Effects of beta cell granule components on human islet amyloid polypeptide fibril formation.
FEBS Lett
; 379(3): 203-6, 1996 Feb 05.
Article
em En
| MEDLINE
| ID: mdl-8603689
ABSTRACT
Formation of amyloid-like fibrils in a solution of human islet amyloid polypeptide (hIAPP) with and without the presence of other beta-cell granule components was studied in vitro. Insulin at less than equimolar concentration strongly inhibited hIAPP fibrillogenesis. Proinsulin had a weaker inhibitory effect while C-peptide, Ca2+ and Zn2+ each individually enhanced fibril formation. C-peptide combined with Ca2+ had an inhibitory effect. Since IAPP was found almost exclusively in the halo fractions of isolated islet secretory granules, primarily the concentrations of C-peptide, Ca2+ and possibly proinsulin may be crucial for the native state of IAPP. It is concluded that an imbalance between fibril formation enhancers and inhibitors may be of importance in the pathogenesis of amyloid in the islets of Langerhans.
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Base de dados:
MEDLINE
Assunto principal:
Ilhotas Pancreáticas
/
Grânulos Citoplasmáticos
/
Amiloide
Idioma:
En
Ano de publicação:
1996
Tipo de documento:
Article