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 0014-5793Full text not available from this repository.
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.
|Journal or Publication Title:||FEBS Letters|
|Uncontrolled Keywords:||Amino Acid Sequence ; Amyloid ; Animals ; Copper ; Diabetes Mellitus, Type 2 ; Electron Spin Resonance Spectroscopy ; Humans ; Hydrogen Peroxide ; Ions ; Islet Amyloid Polypeptide ; Islets of Langerhans ; Microscopy, Atomic Force ; Microscopy, Electron, Transmission ; Molecular Sequence Data ; Sequence Alignment ; Sequence Homology|
|Departments:||Faculty of Science and Technology > Lancaster Environment Centre|
Faculty of Health and Medicine > Biomedical & Life Sciences
|Deposited On:||22 Aug 2011 16:08|
|Last Modified:||07 Jan 2015 16:48|
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