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Titolo:
Advanced glycation end product in familial amyloidotic polyneuropathy (FAP)
Autore:
Nyhlin, N; Ando, Y; Nagai, R; Suhr, O; El Sahly, M; Terazaki, H; Yamashita, S; Ando, M; Horiuchi, S;
Indirizzi:
Kumamoto Univ, Sch Med, Dept Internal Med 1, Kumamoto 860088, Japan Kumamoto Univ Kumamoto Japan 860088 ternal Med 1, Kumamoto 860088, Japan Umea Univ Hosp, Dept Med, Gastroenterol & Hepatol Sect, S-90185 Umea, Sweden Umea Univ Hosp Umea Sweden S-90185 & Hepatol Sect, S-90185 Umea, Sweden Kumamoto Univ, Sch Med, Dept Biochem, Kumamoto 860, Japan Kumamoto Univ Kumamoto Japan 860 Med, Dept Biochem, Kumamoto 860, Japan
Titolo Testata:
JOURNAL OF INTERNAL MEDICINE
fascicolo: 4, volume: 247, anno: 2000,
pagine: 485 - 492
SICI:
0954-6820(200004)247:4<485:AGEPIF>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
DIALYSIS-RELATED AMYLOIDOSIS; MAILLARD REACTION; LIVER-TRANSPLANTATION; ALZHEIMERS-DISEASE; TRANSTHYRETIN; IDENTIFICATION; GLYCOSYLATION; DYSFUNCTION; COLLAGEN; GLUCOSE;
Keywords:
AGE; amyloid; amyloidosis; FAP; TTR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Ando, Y Kumamoto Univ, Sch Med, Dept Internal Med, 1-1-1 Honjo, Kumamoto 860, Japan Kumamoto Univ 1-1-1 Honjo Kumamoto Japan 860 Kumamoto 860, Japan
Citazione:
N. Nyhlin et al., "Advanced glycation end product in familial amyloidotic polyneuropathy (FAP)", J INTERN M, 247(4), 2000, pp. 485-492

Abstract

Objectives. Advanced glycation end products (AGE) are present in amyloid deposits in beta(2)-microglobulin amyloidosis, and it has been postulated that glycation of beta(2)-microglobulin may be involved in fibril formation. The aim of this paper was to ascertain whether AGE occur in amyloid deposits in familial amyloidotic polyneuropathy (FAP). Setting. Department of Medicine, Umea University Hospital and First Department of Internal Medicine, Kumamoto University School of Medicine. Design. The presence of AGE was sought immunohistochemically and biochemically in amyloid-rich tissues from patients with FAP. Subjects. Biopsy specimens from nine patients and 10 controls were used for the immunohistochemical analysis. For amyloid preparation, vitreous samples from three FAP patients were used. Results. Immunohistochemical studies using a polyclonal anti-AGE antibody revealed positive immunoreactivity in intestinal materials, but the patternof reactivity was unevenly distributed; it was often present in the borderof amyloid deposits, or surrounding them. Non-amyloid associated immunoreactivity was also observed in a few regions of the specimens, although the AGE-positive structures were situated in areas containing amyloid deposits. Western blotting of purified amyloid from the vitreous body of FAP patientsrevealed a significant association of AGE with amyloid fibrils. Conclusions. The immunoreactivity for the AGE antibody suggests that AGE may be involved in fibril formation in FAP.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/09/20 alle ore 09:28:44