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Titolo:
Transmission of mouse senile amyloidosis
Autore:
Xing, YM; Nakamura, A; Chiba, T; Kogishi, K; Matsushita, T; Li, F; Guo, ZJ; Hosokawa, M; Mori, M; Higuchi, K;
Indirizzi:
Shinshu Univ, Sch Med, Res Ctr Aging & Adaptat, Dept Aging Angiol, Matsumoto, Nagano 3908621, Japan Shinshu Univ Matsumoto Nagano Japan 3908621 sumoto, Nagano 3908621, Japan Kyoto Univ, Inst Frontier Med Sci, Kyoto, Japan Kyoto Univ Kyoto JapanKyoto Univ, Inst Frontier Med Sci, Kyoto, Japan
Titolo Testata:
LABORATORY INVESTIGATION
fascicolo: 4, volume: 81, anno: 2001,
pagine: 493 - 499
SICI:
0023-6837(200104)81:4<493:TOMSA>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
EXTENSION IN-VITRO; APOA-II; SPONGIFORM ENCEPHALOPATHIES; ENHANCING FACTOR; PRION DISEASES; A AMYLOIDOSIS; YEAST PRION; MICE; SENESCENCE; PROTEIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Higuchi, K Shinshu Univ, Sch Med, Res Ctr Aging & Adaptat, Dept Aging Angiol, Asahi 3-1-1, Matsumoto, Nagano 3908621, Japan Shinshu Univ Asahi 3-1-1 Matsumoto Nagano Japan 3908621 , Japan
Citazione:
Y.M. Xing et al., "Transmission of mouse senile amyloidosis", LAB INV, 81(4), 2001, pp. 493-499

Abstract

In mouse senile amyloidosis, apolipoprotein A-II polymerizes into amyloid fibrils (AApoAII) and deposits systemically. Peripheral injection of AApoAII fibrils into young mice induces systemic amyloidosis (Higuchi et at, 1998). We isolated AApoAII amyloid fibrils from the livers of old R1.P1-Apoa2(c) mice and injected them with feeding needles into the stomachs of young R1. P1-Apoa2(c) mice for 5 consecutive days. After 2 months, all mice had AApoAII deposits in the lamina propria of the small intestine. Amyloid deposition extended to the tongue, stomach, heart, and liver at 3 and 4 months after feeding. AApoAII suspended in drinking water also induced amyloidosis. Amyloid deposition was induced in young mice reared in the same cage for 3 months with old mice who had severe amyloidosis. Detection of AApoAII in feces of old mice and induction of amyloidosis by the injection of an amyloid fraction of feces suggested the propagation of amyloidosis by eating feces. Here, we substantiate the transmissibility of AApoAII amyloidosis and present a possible pathogenesis of amyloidosis, ie, oral transmission of amyloidfibril conformation, where we assert that exogenous amyloid fibrils act astemplates and change the conformation of endogenous amyloid protein to polymerize into amyloid fibrils.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 23:00:45