B cell granule peptides affect human islet amyloid polypeptide (IAPP) fibril formation in vitro

Islet amyloid polypeptide (IAPP) forms fibrils spontaneously. We examined whether other B cell granule peptides affect formation of beta-pleated sheet fibrils in vitro from human IAPP. Quantitative radioassay (radioactivity of soluble IAPP after adding 125I-IAPP) and thioflavine fluorescence spectro...

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Published inBiochemical and biophysical research communications Vol. 236; no. 3; pp. 580 - 585
Main Authors Janciauskiene, S, Eriksson, S, Carlemalm, E, Ahrén, B
Format Journal Article
LanguageEnglish
Published United States 30.07.1997
Subjects
Amyloid - metabolism
Amyloid - ultrastructure
C-Peptide - pharmacology
Chromogranin A
Humans
Insulin - pharmacology
Islet Amyloid Polypeptide
Islets of Langerhans - metabolism
Microscopy, Electron
Pancreatic Hormones - pharmacology
Polymers - metabolism
Spectrometry, Fluorescence
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Summary:Islet amyloid polypeptide (IAPP) forms fibrils spontaneously. We examined whether other B cell granule peptides affect formation of beta-pleated sheet fibrils in vitro from human IAPP. Quantitative radioassay (radioactivity of soluble IAPP after adding 125I-IAPP) and thioflavine fluorescence spectroscopy showed that insulin, C-peptide, and pancreastatin inhibited fibril formation by 60-100% at ratio 100:1 (peptide:IAPP), whereas at 1:10 or 1:100, i.e., IAPP in excess, a potentiated IAPP fibril formation was induced by the peptides. Semi-quantitative analysis by electron microscopy yielded similar effects. Thus, spontaneous IAPP fibrillisation is influenced by other B cell secretory granule peptides in a molar ratio dependent manner.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:0006-291X
DOI:10.1006/bbrc.1997.7014