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Titolo:
Counteracting effects of renal solutes on amyloid fibril formation by immunoglobulin light chains
Autore:
Kim, YS; Cape, SP; Chi, E; Raffen, R; Wilkins-Stevens, P; Stevens, FJ; Manning, MC; Randolph, TW; Solomon, A; Carpenter, JF;
Indirizzi:
Univ Colorado, Hlth Sci Ctr, Sch Pharm, Dept Pharmaceut Sci, Denver, CO 80262 USA Univ Colorado Denver CO USA 80262 pt Pharmaceut Sci, Denver, CO 80262 USA Univ Colorado, Dept Chem Engn, Boulder, CO 80309 USA Univ Colorado Boulder CO USA 80309 Dept Chem Engn, Boulder, CO 80309 USA Argonne Natl Lab, Biosci Div, Argonne, IL 60439 USA Argonne Natl Lab Argonne IL USA 60439 , Biosci Div, Argonne, IL 60439 USA Univ Tennessee, Human Immunol & Canc Program, Grad Sch Med, Knoxville, TN 37920 USA Univ Tennessee Knoxville TN USA 37920 ad Sch Med, Knoxville, TN 37920 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 2, volume: 276, anno: 2001,
pagine: 1626 - 1633
SICI:
0021-9258(20010112)276:2<1626:CEORSO>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
PREFERENTIAL HYDRATION; CHEMICAL CHAPERONES; PROTEIN-STRUCTURE; IN-VITRO; AGGREGATION; DISEASE; SCRAPIE; FIBRILLOGENESIS; TRANSTHYRETIN; CONSEQUENCES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Carpenter, JF Univ Colorado, Hlth Sci Ctr, Sch Pharm, Dept Pharmaceut Sci,Denver, CO 80262 USA Univ Colorado Denver CO USA 80262 Sci, Denver, CO 80262 USA
Citazione:
Y.S. Kim et al., "Counteracting effects of renal solutes on amyloid fibril formation by immunoglobulin light chains", J BIOL CHEM, 276(2), 2001, pp. 1626-1633

Abstract

In primary (light chain-associated) amyloidosis, immunoglobulin light chains deposit as amyloid fibrils in vital organs, especially the kidney. Because the kidney contains high concentrations of urea that can destabilize light chains as well as solutes such as betaine and sorbitol that serve as protein stabilizers, we investigated the effects of these solutes on in vitro amyloid fibril formation and thermodynamic stability of light chains, Two recombinant light chain proteins, one amyloidogenic and the other nonamyloidogenic, were used as models, For both light chains, urea enhanced fibril formation by reducing the nucleation lag time and diminished protein thermodynamic stability. Conversely, betaine or sorbitol increased thermodynamic stability of the proteins and partially inhibited fibril formation. These solutes also counteracted urea-induced reduction in protein thermodynamic stability and accelerated fibril formation. Betaine was more effective than sorbitol. A model is presented to explain how the thermodynamic effects of thesolutes on protein state equilibria can alter nucleation lag time and, hence, fibril formation kinetics. Our results provide evidence that renal solutes control thermodynamic and kinetic stability of light chains and thus may modulate amyloid fibril formation in the kidney.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 08:35:20