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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: Article
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
Subjects: UNSPECIFIED
Departments: Faculty of Science and Technology > Lancaster Environment Centre
Faculty of Health and Medicine > Biomedical & Life Sciences
ID Code: 49162
Deposited By: ep_importer_pure
Deposited On: 22 Aug 2011 16:08
Refereed?: Yes
Published?: Published
Last Modified: 26 Jul 2012 19:25
Identification Number:
URI: http://eprints.lancs.ac.uk/id/eprint/49162

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