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Titolo:
Extension of A beta 2M amyloid fibrils with recombinant human beta 2-microglobulin
Autore:
Yamaguchi, I; Hasegawa, K; Naiki, H; Mitsu, T; Matuo, Y; Gejyo, F;
Indirizzi:
Niigata Univ, Sch Med, Dept Med 2, Niigata 9518510, Japan Niigata Univ Niigata Japan 9518510 d, Dept Med 2, Niigata 9518510, Japan Fukui Med Univ, Dept Pathol, Fukui 9101193, Japan Fukui Med Univ Fukui Japan 9101193 iv, Dept Pathol, Fukui 9101193, Japan Oriental Yeast Co Ltd, Nagahama Inst Biochem Sci, Shiga 5260804, Japan Oriental Yeast Co Ltd Shiga Japan 5260804 chem Sci, Shiga 5260804, Japan
Titolo Testata:
AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS
fascicolo: 1, volume: 8, anno: 2001,
pagine: 30 - 40
SICI:
1350-6129(200103)8:1<30:EOAB2A>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
DIALYSIS-RELATED AMYLOIDOSIS; GLYCATION END-PRODUCTS; IN-VITRO; APOLIPOPROTEIN-E; INTACT BETA-2-MICROGLOBULIN; CHRONIC-HEMODIALYSIS; KINETIC-MODEL; BETA(2)-MICROGLOBULIN; PROTEIN; POLYMERIZATION;
Keywords:
A beta 2M amyloidosis; recombinant beta 2microglobulin; extension reaction;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Gejyo, F Niigata Univ, Sch Med, Dept Med 2, Niigata 9518510, Japan NiigataUniv Niigata Japan 9518510 ed 2, Niigata 9518510, Japan
Citazione:
I. Yamaguchi et al., "Extension of A beta 2M amyloid fibrils with recombinant human beta 2-microglobulin", AMYLOID, 8(1), 2001, pp. 30-40

Abstract

In order to elucidate the pathogenesis of A beta 2M amyloidosis, we established an experimental system to study the mechanism of amyloid fibril formation or degradation in vitro. We compared the kinetics of A beta 2M amyloidfibril (fA4 beta 2M) extension with native beta 2microglobulin (n-beta 2M)purified from the urine of a patient suffering from renal insufficiency, with that with recombinant beta 2M (r-beta 2M) in vitro. n-beta 2M and r-beta 2M were incubated with fA beta 2M purified from synovial tissues excised from A beta 2M amyloidosis patients. ThefAPZM extension reaction could be explained by a first-order kinetic model in both beta 2Ms. The extension reaction was greatly dependent on the pH of the reaction mixture and maximum around pH 2.5-3.0 in both beta 2Ms. The fA beta 2M extended with both beta 2Ms assumed the similar helical filament structure, although the fibrils extended with r-beta 2M were slightly wider than those extended with n-beta 2Mand the former fibrils assumed a helical structure more clearly as compared to the latter In order to obtain pure, unmodified fA beta 2M, we next extended fA beta 2M repeatedly by the algorithmic protocol with r-beta 2M. As the generation of the extended fibrils proceeded, the initial rare of the extension reaction increased The ultrastructure of fibrils was completely preserved throughout the repeated extension steps. Sodium dodecyl sulfate polyacrylamide gel electrophoresis and immunoblotting revealed that fA beta 2Mextended repeatedly with r-beta 2M were composed solely of r-beta 2M. The use of these r-beta 2M and fA beta 2M will be advantageous to assess the effects of several amyloid-associated molecules in the formation or degradation of fA beta 2M in vitro.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/04/20 alle ore 00:21:21