Document Detail


Zn(II) ions co-secreted with insulin suppress inherent amyloidogenic properties of monomeric insulin.
MedLine Citation:
PMID:  20632994     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Insulin, a 51-residue peptide hormone, is an intrinsically amyloidogenic peptide, forming amyloid fibrils in vitro. In the secretory granules, insulin is densely packed together with Zn(II) into crystals of Zn(2)Insulin(6) hexamer, which assures osmotic stability of vesicles and prevents fibrillation of the peptide. However, after release from the pancreatic beta-cells, insulin dissociates into active monomers, which tend to fibrillize not only at acidic, but also at physiological, pH values. The effect of co-secreted Zn(II) ions on the fibrillation of monomeric insulin is unknown, however, it might prevent insulin fibrillation. We showed that Zn(II) inhibits fibrillation of monomeric insulin at physiological pH values by forming a soluble Zn(II)-insulin complex. The inhibitory effect of Zn(II) ions is very strong at pH 7.3 (IC(50)=3.5 microM), whereas at pH 5.5 it progressively weakens, pointing towards participation of the histidine residue(s) in complex formation. The results obtained indicate that Zn(II) ions might suppress fibrillation of insulin at its release sites and in circulation. It is hypothesized that misfolded oligomeric intermediates occurring in the insulin fibrillation pathway, especially in zinc-deficient conditions, might induce autoantibodies against insulin, which leads to beta-cell damage and autoimmune Type 1 diabetes.
Authors:
Andra Noormägi; Julia Gavrilova; Julia Smirnova; Vello Tõugu; Peep Palumaa
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Biochemical journal     Volume:  430     ISSN:  1470-8728     ISO Abbreviation:  Biochem. J.     Publication Date:  2010 Sep 
Date Detail:
Created Date:  2010-08-27     Completed Date:  2010-10-05     Revised Date:  2011-09-06    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  England    
Other Details:
Languages:  eng     Pagination:  511-8     Citation Subset:  IM    
Affiliation:
Department of Gene Technology, Tallinn University of Technology, Estonia.
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MeSH Terms
Descriptor/Qualifier:
Algorithms
Amyloid / chemistry*,  metabolism,  ultrastructure
Hydrogen-Ion Concentration
Insulin / chemistry*,  metabolism
Ions
Kinetics
Microscopy, Electron, Transmission
Organometallic Compounds / chemistry*,  metabolism
Protein Binding
Protein Multimerization
Spectrometry, Mass, Electrospray Ionization
Temperature
Zinc / chemistry*,  metabolism
Chemical
Reg. No./Substance:
0/Amyloid; 0/Ions; 0/Organometallic Compounds; 11061-68-0/Insulin; 7440-66-6/Zinc

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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