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Copper ions induce dityrosine-linked dimers in human but not in murine islet amyloid polypeptide (IAPP/amylin)
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.
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Antal upphovsmän: 72019 (Engelska)Ingår i: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 510, nr 4, s. 520-524Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

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.

Ort, förlag, år, upplaga, sidor
2019. Vol. 510, nr 4, s. 520-524
Nyckelord [en]
Diabetes, Amyloid disease, Protein aggregation, Protein modification, Redox chemistry, Oxidative stress
Nationell ämneskategori
Biologiska vetenskaper
Identifikatorer
URN: urn:nbn:se:su:diva-167587DOI: 10.1016/j.bbrc.2019.01.120ISI: 000460188400006PubMedID: 30737030OAI: oai:DiVA.org:su-167587DiVA, id: diva2:1301629
Tillgänglig från: 2019-04-02 Skapad: 2019-04-02 Senast uppdaterad: 2022-02-26Bibliografiskt granskad

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Svantesson, TeodorWallin, CeciliaJarvet, JüriGräslund, AstridWärmländer, Sebastian K. T. S.

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Svantesson, TeodorWallin, CeciliaJarvet, JüriGräslund, AstridWärmländer, Sebastian K. T. S.
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