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Titolo:
High-resolution ultrastructure of amyloid fibrils in familiar amyloid polyneuropathy
Autore:
Katsuragi, S; Miyakawa, T; Ando, Y; Terazaki, H;
Indirizzi:
Natl Kikuchi Hosp, Div Clin Res, Koshi, Kumamoto 8611116, Japan Natl Kikuchi Hosp Koshi Kumamoto Japan 8611116 i, Kumamoto 8611116, Japan Kumamoto Univ, Sch Med, Dept Internal Med 1, Kumamoto 8600811, Japan Kumamoto Univ Kumamoto Japan 8600811 rnal Med 1, Kumamoto 8600811, Japan Kumamoto Univ, Sch Med, Dept Neuropsychiat, Kumamoto 8600811, Japan Kumamoto Univ Kumamoto Japan 8600811 ropsychiat, Kumamoto 8600811, Japan Kumamoto Univ, Sch Med, Dept Lab Med, Kumamoto 8600811, Japan Kumamoto Univ Kumamoto Japan 8600811 pt Lab Med, Kumamoto 8600811, Japan
Titolo Testata:
JOURNAL OF ELECTRON MICROSCOPY
fascicolo: 4, volume: 49, anno: 2000,
pagine: 579 - 581
SICI:
0022-0744(2000)49:4<579:HUOAFI>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Keywords:
amyloid fibril; amyloid polyneuropathy; electron microscopy; negative stain; transthyretin; alternating twist structure;
Tipo documento:
Letter
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
9
Recensione:
Indirizzi per estratti:
Indirizzo: Katsuragi, S Natl Kikuchi Hosp, Div Clin Res, Koshi, Kumamoto 8611116, Japan Natl Kikuchi Hosp Koshi Kumamoto Japan 8611116 611116, Japan
Citazione:
S. Katsuragi et al., "High-resolution ultrastructure of amyloid fibrils in familiar amyloid polyneuropathy", J ELEC MICR, 49(4), 2000, pp. 579-581

Abstract

The ultrastructure of amyloid fibrils in familial amyloid polyneuropathy (FAP) was clearly demonstrated. Amyloid of three patients with FAP caused bythe point mutation of the 30th amino acid of transthyretin (ATTR Val30Met)and one patient with FAP caused by two point mutations of the 30th and 104th amino acid of transthyretin (ATTR Val30Met/Arg104Cys) were partially isolated, stained negatively and examined with an electron microscope. Amyloidfibrils of both types were composed of two protofilaments and twisted at 180 degrees to the right and left alternately with a periodicity of 125-135 nm. This is the first report demonstrating such unique alternating twist structure of amyloid fibrils. There were no ultrastructural differences between the fibrils caused by the ATTR Val30Met and ATTR Val30Met/Arg104His; therefore, it is suggested that the point mutation of the 30th amino acid of transthyretin might play an important role in the formation of amyloid fibrils. Further biochemical study on the mechanism of this alternating twist formation should be undertaken.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/10/20 alle ore 03:38:20