90187 iv, Dept Med Biophys, S-90187 Umea, Sweden
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 43, volume: 276, anno: 2001,
pagine: 39592 - 39599
SICI:
0021-9258(20011026)276:43<39592:COADID>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN TRANSTHYRETIN; FIBRIL FORMATION; WILD-TYPE; DENATURATION; MUTATION; DISEASE; PROTOFILAMENTS; VARIANTS; INVITRO; PACKING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Lundgren, E Umea Univ, Dept Cell & Mol Biol, S-90187 Umea, Sweden Umea Univ Umea Sweden S-90187 Mol Biol, S-90187 Umea, Sweden
Citazione:
A. Olofsson et al., "Capture of a dimeric intermediate during transthyretin amyloid formation", J BIOL CHEM, 276(43), 2001, pp. 39592-39599

Abstract

Point mutations in the human plasma protein transthyretin are associated with the neurological disorder familial amyloidosis with polyneuropathy type1. The disease is characterized by amyloid fibril deposits causing damage at the site of deposition. Substitution of two amino acids in the hydrophobic core of transthyretin lead to a mutant that was very prone to form amyloid. In addition, this mutant has also been shown to induce a toxic responseon a neuroblastoma cell line. Renaturation of the transthyretin mutant at low temperature facilitated the isolation of an amyloid-forming intermediate state having the apparent size of a dimer. Increasing the temperature effectively enhanced the rate of interconversion from a partly denatured protein to mature amyloid. Using circular dichroism the beta -sheet content of the formed mature fibrils was significantly lower than that of the native fold of transthyretin. Morphology studies using electron microscopy also indicated a temperature-dependent transformation from amorphous aggregates toward mature amyloid fibrils. In addition, 1-anilino-S-naphtalenesulfonate fluorescence studies suggested the loss of the thyroxin-binding channel withinboth the isolated intermediate and the mature fibrils.

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Documento generato il 29/03/20 alle ore 09:29:49