Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz

Gewählte Publikation:

SHR Neuro Krebs Kardio Lipid

Rodriguez Camargo, DC; Tripsianes, K; Buday, K; Franko, A; Göbl, C; Hartlmüller, C; Sarkar, R; Aichler, M; Mettenleiter, G; Schulz, M; Böddrich, A; Erck, C; Martens, H; Walch, AK; Madl, T; Wanker, EE; Conrad, M; de Angelis, MH; Reif, B.
The redox environment triggers conformational changes and aggregation of hIAPP in Type II Diabetes.
SCI REP-UK. 2017; 7(6): 44041-44041. [OPEN ACCESS]
Web of Science PubMed PUBMED Central FullText FullText_MUG


Autor/innen der Med Uni Graz:
Madl Tobias

Dimensions Citations:

Plum Analytics:
Number of Figures: 3
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Type II diabetes (T2D) is characterized by diminished insulin production and resistance of cells to insulin. Among others, endoplasmic reticulum (ER) stress is a principal factor contributing to T2D and induces a shift towards a more reducing cellular environment. At the same time, peripheral insulin resistance triggers the over-production of regulatory hormones such as insulin and human islet amyloid polypeptide (hIAPP). We show that the differential aggregation of reduced and oxidized hIAPP assists to maintain the redox equilibrium by restoring redox equivalents. Aggregation thus induces redox balancing which can assist initially to counteract ER stress. Failure of the protein degradation machinery might finally result in β-cell disruption and cell death. We further present a structural characterization of hIAPP in solution, demonstrating that the N-terminus of the oxidized peptide has a high propensity to form an α-helical structure which is lacking in the reduced state of hIAPP. In healthy cells, this residual structure prevents the conversion into amyloidogenic aggregates.
Find related publications in this database (using NLM MeSH Indexing)
Animals -
Diabetes Mellitus, Type 2 - metabolism
Diabetes Mellitus, Type 2 - pathology
Endoplasmic Reticulum Stress -
Female -
Humans -
Islet Amyloid Polypeptide - chemistry
Islet Amyloid Polypeptide - metabolism
Mice, Inbred BALB C -
Mice, Transgenic -
Oxidation-Reduction -
Protein Aggregation, Pathological -
Protein Conformation -

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