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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?

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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; Hayes, Lee; Tabner, Brian et al.
In: FEBS Letters, Vol. 581, No. 18, 2007, p. 3489-3493.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Masad, A, Hayes, L, Tabner, B, Turnbull, S, Cooper, L, Fullwood, NJ, German, M, Kametani, F, El-Agnaf, OMA & Allsop, D 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, vol. 581, no. 18, pp. 3489-3493. https://doi.org/10.1016/j.febslet.2007.06.061

APA

Masad, A., Hayes, L., Tabner, B., Turnbull, S., Cooper, L., Fullwood, N. J., German, M., Kametani, F., El-Agnaf, O. M. A., & Allsop, D. (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), 3489-3493. https://doi.org/10.1016/j.febslet.2007.06.061

Vancouver

Masad A, Hayes L, Tabner B, Turnbull S, Cooper L, Fullwood NJ et al. 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. 2007;581(18):3489-3493. doi: 10.1016/j.febslet.2007.06.061

Author

Masad, Atef ; Hayes, Lee ; Tabner, Brian et al. / Copper-mediated formation of hydrogen peroxide from the amylin peptide : a novel mechanism for degeneration of islet cells in type-2 diabetes mellitus?. In: FEBS Letters. 2007 ; Vol. 581, No. 18. pp. 3489-3493.

Bibtex

@article{9d820affd0734f44a907c0039a601636,
title = "Copper-mediated formation of hydrogen peroxide from the amylin peptide: a novel mechanism for degeneration of islet cells in type-2 diabetes mellitus?",
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.",
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",
author = "Atef Masad and Lee Hayes and Brian Tabner and Stuart Turnbull and Leanne Cooper and Fullwood, {Nigel J.} and Matthew German and Fuyuki Kametani and El-Agnaf, {Omar M. A.} and David Allsop",
year = "2007",
doi = "10.1016/j.febslet.2007.06.061",
language = "English",
volume = "581",
pages = "3489--3493",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "18",

}

RIS

TY - JOUR

T1 - Copper-mediated formation of hydrogen peroxide from the amylin peptide

T2 - a novel mechanism for degeneration of islet cells in type-2 diabetes mellitus?

AU - Masad, Atef

AU - Hayes, Lee

AU - Tabner, Brian

AU - Turnbull, Stuart

AU - Cooper, Leanne

AU - Fullwood, Nigel J.

AU - German, Matthew

AU - Kametani, Fuyuki

AU - El-Agnaf, Omar M. A.

AU - Allsop, David

PY - 2007

Y1 - 2007

N2 - 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.

AB - 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.

KW - Amino Acid Sequence

KW - Amyloid

KW - Animals

KW - Copper

KW - Diabetes Mellitus, Type 2

KW - Electron Spin Resonance Spectroscopy

KW - Humans

KW - Hydrogen Peroxide

KW - Ions

KW - Islet Amyloid Polypeptide

KW - Islets of Langerhans

KW - Microscopy, Atomic Force

KW - Microscopy, Electron, Transmission

KW - Molecular Sequence Data

KW - Sequence Alignment

KW - Sequence Homology

U2 - 10.1016/j.febslet.2007.06.061

DO - 10.1016/j.febslet.2007.06.061

M3 - Journal article

C2 - 17617411

VL - 581

SP - 3489

EP - 3493

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 18

ER -