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Copper ions induce ...
Copper ions induce dityrosine-linked dimers in human but not in murine islet amyloid polypeptide (IAPP/amylin)
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Dong, Xiaolin (author)
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- Svantesson, Teodor (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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Sholts, Sabrina B. (author)
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- Wallin, Cecilia (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Jarvet, Jüri (author)
- Stockholms universitet,Institutionen för biokemi och biofysik,The National Institute of Chemical Physics and Biophysics, Estonia
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- Gräslund, Astrid (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Wärmländer, Sebastian K. T. S. (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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(creator_code:org_t)
- Elsevier BV, 2019
- 2019
- English.
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In: Biochemical and Biophysical Research Communications - BBRC. - : Elsevier BV. - 0006-291X .- 1090-2104. ; 510:4, s. 520-524
- Related links:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Subject headings
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- Dysregulation and aggregation of the peptide hormone IAPP (islet amyloid polypeptide, a.k.a. amylin) into soluble oligomers that appear to be cell-toxic is a known aspect of diabetes mellitus (DM) Type 2 pathology. IAPP aggregation is influenced by several factors including interactions with metal ions such as Cu(II). Because Cu(II) ions are redox-active they may contribute to metal-catalyzed formation of oxidative tyrosyl radicals, which can generate dityrosine cross-links. Here, we show that such a process, which involves Cu(II) ions bound to the IAPP peptide together with H2O2, can induce formation of large amounts of IAPP dimers connected by covalent dityrosine cross-links. This cross-linking is less pronounced at low pH and for murine IAPP, likely due to less efficient Cu(II) binding. Whether IAPP can carry out its hormonal function as a cross-linked dimer is unknown. As dityrosine concentrations are higher in blood plasma of DM Type 2 patients - arguably due to disease-related oxidative stress - and as dimer formation is the first step in protein aggregation, generation of dityrosine-linked dimers may be an important factor in IAPP aggregation and thus relevant for DM Type 2 progression.
Subject headings
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
Keyword
- Diabetes
- Amyloid disease
- Protein aggregation
- Protein modification
- Redox chemistry
- Oxidative stress
Publication and Content Type
- ref (subject category)
- art (subject category)
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