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

Atef Masad; Lee Hayes; Brian J. Tabner; Stuart Turnbull; Leanne J. Cooper; Nigel J. Fullwood; Matthew J. German; Fuyuki Kametani; Omar M.A. El-Agnaf; David Allsop

doi:10.1016/j.febslet.2007.06.061

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

Atef Masad, Lee Hayes, Brian J. Tabner, Stuart Turnbull, Leanne J. Cooper, Nigel J. Fullwood, Matthew J. German, Fuyuki Kametani, Omar M.A. El-Agnaf, David Allsop

Research output: Contribution to journal › Article › peer-review

75 Citations (Scopus)

Abstract

Amyloid deposits derived from the amylin peptide accumulate within pancreatic islet β-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 H₂O₂ from amylin could contribute to the progressive degeneration of islet cells in T2Dm.

Original language	English
Pages (from-to)	3489-3493
Number of pages	5
Journal	FEBS Letters
Volume	581
Issue number	18
DOIs	https://doi.org/10.1016/j.febslet.2007.06.061
Publication status	Published - Jul 24 2007
Externally published	Yes

Keywords

Amplex red
Amylin
Copper
Electron spin resonance
Hydrogen peroxide
Type-2 diabetes

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Access to Document

10.1016/j.febslet.2007.06.061

Cite this

Masad, A., Hayes, L., Tabner, B. J., Turnbull, S., Cooper, L. J., Fullwood, N. J., German, M. J., 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

Masad, A, Hayes, L, Tabner, BJ, Turnbull, S, Cooper, LJ, Fullwood, NJ, German, MJ, 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

@article{26a2195da35548569bd93e31e8ebc2bb,

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 β-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 H2O2 from amylin could contribute to the progressive degeneration of islet cells in T2Dm.",

keywords = "Amplex red, Amylin, Copper, Electron spin resonance, Hydrogen peroxide, Type-2 diabetes",

author = "Atef Masad and Lee Hayes and Tabner, {Brian J.} and Stuart Turnbull and Cooper, {Leanne J.} and Fullwood, {Nigel J.} and German, {Matthew J.} and Fuyuki Kametani and El-Agnaf, {Omar M.A.} and David Allsop",

note = "Funding Information: We thank The Ford Foundation (USA) for an International Postgraduate Research Studentship (to A.M.) and The Wellcome Trust for a Project Grant (GR065764AIA).",

year = "2007",

month = jul,

day = "24",

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",

}

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 J.

AU - Turnbull, Stuart

AU - Cooper, Leanne J.

AU - Fullwood, Nigel J.

AU - German, Matthew J.

AU - Kametani, Fuyuki

AU - El-Agnaf, Omar M.A.

AU - Allsop, David

N1 - Funding Information: We thank The Ford Foundation (USA) for an International Postgraduate Research Studentship (to A.M.) and The Wellcome Trust for a Project Grant (GR065764AIA).

PY - 2007/7/24

Y1 - 2007/7/24

N2 - Amyloid deposits derived from the amylin peptide accumulate within pancreatic islet β-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 H2O2 from amylin could contribute to the progressive degeneration of islet cells in T2Dm.

AB - Amyloid deposits derived from the amylin peptide accumulate within pancreatic islet β-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 H2O2 from amylin could contribute to the progressive degeneration of islet cells in T2Dm.

KW - Amplex red

KW - Amylin

KW - Copper

KW - Electron spin resonance

KW - Hydrogen peroxide

KW - Type-2 diabetes

UR - http://www.scopus.com/inward/record.url?scp=34447251553&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=34447251553&partnerID=8YFLogxK

U2 - 10.1016/j.febslet.2007.06.061

DO - 10.1016/j.febslet.2007.06.061

M3 - Article

C2 - 17617411

AN - SCOPUS:34447251553

SN - 0014-5793

VL - 581

SP - 3489

EP - 3493

JO - FEBS Letters

JF - FEBS Letters

IS - 18

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this