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Titolo:
Analysis of transthyretin amyloid fibrils from vitreous samples in familial amyloidotic polyneuropathy (Val30Met)
Autore:
Ando, Y; Ando, E; Ohlsson, PI; Olofsson, A; Sandgren, O; Suhr, O; Terazaki, H; Obayashi, K; Lundgren, E; Ando, M; Negi, A;
Indirizzi:
Kumamoto Univ, Sch Med, Dept Internal Med 1, Kumamoto 860, Japan Kumamoto Univ Kumamoto Japan 860 ept Internal Med 1, Kumamoto 860, Japan Umea Univ, Dept Internal Med, S-90185 Umea, Sweden Umea Univ Umea SwedenS-90185 v, Dept Internal Med, S-90185 Umea, Sweden Umea Univ, Dept Med Biochem & Biophys, S-90187 Umea, Sweden Umea Univ Umea Sweden S-90187 ed Biochem & Biophys, S-90187 Umea, Sweden Umea Univ, Dept Appl Cell & Mol Biol, S-90187 Umea, Sweden Umea Univ Umea Sweden S-90187 Appl Cell & Mol Biol, S-90187 Umea, Sweden Umea Univ, Dept Ophthalmol, S-90187 Umea, Sweden Umea Univ Umea Sweden S-90187 niv, Dept Ophthalmol, S-90187 Umea, Sweden Kumamoto Univ, Sch Med, Dept Ophthalmol, Kumamoto 860, Japan Kumamoto Univ Kumamoto Japan 860 d, Dept Ophthalmol, Kumamoto 860, Japan
Titolo Testata:
AMYLOID-INTERNATIONAL JOURNAL OF EXPERIMENTAL AND CLINICAL INVESTIGATION
fascicolo: 2, volume: 6, anno: 1999,
pagine: 119 - 123
SICI:
1350-6129(199906)6:2<119:AOTAFF>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
INDIVIDUALS; VARIANT;
Keywords:
FAP; transthyretin; amyloid; amyloidosis; mass spectrometry; variant TTR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
10
Recensione:
Indirizzi per estratti:
Indirizzo: Ando, Y Kumamoto Univ, Sch Med, Dept Internal Med 1, 1-1-1 Honjo, Kumamoto860, Japan Kumamoto Univ 1-1-1 Honjo Kumamoto Japan 860 Kumamoto 860, Japan
Citazione:
Y. Ando et al., "Analysis of transthyretin amyloid fibrils from vitreous samples in familial amyloidotic polyneuropathy (Val30Met)", AMYLOID, 6(2), 1999, pp. 119-123

Abstract

The aim of the present study was to analyze the forms of wild type and mutated monomeric transthyretin (Val30Met) in the amyloid fibrils of patients with familial amyloidotic polyneuropathy by electrospray ionization mass spectrometry (ESI-MS). The solubility of amyloid fibrils from the vitrectomized samples was examined to determine the appropriate solution for ESI-MS. ESI-MS analysis revealed that heterozygotic Val30Met amyloid fibrils contained 14.6 +/- 7.5 % normal TTR. In all samples, 3 different types of variant ATTR could be identified: Full length ATTR, and -57, and -157 (or 156) Da from ATTR Val30Met were found. The two peaks showing -57, and -157 (or 156) Da from ATTR Val30Met corresponded to the -Gly, and -Gly-Pro sequences of ATTR Val30Met from the N-terminal. The results illustrate the heterogeneity of ATTR amyloid deposits and thismethod may be very useful for analyzing amyloid fibrils in ATTR related amyloidosis.

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Documento generato il 10/07/20 alle ore 00:02:14