Copper-mediated formation of hydrogen peroxide from the amylin peptide:a novel mechanism for degeneration of islet cells in type-2 diabetes mellitus?

Masad, Atef and Hayes, Lee and Tabner, Brian and Turnbull, Stuart and Cooper, Leanne and Fullwood, Nigel J. and German, Matthew and Kametani, Fuyuki and El-Agnaf, Omar M. A. and Allsop, David (2007) Copper-mediated formation of hydrogen peroxide from the amylin peptide:a novel mechanism for degeneration of islet cells in type-2 diabetes mellitus? FEBS Letters, 581 (18). pp. 3489-3493. ISSN 0014-5793

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Abstract

Amyloid deposits derived from the amylin peptide accumulate within pancreatic islet P-cells in most cases of type-2 diabetes mellitus (T2Dm). Human amylin 'oligomers' are toxic to these cells. Using two different experimental techniques, we found that H2O2 was generated during the aggregation of human amylin into amyloid fibrils. This process was greatly stimulated by Cu(II) ions, and human amylin was retained on a copper affinity column. In contrast, rodent amylin, which is not toxic, failed to generate any H2O2 and did not interact with copper. We conclude that the formation Of H202 from amylin could contribute to the progressive degeneration of islet cells in T213m. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Item Type:
Journal Article
Journal or Publication Title:
FEBS Letters
Uncontrolled Keywords:
/dk/atira/pure/subjectarea/asjc/1300/1304
Subjects:
ID Code:
49162
Deposited By:
Deposited On:
22 Aug 2011 15:08
Refereed?:
Yes
Published?:
Published
Last Modified:
17 Jun 2020 01:44